ID   A0A0V1MJ14_9BILA        Unreviewed;      1496 AA.
AC   A0A0V1MJ14;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=NADP-retinol dehydrogenase {ECO:0000256|ARBA:ARBA00012852};
DE            EC=1.1.1.300 {ECO:0000256|ARBA:ARBA00012852};
GN   Name=Erc2 {ECO:0000313|EMBL:KRZ71741.1};
GN   ORFNames=T10_9490 {ECO:0000313|EMBL:KRZ71741.1};
OS   Trichinella papuae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=268474 {ECO:0000313|EMBL:KRZ71741.1, ECO:0000313|Proteomes:UP000054843};
RN   [1] {ECO:0000313|EMBL:KRZ71741.1, ECO:0000313|Proteomes:UP000054843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS1980 {ECO:0000313|EMBL:KRZ71741.1};
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=all-trans-retinol + NADP(+) = all-trans-retinal + H(+) +
CC         NADPH; Xref=Rhea:RHEA:25033, ChEBI:CHEBI:15378, ChEBI:CHEBI:17336,
CC         ChEBI:CHEBI:17898, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         EC=1.1.1.300; Evidence={ECO:0000256|ARBA:ARBA00000975};
CC   -!- PATHWAY: Cofactor metabolism; retinol metabolism.
CC       {ECO:0000256|ARBA:ARBA00004891}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000256|ARBA:ARBA00006484}.
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:KRZ71741.1}.
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DR   EMBL; JYDO01000090; KRZ71741.1; -; Genomic_DNA.
DR   Proteomes; UP000054843; Unassembled WGS sequence.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.120.650; Cupin; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR041667; Cupin_8.
DR   InterPro; IPR019323; ELKS/CAST.
DR   InterPro; IPR003347; JmjC_dom.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR002347; SDR_fam.
DR   PANTHER; PTHR24322; PKSB; 1.
DR   PANTHER; PTHR24322:SF736; RETINOL DEHYDROGENASE 10; 1.
DR   Pfam; PF00106; adh_short; 1.
DR   Pfam; PF10174; Cast; 2.
DR   Pfam; PF13621; Cupin_8; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   SMART; SM00558; JmjC; 1.
DR   SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS51184; JMJC; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Methyltransferase {ECO:0000313|EMBL:KRZ71741.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054843};
KW   Transferase {ECO:0000313|EMBL:KRZ71741.1}.
FT   DOMAIN          470..627
FT                   /note="JmjC"
FT                   /evidence="ECO:0000259|PROSITE:PS51184"
FT   REGION          1288..1310
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          921..1030
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1073..1114
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1159..1283
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1310..1469
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1288..1307
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1496 AA;  169237 MW;  2C03F5E6285E5579 CRC64;
     MILLVRIGLA LLQCCFGYTW SILECFFKKP KSVNDKVVVI TGAARGIGKG LALLLAHLHA
     KIVLVDLDES TNKQTAEELR HETSACVYAY TADVTDPESM RQVANAIVCN PELGCPDVLV
     CSAGVLIPKL LEDHSDVEIS RTMNTIRAFY PYILKRGQGH IVAVSSYGGH FGNSYSCCYS
     ASKFAVRGLM ESLEWEIYDH GFSGEIKTTT IYPFFTRTDL LNSCNVTSDV IPVLSPEETS
     QGILKAILYE QTEAFIPFYG SLICYFFKGR IFKALELEDF EAAVEICNFM LNTGHWSEVN
     ISWRLLYSMD ALCSCDKGLL LGCPISGNVL ARLANLLHCK MIDTYPLEDM LIDDKFDQAL
     ASMNDVCGQF EHCVPRVACP SLETFQRDFL IPQNPIVIEG ALESWQAMKK WNIAYLMSKC
     AYRTVPIEIG SKYTNDEWSQ KLLTIADFVH KYFNSNAREK AYLAQHQLFE QITELKDDIA
     VPDYCCLQCA PEDVDINAWF GPANTVSPLH TDPRDNLFAQ VFGKKYLRLC HPTATKNLYP
     ITDGLMSNTS QIDMENIDYE NFPLVKNVKF YETTVKPGDL LFIPKDTSIA CDVMSSAGSA
     VVQCSLASGL LPSPSNLYYQ SLGHITGGEG ISRNGSRTPV SQRRAGHFTR ARHHSSCDVH
     SLCDGVTFER SFDSQLPPAD PQIHAGGLKG GFPFSARSSN NFYRQPTLSS HLSHGNLGYL
     QPDCDWSSDL DPLVKGSRGA NEASGCGSGS KIVNGRMSTT TNCCPADCDA LREDLRVAME
     KLNATMGSIK SFWSPELKRE RALRKEETAK MNMLQEQLKL SLVNNQKQSV LIEQLQNELR
     FQCNSGRSRR FPDDGPLIGH EDYRTVCQER DMYRRDWLIS SEAVKELQYQ LESQRQLLLS
     KDESVKRLLE ALHSKGVPAS VAQSCAEMEL AQNRIVELEE KCSRLQAHCD DLESHLQQSH
     DGLSNLRKDA VIESLQDEVA SYEAELKRLR AGGAIHEREF TDKMVTDKEY QELKLKADKL
     ELELGQKTVE IQALYTRLST AEESASDFKK HLELMKESNA SKDQQATLLQ SDIDALRGKL
     ESKNEMIDQK AQQITELQAD KNRLLSELNL LNEQHRISEV GLSTKDRKID LLEETIRERD
     CELNLIRTRL NSSPGVIQEK KLQDEINRLV QERDLWRKRF NEEHECLAIE RKRDGEAHEK
     ENKDLRIAIA SLQKEISDRQ VFIESQNEKI NDMVRQTEAL TKENSLYKEL NKTNGVDLLK
     AEIARLNQAV DESRSEVDRL LKIIHTSEKE KNEGRESGND SKRFHSNAEN ADYQAVLMHK
     DRRIEELEEA LKESVSITAE REMAVAQQKL NSQRAEQRIA ACKDQLKTLQ EQYDELSLQL
     KQLRQEKAQS DATIEAMQEE RKRYVDERMQ LKGEALLAAI GEKDAHIALL ENCRGRKSSE
     EIDALQKQKE ELLQRLKEEN ARRVKLHSDP TLNFTDHFPK VSGVDLVDDD GDGIWA
//