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Database: UniProt
Entry: G1SN33_RABIT
LinkDB: G1SN33_RABIT
Original site: G1SN33_RABIT 
ID   G1SN33_RABIT            Unreviewed;      1131 AA.
AC   G1SN33;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2019, sequence version 2.
DT   27-MAR-2024, entry version 59.
DE   RecName: Full=Structural maintenance of chromosomes protein 1A {ECO:0000256|ARBA:ARBA00017530};
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000004366.3, ECO:0000313|Proteomes:UP000001811};
RN   [1] {ECO:0000313|Ensembl:ENSOCUP00000004366.3, ECO:0000313|Proteomes:UP000001811}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Thorbecke inbred {ECO:0000313|Ensembl:ENSOCUP00000004366.3,
RC   ECO:0000313|Proteomes:UP000001811};
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA   Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA   Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA   Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA   Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA   Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA   Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA   Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA   Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA   Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA   Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA   Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA   Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA   Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA   Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0000313|Ensembl:ENSOCUP00000004366.3}
RP   IDENTIFICATION.
RC   STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000004366.3};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the SMC family. SMC1 subfamily.
CC       {ECO:0000256|ARBA:ARBA00005597}.
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DR   EMBL; AAGW02064452; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAGW02064453; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAGW02064454; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; G1SN33; -.
DR   PaxDb; 9986-ENSOCUP00000004366; -.
DR   Ensembl; ENSOCUT00000005040.3; ENSOCUP00000004366.3; ENSOCUG00000005034.3.
DR   eggNOG; KOG0018; Eukaryota.
DR   GeneTree; ENSGT00940000155614; -.
DR   HOGENOM; CLU_057899_1_1_1; -.
DR   Proteomes; UP000001811; Chromosome X.
DR   Bgee; ENSOCUG00000005034; Expressed in autopod skin and 16 other cell types or tissues.
DR   GO; GO:0008278; C:cohesin complex; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0051321; P:meiotic cell cycle; IEA:UniProt.
DR   GO; GO:0007062; P:sister chromatid cohesion; IEA:InterPro.
DR   CDD; cd03275; ABC_SMC1_euk; 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; IPR028468; Smc1_ABC.
DR   InterPro; IPR010935; SMC_hinge.
DR   InterPro; IPR036277; SMC_hinge_sf.
DR   PANTHER; PTHR18937:SF170; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 1A; 1.
DR   PANTHER; PTHR18937; STRUCTURAL MAINTENANCE OF CHROMOSOMES SMC FAMILY MEMBER; 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; 2.
DR   SUPFAM; SSF75553; Smc hinge domain; 1.
PE   3: Inferred from homology;
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW   Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Meiosis {ECO:0000256|ARBA:ARBA00023254};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001811}.
FT   DOMAIN          486..602
FT                   /note="SMC hinge"
FT                   /evidence="ECO:0000259|SMART:SM00968"
FT   REGION          257..280
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          845..866
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          637..684
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          726..823
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          890..963
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        847..866
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1131 AA;  130968 MW;  010381FBDC9A1BB9 CRC64;
     MPGVLTPIRG KSNLMDAISF VLGEKTSNLR VKTLRDLIHG APVGKPAANR AFVSMVYSED
     GAEDRTFARV IVGGSSEYKI NNKVVQLHEY SEELEKLGIL IKARNFLVFQ GAVESIAMKN
     PKERTALFEE ISRSGELAQE YDKRKKEMVK AEEDTQFNYH RKKNIAAERK EAKQEKEEAD
     RYQRLKDEVV RAQVQLQLFK LYHNEVEIEK LNKELASKNK EIEKDKKRMD KVEDELKEKK
     KELGKMMREQ QQIEKEIKEK DSELNQKRPQ YIKAKENTSH KIKKLEAAKK SLQNAQKHYK
     KRKGDMDELE KEMLSVEKAR QEFEERMEEE SQSQGRDLTL EENQVKKYHR LKEEASKRAA
     TLAQELEKFN RDQKADQDRL DLEERKKVET EAKIKQKLRE IEENQKRIEK LEEYITTSKQ
     SLEEQKKLEG ELTEEVEMAK RRIDEINKEL NQVMEQLGDA RIDRQESSRQ QRKAEIMESI
     KRLYPGSVYG RLIDLCQPTQ KKYQIAVTKV LGKNMDAIIV DSEKTGRDCI QYIKEQRGEP
     ETFLPLDYLE VKPTDEKLRE LKGAKLVIDV IRYEPPHIKK ALQYACGNAL VCDNVEDARR
     IAFGGHQRHK TVALDGTLFQ KSGVISGGAS DLKAKARRWD EKAVDKLKEK KERLTEELKE
     QMKAKRKEAE LRQVQSQAHG LQMRLKYSQS DLEQTKTRHL ALNLQLEFEN QKTRLGIQLD
     FEKNQLKEDQ DKVHMWEQTV KKDENEIEKL KKEEQRHMKI IDETMAQLQD LKNQHLAKKS
     EVNDKNHEME EIRKKLGGAN KEMTHLQKEV TAIETKLEQK RSDRHNLLQA CKMQDIKLPL
     SKGTMDDISQ EEGSSQGEDS VSGSQRTSSI YAREALIEID YGDLCEDLKD AQAEEEIKQE
     MNTLQQKLNE QQSVLQRIAA PNMKAMEKLE SVRDKFQETS DEFEAARKRA KKAKQAFEQI
     KKERFDRFNA CFESVATNID EIYKALSRNS SAQAFLGPEN PEEPYLDGIN YNCVAPGKRF
     RPMDNLSGGE KTVAALALLF AIHSYKPAPF FVLDEIDAAL DNTNIGKVAN YIKEQSTCNF
     QAIVISLKEE FYTKAESLIG VYPEQGDCVI SKVLTFDLTK YPDANPNPNE Q
//
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