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Protein

Structural maintenance of chromosomes protein 1A

Gene

smc1a

Organism
Xenopus laevis (African clawed frog)
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)DescriptionActionsGraphical viewLength
Nucleotide bindingi32 – 39ATPSequence analysis8

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, DNA damage, DNA repair, Mitosis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Structural maintenance of chromosomes protein 1A
Short name:
SMC protein 1A
Short name:
SMC-1A
Short name:
xSMC1
Gene namesi
Name:smc1a
Synonyms:smc1, smc1l1
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Subcellular locationi

  • Nucleus
  • Chromosome
  • Chromosomecentromere

  • Note: Associates with chromatin. Before prophase it is scattered along chromosome arms. During prophase, most of cohesin complexes dissociate from chromatin probably because of phosphorylation by PLK, except at centromeres, where cohesin complexes remain. At anaphase, the RAD21 subunit of the cohesin complex is cleaved, leading to the dissociation of the complex from chromosomes, allowing chromosome separation.

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001189921 – 1232Structural maintenance of chromosomes protein 1AAdd BLAST1232

Interactioni

Subunit structurei

Forms a heterodimer with SMC3 in cohesin complex. The cohesin complex is composed of the SMC1A and SMC3 heterodimer attached via their hinge domain, RAD21 which link them, and one STAG protein (STAG1 or STAG2), which interacts with RAD21.2 Publications

Protein-protein interaction databases

BioGridi1078967. 7 interactors.
IntActiO93308. 7 interactors.

Structurei

3D structure databases

ProteinModelPortaliO93308.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni504 – 659Flexible hingeAdd BLAST156

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili163 – 503Sequence analysisAdd BLAST341
Coiled coili660 – 935Sequence analysisAdd BLAST276
Coiled coili997 – 1068Sequence analysisAdd BLAST72

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi1128 – 1163Ala/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 SMC3, 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

HOVERGENiHBG039593.

Family and domain databases

Gene3Di3.40.50.300. 5 hits.
InterProiIPR027417. P-loop_NTPase.
IPR003395. RecF/RecN/SMC_N.
IPR024704. SMC.
IPR029683. SMC1A_metazoan.
IPR010935. SMC_hinge.
[Graphical view]
PANTHERiPTHR18937:SF170. PTHR18937:SF170. 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.

O93308-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGFLKLIEIE NFKSYKGRQI IGPFHRFTAI IGPNGSGKSN LMDAISFVLG
60 70 80 90 100
EKTSNLRVKT LRDLIHGAPV GKPAANRAFV SMVYSEDSGE EKVFSRVIVG
110 120 130 140 150
GSSEYKINNK VVQLSEYSDS LEKLGILIKA RNFLVFQGAV ESIAMKNPKE
160 170 180 190 200
RTALFEEISR SGELAQEYDK RKKEMVKAEE DTQFNYHRKK NIAAERKEAK
210 220 230 240 250
QEKEEAERYQ RLKDEVARAQ IQLQLFKLYH NESEIEKLNK ELSVKNKGIE
260 270 280 290 300
KDKKHMDKVE EELKDKKKEL GKMMREQQAI EKEIKEKDAE LNQKLPQYIK
310 320 330 340 350
AKENPSHKIK KFRAAKKSLQ NAQKQYKKRK ADMDELEKEM LSVEKARQEF
360 370 380 390 400
EERMEEESQS QGRDLTLEEN QVKKYHRLKE EASKRAATLA QELEKFNRDQ
410 420 430 440 450
KADQDRLDLE ERKKVETEAK IKQKLRELEE NQKRIEKLEE YIATSKQSLE
460 470 480 490 500
EQKNLEETLT EEVEMAKRRI DEINSELNQV MEQLGDARID RQESSRQQRK
510 520 530 540 550
AEIMESIKRL YPGSVYGRLI DLCQPTQKKY QIAVTKVLGK NMDAIIVDSE
560 570 580 590 600
KTGRDCIQYI KEQRGEPETF LPLDYLEVKP TDERLRELKG AKLVIDVIRY
610 620 630 640 650
EPPHIKKALQ YACGNALVCD NVEDARRIAF GGHQRHKTVA LDGTLFQKSG
660 670 680 690 700
VISGGASDLK AKARRWDEKA VDKLKEKKER LTEELKEQMK AKRKEAELRQ
710 720 730 740 750
VQSQAHGLQM RLKYSQSDLE QTKTRHLAMN MQEKSKLESE LANFSPRIND
760 770 780 790 800
IKRIIQSRDR EMKDLKEKMN QVEDEVFEEF CREIGVRNIR EFEEEKVKRQ
810 820 830 840 850
NEIAKKRLEF ENQKTRLGIQ LDYEKNQLKE DQGKVQTWEQ SVKKDDNEIE
860 870 880 890 900
KLKKEEQRHM KIIDETMAQL QDLKNQHLAK KSEVNDKNHL MEDIRKKLGS
910 920 930 940 950
ANKEVTHLQK EVTAIETKLE QKRSDRHNLL QACKMSDIKL PLSKGTMDDI
960 970 980 990 1000
SQEEGSSQGE ESASSSQRSS TVYAKEALIE IDYSDLSEDL KDAVADDDIK
1010 1020 1030 1040 1050
QEMSALHQKI NEQQSILQRI SAPNMKAMEK LESVRDKFQE TSDEFEAARK
1060 1070 1080 1090 1100
RAKKAKQAFE QTKKERFDRF NACFESVATN IDEIYKALSR NSSAQAFLGP
1110 1120 1130 1140 1150
ENPEEPYLDG INYNCVAPGK RFRPMDNLSG GEKTVAALAL LFAIHSYKPS
1160 1170 1180 1190 1200
PFFVLDEIDA ALDNTNIGKV ANYIKEQSMS NFQAIVISLK EEFYTKAESL
1210 1220 1230
IGVYPEQGDC VISKVLTFDL TKYPDANPNP ND
Length:1,232
Mass (Da):142,628
Last modified:November 1, 1998 - v1
Checksum:i50920422ED113722
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF051784 mRNA. Translation: AAC26807.1.
RefSeqiNP_001165905.1. NM_001172434.1.
UniGeneiXl.4734.

Genome annotation databases

GeneIDi100379087.
KEGGixla:100379087.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF051784 mRNA. Translation: AAC26807.1.
RefSeqiNP_001165905.1. NM_001172434.1.
UniGeneiXl.4734.

3D structure databases

ProteinModelPortaliO93308.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi1078967. 7 interactors.
IntActiO93308. 7 interactors.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100379087.
KEGGixla:100379087.

Organism-specific databases

CTDi100379087.

Phylogenomic databases

HOVERGENiHBG039593.

Family and domain databases

Gene3Di3.40.50.300. 5 hits.
InterProiIPR027417. P-loop_NTPase.
IPR003395. RecF/RecN/SMC_N.
IPR024704. SMC.
IPR029683. SMC1A_metazoan.
IPR010935. SMC_hinge.
[Graphical view]
PANTHERiPTHR18937:SF170. PTHR18937:SF170. 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 nameiSMC1A_XENLA
AccessioniPrimary (citable) accession number: O93308
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: November 1, 1998
Last modified: November 11, 2015
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. 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.