ID A0A0V1NI09_9BILA Unreviewed; 741 AA.
AC A0A0V1NI09;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=Procollagen-lysine,2-oxoglutarate 5-dioxygenase {ECO:0000313|EMBL:KRZ83629.1};
DE Flags: Fragment;
GN Name=RDH12 {ECO:0000313|EMBL:KRZ83629.1};
GN ORFNames=T08_3686 {ECO:0000313|EMBL:KRZ83629.1};
OS Trichinella sp. T8.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92180 {ECO:0000313|EMBL:KRZ83629.1, ECO:0000313|Proteomes:UP000054924};
RN [1] {ECO:0000313|EMBL:KRZ83629.1, ECO:0000313|Proteomes:UP000054924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS272 {ECO:0000313|EMBL:KRZ83629.1};
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 -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000256|ARBA:ARBA00001961};
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:KRZ83629.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JYDM01000204; KRZ83629.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1NI09; -.
DR Proteomes; UP000054924; Unassembled WGS sequence.
DR GO; GO:0051213; F:dioxygenase activity; 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:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR InterPro; IPR029159; CA109-like.
DR InterPro; IPR006620; Pro_4_hyd_alph.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
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; PF15011; CA109-like; 1.
DR Pfam; PF00096; zf-C2H2; 2.
DR SMART; SM00702; P4Hc; 1.
DR SMART; SM00355; ZnF_C2H2; 3.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE 4: Predicted;
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964, ECO:0000313|EMBL:KRZ83629.1};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000054924};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT DOMAIN 593..620
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 621..648
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 701..728
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRZ83629.1"
SQ SEQUENCE 741 AA; 86849 MW; 604220C1DE9CA6B4 CRC64;
LFVLLMNIFD KVEPHAVKVE HFVNLMDGEY HFVQADSAIS LTERNARDRA VDICLESGCD
YLFVVDAEAR IDFPGTLKTL IEKNKSLIAP MMIRGEELWS NFWGALNDDG FYARSDDYIS
IAKRERLGLW NIPHFSTAYL IRKDRLSLLL SAYSYNGKND PDMSFTQFCR EKGFFMYVDN
TEKYGHIMVS DNYNPLNRFA DFYNIFQNRR EWEERYLDEK YWDTLNNDYE FELPCPDVYH
FPLFSKQFCK EMIAVMENYG RWSSGSNLDS RLAGGYENVP TRDIHMNQVD FERHWLNILD
EYIRPVQEKT FIGYYSKPPH AIMNFVVRYK PDEQPALRPH HDASTYTVDI ALNKAGEDFE
QMSRVGRDGN YPFEARRTFR QIRRLIELAK EMESDGLERI DFLGNLLMQR QSVEEVDLDG
SPLASLPEFQ TTLMAEIDME VTSVFANLME MVIHCQSVCA ELEKDLNTAN WHSENQVEKS
ARLATPFWPA VDQLQMWASE IVVMYSADLH RRKSDLDVLF VDTLTPLTKV TQLKQNWKQP
AWFEQKCNHI MACVHYLINA MIEDLDGPQE QLAHSDVITV KQEKLDTPDQ QNFKCRFCGL
VYNYLSTLKA HERVHDVEEP YVCAKCGLSF RFYSELQTHS EEHKGTYTYK CGCGRSFAKY
TDLLYHKHDS DDEDEPTEET VLAEKKPAYQ GKHYPDPRNA YYCQFCCRGY KTSHELKYHL
YSHRGERAFT VGSSRYLMNR M
//
