ID A0A556U109_BAGYA Unreviewed; 715 AA.
AC A0A556U109;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=Prolyl 4-hydroxylase subunit alpha-1 {ECO:0000256|ARBA:ARBA00040709};
DE EC=1.14.11.2 {ECO:0000256|ARBA:ARBA00012269};
DE AltName: Full=Procollagen-proline,2-oxoglutarate-4-dioxygenase subunit alpha-1 {ECO:0000256|ARBA:ARBA00042979};
GN ORFNames=Baya_7422 {ECO:0000313|EMBL:TSL75267.1};
OS Bagarius yarrelli (Goonch) (Bagrus yarrelli).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Sisoridae; Sisorinae; Bagarius.
OX NCBI_TaxID=175774 {ECO:0000313|EMBL:TSL75267.1, ECO:0000313|Proteomes:UP000319801};
RN [1] {ECO:0000313|EMBL:TSL75267.1, ECO:0000313|Proteomes:UP000319801}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JWS20170419001 {ECO:0000313|EMBL:TSL75267.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:TSL75267.1};
RX PubMed=31274158;
RA Jiang W., Lv Y., Cheng L., Yang K., Chao B., Wang X., Li Y., Pan X.,
RA You X., Zhang Y., Yang J., Li J., Zhang X., Liu S., Sun C., Yang J.,
RA Shi Q.;
RT "Whole-Genome Sequencing of the Giant Devil Catfish, Bagarius yarrelli.";
RL Genome Biol. Evol. 11:2071-2077(2019).
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:TSL75267.1}.
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DR EMBL; VCAZ01000036; TSL75267.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A556U109; -.
DR Proteomes; UP000319801; 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 CDD; cd06257; DnaJ; 1.
DR Gene3D; 6.10.140.1460; -; 1.
DR Gene3D; 1.10.287.110; DnaJ domain; 1.
DR Gene3D; 2.60.120.620; q2cbj1_9rhob like domain; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR018253; DnaJ_domain_CS.
DR InterPro; IPR036869; J_dom_sf.
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 InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR10869; PROLYL 4-HYDROXYLASE ALPHA SUBUNIT; 1.
DR PANTHER; PTHR10869:SF101; PROLYL 4-HYDROXYLASE SUBUNIT ALPHA-1; 1.
DR Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF08336; P4Ha_N; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SMART; SM00702; P4Hc; 1.
DR SUPFAM; SSF46565; Chaperone J-domain; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS00636; DNAJ_1; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
DR PROSITE; PS50005; TPR; 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:UP000319801};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339}.
FT DOMAIN 15..80
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
FT REPEAT 389..422
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 592..700
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT REGION 442..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 715 AA; 82762 MW; 38C4889E4468289B CRC64;
MGLLEQCVEL FNTSNLYEVL CVAKEASDAE LRRGYYKLSL QVHPDRAPED QQATLKFQVL
GKVYAVLSDR EQRSVYDEQG AVDEESESFN QDRDWEKHWR NLFPKGSEEE KEDLKRLYLL
HKGDMDRIME SAMCSSQDDE PRLRDILQQA VDHEEVPAFR LFTHESAKKK AARRRKMEAR
CVWCVFLISW LLHDCTAHND FYTSIGQMTD LLFMEKDLVT SLKDYIKAEE SKLEQVKNWV
EKMETVTSTA VHDPEGFLGH PVNAFKLMKR LNTEWGEVED LVLKDMSDGF ISNLTIHRQY
FPSDDDQTGA AKALLRLQDT YKLETQAIST GDLPGLPADL PYKSTLTVED CFELGKIAYS
EADYYHTELW MAQALRQLDE GEETSVDAVT VLDYLSYSVY QQGELERALE HTKRLLKLDP
DHQRANGNLK YFEYQLAKQR KVEKEQSGTE ERDKRELDSK KDFSTEKGKY EQLCRGEGIR
LTPRRQSRMF CRFYDNNRHP YYVLGPVKQE DEWDRPRIVR FHNIISEREM EKVKELAKPR
LRRATISNPV TGVLETAHYR ISKSAWLAAY EHPVVDRINQ RIQDITGLDV TTAEELQVAN
YGVGGQYEPH FDFGRKDEPD AFKELGTGNR IATWLFYMSD VAAGGATVFP EVGAAVKPMK
GTAVFWYNLF PSGEGDYSTR HAACPVLLGN KWVSNKWIHE RGQEFRRPCD LQNTD
//
