ID A0A1J8QYQ1_9AGAM Unreviewed; 830 AA.
AC A0A1J8QYQ1;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 22-FEB-2023, entry version 21.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OJA14602.1};
GN ORFNames=AZE42_09812 {ECO:0000313|EMBL:OJA14602.1};
OS Rhizopogon vesiculosus.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Suillineae; Rhizopogonaceae; Rhizopogon.
OX NCBI_TaxID=180088 {ECO:0000313|EMBL:OJA14602.1, ECO:0000313|Proteomes:UP000183567};
RN [1] {ECO:0000313|EMBL:OJA14602.1, ECO:0000313|Proteomes:UP000183567}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AM-OR11-056 {ECO:0000313|EMBL:OJA14602.1,
RC ECO:0000313|Proteomes:UP000183567};
RA Mujic A.B., Kuo A., Tritt A., Lipzen A., Chen C., Johnson J., Sharma A.,
RA Barry K., Grigoriev I.V., Spatafora J.W.;
RT "Comparative genomics of the ectomycorrhizal sister species Rhizopogon
RT vinicolor and Rhizopogon vesiculosus (Basidiomycota: Boletales) reveals a
RT divergence of the mating type B locus.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OJA14602.1}.
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DR EMBL; LVVM01003563; OJA14602.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J8QYQ1; -.
DR STRING; 180088.A0A1J8QYQ1; -.
DR OrthoDB; 1459320at2759; -.
DR Proteomes; UP000183567; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR CDD; cd06850; biotinyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.30.700.40; -; 1.
DR Gene3D; 3.40.50.20; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR18866; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 1.
DR PANTHER; PTHR18866:SF33; METHYLCROTONOYL-COA CARBOXYLASE SUBUNIT ALPHA, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00289; Biotin_carb_N; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF02786; CPSase_L_D2; 2.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SMART; SM01209; GARS_A; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Biotin {ECO:0000256|ARBA:ARBA00023267};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000183567}.
FT DOMAIN 129..587
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 248..426
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 749..825
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 480..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 830 AA; 89332 MW; 7F8B472687BE7A6B CRC64;
MISAVRFIEV ARDLYAEGPK AYTRPGPEGV GLALSRPELT VTCRMIPTNR TAASSLLRSS
NHVHLIPRTS LTTAGVGSST NYARTLQTKA SAIGAMGQPR MLVQRSVARR GLATTVQNTL
TFSSERKPHF DKILIANRGE IACRVIRTAT KLGIKTVAVY SEVDATSLHV LEADEAYCIG
PAPSTESYLR MDKIIDVCHR SGAQAVHPGY GFLSENAKFA ERLAKEGIVF IGPPSSAIVS
MGSKSESKNI MSAAGVPCVP GYHGANQDAD LLFAEAEKTG YPVLIKAIHG GGGKGMRVVS
SPSQFKDALA SAQRESLKSF GDADVLVEKY IERPRHVEVQ VFADMLGNTA PAPGLSPELR
ADLSAKAVAA AKAVDYVGAG TVEFIFDNDT EKFYFMEMNT RLQVEHPVTE MITGLDLVEW
QLEVAAGNPL PLSQSQIPLV GHAFEARIYA ENPRNNFLPD SGPLLYLDTP KPTHVFAPPI
LSHSDSRSEV DPMRRSPDTS TNVAPSMRLE QGFTQGAQIG VFYDPMIAKL VVHGRDRTSA
LRVLRRALEE YKVVGVSTNV EFLRSLAGND AFVNGEVETG FIKKHYEDLF PPAESPSAEL
LAQAALFSAL REHPIQSTSL STPWATLTSR RFGGDVYERT ISIQPDDASA EPTQVSLKSI
SPGHFDITVH SATPKSFTGV SARLVSPTTL SMTLNGTSTD ITVVSQSPLP SLPPSRMTNT
MERLHVFSAS GVKTTLAIPP PTYILSLGKD VLAVSKGALR APMPSLVVEV KVSIGDRVEK
GQPVVVLESM KTETVLRAEV SGVVSAVGCV KGEMVEEGRE LIDIKNSEEE
//
