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GCH1L_METJA
ID   GCH1L_METJA             Reviewed;         244 AA.
AC   Q58337;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2002, sequence version 2.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=GTP cyclohydrolase 1 type 2 homolog;
GN   OrderedLocusNames=MJ0927;
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS   10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=243232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA   Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA   Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA   Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA   Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA   Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA   Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA   Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA   Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT   "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT   jannaschii.";
RL   Science 273:1058-1073(1996).
RN   [2]
RP   CRYSTALLIZATION.
RX   PubMed=23295494; DOI=10.1107/s1744309112049408;
RA   Kuan S.M., Chen H.C., Huang C.H., Chang C.H., Chen S.C., Yang C.S.,
RA   Chen Y.;
RT   "Crystallization and preliminary X-ray diffraction analysis of the Nif3-
RT   family protein MJ0927 from Methanocaldococcus jannaschii.";
RL   Acta Crystallogr. F 69:80-82(2013).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.47 ANGSTROMS), AND DNA-BINDING.
RX   PubMed=25243119; DOI=10.1155/2014/171263;
RA   Chen S.C., Huang C.H., Yang C.S., Kuan S.M., Lin C.T., Chou S.H., Chen Y.;
RT   "Crystal structure of a conserved hypothetical protein MJ0927 from
RT   Methanocaldococcus jannaschii reveals a novel quaternary assembly in the
RT   Nif3 family.";
RL   Biomed. Res. Int. 2014:171263-171263(2014).
CC   -!- FUNCTION: DNA-binding protein exhibiting the ability to bind to both
CC       single-stranded and double-stranded DNA. {ECO:0000269|PubMed:25243119}.
CC   -!- SUBUNIT: Homohexamer; trimer of dimers, that forms a hollow cage-like
CC       architecture. {ECO:0000269|PubMed:25243119}.
CC   -!- SIMILARITY: Belongs to the GTP cyclohydrolase I type 2/NIF3 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB98929.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; L77117; AAB98929.1; ALT_INIT; Genomic_DNA.
DR   PIR; G64415; G64415.
DR   RefSeq; WP_064496667.1; NC_000909.1.
DR   PDB; 4IWG; X-ray; 2.47 A; A/B/C=1-244.
DR   PDB; 4IWM; X-ray; 2.70 A; A/B/C/D/E/F=1-244.
DR   PDBsum; 4IWG; -.
DR   PDBsum; 4IWM; -.
DR   AlphaFoldDB; Q58337; -.
DR   SMR; Q58337; -.
DR   MINT; Q58337; -.
DR   STRING; 243232.MJ_0927; -.
DR   EnsemblBacteria; AAB98929; AAB98929; MJ_0927.
DR   GeneID; 1451816; -.
DR   KEGG; mja:MJ_0927; -.
DR   eggNOG; arCOG04454; Archaea.
DR   HOGENOM; CLU_037423_2_0_2; -.
DR   InParanoid; Q58337; -.
DR   OMA; THHSKIL; -.
DR   OrthoDB; 40682at2157; -.
DR   PhylomeDB; Q58337; -.
DR   Proteomes; UP000000805; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR002678; DUF34/NIF3.
DR   InterPro; IPR036069; DUF34/NIF3_sf.
DR   PANTHER; PTHR13799; PTHR13799; 1.
DR   Pfam; PF01784; NIF3; 1.
DR   SUPFAM; SSF102705; SSF102705; 1.
DR   TIGRFAMs; TIGR00486; YbgI_SA1388; 1.
PE   1: Evidence at protein level;
KW   3D-structure; DNA-binding; Metal-binding; Reference proteome.
FT   CHAIN           1..244
FT                   /note="GTP cyclohydrolase 1 type 2 homolog"
FT                   /id="PRO_0000147348"
FT   BINDING         65
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P0AFP6"
FT   BINDING         66
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P0AFP6"
FT   BINDING         102
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P0AFP6"
FT   BINDING         216
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P0AFP6"
FT   BINDING         220
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P0AFP6"
FT   BINDING         220
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P0AFP6"
FT   HELIX           3..13
FT                   /evidence="ECO:0007829|PDB:4IWG"
FT   HELIX           16..18
FT                   /evidence="ECO:0007829|PDB:4IWG"
FT   STRAND          26..29
FT                   /evidence="ECO:0007829|PDB:4IWG"
FT   STRAND          39..44
FT                   /evidence="ECO:0007829|PDB:4IWG"
FT   HELIX           48..56
FT                   /evidence="ECO:0007829|PDB:4IWG"
FT   STRAND          60..66
FT                   /evidence="ECO:0007829|PDB:4IWG"
FT   HELIX           78..89
FT                   /evidence="ECO:0007829|PDB:4IWG"
FT   STRAND          93..96
FT                   /evidence="ECO:0007829|PDB:4IWG"
FT   HELIX           99..103
FT                   /evidence="ECO:0007829|PDB:4IWG"
FT   HELIX           108..115
FT                   /evidence="ECO:0007829|PDB:4IWG"
FT   STRAND          119..125
FT                   /evidence="ECO:0007829|PDB:4IWG"
FT   STRAND          131..134
FT                   /evidence="ECO:0007829|PDB:4IWG"
FT   HELIX           139..149
FT                   /evidence="ECO:0007829|PDB:4IWG"
FT   STRAND          155..157
FT                   /evidence="ECO:0007829|PDB:4IWG"
FT   STRAND          167..174
FT                   /evidence="ECO:0007829|PDB:4IWG"
FT   HELIX           178..184
FT                   /evidence="ECO:0007829|PDB:4IWG"
FT   TURN            185..187
FT                   /evidence="ECO:0007829|PDB:4IWG"
FT   STRAND          189..194
FT                   /evidence="ECO:0007829|PDB:4IWG"
FT   HELIX           198..207
FT                   /evidence="ECO:0007829|PDB:4IWG"
FT   STRAND          210..213
FT                   /evidence="ECO:0007829|PDB:4IWG"
FT   HELIX           216..234
FT                   /evidence="ECO:0007829|PDB:4IWG"
FT   STRAND          237..242
FT                   /evidence="ECO:0007829|PDB:4IWG"
SQ   SEQUENCE   244 AA;  27363 MW;  BC42E5E29AAE399F CRC64;
     MKAKEIIEFI ETFAPKDLAI EGDNIGLQVG DNLDKEIKKL GIALDPSLSV IKKAEKEGVD
     FLFTHHPLLK DPIRNFTGVI YKKLKILMEN DIILYSAHTN LDICKNGLND ALAELYNLEN
     PKPLYDNGLG RVGIFKGSFE EFLEITKKYI HKNPIVVKSK EVDDNFKLAV LSGYGLSQSS
     IKYVAEKADV YLSGDLTHHS KILAEELGLV VVDATHYSTE VFGLKKFKEF LSSNLDLEII
     SLDF
 
 
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