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Database: UniProt
Entry: A0A0V0WZV7_9BILA
LinkDB: A0A0V0WZV7_9BILA
Original site: A0A0V0WZV7_9BILA 
ID   A0A0V0WZV7_9BILA        Unreviewed;       574 AA.
AC   A0A0V0WZV7;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=procollagen-proline 4-dioxygenase {ECO:0000256|ARBA:ARBA00012269};
DE            EC=1.14.11.2 {ECO:0000256|ARBA:ARBA00012269};
GN   Name=phy-2 {ECO:0000313|EMBL:KRX81306.1};
GN   ORFNames=T06_14564 {ECO:0000313|EMBL:KRX81306.1};
OS   Trichinella sp. T6.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=92179 {ECO:0000313|EMBL:KRX81306.1, ECO:0000313|Proteomes:UP000054673};
RN   [1] {ECO:0000313|EMBL:KRX81306.1, ECO:0000313|Proteomes:UP000054673}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS34 {ECO:0000313|EMBL:KRX81306.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the post-translational formation of 4-
CC       hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other
CC       proteins. {ECO:0000256|ARBA:ARBA00002035}.
CC   -!- COFACTOR:
CC       Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC         Evidence={ECO:0000256|ARBA:ARBA00001961};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC       {ECO:0000256|ARBA:ARBA00004319}.
CC   -!- SIMILARITY: Belongs to the P4HA family.
CC       {ECO:0000256|ARBA:ARBA00006511}.
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:KRX81306.1}.
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DR   EMBL; JYDK01000032; KRX81304.1; -; Genomic_DNA.
DR   EMBL; JYDK01000032; KRX81306.1; -; Genomic_DNA.
DR   EMBL; JYDK01000032; KRX81307.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0WZV7; -.
DR   Proteomes; UP000054673; Unassembled WGS sequence.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0031418; F:L-ascorbic acid binding; IEA:InterPro.
DR   GO; GO:0004656; F:procollagen-proline 4-dioxygenase activity; IEA:UniProtKB-EC.
DR   Gene3D; 6.10.140.1460; -; 1.
DR   Gene3D; 2.60.120.620; q2cbj1_9rhob like domain; 2.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR   InterPro; IPR045054; P4HA-like.
DR   InterPro; IPR006620; Pro_4_hyd_alph.
DR   InterPro; IPR044862; Pro_4_hyd_alph_FE2OG_OXY.
DR   InterPro; IPR013547; Pro_4_hyd_alph_N.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   PANTHER; PTHR10869:SF207; P4HA_N DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR10869; PROLYL 4-HYDROXYLASE ALPHA SUBUNIT; 1.
DR   Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
DR   Pfam; PF08336; P4Ha_N; 1.
DR   SMART; SM00702; P4Hc; 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS51471; FE2OG_OXY; 1.
PE   3: Inferred from homology;
KW   Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054673};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..574
FT                   /note="procollagen-proline 4-dioxygenase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007437931"
FT   DOMAIN          415..544
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
FT   REGION          264..289
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   574 AA;  65623 MW;  8207A406A3ADE510 CRC64;
     MLNMIWPLTT ATLLLGAITP FSLGEVFTSM ANIDMLLQMG EDVSRIIDNY VEEDERRLEQ
     LKKLSAEYKS HKVQVHGQES TDSVIVNPVE SFAIVKQLAD NWRYVEQLMK TNSAEKLIQN
     FTHHTHNSVV RPPSEEDVIG MAVGLMRIQD VYKLDTHDMA EGKIRGVLDG RKLTAYDCLE
     IARVAYNKQD FYHTLLWATE AWDRVQKEDE PTIDEATVLE YIAFAMFKQG NIEWAIHYTT
     LIKQVDPNHP RASGNLKYYQ DLLDPEGKPR KIDPKKLPPP TNRRPDDLSI PERDVYEGLC
     RSEYPIPDKD RAKLYCYYKR NRPYLKLAPI KVEVMHWKPK IVYFRGVISD EEIAVIKQLA
     SPLLKRATVH NADTGQLETA SYRISKSAWL KDTEHEVVKR ISDRIDMMTD LTMETAELLQ
     IANYGIGGHY DPHFDMSTRG ESDPYEEGTG NRIATVLFYT NDPYSFESLN AGNRIATVLF
     YISQPEAGGG TVFTSHKITV EPSKYDAAFW FNVLQGGEPD MSTRHAACPV LAGTKWVANK
     WIHERGQEFR RPFFSPGCVT SARGCCLFDE LNNF
//
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