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Database: UniProt
Entry: A1SZA8_PSYIN
LinkDB: A1SZA8_PSYIN
Original site: A1SZA8_PSYIN 
ID   A1SZA8_PSYIN            Unreviewed;       840 AA.
AC   A1SZA8;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 104.
DE   SubName: Full=MCP methyltransferase, CheR-type {ECO:0000313|EMBL:ABM04823.1};
GN   OrderedLocusNames=Ping_3128 {ECO:0000313|EMBL:ABM04823.1};
OS   Psychromonas ingrahamii (strain DSM 17664 / CCUG 51855 / 37).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Psychromonadaceae; Psychromonas.
OX   NCBI_TaxID=357804 {ECO:0000313|EMBL:ABM04823.1, ECO:0000313|Proteomes:UP000000639};
RN   [1] {ECO:0000313|EMBL:ABM04823.1, ECO:0000313|Proteomes:UP000000639}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=37 {ECO:0000313|EMBL:ABM04823.1,
RC   ECO:0000313|Proteomes:UP000000639};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Staley J.,
RA   Richardson P.;
RT   "Complete sequence of Psychromonas ingrahamii 37.";
RL   Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP000510; ABM04823.1; -; Genomic_DNA.
DR   RefSeq; WP_011771377.1; NC_008709.1.
DR   AlphaFoldDB; A1SZA8; -.
DR   STRING; 357804.Ping_3128; -.
DR   KEGG; pin:Ping_3128; -.
DR   eggNOG; COG0840; Bacteria.
DR   eggNOG; COG1352; Bacteria.
DR   eggNOG; COG2201; Bacteria.
DR   HOGENOM; CLU_000892_0_1_6; -.
DR   OrthoDB; 9816309at2; -.
DR   Proteomes; UP000000639; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0000156; F:phosphorelay response regulator activity; IEA:InterPro.
DR   GO; GO:0008984; F:protein-glutamate methylesterase activity; IEA:InterPro.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR   GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-UniRule.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   CDD; cd16434; CheB-CheR_fusion; 1.
DR   Gene3D; 3.40.50.180; Methylesterase CheB, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR035909; CheB_C.
DR   InterPro; IPR022642; CheR_C.
DR   InterPro; IPR000780; CheR_MeTrfase.
DR   InterPro; IPR022641; CheR_N.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR000673; Sig_transdc_resp-reg_Me-estase.
DR   PANTHER; PTHR24422; CHEMOTAXIS PROTEIN METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR24422:SF25; CHEMOTAXIS PROTEIN METHYLTRANSFERASE; 1.
DR   Pfam; PF01339; CheB_methylest; 1.
DR   Pfam; PF01739; CheR; 1.
DR   Pfam; PF03705; CheR_N; 1.
DR   Pfam; PF13596; PAS_10; 1.
DR   PRINTS; PR00996; CHERMTFRASE.
DR   SMART; SM00138; MeTrc; 1.
DR   SUPFAM; SSF47757; Chemotaxis receptor methyltransferase CheR, N-terminal domain; 1.
DR   SUPFAM; SSF52738; Methylesterase CheB, C-terminal domain; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   SUPFAM; SSF57997; Tropomyosin; 1.
DR   PROSITE; PS50122; CHEB; 1.
DR   PROSITE; PS50123; CHER; 1.
PE   4: Predicted;
KW   Chemotaxis {ECO:0000256|PROSITE-ProRule:PRU00050};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00050};
KW   Methyltransferase {ECO:0000313|EMBL:ABM04823.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000639};
KW   Transferase {ECO:0000313|EMBL:ABM04823.1}.
FT   DOMAIN          1..190
FT                   /note="CheB-type methylesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50122"
FT   DOMAIN          210..475
FT                   /note="CheR-type methyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50123"
FT   REGION          653..684
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        653..669
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        670..684
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        13
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT   ACT_SITE        40
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT   ACT_SITE        132
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
SQ   SEQUENCE   840 AA;  94942 MW;  C1EA471CBFCD0D18 CRC64;
     MINTPVIVGI GASAGGFEAL EEFFSHVLTP CNIAFVVIQH LDPTHKGMMP ELLQRDTTMK
     VKQARNNMKV KPNCVYVIPP DKDLSVLHGV LFLLEPVVKH TIRLPIDSFF QSLAADQHER
     AVGVILSGMG SDGTIGLRAI KENAGLSLVQ SPESAKFDSM PQSAINAGLA DITAPAEELP
     ERIIAFLEHG RRGVPNKLEP IVKRKSISAL AQIMMILRER NGNDFSLYKT NTIDRRIERR
     MGLHQLKTIS LYARYLRDNP QEQDLLFKEL LIGVTNFFRD KDVWAQLKST SLPALLANYP
     EGKELRAWVT ACSSGEEAYS LAITVMDVLD EIKPKGHFTL QIFATDLNQD AINIARKGYY
     PAGIEADMSA QQLQRYFIKD GSGYRINKKI RDMVIFAPQN IIMDPPFTRL DILTCRNLLI
     YFAPELQKKL LPLFHYTLTS HGLLILGHSE TIGNATSLFS EIKENTRIYT RIDRPGQQME
     VNFPTKIFPI MPLAENEHEG TRKMTKNISN LQTQADQILL QNYSPAAVLV NAAGDIIYIN
     GRTGKYLEPA AGKANWNIHV MAREELQHQL ELAIKKAQIQ VEPVTIENIT VDGHSVNLTV
     QAIIKPKELL GLIMVVFTEV VRPTRRRRKK LGAVEQESQA ELQMAHDEIK SLREQMQSSH
     EELKSANEEL QSTNEELQST NEELTTSKEE MQSMNEELQT VNTELQSNVD DLSWVNNDME
     NLLNSTEIAT IFLDKGLHIR RFTNHATHLF KLIEGDVGRL LSDIVTDLDY KDLQKDAKEV
     LKRLAFVEKE ITANNERCFK VRIMPYRTQE NVIDGVVITF TNISEAKLLE SELRKTRCKT
//
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