ID H3BD01_LATCH Unreviewed; 891 AA.
AC H3BD01;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSLACP00000019772.1};
GN Name=ACCS {ECO:0000313|Ensembl:ENSLACP00000019772.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000019772.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000019772.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00007441}.
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DR EMBL; AFYH01004920; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01004921; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01004922; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01004923; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01004924; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01004925; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01004926; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01004927; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H3BD01; -.
DR STRING; 7897.ENSLACP00000019772; -.
DR Ensembl; ENSLACT00000019910.1; ENSLACP00000019772.1; ENSLACG00000017384.1.
DR eggNOG; KOG0256; Eukaryota.
DR GeneTree; ENSGT00940000164760; -.
DR HOGENOM; CLU_313728_0_0_1; -.
DR InParanoid; H3BD01; -.
DR OMA; SYHHQFT; -.
DR TreeFam; TF354218; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR Bgee; ENSLACG00000017384; Expressed in muscle tissue and 5 other cell types or tissues.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR GO; GO:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
DR GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
DR CDD; cd00609; AAT_like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR044822; Myb_DNA-bind_4.
DR InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR43795:SF17; 1-AMINOCYCLOPROPANE-1-CARBOXYLATE SYNTHASE-LIKE PROTEIN 1; 1.
DR PANTHER; PTHR43795; BIFUNCTIONAL ASPARTATE AMINOTRANSFERASE AND GLUTAMATE/ASPARTATE-PREPHENATE AMINOTRANSFERASE-RELATED; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR Pfam; PF13837; Myb_DNA-bind_4; 1.
DR PRINTS; PR00753; ACCSYNTHASE.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000008672}.
FT DOMAIN 12..99
FT /note="Myb/SANT-like DNA-binding"
FT /evidence="ECO:0000259|Pfam:PF13837"
FT DOMAIN 420..790
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
FT REGION 159..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..199
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..238
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 891 AA; 101824 MW; BF5B9703D65B09B4 CRC64;
MDFRGKKYER GSNWSDPEVV ELLQLWADES VQIELESCLR NQHVFNRIAE VLREKGIHRT
GDQCREKIKK MKLEYRRIKD NQKTLRGGRT WKFFEVMDRV LTNRPSISYS ALGGTVIAQQ
VLQGSGVDGY HQHHHFVPSV HAFAHAHHPE LMEIKCEEVE SDEPCITPEP PPSMTYQPGS
LEEHELDRSL LERGHNESPV PRADMPVEPS ISPSAYSEQN VAASSSRVQS QTPRPGLSSL
QRLRKKRKAQ RLKDPLDDIL LKFLTSQRAV EERFLQMEER RMQRDTEMEE RRMELEQRRM
ELEREHEFRM FAIFAQMLSA LKPGSGGGGQ SPGLDFSQAY SQFADLGGVA TGSTTGGQDN
KVLQSKAALH KLLCTFDKPN GNPYLSQRGN DIMNFTGTLE EGFAAYTVDK HDEDKNPNGI
INLGTSENKL CFDLLSKRLT QNDMYQIDPP LLQYPDWKGH MFLREEVARF LTYYCKAPTP
LKPENVVVVN GCGSLFSALA TVLCDPGVDA ILIPTPFYGV IASDVFHYSK AKLVFAHLES
QVTGSDSRPF QLTVEKLERA LQEAKFESFV MRGGTLIDPP FPISRWYNPP PPCFQVVQFT
HFNFRHELHV IVDEVYMLSV FDETATFQSV LSFDELPDPQ RTHVMWGISK DFAASGIRVG
TLYLENQDVL RALGRLAYFH GVPGPMQYKV AQLLRDRDWI NQVFLQTNRA RLKQAHKYVT
NELTALGIPY LNRSAGLYVW ADFRKCLKRN TFEEELKLWR RFLENKVLLS CGKGFECQEP
GWFRLIFADK TYRLQLGMQR LGKVLQELVQ ELQLEEQKQG SQSGAEGVEE KMQVTAVQQD
VAGAGLDGLI GLLRQQIRSS DWLQKNTVEQ FAQENPEVYD VFSKLAEKQK K
//
