ID A0A1Z9QGK4_9BACT Unreviewed; 1339 AA.
AC A0A1Z9QGK4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-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=CBD91_00700 {ECO:0000313|EMBL:OUX03097.1};
OS Phycisphaeraceae bacterium TMED231.
OC Bacteria; Planctomycetota; Phycisphaerae; Phycisphaerales;
OC Phycisphaeraceae.
OX NCBI_TaxID=1986831 {ECO:0000313|EMBL:OUX03097.1, ECO:0000313|Proteomes:UP000196960};
RN [1] {ECO:0000313|EMBL:OUX03097.1, ECO:0000313|Proteomes:UP000196960}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TMED231 {ECO:0000313|EMBL:OUX03097.1};
RA Tully B.J., Sachdeva R., Graham E.D., Heidelberg J.F.;
RT "290 Metagenome-assembled Genomes from the Mediterranean Sea: a resource
RT for marine microbiology.";
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
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:OUX03097.1}.
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DR EMBL; NHKC01000009; OUX03097.1; -; Genomic_DNA.
DR Proteomes; UP000196960; 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; -; 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; 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; 2.
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; 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}.
FT DOMAIN 596..714
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 778..797
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1297..1339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 242..441
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 526..553
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 1068..1102
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT BINDING 49..56
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
SQ SEQUENCE 1339 AA; 148625 MW; 5DCBACA5C5888793 CRC64;
MPATARMCGD IDRRSIHVRL AKLTLSGFKS FADRTEFTFD EPIIGVVGPN GCGKSNVVDA
VRWVLGERSA KSLRGSAMQD VIFAGSAARK PMGMAEVTLT FENPRLERPL EAITAAGELP
TELDPDLVID ERSAEVTTDT LDEEELALAA GDGQVVDRTR VRDRRLPIDT DEVSVTRRLY
ADGRSGYLIN DRKCRLRDIK ELFLDTGVGT NAYSIIEQGK VDAMLLANPM ERRSILEEAA
GVAKFRQRKL ESSRKLDAAE RNLVQVREKL ANTERRLRIV RSQAEKAERF RGLDDRRRTL
RTGIARDQFE EFDDRLAGLT RQLAAIETER RGLAASLAEL EEAKQAAEIE RHHIQERRHD
LEQERLTERN RLDQAGQRIE LTTRHRDDAA KAIADETRRI GELEVQVEAL GRDLAEVEAR
IDESAQEAAA AETRLADETT RRHQFEAART EAVATVEDAR DGLAAADRDR IRLESAVRGV
DARETELQQR LRRLAEKTRP FAADLDAHRV QRLRAENRVD VLVDRIARLD AALRGEEERI
VRLDDRRADL TRRIAGNRDE RTGTETRRRL LEEMATAGEG IGDAVREVLD LAGTVEGIIG
PLADHVDVDR NDAEAIEAAL GTHLQAVLVE SSGVADEILR RLPELQGRVE LLPISRFTAG
SVVSTRINAA IHATENLVEA VSLVRTAPRI RGVVEHVLGD TLVVEDFAAG RRLAGRGVGR
RLASRDGHVL NATGEVILRA AAGREEGHGL LGRKAELAEL EGIGSRLEVV RQELEGEAST
LDAEHSTRGE RRQDLSETLR AGRAEEVEQR YAIDRTSQMI DRIARERGEL EGEQSEIVEQ
LTSVHLERRR LDGERAMAIE HEATRSSTLD ASRARLAEIS EASEAAMESV TAERTRLGEI
NARLESTRRE RTRMSTALEE SXRQLDRGRS QVAERQGRIT EYLEAISAAE TEVAASTATL
EGMDGRFVEN DQAMESAASR LEGTTTALEA ARVEAGRLDR DAHALEMSRR EIEIKREALE
ESVLEELGLD PHELRASAPT CSEDEGEGPL PFDRAAAIEE SESLRVEIKR LGNVNLDAIE
ELQDLEVRNE DLATQLEDID SARVLLSDLI ERLDAASRIR FEETFNRVRE NFAGSQGMFR
RLFGGGSADL YLLPGEDGSI DWLESGIEIR AKPPGKEPRV ISQLSGGEKT MTAVGLLMAI
FQSKPSPFCI LDEVDAALDE ANVERFCNVV RQFLDQSHFI VITHHKRTMQ ACDRLFGVTM
PERGVSRRVT VKFDEVGRDG RIDGEAVRRA DEALVESEAV APPEIETEAL DPTSLRGGAA
SLPPASETSG SRLAEAWEN
//
