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Database: UniProt
Entry: A0A2T4A3J8_TRIHA
LinkDB: A0A2T4A3J8_TRIHA
Original site: A0A2T4A3J8_TRIHA 
ID   A0A2T4A3J8_TRIHA        Unreviewed;       724 AA.
AC   A0A2T4A3J8;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   03-MAY-2023, entry version 13.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:PTB51631.1};
GN   ORFNames=M431DRAFT_484607 {ECO:0000313|EMBL:PTB51631.1};
OS   Trichoderma harzianum CBS 226.95.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=983964 {ECO:0000313|EMBL:PTB51631.1, ECO:0000313|Proteomes:UP000241690};
RN   [1] {ECO:0000313|EMBL:PTB51631.1, ECO:0000313|Proteomes:UP000241690}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 226.95 {ECO:0000313|EMBL:PTB51631.1,
RC   ECO:0000313|Proteomes:UP000241690};
RG   DOE Joint Genome Institute;
RA   Aerts A., Atanasova L., Chenthamara K., Zhang J., Grujic M., Henrissat B.,
RA   Kuo A., Salamov A., Lipzen A., Labutti K., Barry K., Miao Y., Rahimi M.J.,
RA   Shen Q., Grigoriev I.V., Kubicek C.P., Druzhinina I.S.;
RT   "Multiple horizontal gene transfer events from other fungi enriched the
RT   ability of initially mycotrophic Trichoderma (Ascomycota) to feed on dead
RT   plant biomass.";
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR   EMBL; KZ679685; PTB51631.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T4A3J8; -.
DR   STRING; 983964.A0A2T4A3J8; -.
DR   OrthoDB; 1459320at2759; -.
DR   Proteomes; UP000241690; 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; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   InterPro; IPR011761; ATP-grasp.
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; 1.
DR   SMART; SM00878; Biotin_carb_C; 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:UP000241690}.
FT   DOMAIN          32..485
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          148..348
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          640..715
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   724 AA;  79223 MW;  C3CD78B3A2747643 CRC64;
     MRSLRANRLS LRPVPRFLST SSASSTLPKP AALSSVLIAN RGEIAIRINK TAERMGIKAT
     TVYTDVDANS WHASSGFQSF GLGPANGYLD GEKIIALAKK HGIQALHPGY GFLSENYKFV
     ERCEEEGIVF VGPPATAMAD MGNKARSKEI MNAANVPCVP GYHGSEQGEA ELLAYAKEIT
     FPVLLKSVRG GGGKGMRIVM KEDEFLTQLK SARAEAKASF GDGGEVMLVE KYIVRPRHVE
     VQVFADKHGN TVALGERDCS VQRRHQKVLE ESPAPDLDEV TRQDLWDKAR KAAEAVGYVG
     AGTVEFILDK DSGKFYFMEM NTRLQVEHPV TEMVTGLDLV EWQFRIAAGE KLPLTQAEVE
     EQMNQRGAAI EARIYAENPE KGFMPDSGKL VHAVLLDAAK NDPDIRLDWG FGSGSVVSEA
     YDGMIAKLIV RGDDRETAIA KLASALRNFE IVGLSTNVEF LKRMCESEAF IAGDVETGFI
     DKWREELFKP RRINNEVFAQ AALGVLSNQL QNIGSSPHGQ SLGFGNTNST SERKLAFKVL
     DGYSEKEGEI VEAAVSQTGH NLYSVTISRK GEEPQLFSNI ISEPTIEGEV TKLKSRFPAE
     RIESTVVPQE NGTETKLAIF QHGLKTDLAL LPPSWYEKAL GLKELTASVA APMPCKILKN
     EVTEGQTVKK GEPLVVIESM KMETVIRSPQ DGVIKKLAHK EGDICKAGTV LVLFEEDASK
     EESS
//
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