ID A0A264W6L8_9BACL Unreviewed; 1181 AA.
AC A0A264W6L8;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, 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 ECO:0000313|EMBL:OZS79254.1};
GN ORFNames=CF394_02220 {ECO:0000313|EMBL:OZS79254.1};
OS Tetzosporium hominis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Tetzosporium.
OX NCBI_TaxID=2020506 {ECO:0000313|EMBL:OZS79254.1, ECO:0000313|Proteomes:UP000217065};
RN [1] {ECO:0000313|EMBL:OZS79254.1, ECO:0000313|Proteomes:UP000217065}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VT-49 {ECO:0000313|EMBL:OZS79254.1,
RC ECO:0000313|Proteomes:UP000217065};
RA Tetz G., Tetz V.;
RT "Tetzosporium hominis gen.nov. sp.nov.";
RL Submitted (JUL-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:OZS79254.1}.
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DR EMBL; NOKQ01000134; OZS79254.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A264W6L8; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000217065; 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; 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; 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.
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:UP000217065}.
FT DOMAIN 520..639
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT COILED 241..475
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 680..721
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 834..908
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; 134573 MW; C1DD734615637C3F CRC64;
MFLKRLEIVG FKSFAERIAV DFVPGVTAVV GPNGSGKSNI TDAIRWVLGE QSAKSLRGAK
MEDVIFAGSA SRKALNFAEV TLVLDNSDQL LQTEYEEVSV TRRVYRSGDS DYLLNRQSCR
LKDITELFMD SGLGKEAFSI ISQGKVDEIL NSKAEDRRAI FEETAGVLKY KQRKKKAEFK
LIETDDNLSR VLDILHELEG RIEPLQIQAS VAKDYLAFAE ELKEREVSLA LYDISHQTVQ
LEESRKEKVS SKEAMDRLTE EREQMLAQLK QSKASLSELE QQLDQLQDEA LQISATLERQ
EGRKLVLVEK QNNRAQQVDK LTRSLEVATQ ELQDIESKLQ QISEQKQEHA QKVKALRSER
AKLEQLTGTS EQQIEQQIEQ LKSDYIELLN EEAALKNEQR LLLQQNEKQL AHLERFSQEV
EEIEIHLADS KKKVDAVALE KEQIDQKLEQ ALSSHRESKQ QADRVTEEYE KKRQLVFDGY
QQLHQLRAKR DSLAELEEEF SGYFQGVKEL LKQRESGKLS GIHGAVAELF TIPSEYIAAI
DTAIGGQAQH VVVESTKDAQ QAISFLKQHR YGRATFLPMD VIKPRQVASH QLQKVNGHPA
FIATANELVT TEPSYQAIRD NLLGTTIVAK NLKGATELAR VIQHSYRIVT LDGDVVHPGG
SLTGGAAKKQ SSVFTRKADL ENYTKLVHKL EKDLARAEAV VADLKEQKIR LDSEVEKVTA
LGEQLRHQQQ TLHRDLVTAS SQLEKWQEKH SVYHLQQREQ GEDRDVASAR LQEIKDQLAL
FAEQTVTIQQ QIQSLTEVKT KTVEEKDALQ HQLGELLTTI AVERERGQQF DRDLSTLSES
RDKAAQQIKL WEDELTWYQS GHDQQTEQEL DQEIVRLAET KQQLSLTIQQ LRDTRMTHQQ
EIRKTELKEE ACSSNLRDVS IRHEKVALVC EQLEKSIHSL HMLLLEDYDL DFEEAKTQFT
LPQDSEKERS KIRLLKKSIE ELGPVNLSAI EEFEQVNERY QFLTEQRTDL LEAKETLHVA
IAEMDEEMTE RFSTTFFEIQ KHFRVVFRKL FGGGQADLVI TQPDNMLETG IEIVAQPPGK
KLQNLSLLSG GERALTAIAL LFAILQTRPV PFCILDEVEA ALDEANVVRY SDYLKQFVED
TQFIVITHRK GTMEGADVLY GVTMQESGVS KLVSVKLEDY V
//
