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Database: UniProt
Entry: A0A016UNU9_9BILA
LinkDB: A0A016UNU9_9BILA
Original site: A0A016UNU9_9BILA 
ID   A0A016UNU9_9BILA        Unreviewed;       281 AA.
AC   A0A016UNU9;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Prolyl 4-hydroxylase alpha subunit domain-containing protein {ECO:0000259|SMART:SM00702};
GN   Name=Acey_s0032.g2547 {ECO:0000313|EMBL:EYC16885.1};
GN   ORFNames=Y032_0032g2547 {ECO:0000313|EMBL:EYC16885.1};
OS   Ancylostoma ceylanicum.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC   Ancylostomatinae; Ancylostoma.
OX   NCBI_TaxID=53326 {ECO:0000313|EMBL:EYC16885.1, ECO:0000313|Proteomes:UP000024635};
RN   [1] {ECO:0000313|Proteomes:UP000024635}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX   PubMed=25730766; DOI=10.1038/ng.3237;
RA   Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA   Aroian R.V.;
RT   "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT   ceylanicum identify infection-specific gene families.";
RL   Nat. Genet. 47:416-422(2015).
CC   -!- COFACTOR:
CC       Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC         Evidence={ECO:0000256|ARBA:ARBA00001961};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EYC16885.1}.
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DR   EMBL; JARK01001368; EYC16885.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A016UNU9; -.
DR   Proteomes; UP000024635; Unassembled WGS sequence.
DR   GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0031418; F:L-ascorbic acid binding; IEA:InterPro.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   Gene3D; 2.60.120.620; q2cbj1_9rhob like domain; 1.
DR   InterPro; IPR045054; P4HA-like.
DR   InterPro; IPR006620; Pro_4_hyd_alph.
DR   PANTHER; PTHR10869:SF207; P4HA_N DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR10869; PROLYL 4-HYDROXYLASE ALPHA SUBUNIT; 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:UP000024635};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..281
FT                   /note="Prolyl 4-hydroxylase alpha subunit domain-containing
FT                   protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001492576"
FT   DOMAIN          100..277
FT                   /note="Prolyl 4-hydroxylase alpha subunit"
FT                   /evidence="ECO:0000259|SMART:SM00702"
FT   REGION          18..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        18..54
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   281 AA;  32370 MW;  84DEC23D666D646E CRC64;
     MKLLILVLVV VLLAEGAKKE DPKKSSKKTD TKKAADVKKK EAPKKKETKK SSFSFEGKDT
     WGPESLKKCY KAMPLPEDYF CYMYYRNYEP VYIDPLNTNP IIIIYRRFIP KKFVDDFLHD
     VKRKQKKMAE NKVEEDFMAQ YMKDNKRRIA NETIISHSAM SGVARVFRRA QALIPMLNFT
     NSGPWQVLSY KEGGHQSPHY DYITYSSPDQ YSKVTRTQGN RFVTFALTLK AADIGGETTF
     VHANHTVTLE AGDVLLFTNI NKDMTPVSRR FSAVPYEMSL E
//
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