ID H8I5T0_METCZ Unreviewed; 1173 AA.
AC H8I5T0;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894,
GN ECO:0000313|EMBL:AFC99747.1};
GN OrderedLocusNames=Mtc_0992 {ECO:0000313|EMBL:AFC99747.1};
OS Methanocella conradii (strain DSM 24694 / JCM 17849 / CGMCC 1.5162 /
OS HZ254).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanocellales; Methanocellaceae; Methanocella.
OX NCBI_TaxID=1041930 {ECO:0000313|EMBL:AFC99747.1, ECO:0000313|Proteomes:UP000005233};
RN [1] {ECO:0000313|EMBL:AFC99747.1, ECO:0000313|Proteomes:UP000005233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24694 / JCM 17849 / CGMCC 1.5162 / HZ254
RC {ECO:0000313|Proteomes:UP000005233};
RX PubMed=22493204; DOI=10.1128/JB.00207-12;
RA Lu Z., Lu Y.;
RT "Complete genome sequence of a thermophilic methanogen, Methanocella
RT conradii HZ254, isolated from Chinese rice field soil.";
RL J. Bacteriol. 194:2398-2399(2012).
CC -!- FUNCTION: Required for chromosome condensation and partitioning.
CC {ECO:0000256|HAMAP-Rule:MF_01894}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01894}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01894}.
CC -!- DOMAIN: Contains large globular domains required for ATP hydrolysis at
CC each terminus and a third globular domain forming a flexible hinge near
CC the middle of the molecule. These domains are separated by coiled-coil
CC structures. {ECO:0000256|HAMAP-Rule:MF_01894}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC3 subfamily.
CC {ECO:0000256|ARBA:ARBA00005917}.
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DR EMBL; CP003243; AFC99747.1; -; Genomic_DNA.
DR RefSeq; WP_014405585.1; NC_017034.1.
DR AlphaFoldDB; H8I5T0; -.
DR STRING; 1041930.Mtc_0992; -.
DR GeneID; 11971115; -.
DR KEGG; mez:Mtc_0992; -.
DR eggNOG; arCOG00371; Archaea.
DR HOGENOM; CLU_001042_2_2_2; -.
DR OrthoDB; 9143at2157; -.
DR Proteomes; UP000005233; Chromosome.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030261; P:chromosome condensation; IEA:InterPro.
DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-UniRule.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR GO; GO:0007062; P:sister chromatid cohesion; IEA:InterPro.
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 HAMAP; MF_01894; Smc_prok; 1.
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 InterPro; IPR011890; SMC_prok.
DR NCBIfam; TIGR02169; SMC_prok_A; 1.
DR NCBIfam; TIGR02168; SMC_prok_B; 1.
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; 1.
DR SMART; SM00968; SMC_hinge; 1.
DR SUPFAM; SSF90257; Myosin rod fragments; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF75553; Smc hinge domain; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01894};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|HAMAP-
KW Rule:MF_01894};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01894};
KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_01894};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01894};
KW Reference proteome {ECO:0000313|Proteomes:UP000005233}.
FT DOMAIN 528..642
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT COILED 189..283
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 327..354
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 439..508
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 716..944
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 987..1024
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT BINDING 32..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
SQ SEQUENCE 1173 AA; 132324 MW; 875A6560DA66DD04 CRC64;
MHIKEIELNN FKSFGRRAKI PFFDDFTTIS GPNGSGKSNV VDSIVFCLGL SNSRSMRAEK
LTDLIYSVDG KSSGTAEVTI RFDNTDRELP VDQDEVTVTR RIKSSDSGYY SYYYFNDKPC
SLSEIHEQLL KARISPNSYN VIMQGDVTRI IEVSDFERRK IIDEIAGTAE FDEKTDKALA
ELDIVRERID RVSIIISEVE ARLAQLKSER DQALLYKSYK DEKARNEGYL VLSELKEAQQ
VLDSLLEDIA DKASKRQAVI AEAEKKGAAV QKLKDDIKAL NDTITEKGEG EQLLIKRRIE
EARAGIKACS NIIEFSRSEI ASRESEKQKL FLEAERAKGQ VEELDGKIAG EEARKLSLAN
EYAFRKGSLE EVQKKMSAID ARFAGVRTRL SEVKAALEAS RNLRNEKLRE KDRILDAARR
KQDEEQDAVA EIASSRSRIE EARVEAGNIE KDIVELQKKA QALDADISDM EGARSRARHE
LSGIEEKLRK LQEEYAKAEA RVRAYEDYDG YSEAVGAILS ARNSHELPGI YGTIAELGKV
REEYATALEV AAGSRLQNIV VDNDEDAARC IYYLKERRLG TATFLPLNRM RQRLPLRAIR
EPGVIDYAIN LVEFDSRFDP AFWYVFGDTL VVDTLETARR LIGTGRIVTL DGDLIEKSGA
MTGGFRSRAK LRFKASEEER IKALAEQITI QESSRDSILK KIESIEGHIY SLKKDRSAIE
AQASKLNARK EELAGRASRL EAAIKEKEAA IEALREERRR LRDELIAAED AISSADKDIA
AVSAEAARLE EELKGSEMPS LTEEAGRIEE EMRRLEGRIR DTESAIAALR MEKGYVSARI
EESRERGARI DEDIASLREK IAQNEAQIHD FEKDIEEMST REKEIDAELA GMKRQREAMS
EALSKADQDL YETRRSLERL TAMLNTLEVS REECLEKIKS LEKAVQERGI QPSEDVPPLE
KVKATISLLE KKMQALEPVN MLSITEYDSV QARLTELTGK RDTLQKEREN ILEKIEHYKK
MKKETFLATF NAINGHFKEI FKELSDGFGE LILENPDDPF SGGLTIHAQP QGKSLHRLEA
MSGGEKSLTA LAFIFAIQRH MPAPFYVFDE IDMFLDGANA ERVARMIKKL AKDAQFIVVS
LRKPMIESAN RTIGIAMQEN NISSITGVKL RAG
//
