ID I0GPN1_SELRL Unreviewed; 1181 AA.
AC I0GPN1;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 60.
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:BAL82718.1};
GN OrderedLocusNames=SELR_10100 {ECO:0000313|EMBL:BAL82718.1};
OS Selenomonas ruminantium subsp. lactilytica (strain NBRC 103574 / TAM6421).
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC Selenomonas.
OX NCBI_TaxID=927704 {ECO:0000313|EMBL:BAL82718.1, ECO:0000313|Proteomes:UP000007887};
RN [1] {ECO:0000313|EMBL:BAL82718.1, ECO:0000313|Proteomes:UP000007887}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 103574 / TAM6421 {ECO:0000313|Proteomes:UP000007887};
RA Oguchi A., Ankai A., Kaneko J., Yamada-Narita S., Fukui S., Takahashi M.,
RA Onodera T., Kojima S., Fushimi T., Abe N., Kamio Y., Yamazaki S.,
RA Fujita N.;
RT "Whole genome sequence of Selenomonas ruminantium subsp. lactilytica
RT TAM6421.";
RL Submitted (OCT-2011) 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}.
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DR EMBL; AP012292; BAL82718.1; -; Genomic_DNA.
DR RefSeq; WP_014424155.1; NC_017068.1.
DR AlphaFoldDB; I0GPN1; -.
DR KEGG; sri:SELR_10100; -.
DR PATRIC; fig|927704.6.peg.1041; -.
DR eggNOG; COG1196; Bacteria.
DR HOGENOM; CLU_001042_2_2_9; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000007887; 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 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; 2.
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}.
FT DOMAIN 521..637
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT COILED 166..200
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 261..435
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 679..856
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 913..944
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 986..1030
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 1181 AA; 134441 MW; 2D01EC48BDAC36C2 CRC64;
MQLKRLEAYG FKSFADKITI DFDQGITAIV GPNGSGKSNI TDAIRWVLGE QNVRNLRGTK
AEDIIFTGSA SRKALGVAEV SLFFANDGTL PVDFREVVVT RRLYRNGDSE FYINRSRCRL
KDIYNLFADT GIGHDGMSII GQNRIDDILN SRPEDRRAFF EETAGITKYR NRKRESVRKL
TDTENNLVRV QDIIHEIENQ LEPLSRHAEK TRIYNGLNEE YRRCKLAKLS FDYGQEAGKR
ADNEAKLTKF RDELLAADTH VQALAAEKEK LHKDIIDLEQ KLQAQAARNE SLRQKMEEAA
REMAKLQERQ DQSDEMRNRI LERRKSLNSE IARMVAEIAQ LTSDHQQQKQ DLALLDELLV
KEQAKQKKFS QLIREQEQAE RELEEERAQQ LEVWNARKQE YALAQRDLEN SEGDQESRED
ELYQAREKLA DLEDAQDVWQ KKLQQITVSF KADEEKWQQT AAHRKNAEAE QAQILRELNH
NSQQLHTAEN KLQFLTRMQQ AYEGFGKAVK AVLKSQESWR KGVAGAVAEL IDVPRDYVTA
IEVALGGNLQ NVVTQDTDTA KAAISFLKRE RQGRVTFLPL STLVVRQSQS IREGRDAGVI
GWANTLVRAD SCYQKAIDFL LARTLVVDNL DNALKIARDH EQRLRIVTLS GELLNPGGSL
SGGSRQHAEA SFLNRSGEIE DLKGKITSLQ AESRKLTALR DERTQQLQAL EHDMQQLQDN
LQQQRISQAE LETNLQAAGQ NLTEQQTKVA AIEEALQTFQ KSFARMQEKK VLAKRAAAEA
EGRYQELDKD LEKAREKLED LVQDAEDLRR YINDREIKRA ALEQEILGNT QFLQLRAKAK
TASEEALKAN EQEERDLDAS LVDSVDRLKV LDAQQHEWQD SYDEGQAAHD DIYKERMDKL
EASQEADKQA TVAAQQRNRL QDAIQSHEIA QNKLDMKLES LQETILAEYG LTPERAAEEA
MEGEPAEIKA NMQQLERKLK ELGPVNPNAL EEFEELQKRH DFMEKQAGDL NTAKEDLEKI
LADMDEAMTK QFKEAFAQIQ VYFGEIFVRL FGGGKAELQL TDKDDVLNAG VDILVTLPQK
KRQNLSALSG GERALTVIAL LFSFLRYRPS PFSVLDEIDA PLDEANVVRF GSFLKEFAEN
TQFIVVTHRK GTMEAVDTLY GVTIEDAGVS KILSVKIDEV E
//
