ID A0A093RBY3_PYGAD Unreviewed; 1225 AA.
AC A0A093RBY3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Structural maintenance of chromosomes protein 3 {ECO:0000256|ARBA:ARBA00018690};
DE Flags: Fragment;
GN ORFNames=AS28_09788 {ECO:0000313|EMBL:KFW68494.1};
OS Pygoscelis adeliae (Adelie penguin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae; Pygoscelis.
OX NCBI_TaxID=9238 {ECO:0000313|EMBL:KFW68494.1, ECO:0000313|Proteomes:UP000054081};
RN [1] {ECO:0000313|EMBL:KFW68494.1, ECO:0000313|Proteomes:UP000054081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_AS28 {ECO:0000313|EMBL:KFW68494.1};
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; KL225167; KFW68494.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093RBY3; -.
DR STRING; 9238.A0A093RBY3; -.
DR Proteomes; UP000054081; 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:UP000054081}.
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 1068..1098
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 394..498
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 670..861
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 895..922
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 970..997
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1075..1098
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFW68494.1"
FT NON_TER 1225
FT /evidence="ECO:0000313|EMBL:KFW68494.1"
SQ SEQUENCE 1225 AA; 142233 MW; EEC1D22F73B090E6 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 NILLLSGKGC PMVWINNEID
QLMNQMQQIE TQQRKFKASR DSILSEMKML KEKRQQSEKT FMPKQRSLQS LEASLHAMES
TRESLKAELG TDLLSQLSLE DQKRVDALND EIRQLQQENR QLLNERIKLE GIITRVETYL
NENLRKRLDQ VEQELNELRE TEGGTVLTAT TSELEAINKR VKDTLARSDD LDNSIDKTEA
GIKELQKSME RWKNMEKEHM DAINHDTKEL EKMTNRQGML LKKKEECMKK IRELGSLPQE
AFEKYQTLSL KQLFRKLEQC NTELKKYSHV NKKALDQFVN FSEQKEKLIK RQEELDRGYK
SIMELMNVLE LRKYEAIQLT FKQVSKNFSE VFQKLVPGGK ATLVMKKGDV EGSQSQDEGE
GSAESERGSG SQSSVPSVDQ FTGVGIRVSF TGKQGEMREM QQLSGGQKSL VALALIFAIQ
KCDPAPFYLF DEIDQALDAQ HRKAVSDMIM ELAEHAQFIT TTFRPELLES ADKFYGVKFR
NKVSHIDVIT AEMAKDFVED DTTHG
//
