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Database: UniProt
Entry: A0A0V1HBS3_9BILA
LinkDB: A0A0V1HBS3_9BILA
Original site: A0A0V1HBS3_9BILA 
ID   A0A0V1HBS3_9BILA        Unreviewed;       579 AA.
AC   A0A0V1HBS3;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   22-FEB-2023, entry version 18.
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:KRZ08254.1};
GN   ORFNames=T11_13323 {ECO:0000313|EMBL:KRZ08254.1};
OS   Trichinella zimbabwensis.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=268475 {ECO:0000313|EMBL:KRZ08254.1, ECO:0000313|Proteomes:UP000055024};
RN   [1] {ECO:0000313|EMBL:KRZ08254.1, ECO:0000313|Proteomes:UP000055024}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS1029 {ECO:0000313|EMBL:KRZ08254.1};
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:KRZ08254.1}.
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DR   EMBL; JYDP01000089; KRZ08254.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V1HBS3; -.
DR   STRING; 268475.A0A0V1HBS3; -.
DR   Proteomes; UP000055024; 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; 3.
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; PROLYL 4-HYDROXYLASE ALPHA SUBUNIT; 1.
DR   PANTHER; PTHR10869:SF207; PROLYL 4-HYDROXYLASE SUBUNIT ALPHA-2; 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   Coiled coil {ECO:0000256|SAM:Coils};
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:UP000055024};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..579
FT                   /note="procollagen-proline 4-dioxygenase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006879021"
FT   DOMAIN          456..562
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
FT   COILED          50..77
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   579 AA;  67159 MW;  D09BE178E918071E CRC64;
     MATLHFIIFI TLMDWWYAMR SSAEVFTAMA DVENLIHTED NVVDVIEQYI ESDLRRLQRL
     KSLAQEYRES KEKALKEGTD RLYNPVNAFL FIKKLTEEWN DVEQLMKSDH ADIYLQNITA
     MRDSSMAKFP TEEDLTGAAE ALLRLQDVYK LDTHELSSGR IKGAKQGLEL DANGCFELGR
     VAYNQKDYYH VILWMQEALN RVEHENPPSV DQAEILEYLA FGMYQQGNVK RALQLTKRLQ
     RIKPDHPRAE GNVKWYLDML AKEGVSRVTD HDLPPIVNAR PNDQALPERK DFEALCRGEY
     LLTEKQRSHL YCYYKRDTPF LILAPIKVEV MHWKPKIVIF RQVISANEIA VLKTLAYPRL
     SRATVQNSET GELETAKYRI SKRCRILRRA TVHNKETGQL EHASYRISKS AWLKEHEHPV
     VERIVKRIHD MTNLNMETAE DLQIANYGLG GHYDPHFDHA RIANYGIGGH YEPHFDMSTR
     DEVDPYEHGH GNRIATALFY KEEVNAFKSL NTGNRIATVL FYGDAAFWFN LKSNGEGDMS
     TRHAACPVLS GVKWVANKWI HERGQEFYRP CGLREDDYE
//
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