ID A0A0V1A9K8_9BILA Unreviewed; 532 AA.
AC A0A0V1A9K8;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=carbonyl reductase (NADPH) {ECO:0000256|ARBA:ARBA00026118};
DE EC=1.1.1.184 {ECO:0000256|ARBA:ARBA00026118};
GN Name=RNF113A {ECO:0000313|EMBL:KRY21011.1};
GN ORFNames=T12_2860 {ECO:0000313|EMBL:KRY21011.1};
OS Trichinella patagoniensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=990121 {ECO:0000313|EMBL:KRY21011.1, ECO:0000313|Proteomes:UP000054783};
RN [1] {ECO:0000313|EMBL:KRY21011.1, ECO:0000313|Proteomes:UP000054783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS2496 {ECO:0000313|EMBL:KRY21011.1};
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:KRY21011.1}.
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DR EMBL; JYDQ01000020; KRY21011.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1A9K8; -.
DR STRING; 990121.A0A0V1A9K8; -.
DR Proteomes; UP000054783; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0033177; C:proton-transporting two-sector ATPase complex, proton-transporting domain; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0015078; F:proton transmembrane transporter activity; IEA:InterPro.
DR CDD; cd18177; ATP-synt_Vo_c_ATP6F_rpt1; 1.
DR CDD; cd18178; ATP-synt_Vo_c_ATP6F_rpt2; 1.
DR CDD; cd05324; carb_red_PTCR-like_SDR_c; 1.
DR Gene3D; 1.20.120.610; lithium bound rotor ring of v- atpase; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR002379; ATPase_proteolipid_c-like_dom.
DR InterPro; IPR045313; CBR1-like.
DR InterPro; IPR035921; F/V-ATP_Csub_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR PANTHER; PTHR43963:SF4; CARBONYL REDUCTASE (NADPH); 1.
DR PANTHER; PTHR43963; CARBONYL REDUCTASE 1-RELATED; 1.
DR Pfam; PF00106; adh_short; 2.
DR Pfam; PF00137; ATP-synt_C; 2.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF81333; F1F0 ATP synthase subunit C; 2.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000054783};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 328..352
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 372..394
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 415..435
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 462..490
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 497..522
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 376..435
FT /note="V-ATPase proteolipid subunit C-like"
FT /evidence="ECO:0000259|Pfam:PF00137"
FT DOMAIN 463..522
FT /note="V-ATPase proteolipid subunit C-like"
FT /evidence="ECO:0000259|Pfam:PF00137"
SQ SEQUENCE 532 AA; 57646 MW; DA1267F003ACC60A CRC64;
MDNKVALVTG ANKGIGYAIA KGLCKLFTGT VYLTARNEEL GKDAVVRIIA EVPKRACKEL
RFYQLDISDK DSVIRAKEYL MKEHGRIDIL INNAGIAFKC NSTVPFGEQA FETMKVNYWG
TKQVCEQFFP LLSPHARVVI VASQLGLLKK ISNEDLKKRL ESADLKMENL NSIVNHFVES
AKNNVHTDFG YPNSAYAMSK IAVIAMTKIL QREMDKDSRE DIVVNACCPG YVATDMSSHK
GTLTPDEGAE TPLYLALAVE NSISGGGMYY LKKQVDWRTA IFFNLLIFVI NIQNCCKELQ
FYRSTTVKSL LSFASYCSVI HYIVMGRVVA TASTVGGVAT AGITILGFYY LLTGKGHRVD
FGWFLSNTSP QLWSSLGIAF AISLSVLGAA WGIFLTGASI VGGGIKAPRI RTKNLVSIIF
CEAVAIYGII MAIVIGSKQQ PFDPENASFR VLSTNLAAGY EMFGAGLTVG FANLFCGICV
GIVGSGAALA DAQNPSLFVK ILIIEIFASA IGLFGVICGI LITNSAKMGN DI
//
