ID S7PG70_MYOBR Unreviewed; 1233 AA.
AC S7PG70;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
GN ORFNames=D623_10001658 {ECO:0000313|EMBL:EPQ09508.1};
OS Myotis brandtii (Brandt's bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=109478 {ECO:0000313|EMBL:EPQ09508.1, ECO:0000313|Proteomes:UP000052978};
RN [1] {ECO:0000313|Proteomes:UP000052978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23962925; DOI=10.1038/ncomms3212;
RA Seim I., Fang X., Xiong Z., Lobanov A.V., Huang Z., Ma S., Feng Y.,
RA Turanov A.A., Zhu Y., Lenz T.L., Gerashchenko M.V., Fan D., Hee Yim S.,
RA Yao X., Jordan D., Xiong Y., Ma Y., Lyapunov A.N., Chen G., Kulakova O.I.,
RA Sun Y., Lee S.G., Bronson R.T., Moskalev A.A., Sunyaev S.R., Zhang G.,
RA Krogh A., Wang J., Gladyshev V.N.;
RT "Genome analysis reveals insights into physiology and longevity of the
RT Brandt's bat Myotis brandtii.";
RL Nat. Commun. 4:2212-2212(2013).
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR005719}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC1 subfamily.
CC {ECO:0000256|ARBA:ARBA00005597}.
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DR EMBL; KE162766; EPQ09508.1; -; Genomic_DNA.
DR RefSeq; XP_005869136.1; XM_005869074.2.
DR AlphaFoldDB; S7PG70; -.
DR SMR; S7PG70; -.
DR GeneID; 102253503; -.
DR KEGG; myb:102253503; -.
DR CTD; 8243; -.
DR eggNOG; KOG0018; Eukaryota.
DR OrthoDB; 231904at2759; -.
DR Proteomes; UP000052978; Unassembled WGS sequence.
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:0007062; P:sister chromatid cohesion; IEA:InterPro.
DR CDD; cd03275; ABC_SMC1_euk; 2.
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; 1.
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 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, ECO:0000256|PIRNR:PIRNR005719};
KW Reference proteome {ECO:0000313|Proteomes:UP000052978}.
FT DOMAIN 513..629
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 284..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 348..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 947..968
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 664..711
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 748..925
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 992..1065
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 949..968
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1233 AA; 143221 MW; E65C81A7489FB8A6 CRC64;
MGFLKLIEIE NFKSYKGRQI IGPFQRFTAI IGPNGSGKSN LMDAISFVLG EKTSNLRVKT
LRDLIHGAPV GKPAANRAFV SMVYSEEGAE DRTFARVIVG GSSEYKINNK VVQLHEYSEE
LEKLGILIKA RNFLVFQGAV ESIAMKNPKE RTALFEEISR SGELAQEYDK RKKEMVKAEE
DTQFNYHRKK NIAAERKEAK QEKEEADRYQ RLKDEVVRAQ VQLQLFKLYH NEVEIEKLNK
ELASKNKEIE KDKKRMDKVE DELKEKKKEL GKMMREQQQI EKEIKEKDSE LNQKRPQYIK
AKENTSHKIK KLEAAKKSLQ NAQKHYKKRK GDMDELEKEM LSVEKARQEF EERMEEESQS
QGRDLTLEEN QVKKYHRLKE EASKRAATLA QELEKFNRDQ KADQDRLDLE ERKKVETEAK
IKQKLREIEE NQKRIEKLEE YITTSKQSLE EQKKLEGELT EEVEMAKRRI DEINKELNQV
MEQLGDARID RQESSRQQRK AEIMESIKRL YPGSVYGRLI DLCQPTQKKY QIAVTKVLGK
NMDAIIVDSE KTGRDCIQYI KEQRGEPETF LPLDYLEVKP TDEKLRELKG AKLVIDVIRY
EPPHIKKALQ YACGNALVCD NVEDARRIAF GGHQRHKTVA LDGTLFQKSG VISGGASDLK
AKARRWDEKA VDKLKEKKER LTEELKEQMK AKRKEAELRQ VQSQAHGLQM RLKYSQSDLE
QTKTRHLALN LQEKSKLESE LANFGPRIND IKRIIQSRER EMKDLKEKMN QVEDEVFEEF
CREIGVRNIR EFEEEKVKRQ NEIAKKRLEF ENQKTRLGIQ LDFEKNQLKE DQDKVHMWEQ
TVKKDENEIE KLKKEEQRHM KIIDETMAQL QDLKNQHLAK KSEVNDKNHE MEEIRKKLGG
ANKEMTHLQK EVTAIETKLE QKRSDRHNLL QACKMQDIKL PLSKGTMDDI SQEEGSSQGE
DSVSGSQRTS SIYAREALIE IDYGDLCEDL KDAQAEEEIK QEMNTLQQKL NEQQSVLQRI
AAPNMKAMEK LESVRDKFQE TSDEFEAARK RAKKAKQAFE QIKKERFDRF NACFESVATN
IDEIYKALSR NSSAQAFLGP ENPEEPYLDG INYNCVAPGK RFRPMDNLSG GEKTVAALAL
LFAIHSYKPA PFFVLDEIDA ALDNTNIGKV ANYIKEQSTC NFQAIVISLK EEFYTKAESL
IGVYPEQGDC VISKVLTFDL TKYPDANPNP NEQ
//
