ID A0A2V1CDQ6_9HELO Unreviewed; 679 AA.
AC A0A2V1CDQ6;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Class II aaRS and biotin synthetase {ECO:0000313|EMBL:PVH83203.1};
GN ORFNames=DL98DRAFT_455525 {ECO:0000313|EMBL:PVH83203.1};
OS Cadophora sp. DSE1049.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Helotiales incertae sedis; Cadophora.
OX NCBI_TaxID=1485229 {ECO:0000313|EMBL:PVH83203.1, ECO:0000313|Proteomes:UP000244409};
RN [1] {ECO:0000313|EMBL:PVH83203.1, ECO:0000313|Proteomes:UP000244409}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSE1049 {ECO:0000313|EMBL:PVH83203.1,
RC ECO:0000313|Proteomes:UP000244409};
RX PubMed=29679020; DOI=10.1038/s41598-018-24686-4;
RA Knapp D.G., Nemeth J.B., Barry K., Hainaut M., Henrissat B., Johnson J.,
RA Kuo A., Lim J.H.P., Lipzen A., Nolan M., Ohm R.A., Tamas L.,
RA Grigoriev I.V., Spatafora J.W., Nagy L.G., Kovacs G.M.;
RT "Comparative genomics provides insights into the lifestyle and reveals
RT functional heterogeneity of dark septate endophytic fungi.";
RL Sci. Rep. 8:6321-6321(2018).
CC -!- SIMILARITY: Belongs to the biotin--protein ligase family.
CC {ECO:0000256|ARBA:ARBA00009934}.
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DR EMBL; KZ804129; PVH83203.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V1CDQ6; -.
DR STRING; 1485229.A0A2V1CDQ6; -.
DR Proteomes; UP000244409; Unassembled WGS sequence.
DR GO; GO:0004077; F:biotin-[acetyl-CoA-carboxylase] ligase activity; IEA:InterPro.
DR GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR CDD; cd16442; BPL; 1.
DR CDD; cd03144; GATase1_ScBLP_like; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR019197; Biotin-prot_ligase_N.
DR InterPro; IPR004408; Biotin_CoA_COase_ligase.
DR InterPro; IPR004143; BPL_LPL_catalytic.
DR InterPro; IPR029062; Class_I_gatase-like.
DR NCBIfam; TIGR00121; birA_ligase; 1.
DR PANTHER; PTHR12835; BIOTIN PROTEIN LIGASE; 1.
DR PANTHER; PTHR12835:SF5; BIOTIN--PROTEIN LIGASE; 1.
DR Pfam; PF03099; BPL_LplA_LipB; 1.
DR Pfam; PF09825; BPL_N; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
PE 3: Inferred from homology;
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Reference proteome {ECO:0000313|Proteomes:UP000244409}.
FT DOMAIN 397..598
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51733"
SQ SEQUENCE 679 AA; 74984 MW; 447CFD5889D8CE00 CRC64;
MATRKMNVLV YSGNGSTIES VRHCLYTLRR LLSPNYAVIP VTDNVILKEP WTASCALLVF
PGGADMGYCR SLNGEGNRRI EQFVRRGGSY LGFCAGGYYG SSKCEFEVGN RVLEVIGNRE
LAFFPGTCRG CAFKGFVYHS EAGAKAVEVK VEKESFKAGV VPQAFRSYYN GGGIFVDAKS
YGDKGVEILA SYSGDVDVEG GSAAVVYCKV GEGGAILTGP HPEFAAVNLD PKSNGPNYPK
LVDELAEDDD SRVNFLKACL AKFGLIVSQE TSSVPSLSRL HLSSMYHYLV PELLASWEDI
ITREDDEEYI KGENDTFHLE KQGSRWSLNQ LAKALPLPGV LKGQEPLADQ VDGASDDRIV
DYNAITKRLI PHETEWPGTK ETPYFNHHAF YANLKKYQEE RGGEAEEYGK YLMYGEVVTS
TNTLLEKNPK LLSTLPPGFT VTATTQVAGR GRGSNVWVSP AGCLIFSTTM KHPMELSNTA
PVVFIQYLAA IAIAEGIQSY DRGYQDVPVK LKWPNDIYAQ HPTKPGKKEY VKIGGILVNS
SYSSGNYDLV VGIGINTTNT APTTSLNALL GPNITPFTLE KLLARILTKF ETIYKGFCRT
GFDKKLEETY YKHWLHTDQI VTLEAEGGVR ARVKGITRDW GLLKAEELGW EDRPTGKIWE
LQSDSNSFDF FKGLLKRKT
//
