位置:首页 > 蛋白库 > DOHH_PHANO
DOHH_PHANO
ID   DOHH_PHANO              Reviewed;         329 AA.
AC   Q0UHL8;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 96.
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=SNOG_08746;
OS   Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS   blotch fungus) (Parastagonospora nodorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC   Parastagonospora.
OX   NCBI_TaxID=321614;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX   PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA   Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA   Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA   Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT   "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT   analysis of the wheat pathogen Stagonospora nodorum.";
RL   Plant Cell 19:3347-3368(2007).
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}.
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; CH445337; EAT83914.1; -; Genomic_DNA.
DR   RefSeq; XP_001799054.1; XM_001799002.1.
DR   AlphaFoldDB; Q0UHL8; -.
DR   SMR; Q0UHL8; -.
DR   STRING; 13684.SNOT_08746; -.
DR   EnsemblFungi; SNOT_08746; SNOT_08746; SNOG_08746.
DR   GeneID; 5975953; -.
DR   KEGG; pno:SNOG_08746; -.
DR   eggNOG; KOG0567; Eukaryota.
DR   HOGENOM; CLU_053974_0_0_1; -.
DR   InParanoid; Q0UHL8; -.
DR   OMA; CIQILNR; -.
DR   OrthoDB; 1441854at2759; -.
DR   UniPathway; UPA00354; -.
DR   Proteomes; UP000001055; 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; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR   GO; GO:0008612; P:peptidyl-lysine modification to peptidyl-hypusine; IBA:GO_Central.
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; IPR004155; PBS_lyase_HEAT.
DR   SMART; SM00567; EZ_HEAT; 6.
DR   SUPFAM; SSF48371; SSF48371; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Hypusine biosynthesis; Iron; Metal-binding; Monooxygenase;
KW   Nucleus; Oxidoreductase; Reference proteome; Repeat.
FT   CHAIN           1..329
FT                   /note="Deoxyhypusine hydroxylase"
FT                   /id="PRO_0000283671"
FT   REPEAT          65..91
FT                   /note="HEAT-like PBS-type 1"
FT   REPEAT          99..124
FT                   /note="HEAT-like PBS-type 2"
FT   REPEAT          232..258
FT                   /note="HEAT-like PBS-type 3"
FT   REPEAT          265..292
FT                   /note="HEAT-like PBS-type 4"
FT   BINDING         67
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03101"
FT   BINDING         68
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03101"
FT   BINDING         100
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03101"
FT   BINDING         101
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03101"
FT   BINDING         234
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03101"
FT   BINDING         235
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03101"
FT   BINDING         267
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03101"
FT   BINDING         268
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03101"
SQ   SEQUENCE   329 AA;  35710 MW;  02709670D3FC2F77 CRC64;
     MAVTEQDTQV PTLRKIVTSE SEPLARRFRA LFSLKHLASL QPPTEQTVPA IEAIAAAFSS
     PSALLKHELA YCLGQSGHDA AIAPLRGVLE DKDEDSMCRH EAAEALGALS DKGSLELLKK
     MRDDANEVDV VRETCDIAVD RIEWEHGLQK GTEKLKKSDF TSVDPAPPMP ESNEAPSIPA
     LEKTLLDTTL PLFQRYRAMF ALRDLSSPPD LPTAVPAVHA LARGFGDPSA LFRHEIAFVF
     GQLSHPASIP SLTEALSNTK EASMVRHEAA EALGSLGDEE GVEETLKKFL NDPEQVVRDS
     VIVALDMAEF EKNGEVEYAI VPQAQAIAA
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2025