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Database: UniProt
Entry: A0A0D8XI47_DICVI
LinkDB: A0A0D8XI47_DICVI
Original site: A0A0D8XI47_DICVI 
ID   A0A0D8XI47_DICVI        Unreviewed;       416 AA.
AC   A0A0D8XI47;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Aminotransferase, class III {ECO:0000313|EMBL:KJH43407.1};
GN   ORFNames=DICVIV_10584 {ECO:0000313|EMBL:KJH43407.1};
OS   Dictyocaulus viviparus (Bovine lungworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Metastrongylidae; Dictyocaulus.
OX   NCBI_TaxID=29172 {ECO:0000313|EMBL:KJH43407.1, ECO:0000313|Proteomes:UP000053766};
RN   [1] {ECO:0000313|EMBL:KJH43407.1, ECO:0000313|Proteomes:UP000053766}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HannoverDv2000 {ECO:0000313|EMBL:KJH43407.1,
RC   ECO:0000313|Proteomes:UP000053766};
RA   Mitreva M.;
RT   "Draft genome of the bovine lungworm Dictyocaulus viviparus.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000053766}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HannoverDv2000 {ECO:0000313|Proteomes:UP000053766};
RX   PubMed=26856411; DOI=10.1038/srep20316;
RA   McNulty S.N., Strube C., Rosa B.A., Martin J.C., Tyagi R., Choi Y.J.,
RA   Wang Q., Hallsworth Pepin K., Zhang X., Ozersky P., Wilson R.K.,
RA   Sternberg P.W., Gasser R.B., Mitreva M.;
RT   "Dictyocaulus viviparus genome, variome and transcriptome elucidate
RT   lungworm biology and support future intervention.";
RL   Sci. Rep. 6:20316-20316(2016).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC       ECO:0000256|RuleBase:RU003560}.
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DR   EMBL; KN716562; KJH43407.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D8XI47; -.
DR   STRING; 29172.A0A0D8XI47; -.
DR   Proteomes; UP000053766; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   CDD; cd00610; OAT_like; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR049704; Aminotrans_3_PPA_site.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR45688; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR45688:SF3; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:KJH43407.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053766};
KW   Transferase {ECO:0000313|EMBL:KJH43407.1}.
SQ   SEQUENCE   416 AA;  46274 MW;  D4958A6218406898 CRC64;
     MVSKASMQYL YDEKGMQYLD CISNVQHVGH CHPQVVETIS RQLATSTCNV RFVSQKLTDC
     AESLLQTLPG LDTVLFCNSG SEANDLALRL ARDYTKHTDA IVLNHAYHGH VTTTMQLSPY
     KFDHGSTITK PEWVHVAPTP DVYRGDYRLA DDELIDTEKL EKAGIYYAET VTNIIEQAEK
     NGRTIAAYFA EALQSCGGQV IPPPGYFTEV ARSVRRHGGL VVIDEVQTGF GRVGKKFWAY
     QLYDDGFCPD IVTMGKPMGN GFPVSAVVTT RKIANALGGS VGYFNTYGGN PVACAAVLGV
     MRVIREEKLL NHSEMMGEEF KKQLNQLKKK YKCIGDIRGV GLFWGIDLVK DRETREPDQK
     LALSLILKLR RERGILLNAD GPFTNILKIK PPLCFNMQNL IDTINALDRT LAELGQ
//
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