ID S7Q4T7_MYOBR Unreviewed; 471 AA.
AC S7Q4T7;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Ubiquitin-conjugating enzyme E2 variant 3 {ECO:0000313|EMBL:EPQ18378.1};
GN ORFNames=D623_10020588 {ECO:0000313|EMBL:EPQ18378.1};
OS Myotis brandtii (Brandt's bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=109478 {ECO:0000313|EMBL:EPQ18378.1, ECO:0000313|Proteomes:UP000052978};
RN [1] {ECO:0000313|Proteomes:UP000052978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23962925; DOI=10.1038/ncomms3212;
RA Seim I., Fang X., Xiong Z., Lobanov A.V., Huang Z., Ma S., Feng Y.,
RA Turanov A.A., Zhu Y., Lenz T.L., Gerashchenko M.V., Fan D., Hee Yim S.,
RA Yao X., Jordan D., Xiong Y., Ma Y., Lyapunov A.N., Chen G., Kulakova O.I.,
RA Sun Y., Lee S.G., Bronson R.T., Moskalev A.A., Sunyaev S.R., Zhang G.,
RA Krogh A., Wang J., Gladyshev V.N.;
RT "Genome analysis reveals insights into physiology and longevity of the
RT Brandt's bat Myotis brandtii.";
RL Nat. Commun. 4:2212-2212(2013).
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DR EMBL; KE164521; EPQ18378.1; -; Genomic_DNA.
DR RefSeq; XP_005883397.1; XM_005883335.2.
DR AlphaFoldDB; S7Q4T7; -.
DR GeneID; 102248610; -.
DR KEGG; myb:102248610; -.
DR CTD; 55293; -.
DR eggNOG; KOG1495; Eukaryota.
DR eggNOG; KOG2391; Eukaryota.
DR OrthoDB; 5344346at2759; -.
DR Proteomes; UP000052978; 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 CDD; cd05293; LDH_1; 1.
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 4: Predicted;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000052978}.
FT DOMAIN 2..145
FT /note="UEV"
FT /evidence="ECO:0000259|PROSITE:PS51322"
SQ SEQUENCE 471 AA; 52363 MW; 3FB1CC5B217C67BE CRC64;
MEFDCEGLRR LLGKYKFRDL TVEELKNVNM FFPHFRYSMD TYVFKDSSQK DLLNFTGTVP
VMYQGNTYNI PIRLWILDSH PFAPPICFLK PTANMGISVG KHVDAQGRIY LPYLQNWSHP
KSVVVGLIKE MIAKFQEELP LYSLSSSDEA RQVDLLAYIA KITEGISDIN SKNWTNHENK
AVKKITVVGG GELGVACTLA ISAKGIADRL VLLDLSEETK GGMMDLEIFN LPNVEISKDL
SASAHSKVVI FTVNSLGSSQ SYLDVVQRNV DMFRALVPAL GHYSQHSVLL VASQPVEIMT
YVTWKLSAFP ANRVIGIGCN LDSQRLQYII TNVLKAETSG KPVWVIGEQG EDKVTKWGGQ
EEVMSHNSQV QLSSRAMELL KVKGQRSWSV GLSVADLVDS LINDRKKVHS VSTLAKGYYD
INSEVFLSLP CILGTSGVSE VIKSTVQEDR VTEKLQSSAS SLCDLQQQLK L
//
