ID V5IHQ6_IXORI Unreviewed; 797 AA.
AC V5IHQ6;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Putative dimethylglycine dehydrogenase {ECO:0000313|EMBL:JAB79946.1};
OS Ixodes ricinus (Common tick) (Acarus ricinus).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Ixodinae; Ixodes.
OX NCBI_TaxID=34613 {ECO:0000313|EMBL:JAB79946.1};
RN [1] {ECO:0000313|EMBL:JAB79946.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Salivary gland and midgut {ECO:0000313|EMBL:JAB79946.1};
RX PubMed=25765539;
RA Kotsyfakis M., Schwarz A., Erhart J., Ribeiro J.M.;
RT "Tissue- and time-dependent transcription in Ixodes ricinus salivary glands
RT and midguts when blood feeding on the vertebrate host.";
RL Sci. Rep. 5:9103-9103(2015).
CC -!- SIMILARITY: Belongs to the GcvT family.
CC {ECO:0000256|ARBA:ARBA00008609}.
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DR EMBL; GANP01004522; JAB79946.1; -; mRNA.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 2.40.30.110; Aminomethyltransferase beta-barrel domains; 1.
DR Gene3D; 3.30.70.1400; Aminomethyltransferase beta-barrel domains; 1.
DR Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR032503; FAO_M.
DR InterPro; IPR006222; GCV_T_N.
DR InterPro; IPR029043; GcvT/YgfZ_C.
DR InterPro; IPR027266; TrmE/GcvT_dom1.
DR PANTHER; PTHR13847:SF193; PYRUVATE DEHYDROGENASE PHOSPHATASE REGULATORY SUBUNIT, MITOCHONDRIAL; 1.
DR PANTHER; PTHR13847; SARCOSINE DEHYDROGENASE-RELATED; 1.
DR Pfam; PF01266; DAO; 1.
DR Pfam; PF16350; FAO_M; 1.
DR Pfam; PF01571; GCV_T; 1.
DR SUPFAM; SSF101790; Aminomethyltransferase beta-barrel domain; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF103025; Folate-binding domain; 1.
PE 2: Evidence at transcript level;
FT DOMAIN 11..365
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 370..426
FT /note="FAD dependent oxidoreductase central"
FT /evidence="ECO:0000259|Pfam:PF16350"
FT DOMAIN 431..705
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
SQ SEQUENCE 797 AA; 89132 MW; 046A0B396FA5167D CRC64;
MSERVLPKLA RVVICGAGVV GNSIAYHLVK RGWTDLVVLE KGRIGCGATW RSSGLAGQLH
PTVNGIIARS SVKLYNSLQQ EGHDIGWQQC GTLSIARTRK RMVSLQRLAA EARARGVDCT
VHQPQSLKEL HPFLRTEDLA GGVFVPGDGV VDTEALCQTL AKLAQEGGAQ YVEECQVHRV
LSHEGTVVGA DTELGTINCE YFILAGGMWS RELAQASQPK FSVPIHAAKH SFGVTKPLDD
TDRSLPVVWD YDGRVYSRTF GRGFLVGGFE ETAKPLFHYD VPDKFEFLRL APDYPQFKGI
YEQFQHRFPD LRHLELAELV TAPETFTPDN HCILGETSEV EGLFLAVGMN GAQAQSAGGV
GRALALWLCD GAPRAYLLPC DCRRFLDLHN NAKFLRERVT EAVGRTCLEP HPLQAEFRTG
RRLRCSPLLP LQEQQGAVLG ERMGFERALF FDTQHESGER QLSASPTYGQ PDWLELVHQE
YVACRERVGI SDMSSFTKFY LESGGLEVVS LLQMLCSNEV DVPVGHIVQT GMQNDRGGYE
NDCSLIRLEK NRYLIIAPTK QQMRCQTWIR RHVAPDSPIV VADVTSMYTA ICIMGQWAPD
LMAELTDSPL GAKDFPLFTW KELDIGLASG IKVCHMTHTG DRGWVLYIPN EYALHVYDRI
LQVGLKYGIQ HAGYFAMKTL RIEKFFAXXX GKDLDCTTTP FECGRAFRVK FDKDFVGREA
LLRQKEQGVR RRYVQLLLQD HDPDCDPWPW GREPILWEDR CVGFTSSTCY GFTLGGQVCL
GFCGEQGREG RAPDSHQ
//
