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Protein

Structural maintenance of chromosomes protein 1

Gene

psm1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in chromosome cohesion during cell cycle and in DNA repair. Central component of cohesin complex. The cohesin complex is required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi32 – 398ATPCurated

GO - Molecular functioni

GO - Biological processi

  • cell division Source: UniProtKB-KW
  • mitotic sister chromatid cohesion Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-SPO-2500257. Resolution of Sister Chromatid Cohesion.

Names & Taxonomyi

Protein namesi
Recommended name:
Structural maintenance of chromosomes protein 1
Alternative name(s):
Chromosome segregation protein smc1
Cohesin complex subunit psm1
Gene namesi
Name:psm1
Synonyms:smc1
ORF Names:SPBC29A10.04
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC29A10.04.
PomBaseiSPBC29A10.04. psm1.

Subcellular locationi

GO - Cellular componenti

  • chromosome Source: UniProtKB
  • cohesin complex Source: UniProtKB
  • cohesin core heterodimer Source: PomBase
  • nuclear mitotic cohesin complex Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12281228Structural maintenance of chromosomes protein 1PRO_0000119010Add
BLAST

Proteomic databases

MaxQBiO94383.
PRIDEiO94383.

Interactioni

Subunit structurei

Cohesin complexes are composed of the psm1/smc1 and psm3/smc3 heterodimer attached via their hinge domain, rad21/scc1 which link them, and psc3/scc3, which interacts with rad21.

Binary interactionsi

WithEntry#Exp.IntActNotes
psm3O426493EBI-1151900,EBI-1151879

Protein-protein interaction databases

BioGridi277084. 10 interactions.
IntActiO94383. 2 interactions.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni511 – 709199Flexible hingeAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili197 – 510314Sequence analysisAdd
BLAST
Coiled coili710 – 78374Sequence analysisAdd
BLAST
Coiled coili814 – 926113Sequence analysisAdd
BLAST
Coiled coili984 – 106885Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1132 – 116736Ala/Asp-rich (DA-box)Add
BLAST

Domaini

The flexible hinge domain, which separates the large intramolecular coiled coil regions, allows the heterotypic interaction with the corresponding domain of psm3, forming a V-shaped heterodimer. The two heads of the heterodimer are then connected by different ends of the cleavable rad21 protein, forming a ring structure (By similarity).By similarity

Sequence similaritiesi

Belongs to the SMC family. SMC1 subfamily.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

HOGENOMiHOG000195481.
InParanoidiO94383.
KOiK06636.
OMAiGPGMQFI.
OrthoDBiEOG092C0XGI.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR027417. P-loop_NTPase.
IPR003395. RecF/RecN/SMC_N.
IPR024704. SMC.
IPR028468. Smc1.
IPR010935. SMC_hinge.
[Graphical view]
PANTHERiPTHR18937:SF169. PTHR18937:SF169. 3 hits.
PfamiPF06470. SMC_hinge. 1 hit.
PF02463. SMC_N. 1 hit.
[Graphical view]
PIRSFiPIRSF005719. SMC. 1 hit.
SMARTiSM00968. SMC_hinge. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
SSF75553. SSF75553. 1 hit.

Sequencei

Sequence statusi: Complete.

O94383-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGRLLRLEVE NFKSYRGHQI IGPFEDFTSI IGPNGAGKSN LMDAISFVLG
60 70 80 90 100
VKSSHLRSTN VKELIYRGKI LQRDNTDFTD SSNPTTAYVK LMYELDNGEQ
110 120 130 140 150
REYKRAITPS GATEYKIDEE IVTFSEYCGS LQKENILVRA RNFLVFQGDV
160 170 180 190 200
ETIASQSPLE LSKLVEQISG SLEYKSEYDK SKDEQDKAVN LSAHSFNKKR
210 220 230 240 250
GINAELRQYQ EQKTEAERYQ SQKEKRDSAQ LVYLLWKLFH LEKSISSNMA
260 270 280 290 300
EVTRLKADSI QLIERRDENT KEIEKLKEKE GSIRRNLLAF DRKVRKQEKL
310 320 330 340 350
IASKRPELIS IAEKALESKS NLRKIQRKAA EIEKDYSDQA STLQVLENQL
360 370 380 390 400
TSLSAAEKEF LKDMQEKEQL KGLRLLPEDK EEYEGLRSEA DKLNSNLLFK
410 420 430 440 450
LQTLNRNIKV TSQSKDSLTS IVGDLESKIK SLHESVSSLD TERADLLAKI
460 470 480 490 500
NEKIESLELE KHDQQKKRLT YSELFHKTQE LNEELQSCLQ KILEASADRN
510 520 530 540 550
ESKQDAKKRE ALYALKRIYP EVKGRIIDLC TPTQKKYESA IAAALGKNFD
560 570 580 590 600
AIVVETQAVA KECIDYIKEQ RIGIMTFFPM DTIAASPVNQ KFRGTHKGAR
610 620 630 640 650
LAIDVLNFES EYERVMISAV GNTLICDSMT VARDLSYNKR LNAKTVTLEG
660 670 680 690 700
TVIHKTGLIT GGSSNNRSAK HWDDHDFDLL TQTKDRLMHQ IGEIEYQKSS
710 720 730 740 750
CVITESDTVK LHSLESEISL LKDKYTVVSR SVEDKKKEIG HYESLIKEKQ
760 770 780 790 800
PHLSELEMEL RNFVKSRDEL QIQVEKVEEK IFSGFCKRIG ISDIHTYDEI
810 820 830 840 850
HRTFTQSFTQ KQLEFTKQKS LLENRISFEK QRVSDTRLRL ERMHKFIEKD
860 870 880 890 900
QESIDNYEQN REALESEVAT AEAELELLKE DFASENSKTE KILLAASEKK
910 920 930 940 950
LVGKRLVSEL TKLSGNITLL ESEIDRYVSE WHAILRKCKL EDIDVPLREG
960 970 980 990 1000
SLTSIPIDDV SNSGDITMGE EPSEPVINFE KFGVEVDYDE LDEELRNDGS
1010 1020 1030 1040 1050
ESMASVLQEK LREYSEELDQ MSPNLRAIER LETVETRLAK LDEEFAAARK
1060 1070 1080 1090 1100
AAKNAKERFN AVKQKRLQKF QAAFSHISEQ IDPIYKELTK SPAFPLGGTA
1110 1120 1130 1140 1150
YLTLDDLDEP YLGGIKFHAM PPMKRFRDMD QLSGGEKTMA ALALLFAIHS
1160 1170 1180 1190 1200
YQPSPFFVLD EIDAALDQTN VTKIANYIRQ HASSGFQFVV ISLKNQLFSK
1210 1220
SEALVGIYRD QQENSSRTLS INLEGYVE
Length:1,228
Mass (Da):140,522
Last modified:October 3, 2012 - v2
Checksum:i915817D9AF404CEC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAA22432.2.
PIRiT40059.
RefSeqiNP_596049.2. NM_001021960.2.

Genome annotation databases

EnsemblFungiiSPBC29A10.04.1; SPBC29A10.04.1:pep; SPBC29A10.04.
GeneIDi2540557.
KEGGispo:SPBC29A10.04.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAA22432.2.
PIRiT40059.
RefSeqiNP_596049.2. NM_001021960.2.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi277084. 10 interactions.
IntActiO94383. 2 interactions.

Proteomic databases

MaxQBiO94383.
PRIDEiO94383.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC29A10.04.1; SPBC29A10.04.1:pep; SPBC29A10.04.
GeneIDi2540557.
KEGGispo:SPBC29A10.04.

Organism-specific databases

EuPathDBiFungiDB:SPBC29A10.04.
PomBaseiSPBC29A10.04. psm1.

Phylogenomic databases

HOGENOMiHOG000195481.
InParanoidiO94383.
KOiK06636.
OMAiGPGMQFI.
OrthoDBiEOG092C0XGI.

Enzyme and pathway databases

ReactomeiR-SPO-2500257. Resolution of Sister Chromatid Cohesion.

Miscellaneous databases

PROiO94383.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR027417. P-loop_NTPase.
IPR003395. RecF/RecN/SMC_N.
IPR024704. SMC.
IPR028468. Smc1.
IPR010935. SMC_hinge.
[Graphical view]
PANTHERiPTHR18937:SF169. PTHR18937:SF169. 3 hits.
PfamiPF06470. SMC_hinge. 1 hit.
PF02463. SMC_N. 1 hit.
[Graphical view]
PIRSFiPIRSF005719. SMC. 1 hit.
SMARTiSM00968. SMC_hinge. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
SSF75553. SSF75553. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiSMC1_SCHPO
AccessioniPrimary (citable) accession number: O94383
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 10, 2003
Last sequence update: October 3, 2012
Last modified: September 7, 2016
This is version 121 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.