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
//