ID V8P4X0_OPHHA Unreviewed; 377 AA.
AC V8P4X0;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Ubiquitin-conjugating enzyme E2 variant 3 {ECO:0000313|EMBL:ETE69609.1};
DE Flags: Fragment;
GN Name=UEVLD {ECO:0000313|EMBL:ETE69609.1};
GN ORFNames=L345_04583 {ECO:0000313|EMBL:ETE69609.1};
OS Ophiophagus hannah (King cobra) (Naja hannah).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Ophiophagus.
OX NCBI_TaxID=8665 {ECO:0000313|EMBL:ETE69609.1, ECO:0000313|Proteomes:UP000018936};
RN [1] {ECO:0000313|EMBL:ETE69609.1, ECO:0000313|Proteomes:UP000018936}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Blood {ECO:0000313|EMBL:ETE69609.1};
RX PubMed=24297900; DOI=10.1073/pnas.1314702110;
RA Vonk F.J., Casewell N.R., Henkel C.V., Heimberg A.M., Jansen H.J.,
RA McCleary R.J., Kerkkamp H.M., Vos R.A., Guerreiro I., Calvete J.J.,
RA Wuster W., Woods A.E., Logan J.M., Harrison R.A., Castoe T.A.,
RA de Koning A.P., Pollock D.D., Yandell M., Calderon D., Renjifo C.,
RA Currier R.B., Salgado D., Pla D., Sanz L., Hyder A.S., Ribeiro J.M.,
RA Arntzen J.W., van den Thillart G.E., Boetzer M., Pirovano W., Dirks R.P.,
RA Spaink H.P., Duboule D., McGlinn E., Kini R.M., Richardson M.K.;
RT "The king cobra genome reveals dynamic gene evolution and adaptation in the
RT snake venom system.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:20651-20656(2013).
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily.
CC {ECO:0000256|RuleBase:RU003369}.
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:ETE69609.1}.
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DR EMBL; AZIM01000731; ETE69609.1; -; Genomic_DNA.
DR AlphaFoldDB; V8P4X0; -.
DR Proteomes; UP000018936; Unassembled WGS sequence.
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:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR GO; GO:0015031; P:protein transport; IEA:InterPro.
DR Gene3D; 3.90.110.10; Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1.
DR InterPro; IPR001557; L-lactate/malate_DH.
DR InterPro; IPR022383; Lactate/malate_DH_C.
DR InterPro; IPR001236; Lactate/malate_DH_N.
DR InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR InterPro; IPR008883; UEV_N.
DR PANTHER; PTHR43128; L-2-HYDROXYCARBOXYLATE DEHYDROGENASE (NAD(P)(+)); 1.
DR PANTHER; PTHR43128:SF32; UBIQUITIN-CONJUGATING ENZYME E2 VARIANT 3; 1.
DR Pfam; PF02866; Ldh_1_C; 1.
DR Pfam; PF00056; Ldh_1_N; 1.
DR Pfam; PF05743; UEV; 1.
DR PRINTS; PR00086; LLDHDRGNASE.
DR SUPFAM; SSF56327; LDH C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF54495; UBC-like; 1.
DR PROSITE; PS51322; UEV; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003369};
KW Reference proteome {ECO:0000313|Proteomes:UP000018936}.
FT DOMAIN 1..51
FT /note="UEV"
FT /evidence="ECO:0000259|PROSITE:PS51322"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ETE69609.1"
SQ SEQUENCE 377 AA; 41349 MW; C5FA46813D8DA83A CRC64;
MGISVGKHVD VRGRIYLPYL QAWSHPQSVI IGLLQEMSIK FEEELPLYAL SSSDEARQMD
LLSYITKIVE GENNGQSKGE EKKNDGGLRK VTIIGAGDLG LACILAISAK DVADKVVVLD
CSEATVKGGT MDLEIFDLPK VEISRADSKL VVLTVNSLGN AQSYLEVVQS NVELFRGIIP
SIAHYSQHSV LLIASQPVEI MTYVSWKLSG FPKSRVIGIG CNLDSARFQY VIRNLLKAQS
RSKDNWIIGE QGVNKVAAWS SNSVINHPGD KLTNDQQVLT NRAMEILKGK GQRSWSVGLS
IADLTDTILN DKRKIHSVST TVKGYYNINS EVFLSMPCVL GISGVIEMMK PVEEDNVVEK
LQTSAASVND LQQQLKL
//
