Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Structural maintenance of chromosomes protein 6

Gene

smc6

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

Acts in a DNA repair pathway for removal of UV-induced DNA damage that is distinct from classical nucleotide excision repair and in repair of ionizing radiation damage. Functions in homologous recombination repair of DNA double strand breaks and in recovery of stalled replication forks. Plays a critical role in meiosis.1 Publication

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi124 – 131ATPSequence analysis8

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • double-stranded DNA-dependent ATPase activity Source: PomBase

GO - Biological processi

  • double-strand break repair via homologous recombination Source: PomBase
  • meiotic cell cycle Source: UniProtKB-KW
  • resolution of recombination intermediates Source: InterPro
Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA recombination, DNA repair, Meiosis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Structural maintenance of chromosomes protein 6
Alternative name(s):
DNA repair protein rad18
Gene namesi
Name:smc6
Synonyms:rad18
ORF Names:SPCC5E4.06
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome III

Organism-specific databases

EuPathDBiFungiDB:SPCC5E4.06.
PomBaseiSPCC5E4.06. smc6.

Subcellular locationi

GO - Cellular componenti

  • nucleus Source: PomBase
  • Smc5-Smc6 complex Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi151A → T in NA74; induces defects in DNA repair. 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001190211 – 1140Structural maintenance of chromosomes protein 6Add BLAST1140

Post-translational modificationi

Sumoylated by nse2.1 Publication

Keywords - PTMi

Ubl conjugation

Proteomic databases

MaxQBiP53692.
PRIDEiP53692.

Interactioni

Subunit structurei

Two subcomplexes smc5-smc6-nse2 and nse1-nse3-nse4 exist. These subcomplexes are then brought together via a number of interactions, forming the Smc5-Smc6 complex.

Binary interactionsi

WithEntry#Exp.IntActNotes
nse1Q53EK24EBI-603745,EBI-605440
nse2Q4PIR33EBI-603745,EBI-605449
nse3Q9Y7U45EBI-603745,EBI-605466
nse4Q6BDR84EBI-603745,EBI-605484
nse5O946682EBI-603745,EBI-1150352
nse6O136884EBI-603745,EBI-1150368
smc5O1371010EBI-603745,EBI-603756

Protein-protein interaction databases

BioGridi275593. 26 interactors.
IntActiP53692. 8 interactors.
MINTiMINT-4690882.

Structurei

3D structure databases

ProteinModelPortaliP53692.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni494 – 710Flexible hingeAdd BLAST217

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili262 – 290Sequence analysisAdd BLAST29
Coiled coili329 – 369Sequence analysisAdd BLAST41
Coiled coili448 – 493Sequence analysisAdd BLAST46
Coiled coili711 – 978Sequence analysisAdd BLAST268
Coiled coili1113 – 1140Sequence analysisAdd BLAST28

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi22 – 25Nuclear localization signalSequence analysis4
Motifi41 – 44Nuclear localization signalSequence analysis4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi1044 – 1079Ala/Asp-rich (DA-box)Add BLAST36

Domaini

The flexible hinge domain, which separates the large intramolecular coiled coil regions, allows the heterotypic interaction with the corresponding domain of smc5, forming a V-shaped heterodimer.By similarity

Sequence similaritiesi

Belongs to the SMC family. SMC6 subfamily.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

InParanoidiP53692.
OMAiHKENIST.
OrthoDBiEOG092C08UT.
PhylomeDBiP53692.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR027417. P-loop_NTPase.
IPR003395. RecF/RecN/SMC_N.
IPR033268. Smc5/Smc6.
IPR027132. SMC6.
[Graphical view]
PANTHERiPTHR19306. PTHR19306. 1 hit.
PTHR19306:SF6. PTHR19306:SF6. 1 hit.
PfamiPF02463. SMC_N. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.

Sequencei

Sequence statusi: Complete.

P53692-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTELTNVSL EEAITEKTSE NRRKRDSDVL QTEEVDLSNV KRIRASRNQD
60 70 80 90 100
NRPERQSRLQ RSSSLIEQVR GNEDGENDVL NQTRETNSNF DNRVGVIECI
110 120 130 140 150
HLVNFMCHDS LKINFGPRIN FVIGHNGSGK SAILTGLTIC LGAKASNTNR
160 170 180 190 200
APNMKSLVKQ GKNYARISVT ISNRGFEAYQ PEIYGKSITI ERTIRREGSS
210 220 230 240 250
EYRLRSFNGT VISTKRDELD NICDHMGLQI DNPMNILTQD TARQFLGNSS
260 270 280 290 300
PKEKYQLFMK GIQLKQLEEN YSLIEQSLIN TKNVLGNKKT GVSYLAKKEE
310 320 330 340 350
EYKLLWEQSR ETENLHNLLE QKKGEMVWAQ VVEVEKELLL AEKEFQHAEV
360 370 380 390 400
KLSEAKENLE SIVTNQSDID GKISSKEEVI GRAKGETDTT KSKFEDIVKT
410 420 430 440 450
FDGYRSEMND VDIQKRDIQN SINAAKSCLD VYREQLNTER ARENNLGGSQ
460 470 480 490 500
IEKRANESNN LQREIADLSE QIVELESKRN DLHSALLEMG GNLTSLLTKK
510 520 530 540 550
DSIANKISDQ SEHLKVLEDV QRDKVSAFGK NMPQLLKLIT RETRFQHPPK
560 570 580 590 600
GPMGKYMTVK EQKWHLIIER ILGNVINGFI VRSHHDQLIL KELMRQSNCH
610 620 630 640 650
ATVVVGKYDP FDYSSGEPDS QYPTVLKIIK FDDDEVLHTL INHLGIEKML
660 670 680 690 700
LIEDRREAEA YMKRGIANVT QCYALDPRNR GYGFRIVSTQ RSSGISKVTP
710 720 730 740 750
WNRPPRIGFS SSTSIEAEKK ILDDLKKQYN FASNQLNEAK IEQAKFKRDE
760 770 780 790 800
QLLVEKIEGI KKRILLKRRE VNSLESQELS VLDTEKIQTL ERRISETEKE
810 820 830 840 850
LESYAGQLQD AKNEEHRIRD NQRPVIEEIR IYREKIQTET QRLSSLQTEL
860 870 880 890 900
SRLRDEKRNS EVDIERHRQT VESCTNILRE KEAKKVQCAQ VVADYTAKAN
910 920 930 940 950
TRCERVPVQL SPAELDNEIE RLQMQIAEWR NRTGVSVEQA AEDYLNAKEK
960 970 980 990 1000
HDQAKVLVAR LTQLLQALEE TLRRRNEMWT KFRKLITLRT KELFELYLSQ
1010 1020 1030 1040 1050
RNFTGKLVIK HQEEFLEPRV YPANRNLATA HNRHEKSKVS VQGLSGGEKS
1060 1070 1080 1090 1100
FATICMLLSI WEAMSCPLRC LDEFDVFMDA VNRLVSIKMM VDSAKDSSDK
1110 1120 1130 1140
QFIFITPQDM GQIGLDKDVV VFRLSDPVVS SSALPPSTAP
Length:1,140
Mass (Da):130,929
Last modified:October 1, 1996 - v1
Checksum:i2D9680F4771016ED
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X80929 Genomic DNA. Translation: CAA56900.1.
CU329672 Genomic DNA. Translation: CAA21961.1.
PIRiT41457.
RefSeqiNP_587906.1. NM_001022898.2.

Genome annotation databases

EnsemblFungiiSPCC5E4.06.1; SPCC5E4.06.1:pep; SPCC5E4.06.
GeneIDi2539020.
KEGGispo:SPCC5E4.06.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X80929 Genomic DNA. Translation: CAA56900.1.
CU329672 Genomic DNA. Translation: CAA21961.1.
PIRiT41457.
RefSeqiNP_587906.1. NM_001022898.2.

3D structure databases

ProteinModelPortaliP53692.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi275593. 26 interactors.
IntActiP53692. 8 interactors.
MINTiMINT-4690882.

Proteomic databases

MaxQBiP53692.
PRIDEiP53692.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPCC5E4.06.1; SPCC5E4.06.1:pep; SPCC5E4.06.
GeneIDi2539020.
KEGGispo:SPCC5E4.06.

Organism-specific databases

EuPathDBiFungiDB:SPCC5E4.06.
PomBaseiSPCC5E4.06. smc6.

Phylogenomic databases

InParanoidiP53692.
OMAiHKENIST.
OrthoDBiEOG092C08UT.
PhylomeDBiP53692.

Miscellaneous databases

PROiP53692.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR027417. P-loop_NTPase.
IPR003395. RecF/RecN/SMC_N.
IPR033268. Smc5/Smc6.
IPR027132. SMC6.
[Graphical view]
PANTHERiPTHR19306. PTHR19306. 1 hit.
PTHR19306:SF6. PTHR19306:SF6. 1 hit.
PfamiPF02463. SMC_N. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
ProtoNetiSearch...

Entry informationi

Entry nameiSMC6_SCHPO
AccessioniPrimary (citable) accession number: P53692
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 2, 2016
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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.