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DOHH_CHAGB
ID   DOHH_CHAGB              Reviewed;         344 AA.
AC   Q2H0C0;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Deoxyhypusine hydroxylase {ECO:0000255|HAMAP-Rule:MF_03101};
DE            Short=DOHH {ECO:0000255|HAMAP-Rule:MF_03101};
DE            EC=1.14.99.29 {ECO:0000255|HAMAP-Rule:MF_03101};
DE   AltName: Full=Deoxyhypusine dioxygenase {ECO:0000255|HAMAP-Rule:MF_03101};
DE   AltName: Full=Deoxyhypusine monooxygenase {ECO:0000255|HAMAP-Rule:MF_03101};
GN   Name=LIA1 {ECO:0000255|HAMAP-Rule:MF_03101}; ORFNames=CHGG_04776;
OS   Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS   NRRL 1970) (Soil fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX   NCBI_TaxID=306901;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970;
RX   PubMed=25720678; DOI=10.1128/genomea.00021-15;
RA   Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT   "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL   Genome Announc. 3:E0002115-E0002115(2015).
CC   -!- FUNCTION: Catalyzes the hydroxylation of the N(6)-(4-aminobutyl)-L-
CC       lysine intermediate to form hypusine, an essential post-translational
CC       modification only found in mature eIF-5A factor. {ECO:0000255|HAMAP-
CC       Rule:MF_03101}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[eIF5A protein]-deoxyhypusine + AH2 + O2 = [eIF5A protein]-
CC         hypusine + A + H2O; Xref=Rhea:RHEA:14101, Rhea:RHEA-COMP:10144,
CC         Rhea:RHEA-COMP:12592, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:82657,
CC         ChEBI:CHEBI:91175; EC=1.14.99.29; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_03101};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03101};
CC       Note=Binds 2 Fe(2+) ions per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_03101};
CC   -!- PATHWAY: Protein modification; eIF5A hypusination. {ECO:0000255|HAMAP-
CC       Rule:MF_03101}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03101}.
CC       Nucleus {ECO:0000255|HAMAP-Rule:MF_03101}.
CC   -!- SIMILARITY: Belongs to the deoxyhypusine hydroxylase family.
CC       {ECO:0000255|HAMAP-Rule:MF_03101}.
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DR   EMBL; CH408032; EAQ88157.1; -; Genomic_DNA.
DR   RefSeq; XP_001223990.1; XM_001223989.1.
DR   AlphaFoldDB; Q2H0C0; -.
DR   SMR; Q2H0C0; -.
DR   STRING; 38033.XP_001223990.1; -.
DR   EnsemblFungi; EAQ88157; EAQ88157; CHGG_04776.
DR   GeneID; 4391909; -.
DR   eggNOG; KOG0567; Eukaryota.
DR   HOGENOM; CLU_053974_0_0_1; -.
DR   InParanoid; Q2H0C0; -.
DR   OMA; CIQILNR; -.
DR   OrthoDB; 1441854at2759; -.
DR   UniPathway; UPA00354; -.
DR   Proteomes; UP000001056; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0019135; F:deoxyhypusine monooxygenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008612; P:peptidyl-lysine modification to peptidyl-hypusine; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.25.10.10; -; 2.
DR   HAMAP; MF_03101; Deoxyhypusine_hydroxylase; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR027517; Deoxyhypusine_hydroxylase.
DR   InterPro; IPR021133; HEAT_type_2.
DR   InterPro; IPR004155; PBS_lyase_HEAT.
DR   SMART; SM00567; EZ_HEAT; 6.
DR   SUPFAM; SSF48371; SSF48371; 1.
DR   PROSITE; PS50077; HEAT_REPEAT; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Hypusine biosynthesis; Iron; Metal-binding; Monooxygenase;
KW   Nucleus; Oxidoreductase; Reference proteome; Repeat.
FT   CHAIN           1..344
FT                   /note="Deoxyhypusine hydroxylase"
FT                   /id="PRO_0000283660"
FT   REPEAT          81..107
FT                   /note="HEAT-like PBS-type 1"
FT   REPEAT          115..140
FT                   /note="HEAT-like PBS-type 2"
FT   REPEAT          210..240
FT                   /note="HEAT-like PBS-type 3"
FT   REPEAT          248..274
FT                   /note="HEAT-like PBS-type 4"
FT   REPEAT          281..308
FT                   /note="HEAT-like PBS-type 5"
FT   REGION          169..188
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         83
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03101"
FT   BINDING         84
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03101"
FT   BINDING         116
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03101"
FT   BINDING         117
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03101"
FT   BINDING         250
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03101"
FT   BINDING         251
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03101"
FT   BINDING         283
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03101"
FT   BINDING         284
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03101"
SQ   SEQUENCE   344 AA;  36538 MW;  3BB807BE1D02E4A3 CRC64;
     MTAPTTTSPS SEATTTTTTT TLNTIATLHQ SLTTETTPLP VRFRALFSLK HVAATHPATS
     AESLAAIDAI AAGFASPSAL LKHELAYCLG QTANGAAIPY LTAVLEDTGE DAMCRHEAAE
     ALGALGDVAS LGVLKRFRDR EGEEVVVTET CELAVERIEW ENGEGKKAEK LRASDFSSVD
     PAPPTAQGQE EQTVEELGNA LMDTSLPLFK RYRAMFALRD LASPPDLPTA VPAVLALAKG
     FADSSALFRH EIAFVFGQLA HPASIPALTE ALSNTEEASM VRHEAAEALG SLGDEEGVEE
     TLRKFLHDAE AVVRESVIVA LDMAEYEKSN ETEYALIPEA QGTA
 
 
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