ID A0A093FP89_GAVST Unreviewed; 1214 AA.
AC A0A093FP89;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Structural maintenance of chromosomes protein 3 {ECO:0000256|ARBA:ARBA00018690};
DE Flags: Fragment;
GN ORFNames=N328_08046 {ECO:0000313|EMBL:KFV58475.1};
OS Gavia stellata (Red-throated diver) (Colymbus stellatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Gaviiformes; Gaviidae; Gavia.
OX NCBI_TaxID=37040 {ECO:0000313|EMBL:KFV58475.1, ECO:0000313|Proteomes:UP000054313};
RN [1] {ECO:0000313|EMBL:KFV58475.1, ECO:0000313|Proteomes:UP000054313}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N328 {ECO:0000313|EMBL:KFV58475.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Central component of cohesin, a complex required for
CC chromosome cohesion during the cell cycle. The cohesin complex may form
CC a large proteinaceous ring within which sister chromatids can be
CC trapped. At anaphase, the complex is cleaved and dissociates from
CC chromatin, allowing sister chromatids to segregate. Cohesion is coupled
CC to DNA replication and is involved in DNA repair. The cohesin complex
CC also plays an important role in spindle pole assembly during mitosis
CC and in chromosomes movement. {ECO:0000256|ARBA:ARBA00034085}.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC3 subfamily.
CC {ECO:0000256|ARBA:ARBA00005917}.
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DR EMBL; KK636185; KFV58475.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093FP89; -.
DR Proteomes; UP000054313; Unassembled WGS sequence.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051276; P:chromosome organization; IEA:InterPro.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR CDD; cd03272; ABC_SMC3_euk; 1.
DR Gene3D; 1.10.287.1490; -; 1.
DR Gene3D; 1.20.1060.20; -; 1.
DR Gene3D; 3.30.70.1620; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR003395; RecF/RecN/SMC_N.
DR InterPro; IPR024704; SMC.
DR InterPro; IPR041741; SMC3_ABC_euk.
DR InterPro; IPR010935; SMC_hinge.
DR InterPro; IPR036277; SMC_hinge_sf.
DR PANTHER; PTHR43977; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 3; 1.
DR PANTHER; PTHR43977:SF1; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 3; 1.
DR Pfam; PF06470; SMC_hinge; 1.
DR Pfam; PF02463; SMC_N; 1.
DR PIRSF; PIRSF005719; SMC; 2.
DR SMART; SM00968; SMC_hinge; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF75553; Smc hinge domain; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Cell division {ECO:0000256|ARBA:ARBA00022618};
KW Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Meiosis {ECO:0000256|ARBA:ARBA00023254};
KW Mitosis {ECO:0000256|ARBA:ARBA00022776};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000054313}.
FT DOMAIN 525..638
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 237..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1056..1087
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 394..498
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 670..850
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 884..911
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 959..986
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1064..1087
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFV58475.1"
FT NON_TER 1214
FT /evidence="ECO:0000313|EMBL:KFV58475.1"
SQ SEQUENCE 1214 AA; 141151 MW; DDD93176CCA0A872 CRC64;
VIIQGFRSYR DQTIVDPFSS KHNVIVGRNG SGKSNFFYAI QFVLSDEFSH LRPEQRLALL
HEGTGPRVIS AFVEIIFDNS DNRLPIDKEE VSLRRVIGAK KDQYFLDKKM VTKNDVMNLL
ESAGFSRSNP YYIVKQGKIN QMATAPDSQR LKLLREVAGT RVYDERKEES ISLMKETEGK
REKINELLKY IEERLHTLEE EKEELAQYQK WDKMRRALEY TIYNQELNET RAKLDELSAK
RETSGEKSRQ LRDAQQDARD KMEEIERQVR ELKTKISAMK EEKEQLSAER QEQIKQRTKL
ELKAKDLQDE LAGNSEQRKR LLKERQKLLE KIEEKQKELA ETEPKFNSVK EKEERGIARL
AQATQERTDL YAKQGRGSQF TSKEERDKWI KKELKSLDQA INDKKRQIAA IHKDLEDTEA
NKEKNLEQYS KLDQDLNEVK ARVEELDRKY YEVKNKKDEL QSERNYLWRE ENAEQQALAA
KREDLEKKQQ LLRAATGKAI LNGIDSINKV LEHFRRKGIN QHVLNGYHGI VMNNFECEPA
FYTCVEVTAG NRLFYHIVDS DEVSTKILME FNKMNLPGEV TFLPLNKLDV RDTAYPETND
AIPMISKLRY NPRFDKAFKH VFGKTLICRS MEVSTQLARA FTMDCITLEG DQVSHRGALT
GGYYDTRKSR LELQKDVRKA EEELGELEAK LNENLRRNIE NILFNNEIDQ LMNQMQQIET
QQRKFKASRD SILSEMKMLK EKRQQSEKTF MPKQRSLQSL EASLHAMEST RESLKAELGT
DLLSQLSLED QKRVDALNDE IRQLQQENRQ LLNERIKLEG IITRVETYLN ENLRKRLDQV
EQELNELRET EGGTVLTATT SELEAINKRV KDTLARSDDL DNSIDKTEAG IKELQKSMER
WKNMEKEHMD AINHDTKELE KMTNRQGMLL KKKEECMKKI RELGSLPQEA FEKYQTLSLK
QLFRKLEQCN TELKKYSHVN KKALDQFVNF SEQKEKLIKR QEELDRGYKS IMELMNVLEL
RKYEAIQLTF KQVSKNFSEV FQKLVPGGKA TLVMKKGDVE GNQSQDEGEG STESERGSGS
QSSVPSVDQF TGVGIRVSFT GKQGEMREMQ QLSGGQKSLV ALALIFAIQK CDPAPFYLFD
EIDQALDAQH RKAVSDMIME LAEHAQFITT TFRPELLESA DKFYGVKFRN KVSHIDVITA
EMAKDFVEDD TTHG
//
