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DGT1B_RHILO
ID   DGT1B_RHILO             Reviewed;         476 AA.
AC   Q989G8;
DT   06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   25-MAY-2022, entry version 100.
DE   RecName: Full=Deoxyguanosinetriphosphate triphosphohydrolase-like protein 2 {ECO:0000255|HAMAP-Rule:MF_01212};
GN   OrderedLocusNames=mlr6429;
OS   Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS   (Mesorhizobium loti (strain MAFF 303099)).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=266835;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX   PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA   Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA   Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT   Mesorhizobium loti.";
RL   DNA Res. 7:331-338(2000).
CC   -!- SIMILARITY: Belongs to the dGTPase family. Type 2 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01212}.
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DR   EMBL; BA000012; BAB52728.1; -; Genomic_DNA.
DR   RefSeq; WP_010914043.1; NC_002678.2.
DR   AlphaFoldDB; Q989G8; -.
DR   SMR; Q989G8; -.
DR   STRING; 266835.14026130; -.
DR   EnsemblBacteria; BAB52728; BAB52728; BAB52728.
DR   KEGG; mlo:mlr6429; -.
DR   PATRIC; fig|266835.9.peg.5104; -.
DR   eggNOG; COG0232; Bacteria.
DR   HOGENOM; CLU_028163_0_1_5; -.
DR   OMA; SIECQIM; -.
DR   OrthoDB; 370035at2; -.
DR   Proteomes; UP000000552; Chromosome.
DR   GO; GO:0008832; F:dGTPase activity; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0006203; P:dGTP catabolic process; IEA:InterPro.
DR   CDD; cd00077; HDc; 1.
DR   Gene3D; 1.10.3410.10; -; 1.
DR   HAMAP; MF_01212; dGTPase_type2; 1.
DR   InterPro; IPR023293; dGTP_triP_hydro_central_sf.
DR   InterPro; IPR006261; dNTPase.
DR   InterPro; IPR020779; dNTPase_1.
DR   InterPro; IPR023023; dNTPase_2.
DR   InterPro; IPR003607; HD/PDEase_dom.
DR   InterPro; IPR006674; HD_domain.
DR   InterPro; IPR026875; PHydrolase_assoc_dom.
DR   PANTHER; PTHR11373:SF32; PTHR11373:SF32; 1.
DR   Pfam; PF01966; HD; 1.
DR   Pfam; PF13286; HD_assoc; 1.
DR   SMART; SM00471; HDc; 1.
DR   TIGRFAMs; TIGR01353; dGTP_triPase; 1.
DR   PROSITE; PS51831; HD; 1.
PE   3: Inferred from homology;
KW   Hydrolase.
FT   CHAIN           1..476
FT                   /note="Deoxyguanosinetriphosphate triphosphohydrolase-like
FT                   protein 2"
FT                   /id="PRO_0000205315"
FT   DOMAIN          60..233
FT                   /note="HD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   476 AA;  53620 MW;  A7583FC2F87A5483 CRC64;
     MYTDADRSRE VVPEKDGHDK KWRDEFGRDY GRIIHSASFR RQQGKTQVFP SRESDFFRNR
     LTHSLEVAQI AQGIAERINY DYDKDLGGKI DPRLCATAGL VHDIGHPPFG HNGESALDKA
     MQRYGGFEGN AQTLRILTRL EKKLRYAEPL AGDDRAGLNL CHRTIAATLK YDNEIPAIRK
     AADGFVKGYY GSEKIIVDRV KASVLNGYVL GAEEKFCTIE CSIMDLADDI AYSVYDLEDC
     FKVGFLSPAE MLASDDALLS AVAKRASKPM KRTVTINEIQ AVFMEIFSEI IEQPAEDADS
     PLDGIVIEDD IAQQAKRDES LLTFAEAYRT SKVMSEDGYK RTEFSSELVH QFISGVELKA
     HKECPSLSQI YLPEKLMLRK EVLKQYTFVA AIYAPRVKLG EYRGYDLVTD IFKALMGDRG
     DLLMPADVRG RIRKAPNVSV KAREVCDFVA GMTDRYAMEF WARLNSDAAE SMFKPI
 
 
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