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Database: UniProt
Entry: A0A1G1PYY7_9BACT
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Original site: A0A1G1PYY7_9BACT 
ID   A0A1G1PYY7_9BACT        Unreviewed;      1134 AA.
AC   A0A1G1PYY7;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN   Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN   ORFNames=A2243_05740 {ECO:0000313|EMBL:OGX46834.1};
OS   Omnitrophica WOR_2 bacterium RIFOXYA2_FULL_38_17.
OC   Bacteria; Candidatus Omnitrophota.
OX   NCBI_TaxID=1801873 {ECO:0000313|EMBL:OGX46834.1, ECO:0000313|Proteomes:UP000179162};
RN   [1] {ECO:0000313|EMBL:OGX46834.1, ECO:0000313|Proteomes:UP000179162}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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. {ECO:0000256|HAMAP-
CC       Rule:MF_01894}.
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:OGX46834.1}.
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DR   EMBL; MHHG01000073; OGX46834.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G1PYY7; -.
DR   Proteomes; UP000179162; Unassembled WGS sequence.
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; 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; IPR011890; SMC_prok.
DR   PANTHER; PTHR43977; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 3; 1.
DR   PANTHER; PTHR43977:SF1; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 3; 1.
DR   Pfam; PF02463; SMC_N; 1.
DR   PIRSF; PIRSF005719; SMC; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01894};
KW   Coiled coil {ECO:0000256|HAMAP-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          2..1113
FT                   /note="RecF/RecN/SMC N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02463"
FT   COILED          167..272
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          311..492
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          711..829
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          885..949
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   1134 AA;  130509 MW;  11BF3BEC2B037AFA CRC64;
     MYLKRLEIFG FKSFADKTVL NFEPGITAVV GPNGCGKSNV FDSIRWVLGE QSAKELRGSA
     MGDVIFNGTE KKASLGFAEV SLTFSNESKM LPIDYDEVTI TRRLFRSGES EYLLNKTPVR
     LKDIQELLMG TGIGAEAYSL LPQGKVDMVV SAKPEERRMI LDEASGITKY KAKKKEALNR
     LKDTENNLLR VNDITIEVKR QIASIERQAK KASKYKEKFE FLKKQETKYS RCQIKELEDE
     KSSMDVHVKE VTEKINSLNQ ELEEASEHLT NEINYLGEVE HKINELNSQG IKLDGQIDLD
     NRQVGFNQER IENLMQNDRK LKEQKGQLIE KCKIQQEKIE ELEQALITLE EAKIHNERSL
     KEKRDVLAIL ERLVKEAKDK IKGNEENILS LSAKQANTRN DLTDVMKEMQ GYLARKRRLE
     LETEKVLIEK QQVNERLDEV NGQINSLDLE INEFKQIKDS RGEKLRSYEA EFEQLKSTIE
     DLEKKTLFLK SQKEFIEKLH AQYQDMPDPV VEGRYYASAA PMDHHTGIIG KVKEVNALAD
     DQLQQLKQRF NQSVGNGLEQ SLQLYEIVCE TKFVELDPQQ ISLKINEINL QISEYVARRD
     FVSGQIVEHR ELFKEVIYKI QDKEKKHSIL ESQRNDILAE EQKLQGEMEL VCSEIEEVKE
     FMAETKKNEE RISYELETIT QDIEWCQNDI HDKREAIASK SKEKENVIVS IAQLETEIAA
     DSDKLTSYKK NQSMFSETLD GWLEDINKID NEAIGQEDKK SLYEREIEGL ERRIEEVRSE
     RESFKNVLND YIVQKEDIAQ RINSSRANMN ALELEIDDIK QKVHEKQLKE QEISFSIRAI
     KDRMSQTYKI DLDAPERDMN TSFSEKDATQ CPLIQLEAEI FGKVLEVKEL KAEKAFEEVE
     EQAEQIDMNE LALEIEKLRK QCDSFGSVNL VAIEEYEQLK ERFEFLTKQQ SDLFEAKSQL
     MSTINKINRS TRQMFMETFT KVSEQFRIYF RMLFGGGEAQ LVLLEPDNVL ESGIEIIARP
     PGKKLQSISL LSGGEKTLTA IALIFGVFKV NPSPFCVLDE IDAALDESNV GRFGFLLKDF
     AKIAQFIVIT HNKKTIANAN IMYGITMPET GCSRVVSVKF SSEEKQEEVL TAGV
//
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