ID G3N365_BOVIN Unreviewed; 1178 AA.
AC G3N365;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 2.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
GN Name=SMC3 {ECO:0000313|Ensembl:ENSBTAP00000056339.2,
GN ECO:0000313|VGNC:VGNC:35000};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000056339.2, ECO:0000313|Proteomes:UP000009136};
RN [1] {ECO:0000313|Ensembl:ENSBTAP00000056339.2, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000056339.2,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBTAP00000056339.2}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000056339.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC Nucleus {ECO:0000256|PIRNR:PIRNR005719}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC3 subfamily.
CC {ECO:0000256|ARBA:ARBA00005917}.
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DR AlphaFoldDB; G3N365; -.
DR Ensembl; ENSBTAT00000063829.2; ENSBTAP00000056339.2; ENSBTAG00000013905.6.
DR VEuPathDB; HostDB:ENSBTAG00000013905; -.
DR VGNC; VGNC:35000; SMC3.
DR GeneTree; ENSGT00580000081628; -.
DR Proteomes; UP000009136; Chromosome 26.
DR Bgee; ENSBTAG00000013905; Expressed in thymus and 111 other cell types or tissues.
DR ExpressionAtlas; G3N365; baseline and differential.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0051276; P:chromosome organization; IEA:InterPro.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
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; 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; 3.
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 Centromere {ECO:0000256|ARBA:ARBA00023328};
KW Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Nucleus {ECO:0000256|PIRNR:PIRNR005719};
KW Reference proteome {ECO:0000313|Proteomes:UP000009136}.
FT DOMAIN 496..609
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 208..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1020..1051
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 365..469
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 641..814
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 841..875
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 923..950
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1028..1051
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1178 AA; 137040 MW; A57CDA5820467759 CRC64;
MYIKQVIIQG FRSYRDQTIV DPFSSKHNVI GKFIFMFLAI QFVLSDEFSH LRPEQRLALL
HEGTGPRVIS AFVEIIFDNS DNRKNDVMNL LESAGFSRSN PYYIVKQGKI NQMATAPDSQ
RLKLLREVAG TRVYDERKEE SISLMKETEG KREKINELLK YIEERLHTLE EEKEELAQYQ
KWDKMRRALE YTIYNQELNE TRAKLDELSA KRETSGEKSR QLRDAQQDAR DKMEDIERQV
RELKTKISAM KEEKEQLSAE RQEQIKQRTK LELKAKDLQD ELAGNSEQRK RLLKERQKLL
EKIEEKQKEL AETEPKFNSV KEKEERGIAR LAQATQERTD LYAKQGRGSQ FTSKEERDKW
IKKELKSLDQ AINDKKRQIA AIHKDLEDTE ANKEKNLEQY NKLDQDLNEV KARVEELDRK
YYEVKNKKDE LQSERNYLWR EENAEQQALA AKREDLEKKQ QLLRAATGKA ILNGIDSINK
VLDHFRRKGI NQHVQNGYHG IVMNNFECEP AFYTCVEVTA GNRLFYHIVD SDEVSTKILM
EFNKMNLPGE VTFLPLNKLD VRDTAYPETN DAIPMISKLR YNPRFDKAFK HVFGKTLICR
SMEVSTQLAR AFTMDCITLE GDQVSHRGAL TGGYYDTRKS RLELQKDVRK AEEELGELEA
KLNENLRINN EIDQLMNQMQ QIETQQRKFK ASRDSILSEM KMLKEKRQQS EKTFMPKQRS
LQSLEASLHA MESTRESLKA ELGTDLLSQL SLEDQKRVDA LNDEIRQLQQ ENRQLLNERI
KLEGIITRVE TYLNENLRKR LDQVEQELNE LRETEGGTVL TATTSELEAI NKRVKDTMAR
SEDLDNSIDK TEAGIKELQK SMERWKNMEK EHMDAINHDT KELEKMTNRQ GMLLKKKEEC
MKKIRELGSL PQEAFEKYQT LSLKQLFRKL EQCNTELKKY SHVNKKALDQ FVNFSEQKEK
LIKRQEELDR GYKSIMELMN VLELRKYEAI QLTFKQVSKN FSEVFQKLVP GGKATLVMKK
GDVEGSQSQD EGEGSGESER GSGSQSSVPS VDQFTGVGIR VSFTGKQGEM REMQQLSGGQ
KSLVALALIF AIQKCDPAPF YLFDEIDQAL DAQHRKAVSD MIMELAVHAQ FITTTFRPEL
LESADKFYGV KFRNKVSHID VITAEMAKDF VEDDTTHG
//
