ID A0A1G0WB80_9BACT Unreviewed; 1178 AA.
AC A0A1G0WB80;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=A2475_08975 {ECO:0000313|EMBL:OGV18732.1};
OS Ignavibacteria bacterium RIFOXYC2_FULL_35_21.
OC Bacteria; Ignavibacteriota; Ignavibacteria.
OX NCBI_TaxID=1798452 {ECO:0000313|EMBL:OGV18732.1, ECO:0000313|Proteomes:UP000177327};
RN [1] {ECO:0000313|EMBL:OGV18732.1, ECO:0000313|Proteomes:UP000177327}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OGV18732.1}.
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DR EMBL; MHAY01000102; OGV18732.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G0WB80; -.
DR STRING; 1798452.A2475_08975; -.
DR Proteomes; UP000177327; Unassembled WGS sequence.
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 CDD; cd03278; ABC_SMC_barmotin; 1.
DR Gene3D; 1.10.287.1490; -; 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 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; 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; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF75553; Smc hinge domain; 1.
DR SUPFAM; SSF57997; Tropomyosin; 2.
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}.
FT DOMAIN 518..633
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT COILED 262..492
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 667..701
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 728..895
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 1178 AA; 133173 MW; 0CB123959723620D CRC64;
MYLSGLEIIG FKSFPHKTNI KFADGLTSIV GPNGCGKTNI VDAIRWVLGE QKSSILRSEI
MDNVIFNGTD TRKPIGMAEV SIFIENTKGI LPIEYNDVKV TRRLFRNGDS QYLLNNTQCR
LRDILDLFMD TGIGADTYSV IELKMVEAIL NGKPEERRHL IEEASGVTRY KHQRKEAGRK
LTTVESDLLR VYDINQEVQK NVNSLSRQAA KTRRYNKLLE ELKNIELNLI YHEYALIKNE
SSSLEIEFEK IQEDGQKQEH ELHLKETEIS ALKGNLDAVE ADYDEALAHE SSLINTISGK
NKDKAVSEEK IQSLQNAKER ILNEISDSVS LQSELKEKIE KTNENLLSAN KRLDSFAGEL
NEANEQKEQA QNSVNTSREK FNRANEDLVN LQGKIDSSKD AIERNNSRLV NISESIDSGK
NDIEKIESEI SEIDSQIITS QSNQIELNQI FESTGNDYKS AQQKKSSLES KLDNTRTELA
DLKNELNRNQ AALEFITGIV DSDETTKFLI NTKEWKPSGE KLLLAEAIGA DEQHRIAVDA
ALGDAVRFFV TDTLSEALSG IEKLKASGKG KASFIVRELI PDVPAPENIS ANDGIIGWLS
EIVRVDVVLR NALRAILGKT LLIDNIDNAL KLIKSGIADT IVTLEGELVR SKGIIRGGAV
TKTEGLTVGK KERLANLNKE ISNLEKKVET IETQLSEIKS EYDSIDLIAF GEQLRKAEID
KNNNEQFISQ LALKKENAEN NFKIFENNIR LFNEETTRLT RENESFSNDI RETENRLIIL
NDELLTLQEE LAAAESNLSE KTSALQEAEI KRARLEEEIK ALEKEITTFQ EQIKSLSEKD
IKNHSEIESF DTKSGELKAH SISIDAELEE LQKELDKAQN KREQLHDKIL SVQEEIQQQT
NYLLMARKQY DKTIEQSHSL DVRLSEFRVR SSSLIQKALE DYNITLEQAE FELQEIFNIE
ESKSTITSLK EKLSLLGNVN FMALEEYEEQ SQRLQFYTMQ IKDLEESKKN LQESIAEINE
TAVQRFTETF EKIQGNFSHL FKTLFGPEGE AELILGEGDP LDAEISIKAK PPGKKPHSID
MLSGGEKALT AIAMLFSIYL VKPSPFCILD EVDAPLDDTN IDKFINLLRE FSNNTQFIIV
THSKRTMEAA DYLYGITMQE KGISKIVSVR LEQPKAVN
//
