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Database: UniProt
Entry: M9SFH2_METAX
LinkDB: M9SFH2_METAX
Original site: M9SFH2_METAX 
ID   M9SFH2_METAX            Unreviewed;      1203 AA.
AC   M9SFH2;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN   Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN   ORFNames=MMALV_02170 {ECO:0000313|EMBL:AGI84973.1};
OS   Methanomethylophilus alvi (strain Mx1201).
OC   Archaea; Candidatus Thermoplasmatota; Thermoplasmata;
OC   Methanomassiliicoccales; Methanomethylophilaceae; Methanomethylophilus.
OX   NCBI_TaxID=1236689 {ECO:0000313|EMBL:AGI84973.1, ECO:0000313|Proteomes:UP000012672};
RN   [1] {ECO:0000313|EMBL:AGI84973.1, ECO:0000313|Proteomes:UP000012672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mx1201 {ECO:0000313|EMBL:AGI84973.1,
RC   ECO:0000313|Proteomes:UP000012672};
RX   PubMed=23209209; DOI=10.1128/JB.01867-12;
RA   Borrel G., Harris H.M., Tottey W., Mihajlovski A., Parisot N.,
RA   Peyretaillade E., Peyret P., Gribaldo S., O'Toole P.W., Brugere J.F.;
RT   "Genome sequence of 'Candidatus Methanomethylophilus alvus' Mx1201, a
RT   methanogenic archaeon from the human gut belonging to a seventh order of
RT   methanogens.";
RL   J. Bacteriol. 194:6944-6945(2012).
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       Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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. {ECO:0000256|HAMAP-
CC       Rule:MF_01894}.
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DR   EMBL; CP004049; AGI84973.1; -; Genomic_DNA.
DR   RefSeq; WP_015504122.1; NC_020913.1.
DR   AlphaFoldDB; M9SFH2; -.
DR   STRING; 1236689.MMALV_02170; -.
DR   GeneID; 41321016; -.
DR   KEGG; max:MMALV_02170; -.
DR   eggNOG; arCOG00371; Archaea.
DR   HOGENOM; CLU_001042_2_2_2; -.
DR   InParanoid; M9SFH2; -.
DR   OrthoDB; 9143at2157; -.
DR   Proteomes; UP000012672; 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   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; TIGR02169; SMC_prok_A; 1.
DR   NCBIfam; TIGR02168; SMC_prok_B; 1.
DR   PANTHER; PTHR18937; STRUCTURAL MAINTENANCE OF CHROMOSOMES SMC FAMILY MEMBER; 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.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000012672}.
FT   DOMAIN          531..647
FT                   /note="SMC hinge"
FT                   /evidence="ECO:0000259|SMART:SM00968"
FT   REGION          368..388
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          193..220
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          694..798
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          832..957
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   1203 AA;  132559 MW;  1DF51D29158770E2 CRC64;
     MYLKQIELEN FKSFGGKVTV PLMEGYMAVT GPNGSGKSNI ADAILFVLGP RSSKAVRASR
     ITDLIFDGGA AKSKAKFMKV SLVFDNSDRI MPWDDDTVIL TRYVKLSENG TDYTSYFFIN
     DQKSSLSEFD TLLTKARISA DGYNIVQQGD VTHIVQMGNI ERRRILDGIS GIASFDADID
     KAKGERAEAS SNLERIDIIR AEKERQISAL EKDREQAKVY LEAKKDLDIA NAQMVYRLRD
     NEKATFDSLG ANIALIQKDI EGLRKDKAAL LGQRQENEAA VRAKEDEIAA KVGPDYLRIK
     GDVEQAKIDV ATEKSKHDSA VEDAEDQREF REGFVQDVEE NRNQYATSAQ NLSDLQIRLE
     GAQADLAAAE EEERRISEET SKHGGELTEL QKRLETLERD IDAAGHVQQD AQAKAAGAQA
     VLDEARVAKA KAEEDLESAR FEVKDADWNL QEVKRQAGPQ NEIDELGKQI MALKKEEAAK
     EKEEEELKDI AEKRTAEFNR LSTEKRVSES MNKGSEAMSR ILALKESGQM PGIHGTVAEL
     ATVDPGYETA LSVAAGNKMG AIVVDNKDVA ARCIEYLKKN GLGRVTFLPL TELLPGKPRA
     KAIIALKSTD GYATDFVTYK PEYANVFWYV FGDTLVVGTL DKAKEVMGGV RIVTKAGELI
     EASGAMTGGT IDKRKVQQFG PSGQSALEAA GAEMRKAVEA LAVLRSDLRQ LRDAIRQTDD
     LMRAAGTKGI DMKGKIVAAE AALEQARKGV KSAEEVLSKR TSDVTAAEKA LSDAAAALDA
     ANSKLDSLRE ERTAARDRMA VIAPAGLQER IQKARDAVYC HTQTVTDLLQ QIGGLKAEMS
     GLDKQKEALE EQISKIDSQI AEDEKAASEH AAKVEEFRVR LEAVKRIQDE MESKIEDLKA
     ERDALIQNGY SLDNAVEKAQ NGIEAKDGYL QSQTAQMETS RINLEQYEEQ VKALTVEVPE
     PIPSESSLKV AIRQCQAKID ALGHVNLRAI EDYDICKQEY DLMMGQVAIL NNRISDLDRL
     TEDLSRKKKG LFMEAYDAVD SNFKAIYAQL SGGGQAFMAL DVPEDPFSGG LQINAKPRNG
     KMLRLEALSG GEKSLTALAF IFAIQEYQPS PFYVLDEVDM FLDAVNAEMV ARRVKESSAR
     TQFIQVSLRK VTLTLADHLI GVTRPPTGIS RVIMQPDIAE VSKYEEEALR RQREEGSSDN
     IEG
//
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