ID A0A1V2YBH1_9FIRM Unreviewed; 1183 AA.
AC A0A1V2YBH1;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=BEN19_03535 {ECO:0000313|EMBL:OOB76884.1};
OS Epulopiscium sp. Nuni2H_MBin003.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Candidatus Epulonipiscium.
OX NCBI_TaxID=1884657 {ECO:0000313|EMBL:OOB76884.1, ECO:0000313|Proteomes:UP000189211};
RN [1] {ECO:0000313|EMBL:OOB76884.1, ECO:0000313|Proteomes:UP000189211}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nuni2H_MBin003 {ECO:0000313|EMBL:OOB76884.1};
RA Ngugi D.K., Miyake S., Stingl U.;
RL Submitted (JUL-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:OOB76884.1}.
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DR EMBL; MDJN01000205; OOB76884.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V2YBH1; -.
DR STRING; 1884657.BEN19_03535; -.
DR Proteomes; UP000189211; 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; 1.20.1060.20; -; 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:UP000189211}.
FT DOMAIN 519..637
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT COILED 181..289
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 318..345
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 381..464
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 740..801
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 858..934
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 1001..1028
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 1183 AA; 136192 MW; F4C60D3F7DA7AFA9 CRC64;
MYLEKVEIVG FKSFADKIKL EVPQGITAII GPNGSGKSNI ADAIRWVLGE QNIKVLRGQK
TQDIIFTGSE KRRALGYAEV CLYINNSTHD LKIDFTEVAV KRRIYRSGES EYLLNNSICR
LKDIQEIFMD TGVGKEGYSI IGQGQIEKIL SSKPEERRNV FEEAAGIYKY KVKRLETYKK
LDKERENIKR VEDILSEIEQ RIEPLRKEAD KTKQYLTLKD RLKSIEINLF LTQLEQIEKD
LTELNNNSNI VNNQIIDKKE NISHYITQST NLKKQQHNLQ LKIDALLNET IEIEKLIATQ
LAQISIYEEK THLSVNLNQQ LDQDKDKLGE NEKELSKNLQ LYKTKLIAEQ EQHISMKKTL
VDIEQEFEYI KQIKQDKKTK LEEAKQHKIS SLNKLEFLQL EISRNKKAKE VLLAKQETTN
TTLSTLNTEL TTYKQQLVDI NEQSQQLEKD FIILEKQLLK QEANKNAIVD KYNILEKEYV
TLMNDEETTK NKIQFLNQLK NEFEGYSKSV KEVLKLKCTG VVGVISDLIE VKKEYEIAIS
ISLGSSVHHI VTHTEQDAKN IITTMKKKKI GRVTFLPRDT IKSAKNIKEY PELAKQPGFI
GIASNLISYK KEDKDIISHL LGKIIIIDNM QNASNIAKKF NYKYKLVTLG GELFNIGGAL
SGGSQKANNL FTRSRELKEC EQKLIQLTIS KDETKINVEE LKINLDKVNI ILTEHASSIK
VVENKQTNLG IEQKIISEKV TFLQNNKAEL QATVKDIQHE IKKTDLQLSE DTEKVQEYQN
NKFQDEESNK LEQELIKLET IGEEKLNKIA QCKMDIYKVS TNIDMINNSI INMDKQLQKN
MQDINQLRTQ KALNLKNQQD YSTNIADLNK QIIQLKNKVQ QQQQAKLECT DRIEHIQKTN
QNVNKNILDT TAEVSELEKD AIRLDAKKDA MLKDKHNLNQ YIWQEYQLTP SACNIKKEFL
YSQNKLKQVQ LEHKEQIRQI GNVNVNAVEE YTNITQRFEF LTAQKEDIQN AEKTLLKLID
NLTNEMNDIF REQFKNIAEN FGKVFKELFE GGSAFLELTD KENILESGID IIVRPPGKKL
QNMSLLSGGE RTLTAIALLF GILTLKASPF CVLDEIEASL DEANVLRFIK YLKTLAKDTQ
FVVITHRKGT MEYANTLYGV TQQEKGVSAI VSVKLDEAKE YVK
//
