ID G3TBD2_LOXAF Unreviewed; 1235 AA.
AC G3TBD2;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
GN Name=SMC1B {ECO:0000313|Ensembl:ENSLAFP00000011273.4};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000011273.4, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000011273.4, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000011273.4,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000011273.4}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000011273.4};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 RefSeq; XP_003420933.1; XM_003420885.2.
DR AlphaFoldDB; G3TBD2; -.
DR STRING; 9785.ENSLAFP00000011273; -.
DR Ensembl; ENSLAFT00000013468.4; ENSLAFP00000011273.4; ENSLAFG00000013462.4.
DR GeneID; 100654641; -.
DR KEGG; lav:100654641; -.
DR CTD; 27127; -.
DR eggNOG; KOG0018; Eukaryota.
DR GeneTree; ENSGT00940000157633; -.
DR InParanoid; G3TBD2; -.
DR OMA; HKARCWD; -.
DR OrthoDB; 231904at2759; -.
DR TreeFam; TF101156; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0000800; C:lateral element; IEA:Ensembl.
DR GO; GO:0030893; C:meiotic cohesin complex; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:Ensembl.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:Ensembl.
DR GO; GO:0007062; P:sister chromatid cohesion; IEA:Ensembl.
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:SF147; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 1B; 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; 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, ECO:0000256|PIRNR:PIRNR005719};
KW Reference proteome {ECO:0000313|Proteomes:UP000007646}.
FT DOMAIN 513..629
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT COILED 161..483
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 748..911
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1235 AA; 143678 MW; 1A8D62801204812F CRC64;
MGHLELLLVE NFKSWRGRQV IGPFKRFTCI IGPNGSGKSN VMDALSFVMG EKITNLRVKN
IQELIHGAHI GKPVSSFASV KIVYVEESGE EKTFARIIRG ACSEFHFDDK PVSRSAYLAE
LEKIGIIAKA RNCLVFQGTV ELISMKKPKE RTQFFEEISS SGELIGEYEE KKKKLQKAEE
DAQFNFNKKK SVAAERKHAK LEKEEADRYQ SLLEELKINK IQLQLFRLYH NERKIRSLNT
ELEHVNRELS VTKESLSHQE NIVKAKKKEH GMLTRQLQQT EKELKSVEAL LNQKKPQYIK
AKENTSHHLK KLDVAKKSIK DSEKQRSKQE DDIRALEAEL VDLDVAWKSF EKQVEEEILY
KGREIELEAS QLDRYKELKD KVRKKVAIMT QQLEKLQREQ KADEDRLAFE KRRHGEVQGN
IKQIHEQIED HKKRIEKLEE YTKTCIDCLK EKKQQEEILE DEIKKAKSRM SEVNEELNLI
RSELQNAGID KHEGKRQQKR AEVLEHLRRL YPESVFGRLL DLCHPIHKKY QLAVTKLFGR
YMVAIVVASE KVAKDCIRFL KEERAEPETF LALDYLDIKP INERLREIKG CKMAIDVIKT
QFPQLKKVIQ FVCGNGLVCE TVEEARHIAF GGPERRKTVA LDGTLFLKSG VISGGSSDLK
YKARYWDEKE LKSLKDRRTQ LIQELKGLMK TLRKETDLKQ IQTLAQGTHT RLKYSQSELE
MIKKKHLAAF YREQSQLQSE LLNIESQCAM LREGIKERQQ RIEEFQEKID KVEDDIFQHF
CEEIGVENIR EFENKHVKRQ QEIDQKRLEF EKQKTRLNVQ LEYSRNHLKK KQNKIDALKE
TLQKGTEDTD NLKKTEENCL QIVNELRDKR QQLKDMFVTQ NSNIEKVQAQ VEEERKKLLA
VDREVGKLQK EVVKIQTSLE QKRLEKHNML LDCKVQDIEI VLLLGSLDDI IEVELGAEAE
STQATIDIYE KEEAIEVDYS SLREDLKALQ TDKEVEAQLT LLLQQVASQE DILLKTAAPN
LRALEKLKTV RDKFQESADA FEASRKEARI CRQEFEQVKK RRYDLFSQCF EHVSISIDQI
YKKLCRSDSA QAFLSPENPE EPYLEGISYN CVAPGKRFMP MDNLSGGEKC VAALALLFAV
HSFRPAPFFV LDEVDAALDN TNIGKVSSYI REQTQEQVQM IIISLKEELY SRADALIGIY
PEHDDYMFSR VLTLDLSQYP DTEDQESSRG HRESR
//
