ID A0A0V0VM01_9BILA Unreviewed; 1165 AA.
AC A0A0V0VM01;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
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:KRX64373.1};
GN ORFNames=T09_5176 {ECO:0000313|EMBL:KRX64373.1};
OS Trichinella sp. T9.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX64373.1, ECO:0000313|Proteomes:UP000054681};
RN [1] {ECO:0000313|EMBL:KRX64373.1, ECO:0000313|Proteomes:UP000054681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS409 {ECO:0000313|EMBL:KRX64373.1};
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:KRX64373.1}.
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DR EMBL; JYDN01000024; KRX64373.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0VM01; -.
DR Proteomes; UP000054681; 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; 4.
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:UP000054681};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 79..100
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 494..623
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT DOMAIN 1042..1148
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT REGION 343..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 654..681
FT /evidence="ECO:0000256|SAM:Coils"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRX64373.1"
FT NON_TER 1165
FT /evidence="ECO:0000313|EMBL:KRX64373.1"
SQ SEQUENCE 1165 AA; 134260 MW; 5CA2B81E902ACE27 CRC64;
HDRIAYVRCK QNGWLRAKSS STNRKHLGQT DKQARNLSGL IAPQTITFSS PQQQITKRFQ
QFSSATTKIR KYFKKKNTIM LNMIWPLTTA TLLLGAITPF SRGEVFTSMA NIDMLLQMGE
DVSRIIDNYV EEDERRLEQL KKLSAEYKSH KVQVHGQEST DSVIVNPVES FAIVKQLADN
WRYVEQLMKT NSAEKLIQNF THHTHNSVVR PPSEEDVIGM AVGLMRIQDV YKLDTHDMAE
GKIRGVLDGR KLTAYDCLEI ARVAYNKQDF YHTLLWATEA WDRVQKEDKP TIDEATVLEY
IAFAMFKQGN IEWAIHYTTL IKQVDPNHPR ASGNLKYYQD LLDPEGKPRK IDPKKLPPPT
NRRPDDLSIP ERDVYEGLCR SEYPIPDKDR AKLYCYYKRN RPYLKLAPIK VEVMHWKPKI
VYFRGVISDE EIAVIKQLAS PLLKRATVHN ADTGQLETAS YRISKSAWLK DTEHEVVKRI
SDRIDMMTDL TMETAELLQI ANYGIGGHYD PHFDMSTRGE SDPYEEGTGN RIATVLFYTN
DPYSFESLNA GNRIATVLFY ISQPEAGGGT VFTSHKITVE PSKYDAAFWF NVLQGGEPDM
STRHAACPVL AGTKWVANKW IHERGQEFRR PSMADVENLI HTEDNVVDVI EQYIESDLRR
LQRLKSLAQE YRESKEKALK EGADRLYNPV NAFLFIKKLT EEWNDVELLM KSDHADIYLQ
NITAMRDSSL AKFPTEEDLT GAAEALLRLQ DVYKLDTHEL SSGRIKGAKQ GLELDANGCF
ELGRVAYNQK DYYHVILWMQ EALNRVEHEN PPSVDQAEIL EYLAYGMYQQ GNVKRALQLT
KRLQRIKPDH PRAEGNVKWY LDLLAKEGVS RVTDHDLPPI VNARPNDQAL PERKDFEALC
RGEYLLTEKQ RSRLYCYYKR DTPFLNLAPI KVEVMHWKPK IVIFRQVISA NEIAVLKTLA
YPRLSRATVQ NSETGELETA KYRISKRCRT LRRATVHNKE TGQLEHASYR ISKSAWLKEH
EHPVVDRIVK RIHDMTNLNM ETAEDLQIAN YGLGGHYDPH FDHARRDEVD PYEHGHGNRI
ATTLFYKEEV NAFKSLNTGN RIATVLFYGD AAFWFNLKPN GEGDMSTRHA ACPVLAGVKW
VANKWIHERG QEFYRPCGLR EDDYE
//
