ID A0A0V1KXA6_9BILA Unreviewed; 1195 AA.
AC A0A0V1KXA6;
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:KRZ51952.1};
GN ORFNames=T02_15543 {ECO:0000313|EMBL:KRZ51952.1};
OS Trichinella nativa.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6335 {ECO:0000313|EMBL:KRZ51952.1, ECO:0000313|Proteomes:UP000054721};
RN [1] {ECO:0000313|EMBL:KRZ51952.1, ECO:0000313|Proteomes:UP000054721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS10 {ECO:0000313|EMBL:KRZ51952.1};
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:KRZ51952.1}.
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DR EMBL; JYDW01000208; KRZ51952.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1KXA6; -.
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; 6.
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 444..573
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT DOMAIN 1049..1178
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 643..670
FT /evidence="ECO:0000256|SAM:Coils"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRZ51952.1"
FT NON_TER 1195
FT /evidence="ECO:0000313|EMBL:KRZ51952.1"
SQ SEQUENCE 1195 AA; 137358 MW; 80D8E0DF68578923 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 PLLKRATVHN ADTGQLETAS YRISKSAWLK
DTEHEVVKRI SDRIDMMTDL TMETAELLQI ANYGIGGHYD PHFDMSTRGE SDPYEEGTGN
RIATVLFYTN DPYSFESLNA GNRIATVLFY ISQPEAGGGT VFTSHKITVE PSKYDAAFWF
NVLQGGEPDM STRHAACPVL AGTKWVANKW IHERGQEFRR PFFSPGCLLK TPTMALLHII
IFITLMDWWC VMRSSAEVFT AMADVENLIH TEDNVVDVIE QYIESDLRRL QRLKSLAQEY
RESKEKALKE GADRLYNPVN AFLFIKKLTE EWNDVELLMK SDHADIYLQN ITAMRDSSLA
KFPTEEDLTG AAEALLRLQD VYKLDTHELS SGRIKGAKQG LELDANGCFE LGRVAYNQKD
YYHVILWMQE ALNRVEHENP PSVDQAEILE YLAYGMYQQG NVKRALQLTK RLQRIKPDHP
RAEGNVKWYL DLLAKEGVSR VTDHDLPPIV NARPNDQALP ERKDFEALCR GEYLLTEKQR
SRLYCYYKRD TPFLNLAPIK VEVMHWKPKI VIFRQVISAN EIAVLKTLAY PRLSRATVQN
SETGELETAK YRISKRCRTL RRATVHNKET GQLEHASYRI SKSAWLKEHE HPVVDRIVKR
IHDMTNLNME TAEDLQIANY GLGGHYDPHF DHARIANYGI GGHYEPHFDM STRDEVDPYE
HGHGNRIATT LFYKEEVNAF KSLNTGNRIA TVLFYISQPE AGGATVFITH KLAIFPVEGD
AAFWFNLKPN GEGDMSTRHA ACPVLAGVKW VANKWIHERG QEFYRPCGLR EDDYE
//
