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Database: UniProt
Entry: K1VFZ8_TRIAC
LinkDB: K1VFZ8_TRIAC
Original site: K1VFZ8_TRIAC 
ID   K1VFZ8_TRIAC            Unreviewed;       672 AA.
AC   K1VFZ8;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=CoA-binding domain-containing protein {ECO:0000259|SMART:SM00881};
GN   ORFNames=A1Q2_07793 {ECO:0000313|EMBL:EKC97996.1};
OS   Trichosporon asahii var. asahii (strain CBS 8904) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Trichosporonales; Trichosporonaceae; Trichosporon.
OX   NCBI_TaxID=1220162 {ECO:0000313|EMBL:EKC97996.1, ECO:0000313|Proteomes:UP000006757};
RN   [1] {ECO:0000313|EMBL:EKC97996.1, ECO:0000313|Proteomes:UP000006757}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 8904 {ECO:0000313|EMBL:EKC97996.1,
RC   ECO:0000313|Proteomes:UP000006757};
RX   PubMed=23193141; DOI=10.1128/EC.00264-12;
RA   Yang R.Y., Li H.T., Zhu H., Zhou G.P., Wang M., Wang L.;
RT   "Genome sequence of the Trichosporon asahii environmental strain CBS
RT   8904.";
RL   Eukaryot. Cell 11:1586-1587(2012).
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:EKC97996.1}.
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DR   EMBL; AMBO01000400; EKC97996.1; -; Genomic_DNA.
DR   AlphaFoldDB; K1VFZ8; -.
DR   STRING; 1220162.K1VFZ8; -.
DR   eggNOG; KOG1255; Eukaryota.
DR   eggNOG; KOG2799; Eukaryota.
DR   HOGENOM; CLU_408912_0_0_1; -.
DR   InParanoid; K1VFZ8; -.
DR   OrthoDB; 1473492at2759; -.
DR   Proteomes; UP000006757; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.40.50.261; Succinyl-CoA synthetase domains; 2.
DR   InterPro; IPR003781; CoA-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR005811; SUCC_ACL_C.
DR   InterPro; IPR016102; Succinyl-CoA_synth-like.
DR   PANTHER; PTHR11117:SF2; SUCCINATE--COA LIGASE [ADP_GDP-FORMING] SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11117; SUCCINYL-COA LIGASE SUBUNIT ALPHA; 1.
DR   Pfam; PF02629; CoA_binding; 1.
DR   Pfam; PF00549; Ligase_CoA; 2.
DR   PRINTS; PR01798; SCOASYNTHASE.
DR   SMART; SM00881; CoA_binding; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   SUPFAM; SSF52210; Succinyl-CoA synthetase domains; 2.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000006757}.
FT   DOMAIN          376..471
FT                   /note="CoA-binding"
FT                   /evidence="ECO:0000259|SMART:SM00881"
SQ   SEQUENCE   672 AA;  71286 MW;  232414D144D9ECDF CRC64;
     MARSNLLCQL PKSRAPRYLD TGARANIHRS ISEPHLRLTG TPNWTQADLQ NLPPFITPTS
     TSGSGIPFKL IASRVAHKPM LEAETPDGPI QLPLDVSKDT LPVESDAFFA KLGGNPKGAK
     DVVQGLWKTW RDNDLLRITG KLDVGSGKLN DLHVVADDFG LYRSNLKELA DAAKVHPLET
     QAEAGRLFYH KSREGGNIAC YGYGAGIAMS TMDALLGAGG KAANFLDGGG GATEANVRAA
     MGVITSDPDA DVIFINSFGG LTKMDLIAEG MVKFLRERRD AGERLVPIVA RLRGTGEESA
     AQILKDATDL SGIITVIPDL KEAAEAAVRI AAQEAEKNGT ELPKPSAAEQ APVAVRDTPV
     TFSRDGQYEQ TLGNLKVKNG DPVLMLGLGG AAKLNAKIAS DYGTNIVGFA APNKGGQEFI
     GKPVYGSMGE AIKELKPRIA SLFVPVHAAA DAMIDAIEAE IPLIVAYAEG IPTRDQLRVQ
     AALRSQNKSR VVGANCPGVI FPHERVKLGI QPLPVHSPGD IGIVSRSGTI SYDLAAQTSA
     LGLGQSAVYG LGGDPFPCTR TWEAVQLMIE DPKTKVICIV GECGGQMEEE AAQVYAEYVR
     NLPAGQVPKP AVGFVAGEAT KRGLMYGHAG AVWWEPEERT LAKKKFMQNA GITMADTLGD
     LGALIKQTHA KL
//
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