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Database: UniProt
Entry: D5E817_METMS
LinkDB: D5E817_METMS
Original site: D5E817_METMS 
ID   D5E817_METMS            Unreviewed;      1173 AA.
AC   D5E817;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   24-JAN-2024, entry version 72.
DE   RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN   Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN   OrderedLocusNames=Mmah_1810 {ECO:0000313|EMBL:ADE37305.1};
OS   Methanohalophilus mahii (strain ATCC 35705 / DSM 5219 / SLP).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanohalophilus.
OX   NCBI_TaxID=547558 {ECO:0000313|EMBL:ADE37305.1, ECO:0000313|Proteomes:UP000001059};
RN   [1] {ECO:0000313|EMBL:ADE37305.1, ECO:0000313|Proteomes:UP000001059}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35705 / DSM 5219 / SLP
RC   {ECO:0000313|Proteomes:UP000001059};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Lykidis A., Saunders E., Brettin T., Detter J.C., Han C., Land M.,
RA   Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA   Spring S., Schneider S., Schroeder M., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Methanohalophilus mahii DSM 5219.";
RL   Submitted (MAR-2010) 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; CP001994; ADE37305.1; -; Genomic_DNA.
DR   RefSeq; WP_013038247.1; NC_014002.1.
DR   AlphaFoldDB; D5E817; -.
DR   STRING; 547558.Mmah_1810; -.
DR   GeneID; 8983995; -.
DR   KEGG; mmh:Mmah_1810; -.
DR   HOGENOM; CLU_001042_2_2_2; -.
DR   OMA; HNKIAME; -.
DR   OrthoDB; 9143at2157; -.
DR   Proteomes; UP000001059; 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; 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.
DR   SUPFAM; SSF57997; Tropomyosin; 2.
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:UP000001059}.
FT   DOMAIN          529..644
FT                   /note="SMC hinge"
FT                   /evidence="ECO:0000259|SMART:SM00968"
FT   REGION          875..915
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          169..291
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          342..509
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          982..1009
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   1173 AA;  135429 MW;  7E12BF3196BD7863 CRC64;
     MYIKKIEFMN FKSFGKKVKI PFFDDFTTIS GPNGSGKSNI IDGILFVLGL SSSRTLRAEK
     LTDLIYNGEK SKNPDNAQVT IYFDNKDREL PVDNDEVVIS RKVRSTDNGY YSYFYFNGKS
     VSLGDVHNYL AKARVTPEGY NVVMQGDVTR IITMTAGERR KIIDEIAGVA EFDNKKERAL
     NELEVVRERI ERADILIDEV DKQKEKLQGE RDQAVKYQSL KEEKMKFEGF VLLSKLKDAK
     TELEGVGQEY DTQQEKLEKI SSELKQKKEV LEQREEELRL LNQRIQKMGE DEQIEVKRRI
     EEIRGEISGC SDRIDYAGQE IDEIDAARRR FFLEIDESKG KVDDIEEKVG EHNFQKETLQ
     SEISEKRTQR MLLQSRIADV DEKFARTRDE LSANKDELEQ LKTQKNELMR NEDRLLDSLR
     RKSADVAEIE DEIRQAKEKA KSSESDTKSV QYDIDKLNEK IEGLTKDLDD LESNRHQIKK
     VVSDLENDIR RKQQDYAMLE ARVRAAEDTS RYSRAVDAVI KEKDKHGLPG IYGTIAELGK
     VNQKYSTALG IAAGGRMQAV VVDTDEDASR AIAYLKRQRS GRATFLPLNK MEARRPYKNL
     SDREGVIGYA IDLIDFDPKF EAAFWYVFRD TLVVDTLENA RKLMGGLRMV TLEGEIVEKS
     GAMSGGSQRK SGLSFAASEK DKLVRISEEL TKLESRRSNA INKLDTTEGH ISSTNKEIQQ
     YENEVSRKQM QFEEIGNRGE TLEKLLNSKD EELKQIEEER QQMRTEMNET VEKKEHLEER
     EQSLQQNILQ IEEKLADSEI PELNKQAEDL DEELRRLDGR IRDIDGQINA LELDKKYATE
     KMEQNREQIA QMDEKKRTLK ERIEELKNKI TSLESELEEK KQREEELTGE LRQLQGEREN
     KETAYSTQRD EVDRVKSRYE KAENQKMALE ATLDAVKEQI EQLREEVTRR GLEETDEVPG
     YETVRTRITS IEKAMEALEP VNMRAIDEYE EVEQRIVDLK SRRAILFNER EQILDRIDQY
     DNLKKETFME TYNGINDAFK EIFNELSDGA GELVLDNEED PFSGGMTLKA QPRDKTLQRL
     EAMSGGEKSL TALAFLFAIQ QYRPAPFYAF DEIDMFLDGV NAERVARRVK KAAGNAQFIV
     VSLRKPMIEA AERTIGVTMQ QDNITSITGM KIR
//
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