GenomeNet

Database: UniProt
Entry: A1HN79_9FIRM
LinkDB: A1HN79_9FIRM
Original site: A1HN79_9FIRM 
ID   A1HN79_9FIRM            Unreviewed;      1185 AA.
AC   A1HN79;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   24-JAN-2024, entry version 74.
DE   RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN   Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN   ORFNames=TcarDRAFT_2177 {ECO:0000313|EMBL:EAX48705.1};
OS   Thermosinus carboxydivorans Nor1.
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC   Thermosinus.
OX   NCBI_TaxID=401526 {ECO:0000313|EMBL:EAX48705.1, ECO:0000313|Proteomes:UP000005139};
RN   [1] {ECO:0000313|EMBL:EAX48705.1, ECO:0000313|Proteomes:UP000005139}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nor1 {ECO:0000313|EMBL:EAX48705.1,
RC   ECO:0000313|Proteomes:UP000005139};
RG   US DOE Joint Genome Institute (JGI-ORNL);
RA   Larimer F., Land M., Hauser L.;
RT   "Annotation of the draft genome assembly of Thermosinus carboxydivorans
RT   Nor1.";
RL   Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EAX48705.1, ECO:0000313|Proteomes:UP000005139}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nor1 {ECO:0000313|EMBL:EAX48705.1,
RC   ECO:0000313|Proteomes:UP000005139};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Pitluck S., Richardson P.;
RT   "Sequencing of the draft genome and assembly of Thermosinus carboxydivorans
RT   Nor1.";
RL   Submitted (JAN-2007) 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:EAX48705.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AAWL01000002; EAX48705.1; -; Genomic_DNA.
DR   RefSeq; WP_007288476.1; NZ_AAWL01000002.1.
DR   AlphaFoldDB; A1HN79; -.
DR   eggNOG; COG1196; Bacteria.
DR   OrthoDB; 9808768at2; -.
DR   Proteomes; UP000005139; 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; 1.10.287.1490; -; 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; 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.
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:UP000005139}.
FT   DOMAIN          522..640
FT                   /note="SMC hinge"
FT                   /evidence="ECO:0000259|SMART:SM00968"
FT   COILED          167..201
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          234..310
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          346..450
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          682..856
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          899..933
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   1185 AA;  133747 MW;  45687B915C3AE19B CRC64;
     MLLRKLELYG FKSFADKTEV EFGPGITAIV GPNGSGKSNI TDAIRWALGE QNIRNLRGAK
     VEDVIFAGSA KRRPLGVAEV SLVFDNSSGT LPLDFNEVTI TRRVYRSGDS EYYINKAPCR
     LKDIHELLFD VGIGRDSLTV IGQNKIDEVL NAKAEERRLF FEEAAGITKY KHRKREALRK
     LEETEQNLVR VNDLIAEIHN QLGPLAESAE RTKRYNVLRQ ELISCQVTVL LDRLERATKM
     AESARLEQET LTEQEVVAAA QLSVRESEKE RLTDEINRYS EQQSILDQQI SQAATELERI
     DGKLAVLRER IEQGHRSGER VAREITRLED TAQGLDAKIT FLKSTLAAKE TQLAAAKETL
     AASNTNYEKL VMDIHQAEQE LEQGKAQTFV HIQQLVDERN KLRLMERDLA KLVARRDSLA
     AERQNYLAQL TKAEEQRQNL TAERDWLIQQ IGSAKDRISV LTSEKEKWEQ HLQDFVRIQH
     NLQAERDELR SRLKILTGMQ QDYEGFSRGI KSLLKTDAPW RRYIHGAVAE VIGVARPYLT
     AIEVALGGAL QYIITDNDET AKQAIAFLKT HNLGRATFLP LNTVRPSLPR PAEIAAAKAR
     GAIGLAASLV DCAPIYRPVI DFLLGHTVVV ETLDAAVKIA KEQSFTVRLV TLDGQQVNPG
     GTLTGGSTAK KENSFLGRSH EIEKLKERLA EMDQRLAAQQ AQAVAARTEV ERLAAEIAAV
     QREMQGKEVR LAEVAVHFDT VRADAARLRL ALQTIEQEME TNEAEQQELA QSVKNLENGI
     ALMESRDSQQ KETMVRLQQE LKKLQEQKEE LLAELAERRV QLATLEQDIH TGQANCLQYE
     QDKGALDRQL QNLRDEQVHI ADQIARAGAE IDALTVARLK RSTEKCEWER QRQETVQTKV
     NLLAELQRVD KDIRELRRKH QELRNRLHDV SLIAAKYNYE IAHCQEQLRD SCSLSVEEAA
     MLRRNDPPEV LEGLIRRLEM EIAAIGPVNP AAVEEYNRLN QRYNFYQSQS QDLIAAKEYL
     TSVINQIDDT MAKQFKTAFS AINRYFGEIF TRLFGGGKAE LVLQQPDDIL NTGIDVIAQP
     PGKKLQNLAL LSGGERALTV IALLFAFLTY RPSPFCVVDE IDAALDEANV QRFSEFLRDY
     KGKTQFIVVT HRKGTMEFAD IMQGVTMEES GVSRLVSVKF MDKAG
//
DBGET integrated database retrieval system