ID A0A0V1KX82_9BILA Unreviewed; 1192 AA.
AC A0A0V1KX82;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=procollagen-proline 4-dioxygenase {ECO:0000256|ARBA:ARBA00012269};
DE EC=1.14.11.2 {ECO:0000256|ARBA:ARBA00012269};
DE Flags: Fragment;
GN Name=phy-2 {ECO:0000313|EMBL:KRZ51951.1};
GN ORFNames=T02_15543 {ECO:0000313|EMBL:KRZ51951.1};
OS Trichinella nativa.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6335 {ECO:0000313|EMBL:KRZ51951.1, ECO:0000313|Proteomes:UP000054721};
RN [1] {ECO:0000313|EMBL:KRZ51951.1, ECO:0000313|Proteomes:UP000054721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS10 {ECO:0000313|EMBL:KRZ51951.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (MAY-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:KRZ51951.1}.
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DR EMBL; JYDW01000208; KRZ51951.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1KX82; -.
DR Proteomes; UP000054721; Unassembled WGS sequence.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; 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:0004656; F:procollagen-proline 4-dioxygenase activity; IEA:UniProtKB-EC.
DR Gene3D; 6.10.140.1460; -; 2.
DR Gene3D; 2.60.120.620; q2cbj1_9rhob like domain; 5.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
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; 2.
DR Pfam; PF08336; P4Ha_N; 2.
DR SMART; SM00702; P4Hc; 2.
DR SUPFAM; SSF48452; TPR-like; 2.
DR PROSITE; PS51471; FE2OG_OXY; 2.
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}; Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000054721};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 29..50
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 462..570
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT DOMAIN 1046..1175
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT REGION 293..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 640..667
FT /evidence="ECO:0000256|SAM:Coils"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRZ51951.1"
FT NON_TER 1192
FT /evidence="ECO:0000313|EMBL:KRZ51951.1"
SQ SEQUENCE 1192 AA; 137200 MW; 95F7D66C526B512D CRC64;
LKKSHTTNLI DIKNPLTHCL SNQLYRNTIM LNMIWPLTTA TLLLGAITPF SRGEVFTSMA
NIDMLLQMGE DVSRIIDNYV EEDERRLEQL KKLSAEYKSH KVQVHGQEST DSVIVNPVES
FAIVKQLADN WRYVEQLMKT NSAEKLIQNF THHTHNSVVR PPSEEDVIGM AVGLMRIQDV
YKLDTHDMAE GKIRGVLDGR KLTAYDCLEI ARVAYNKQDF YHTLLWATEA WDRVQKEDEP
TIDEATVLEY IAFAMFKQGN IEWAIHYTTL IKQVDPNHPR ASGNLKYYQD LLDPEGKPRK
IDPKKLPPPT NRRPDDLSIP ERDVYEGLCR SEYPIPDKDR AKLYCYYKRN RPYLKLAPIK
VEVMHWKPKI VYFRGVISDE EIAVIKQLAS PLFIKNQPKL FKNLNSIHFQ LKRATVHNAD
TGQLETASYR ISKSAWLKDT EHEVVKRISD RIDMMTDLTM ETAELLQIAN YGIGGHYDPH
FDMSTTNDPY SFESLNAGNR IATVLFYISQ PEAGGGTVFT SHKITVEPSK YDAAFWFNVL
QGGEPDMSTR HAACPVLAGT KWVANKWIHE RGQEFRRPFF SPGCLLKTPT MALLHIIIFI
TLMDWWCVMR SSAEVFTAMA DVENLIHTED NVVDVIEQYI ESDLRRLQRL KSLAQEYRES
KEKALKEGAD RLYNPVNAFL FIKKLTEEWN DVELLMKSDH ADIYLQNITA MRDSSLAKFP
TEEDLTGAAE ALLRLQDVYK LDTHELSSGR IKGAKQGLEL DANGCFELGR VAYNQKDYYH
VILWMQEALN RVEHENPPSV DQAEILEYLA YGMYQQGNVK RALQLTKRLQ RIKPDHPRAE
GNVKWYLDLL AKEGVSRVTD HDLPPIVNAR PNDQALPERK DFEALCRGEY LLTEKQRSRL
YCYYKRDTPF LNLAPIKVEV MHWKPKIVIF RQVISANEIA VLKTLAYPRL SRATVQNSET
GELETAKYRI SKRCRTLRRA TVHNKETGQL EHASYRISKS AWLKEHEHPV VDRIVKRIHD
MTNLNMETAE DLQIANYGLG GHYDPHFDHA RIANYGIGGH YEPHFDMSTR DEVDPYEHGH
GNRIATTLFY KEEVNAFKSL NTGNRIATVL FYISQPEAGG ATVFITHKLA IFPVEGDAAF
WFNLKPNGEG DMSTRHAACP VLAGVKWVAN KWIHERGQEF YRPCGLREDD YE
//
