ID   A0A085NB86_9BILA        Unreviewed;      1379 AA.
AC   A0A085NB86;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=procollagen-lysine 5-dioxygenase {ECO:0000256|ARBA:ARBA00012264};
DE            EC=1.14.11.4 {ECO:0000256|ARBA:ARBA00012264};
GN   ORFNames=M514_21081 {ECO:0000313|EMBL:KFD66732.1};
OS   Trichuris suis (pig whipworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichuridae; Trichuris.
OX   NCBI_TaxID=68888 {ECO:0000313|EMBL:KFD66732.1};
RN   [1] {ECO:0000313|EMBL:KFD66732.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DCEP-RM93F {ECO:0000313|EMBL:KFD66732.1};
RX   PubMed=24929829; DOI=10.1038/ng.3012;
RA   Jex A.R., Nejsum P., Schwarz E.M., Hu L., Young N.D., Hall R.S.,
RA   Korhonen P.K., Liao S., Thamsborg S., Xia J., Xu P., Wang S.,
RA   Scheerlinck J.P., Hofmann A., Sternberg P.W., Wang J., Gasser R.B.;
RT   "Genome and transcriptome of the porcine whipworm Trichuris suis.";
RL   Nat. Genet. 46:701-706(2014).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + L-lysyl-[collagen] + O2 = (5R)-5-hydroxy-L-
CC         lysyl-[collagen] + CO2 + succinate; Xref=Rhea:RHEA:16569, Rhea:RHEA-
CC         COMP:12751, Rhea:RHEA-COMP:12752, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:29969,
CC         ChEBI:CHEBI:30031, ChEBI:CHEBI:133442; EC=1.14.11.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00024166};
CC   -!- COFACTOR:
CC       Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC         Evidence={ECO:0000256|ARBA:ARBA00001961};
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DR   EMBL; KL367521; KFD66732.1; -; Genomic_DNA.
DR   Proteomes; UP000030758; Unassembled WGS sequence.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
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:UniProtKB-KW.
DR   GO; GO:0008475; F:procollagen-lysine 5-dioxygenase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR044861; IPNS-like_FE2OG_OXY.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR   InterPro; IPR006620; Pro_4_hyd_alph.
DR   InterPro; IPR002347; SDR_fam.
DR   PANTHER; PTHR10730:SF45; PROCOLLAGEN-LYSINE,2-OXOGLUTARATE 5-DIOXYGENASE; 1.
DR   PANTHER; PTHR10730; PROCOLLAGEN-LYSINE,2-OXOGLUTARATE 5-DIOXYGENASE/GLYCOSYLTRANSFERASE 25 FAMILY MEMBER; 1.
DR   Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR   Pfam; PF00106; adh_short; 1.
DR   SMART; SM00702; P4Hc; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR   PROSITE; PS51471; FE2OG_OXY; 1.
PE   4: Predicted;
KW   Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
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   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Vitamin C {ECO:0000256|ARBA:ARBA00022896}.
FT   TRANSMEM        265..284
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        366..392
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1042..1148
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
SQ   SEQUENCE   1379 AA;  158499 MW;  944C622F56B3FEEC CRC64;
     MKASLWYWLS IFLLGEALKF VPLFRSYLIL RLLCWYVVSQ WIKRFVFKTC PFEVRFPDKE
     HVVIVTGASA GIGTATAADL CARGGKVIWA ARDTAKAQRK LNDLAWTAHH GKRGYIIKLD
     LASKKKIDQF VDEFKKREKN LHCLILNAAY WGPRRTTEDG FEQNFGVNHL GHMYLVYKLM
     DVLKASAPSR VVVVGSDIHR LYSGVNFDDL MMERNYSAWR AYGHSKLCTI LFGRELARRL
     EGTGITVSIA HPGTPVPSEL MRNSWAFWSI FHMFVLQPAF HLFCRTTMQG AQTTVYCACS
     EECGKVTGNY YESVVHSFGQ FLTHILFKKR EEGLSERGGT RRCCCQTPMG YFLRDAENQR
     KLDLNYFGYF LCWGYGAMCY FAAVLLALAF VADAEHLLVL TVATERTDGF LRTERSLLQF
     SLNYRVLGLG TKWNGGDVRR TVGGGQKIRL LREALDQYKH EQDLVILFID GYDVIVNGDE
     KLILERFLQT GAKVLFSAEG FCWPDKSLAV SYPVVKRGKR YLNSGAFIGY ASYIRKLLSE
     GQVKDDGDDQ LFYTLVFLND KLREKYEIKL DSTAELFQNL NGAVDDVDLD LSPDPQSDPR
     RGVRLANLAY SSEPLIVHGN GPSKVGFDRF FEECQLDFSK QIHLNMLGNY LGNWWNPSIG
     CIACEEDELQ LDQDEEKWPF VVLASFITKP SPFVDLYFEN LLSLSYPKSR MGIYLYNGVE
     NYTQIVADFR QEALKSFAFV ESPSITSGDE RFAFVKISTG SAADERQARD NAVQWCQERN
     CDYLLVWDAN ARLERPDTLQ LLIKRNKPVV APLLHTEGRL WSNFWGAISD NGFYSRSDDY
     VAIVERQRLG IWNVPYVTLL YLVRKERLSK MVNPYSYNMN ADADMSFCQY CREKDYFMYV
     DNTVEYGHSV DDYGYDSTNS SSDLGNLLRN KKEWERKYLH KDYTNVLEDD YVLGMACPDV
     YSFPIFSLAF CKDLIDTMEA YGKWSSGSHQ DSRLLGGYEN VPTRDIHMNQ VGLEPVWLKI
     LDDYVRPVQE KAFTGYYSRP PKALMNFVVR YKPEEQASLR PHHDASTYTV DVALNKAGVD
     YEGGGVRYVR YNCTARDLEP GWALMHPGRL THMHEVKVNH RMDGLHMRIG VYDCLPMLRW
     SYCYLQVPLA FVIGFRVDKK MSAEQWTESK FIRTTKQAFL HARQLLDALS KIENSHLETI
     DSIINQLMQK SCVEKADLSQ SQLRTIVGEH VSTFLLAKID KQVTNLCIAI KQDLEGCQQL
     ADATKGYYGR LVEGYSVVGE DDRLHERLKR RTPKRPSILE MCSWLDDVLT TCRQELKDRQ
     ELLARLALVR TEEAIEMLKH AKYCWKRPPS VVQRMNTHIA FTWHFVGEQN DQLQSALDE
//