ID A0A2H3L5C3_9CHLR Unreviewed; 1199 AA.
AC A0A2H3L5C3;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=A9Q02_22500 {ECO:0000313|EMBL:PDV97440.1};
OS Candidatus Chloroploca asiatica.
OC Bacteria; Chloroflexota; Chloroflexia; Chloroflexales; Chloroflexineae;
OC Oscillochloridaceae; Candidatus Chloroploca.
OX NCBI_TaxID=1506545 {ECO:0000313|EMBL:PDV97440.1, ECO:0000313|Proteomes:UP000220922};
RN [1] {ECO:0000313|EMBL:PDV97440.1, ECO:0000313|Proteomes:UP000220922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B7-9 {ECO:0000313|EMBL:PDV97440.1,
RC ECO:0000313|Proteomes:UP000220922};
RA Lavstsen T., Jespersen J.S.;
RL Submitted (MAY-2016) 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:PDV97440.1}.
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DR EMBL; LYXE01000144; PDV97440.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3L5C3; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000220922; 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 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.
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:UP000220922}.
FT DOMAIN 519..636
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT COILED 308..363
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 392..489
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 698..760
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 866..900
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 1199 AA; 133009 MW; 3E82E231E88E9FA9 CRC64;
MHLKRLEIQG FKTFASRTIL EFRAGITAVV GPNGSGKSNL ADAVRWVLGE QSLTNLRCKR
SEELLYAGGG RRAPAGFAEV SLTVDNSDRL LPVEFDEVTL TRRTTRAGES EYLLNRTRVR
LRDLLEVTAP LGGSYTIINQ GLVDAALTLR PEERRKLFED AADLGGFELR KAEALRRLRE
TEGNLQRLGD LLAELEPRLR VLKRQAAQAR QYHEYAAELA LLQQQYYVEL WGAALRMTAQ
TRADLQVAET HLTEARTGQA GVTAELQALR SSLRTRRDEL GALHQQSSLL HRQAETVQRD
LAVGNERVAA LARRTEDLER QRHELALRQA QAEQQHAEAI AETRQTEAEL AEREQALREV
ETELAGRADE VQALVRALRE AEEAALRTTR AAAEAHARLE QINAQTQRLA RETSELEASI
AQAEAHVASS TEQVADARAQ VSYAETARHE AATAEQALRH DIETLRQHYA QADEQRVTAR
RALADVEARF ESLSRLARSY TGTFAGVRAA MQWAERTQRQ GFALVQSLIR TPAELETALE
VALGSRLQNI VVEQWSDAEA AIAELKQRDV GRATFMPLDT LRVNESDQRP LTFDDEAVLG
VAADLVAYDA PYRPVVEQLL GRVLIVRDLS TARRELRRLR TGWNIVTLQG EQVNSGGSLT
GGARTKESGA LRRERELREL PAQVAAARQN VEAADTLRVQ LDTQLKTLNG QLREVEGRTR
ESQRLLETAR SGVAAAERRL AQAEQERTWA AQRRERLDSE HQSLDMQQHE VRLRLGEVEN
TAHATEVTLA ELRTRQAHEA SNDRLVQERL AGLRTEVATT RQRLRAAEQL RNNHAQSLAL
VQRQTSELDQ AALSLRDERD ALAAQHERHE ALHTALLTEI DQLRQRIDPA EAALHNDEAN
VRQLEAHEEA ATAHLLAMEA AQSKAALDAQ RAADRQEALF ERAAADGVNL EHVATSDAQA
GPAIDATHLQ ASIEALKTKI LRLGAVNQLA LEEYETTAER QRFLATQLAD LRAAGATLLE
LIGELDEAMN HRFTTTFHAI AAEFEQSFTR LFGGGSARLI LTSTARQNGQ ASNGTEPETV
DTRSLGVEII ARPPGKKQQN IALLSGGERS LTATALLFAI LTVHPTPFCI LDETDAALDE
ANVGRFREAL QHLTNQTQFI LITHNRGTIE AADTLYGVTM GDDGASKMMS LRIEQYIEG
//