ID A0A167NW30_CALVF Unreviewed; 640 AA.
AC A0A167NW30;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Prolyl 4-hydroxylase alpha subunit domain-containing protein {ECO:0000259|SMART:SM00702};
GN ORFNames=CALVIDRAFT_479244 {ECO:0000313|EMBL:KZO98146.1};
OS Calocera viscosa (strain TUFC12733).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Calocera.
OX NCBI_TaxID=1330018 {ECO:0000313|EMBL:KZO98146.1, ECO:0000313|Proteomes:UP000076738};
RN [1] {ECO:0000313|EMBL:KZO98146.1, ECO:0000313|Proteomes:UP000076738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TUFC12733 {ECO:0000313|EMBL:KZO98146.1,
RC ECO:0000313|Proteomes:UP000076738};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000256|ARBA:ARBA00001961};
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DR EMBL; KV417277; KZO98146.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A167NW30; -.
DR STRING; 1330018.A0A167NW30; -.
DR OrthoDB; 100633at2759; -.
DR Proteomes; UP000076738; Unassembled WGS sequence.
DR GO; GO:0016706; F:2-oxoglutarate-dependent dioxygenase activity; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:InterPro.
DR GO; GO:0008152; P:metabolic process; IEA:UniProt.
DR Gene3D; 3.60.130.20; Oxoglutarate/iron-dependent oxygenase, C-terminal degradation domain; 1.
DR Gene3D; 2.60.120.620; q2cbj1_9rhob like domain; 1.
DR InterPro; IPR019601; Oxoglutarate/Fe-dep_Oase_C.
DR InterPro; IPR006620; Pro_4_hyd_alph.
DR InterPro; IPR043044; TPA1/Ofd1_C.
DR InterPro; IPR039558; TPA1/OFD1_N.
DR PANTHER; PTHR12117; HISTONE ACETYLTRANSFERASE COMPLEX; 1.
DR PANTHER; PTHR12117:SF0; PROLYL 3-HYDROXYLASE OGFOD1; 1.
DR Pfam; PF13661; 2OG-FeII_Oxy_4; 1.
DR Pfam; PF10637; Ofd1_CTDD; 1.
DR SMART; SM00702; P4Hc; 1.
PE 4: Predicted;
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000076738};
KW Vitamin C {ECO:0000256|ARBA:ARBA00022896}.
FT DOMAIN 48..274
FT /note="Prolyl 4-hydroxylase alpha subunit"
FT /evidence="ECO:0000259|SMART:SM00702"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 533..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 640 AA; 69106 MW; 05E651468E28804D CRC64;
MPSTRPRPSS PSPAPSPKRQ KLARPSSTTD EEHTSAFVPG LFDPPTVAGL AQAYEASEPY
KHAVLPALVD DALLREVKDE ILNELRFAEK ETDIYKVHQT GDLASLNYLT PAQLALFPSL
LRLRNALYSR PFRQFMRSVT GCGPLSGTKQ DMSANSYRAG CHLLNHDDVI GTRRVSYILY
LPLAGGGEVG WQDAWGGALE LYPVSSPAAG ELPEPAAVPT KRLPPSWNQF VFFEVQPGHS
FHSVEEVVVP LHPNDSVGGS GEGRQRLSIS GWFHMAQPGE EGYEESRAQD RTERLQSSLE
QLSASEPAAL TPYPNPAPFL PSTPLTEAEL LFLSTYLNPV YLQPRSLLLL ADQFAADSSL
NLKDFLCSPL AQKLEPALRG RDAADGLGPE RAGHIPPHSA GVGHGWQLSG PPHKLRYCVL
SPSSSAQNDP AAALLQDLQE TLLPSPAFRA WLGLVTSLVP LSHQARARRF RPGLDYTLAQ
AEEGEARLDV VICVTPQPAE GEEVGKAEGG WASCAWGGWE CYMAPHEGEE DPAVYRSGGK
VNGHANGNGK EEVNGSGSGG ANGNEADREA ETADSDDSEE DETGTLLTAP ASFNGLLIVL
RDPKLMRFVK YVSAAAEGSR WDVCGEWQVG DLQVDEGDDE
//