P14242 (PMS1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
DNA mismatch repair protein PMS1

Alternative name(s):
Postmeiotic segregation protein 1

Gene names

Name:	PMS1
Ordered Locus Names:	YNL082W
ORF Names:	N2317

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	873 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Required for DNA mismatch repair (MMR), correcting base-base mismatches and insertion-deletion loops (IDLs) resulting from DNA replication, DNA damage or from recombination events between non-identical sequences during meiosis. Component of the MutLalpha heterodimer that forms a ternary complex with the MutS heterodimers, which initially recognize the DNA mismatches. This complex is thought to be responsible for directing the downsteam MMR events, including strand discrimination, excision, and resynthesis. Plays a major role in maintaining the genetic stability of simple sequence repeats and in the repair of heteroduplex sites present in meiotic recombination intermediates. Ref.10 Ref.11 Ref.19
Subunit structure	Heterodimer of MLH1 and PMS1, called MutLalpha, which is the major MMR MutL activity correcting base-base mismatches as well as IDLs. The heterodimer binds double strand DNA independently of a mismatch with positive cooperativity and has more than one DNA binding site. Forms a ternary complex with either the MSH2-MSH6 (MutSalpha) or the MSH2-MSH3 heterodimer (MutSbeta), which recognize and bind to mismatch DNA. Ternary complex formation is promoted by ATP binding. Ref.10
Subcellular location	Nucleus Ref.16.
Miscellaneous	Present with 521 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the DNA mismatch repair MutL/HexB family.
Biophysicochemical properties	Kinetic parameters: KM=1.5 mM for ATP Ref.14
Sequence caution	The sequence AAA34885.1 differs from that shown. Reason: Erroneous initiation. The sequence AAM00521.1 differs from that shown. Reason: Erroneous initiation. The sequence AAM00533.1 differs from that shown. Reason: Erroneous initiation. The sequence AAM00545.1 differs from that shown. Reason: Erroneous initiation. The sequence AAM00551.1 differs from that shown. Reason: Erroneous initiation. The sequence AAM00563.1 differs from that shown. Reason: Erroneous initiation. The sequence AAM00569.1 differs from that shown. Reason: Erroneous initiation. The sequence CAA60176.1 differs from that shown. Reason: Erroneous initiation. The sequence CAA61428.1 differs from that shown. Reason: Erroneous initiation. The sequence CAA95956.1 differs from that shown. Reason: Erroneous initiation. The sequence CAA95957.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	DNA damage DNA repair
Cellular component	Nucleus
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	meiotic mismatch repair Inferred from mutant phenotype PubMed 16702432. Source: SGD reciprocal meiotic recombination Inferred from Biological aspect of Ancestor. Source: RefGenome
Cellular_component	MutLalpha complex Inferred from physical interaction Ref.11. Source: SGD cytoplasm Inferred from direct assay Ref.16. Source: SGD
Molecular_function	ATP binding Inferred from mutant phenotype Ref.12. Source: SGD ATPase activity Inferred from direct assay Ref.14. Source: SGD mismatched DNA binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MLH1	P38920	7	EBI-13561,EBI-11003

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 873

873

DNA mismatch repair protein PMS1

PRO_0000245571

Regions

Region

1 – 357

357

DNA- and ATP-binding

Region

661 – 873

213

Interaction with MLH1

Amino acid modifications

Modified residue

393

1

Phosphoserine Ref.20 Ref.21

Modified residue

598

1

Phosphoserine Ref.21

Natural variations

Natural variant

41

1

N → S in strain: SK1 and YJM421. Ref.2 Ref.3

Natural variant

112

1

I → T in strain: SK1 and YJM421. Ref.2 Ref.3

Natural variant

384

1

F → V in strain: SK1, YJM320, YJM339 and YJM421. Ref.2 Ref.3

Natural variant

392

1

E → V in strain: YJM320. Ref.2

Natural variant

400

1

T → S in strain: SK1, YJM320, YJM339 and YJM421. Ref.2 Ref.3

Natural variant

401

1

A → S in strain: YJM320 and YJM421. Ref.2

Natural variant

416

1

T → TCEGT in strain: SK1, YJM320, YJM339 and YJM421.

Natural variant

458

1

D → Y in strain: EAY1068. Ref.4

Natural variant

475

1

D → N in strain: YJM339. Ref.2

Natural variant

513

1

Y → F in strain: SK1. Ref.3

Natural variant

564

1

A → V in strain: YJM320. Ref.2

Natural variant

768

1

K → R in strain: YJM320. Ref.2

Natural variant

818

1

R → K in strain: SK1 and YJM320; forms a non-functional heterodimer with MHL1 from strain S288c, resulting in an accumulation of mutations in spore progeny of crosses between these strains. Ref.2 Ref.3

Experimental info

Mutagenesis

30

1

E → A: Reduces ATPase activity by 62%. Displays 60-fold increase in spontaneous mutation accumulation. Ref.12 Ref.14

Mutagenesis

34

1

N → A: Reduces ATPase activity by 84%. Displays 11000-fold increase in spontaneous mutation accumulation. Ref.14

Mutagenesis

95

1

F → A: Displays an increase in spontaneous mutation accumulation. Does not impair heterodimer formation. Ref.9

Mutagenesis

97

1

G → A: Displays an increase in spontaneous mutation accumulation. Ref.12

Mutagenesis

297

1

K → E: Displays a 60-fold increase in spontaneous mutation accumulation. Ref.18

Mutagenesis

851

1

G → E: Confers a strong defect in the repair of primer strand-specific 1-bp loops during DNA replication, but not during meoitic recombination. Does not impair heterodimer formation. Ref.19

Mutagenesis

857

1

H → R: Confers a strong defect in the repair of primer strand-specific 1-bp loops during DNA replication, but not during meoitic recombination. Does not impair heterodimer formation. Ref.19

Sequence conflict

695

1

Y → S in AAA34885. Ref.1

Sequence conflict

861

1

L → I in AAA34885. Ref.1

Secondary structure

1

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873

Helix Strand Turn

Details...

Helix

13 – 20

8

Helix

24 – 37

14

Beta strand

41 – 48

8

Turn

49 – 52

4

Beta strand

53 – 59

7

Helix

66 – 68

3

Turn

69 – 73

5

Beta strand

92 – 95

4

Helix

98 – 105

8

Beta strand

106 – 116

11

Beta strand

120 – 125

6

Beta strand

131 – 137

7

Beta strand

140 – 149

10

Turn

150 – 153

4

Helix

155 – 162

8

Helix

165 – 182

18

Beta strand

187 – 193

7

Beta strand

199 – 204

6

Helix

211 – 219

9

Turn

221 – 226

6

Beta strand

227 – 235

9

Helix

237 – 239

3

Beta strand

259 – 267

9

Beta strand

274 – 285

12

Beta strand

288 – 290

3

Helix

293 – 304

12

Beta strand

314 – 319

6

Helix

322 – 324

3

Beta strand

330 – 332

3

Helix

341 – 361

21

Helix

650 – 652

3

Helix

653 – 665

13

Helix

668 – 672

5

Beta strand

675 – 680

6

Turn

681 – 683

3

Beta strand

684 – 690

7

Beta strand

695 – 701

7

Helix

702 – 717

16

Beta strand

722 – 731

10

Helix

739 – 742

4

Helix

747 – 750

4

Beta strand

767 – 773

7

Helix

782 – 794

13

Helix

806 – 819

14

Helix

829 – 838

10

Helix

839 – 841

3

Beta strand

842 – 844

3

Beta strand

853 – 860

8

Helix

869 – 871

3

Sequences

	Sequence		Length	Mass (Da)
	P14242 [UniParc]. Last modified July 11, 2006. Version 3. Checksum: 2E0FFBC59B718854	FASTA	873	99,355
	10 20 30 40 50 60 MTQIHQINDI DVHRITSGQV ITDLTTAVKE LVDNSIDANA NQIEIIFKDY GLESIECSDN 70 80 90 100 110 120 GDGIDPSNYE FLALKHYTSK IAKFQDVAKV QTLGFRGEAL SSLCGIAKLS VITTTSPPKA 130 140 150 160 170 180 DKLEYDMVGH ITSKTTTSRN KGTTVLVSQL FHNLPVRQKE FSKTFKRQFT KCLTVIQGYA 190 200 210 220 230 240 IINAAIKFSV WNITPKGKKN LILSTMRNSS MRKNISSVFG AGGMRGLEEV DLVLDLNPFK 250 260 270 280 290 300 NRMLGKYTDD PDFLDLDYKI RVKGYISQNS FGCGRNSKDR QFIYVNKRPV EYSTLLKCCN 310 320 330 340 350 360 EVYKTFNNVQ FPAVFLNLEL PMSLIDVNVT PDKRVILLHN ERAVIDIFKT TLSDYYNRQE 370 380 390 400 410 420 LALPKRMCSQ SEQQAQKRLK TEVFDDRSTT HESDNENYHT ARSESNQSNH AHFNSTTGVI 430 440 450 460 470 480 DKSNGTELTS VMDGNYTNVT DVIGSECEVS VDSSVVLDEG NSSTPTKKLP SIKTDSQNLS 490 500 510 520 530 540 DLNLNNFSNP EFQNITSPDK ARSLEKVVEE PVYFDIDGEK FQEKAVLSQA DGLVFVDNEC 550 560 570 580 590 600 HEHTNDCCHQ ERRGSTDTEQ DDEADSIYAE IEPVEINVRT PLKNSRKSIS KDNYRSLSDG 610 620 630 640 650 660 LTHRKFEDEI LEYNLSTKNF KEISKNGKQM SSIISKRKSE AQENIIKNKD ELEDFEQGEK 670 680 690 700 710 720 YLTLTVSKND FKKMEVVGQF NLGFIIVTRK VDNKYDLFIV DQHASDEKYN FETLQAVTVF 730 740 750 760 770 780 KSQKLIIPQP VELSVIDELV VLDNLPVFEK NGFKLKIDEE EEFGSRVKLL SLPTSKQTLF 790 800 810 820 830 840 DLGDFNELIH LIKEDGGLRR DNIRCSKIRS MFAMRACRSS IMIGKPLNKK TMTRVVHNLS 850 860 870 ELDKPWNCPH GRPTMRHLME LRDWSSFSKD YEI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and nucleotide sequence of DNA mismatch repair gene PMS1 from Saccharomyces cerevisiae: homology of PMS1 to procaryotic MutL and HexB." Kramer W., Kramer B., Williamson M.S., Fogel S. J. Bacteriol. 171:5339-5346(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Dissecting the architecture of a quantitative trait locus in yeast." Steinmetz L.M., Sinha H., Richards D.R., Spiegelman J.I., Oefner P.J., McCusker J.H., Davis R.W. Nature 416:326-330(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS SER-41; THR-112; VAL-384; VAL-392; SER-400; SER-401; 416-THR--THR-420; ASN-475; VAL-564; ARG-768 AND LYS-818. Strain: ATCC 200060 / W303, S96, SK1, YJM 339 and YJM 421.
[3]	"Quantitative trait loci mapped to single-nucleotide resolution in yeast." Deutschbauer A.M., Davis R.W. Nat. Genet. 37:1333-1340(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS SER-41; THR-112; VAL-384; SER-400; 416-THR--THR-420; PHE-513 AND LYS-818. Strain: SK1.
[4]	"Negative epistasis between natural variants of the Saccharomyces cerevisiae MLH1 and PMS1 genes results in a defect in mismatch repair." Heck J.A., Argueso J.L., Gemici Z., Reeves R.G., Bernard A., Aquadro C.F., Alani E. Proc. Natl. Acad. Sci. U.S.A. 103:3256-3261(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT TYR-458. Strain: EAY1066, EAY1068, M2-8, M5-7 and M7-8.
[5]	"Sequencing a cosmid clone of Saccharomyces cerevisiae chromosome XIV reveals 12 new open reading frames (ORFs) and an ancient duplication of six ORFs." Poehlmann R., Philippsen P. Yeast 12:391-402(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[6]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications." Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J. , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J. Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[7]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[8]	"The sequence of a 17,933 bp segment of Saccharomyces cerevisiae chromosome XIV contains the RHO2, TOP2, MKT1 and END3 genes and five new open reading frames." Soler-Mira A., Saiz J.E., Ballesta J.P.G., Remacha M.A. Yeast 12:485-491(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-225. Strain: ATCC 96604 / S288c / FY1679.
[9]	"Functional domains of the Saccharomyces cerevisiae Mlh1p and Pms1p DNA mismatch repair proteins and their relevance to human hereditary nonpolyposis colorectal cancer-associated mutations." Pang Q., Prolla T.A., Liskay R.M. Mol. Cell. Biol. 17:4465-4473(1997) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MLH1, MUTAGENESIS OF PHE-95.
[10]	"ATP-dependent assembly of a ternary complex consisting of a DNA mismatch and the yeast MSH2-MSH6 and MLH1-PMS1 protein complexes." Habraken Y., Sung P., Prakash L., Prakash S. J. Biol. Chem. 273:9837-9841(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBUNIT.
[11]	"Functional specificity of MutL homologs in yeast: evidence for three Mlh1-based heterocomplexes with distinct roles during meiosis in recombination and mismatch correction." Wang T.-F., Kleckner N., Hunter N. Proc. Natl. Acad. Sci. U.S.A. 96:13914-13919(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH MLH1.
[12]	"Functional studies on the candidate ATPase domains of Saccharomyces cerevisiae MutLalpha." Tran P.T., Liskay R.M. Mol. Cell. Biol. 20:6390-6398(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MLH1, ATP-BINDING, MUTAGENESIS OF GLU-30 AND GLY-97.
[13]	"DNA binding properties of the yeast Msh2-Msh6 and Mlh1-Pms1 heterodimers." Drotschmann K., Hall M.C., Shcherbakova P.V., Wang H., Erie D.A., Brownewell F.R., Kool E.T., Kunkel T.A. Biol. Chem. 383:969-975(2002) [PubMed] [Europe PMC] [Abstract] Cited for: DNA-BINDING.
[14]	"Differential ATP binding and intrinsic ATP hydrolysis by amino-terminal domains of the yeast Mlh1 and Pms1 proteins." Hall M.C., Shcherbakova P.V., Kunkel T.A. J. Biol. Chem. 277:3673-3679(2002) [PubMed] [Europe PMC] [Abstract] Cited for: ATP-BINDING, MUTAGENESIS OF GLU-30 AND ASN-34, BIOPHYSICOCHEMICAL PROPERTIES.
[15]	"Sequencing and comparison of yeast species to identify genes and regulatory elements." Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S. Nature 423:241-254(2003) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION OF PROBABLE INITIATION SITE.
[16]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[17]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[18]	"DNA binding by yeast Mlh1 and Pms1: implications for DNA mismatch repair." Hall M.C., Shcherbakova P.V., Fortune J.M., Borchers C.H., Dial J.M., Tomer K.B., Kunkel T.A. Nucleic Acids Res. 31:2025-2034(2003) [PubMed] [Europe PMC] [Abstract] Cited for: DNA-BINDING, MUTAGENESIS OF LYS-297.
[19]	"Novel PMS1 alleles preferentially affect the repair of primer strand loops during DNA replication." Erdeniz N., Dudley S., Gealy R., Jinks-Robertson S., Liskay R.M. Mol. Cell. Biol. 25:9221-9231(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF GLY-851 AND HIS-857.
[20]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393, MASS SPECTROMETRY.
[21]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393 AND SER-598, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M29688 Genomic DNA. Translation: AAA34885.1. Different initiation.
AF458969 Genomic DNA. Translation: AAM00521.1. Different initiation.
AF458971 Genomic DNA. Translation: AAM00533.1. Different initiation.
AF458973 Genomic DNA. Translation: AAM00545.1. Different initiation.
AF458974 Genomic DNA. Translation: AAM00551.1. Different initiation.
AF458976 Genomic DNA. Translation: AAM00563.1. Different initiation.
AF458977 Genomic DNA. Translation: AAM00569.1. Different initiation.
DQ115393 Genomic DNA. Translation: AAZ22526.1.
DQ356628 Genomic DNA. Translation: ABC86932.1.
DQ356629 Genomic DNA. Translation: ABC86933.1.
DQ356630 Genomic DNA. Translation: ABC86934.1.
DQ356631 Genomic DNA. Translation: ABC86935.1.
DQ356632 Genomic DNA. Translation: ABC86936.1.
X86470 Genomic DNA. Translation: CAA60176.1. Different initiation.
Z71357 Genomic DNA. Translation: CAA95956.1. Different initiation.
Z71358 Genomic DNA. Translation: CAA95957.1. Different initiation.
X89016 Genomic DNA. Translation: CAA61428.1. Different initiation.
BK006947 Genomic DNA. Translation: DAA10463.1.

PIR

S53896.

RefSeq

NP_014317.4. NM_001182920.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3H4L	X-ray	2.50	A/B	1-365	[»]
4E4W	X-ray	2.50	B	635-873	[»]
4FMN	X-ray	2.69	B	635-873	[»]
4FMO	X-ray	3.04	B	635-873	[»]

ProteinModelPortal

P14242.

SMR

P14242. Positions 6-362.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-2416N.

IntAct

P14242. 4 interactions.

MINT

MINT-625253.

Proteomic databases

PaxDb

P14242.

PeptideAtlas

P14242.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YNL082W; YNL082W; YNL082W.

GeneID

855642.

KEGG

sce:YNL082W.

Organism-specific databases

CYGD

YNL082w.

SGD

S000005026. PMS1.

Phylogenomic databases

eggNOG

COG0323.

GeneTree

ENSGT00530000063289.

KO

K10858.

OMA

LDKPWNC.

OrthoDB

EOG4FFH9B.

Enzyme and pathway databases

BioCyc

YEAST:G3O-33111-MONOMER.

Gene expression databases

Genevestigator

P14242.

GermOnline

YNL082W. Saccharomyces cerevisiae.

Family and domain databases

Gene3D

3.30.230.10. 1 hit.
3.30.565.10. 1 hit.

InterPro

IPR002099. DNA_mismatch_repair.
IPR013507. DNA_mismatch_repair_C.
IPR014762. DNA_mismatch_repair_CS.
IPR014763. DNA_mismatch_repair_N.
IPR003594. HATPase_ATP-bd.
IPR014790. MutL_C.
IPR015434. Pms1/Mlh2.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
[Graphical view]

PANTHER

PTHR10073. PTHR10073. 1 hit.
PTHR10073:SF9. PTHR10073:SF9. 1 hit.

Pfam

PF01119. DNA_mis_repair. 1 hit.
PF02518. HATPase_c. 1 hit.
PF08676. MutL_C. 1 hit.
[Graphical view]

SMART

SM00387. HATPase_c. 1 hit.
SM00853. MutL_C. 1 hit.
[Graphical view]

SUPFAM

SSF55874. ATP_bd_ATPase. 1 hit.
SSF54211. Ribosomal_S5_D2-typ_fold. 1 hit.

TIGRFAMs

TIGR00585. mutl. 1 hit.

PROSITE

PS00058. DNA_MISMATCH_REPAIR_1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P14242.

NextBio

979872.

Entry information

Entry name

PMS1_YEAST

Accession

Primary (citable) accession number: P14242
Secondary accession number(s): D6W197 , Q2I044, Q2I045, Q45TY4, Q8TG48, Q8TG50, Q8TG54, Q8TG57

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	July 11, 2006
Last modified:	May 29, 2013
This is version 136 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program