ID A0A401KSC4_ASPAW Unreviewed; 1110 AA.
AC A0A401KSC4;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Succinate--hydroxymethylglutarate CoA-transferase {ECO:0000313|EMBL:GCB22186.1};
GN ORFNames=AAWM_05071 {ECO:0000313|EMBL:GCB22186.1};
OS Aspergillus awamori (Black koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=105351 {ECO:0000313|EMBL:GCB22186.1, ECO:0000313|Proteomes:UP000286921};
RN [1] {ECO:0000313|EMBL:GCB22186.1, ECO:0000313|Proteomes:UP000286921}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFM 58123 {ECO:0000313|EMBL:GCB22186.1,
RC ECO:0000313|Proteomes:UP000286921};
RA Kusuya Y., Shimizu M., Takahashi H., Yaguchi T.;
RT "Aspergillus awamori IFM 58123T.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the CoA-transferase III family.
CC {ECO:0000256|ARBA:ARBA00008383}.
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:GCB22186.1}.
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DR EMBL; BDHI01000014; GCB22186.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401KSC4; -.
DR STRING; 105351.A0A401KSC4; -.
DR Proteomes; UP000286921; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR CDD; cd15502; PHD_Phf1p_Phf2p_like; 1.
DR Gene3D; 3.30.1540.10; formyl-coa transferase, domain 3; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR003673; CoA-Trfase_fam_III.
DR InterPro; IPR044855; CoA-Trfase_III_dom3_sf.
DR InterPro; IPR023606; CoA-Trfase_III_dom_1_sf.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR48207; SUCCINATE--HYDROXYMETHYLGLUTARATE COA-TRANSFERASE; 1.
DR PANTHER; PTHR48207:SF3; SUCCINATE--HYDROXYMETHYLGLUTARATE COA-TRANSFERASE; 1.
DR Pfam; PF02515; CoA_transf_3; 1.
DR Pfam; PF00628; PHD; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF89796; CoA-transferase family III (CaiB/BaiF); 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000286921};
KW Transferase {ECO:0000313|EMBL:GCB22186.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 842..898
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 446..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 627..800
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 990..1051
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..498
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..691
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 713..732
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 759..776
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 779..796
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 992..1039
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1110 AA; 118867 MW; 42D683DD3F5B4267 CRC64;
MNPTAALRVQ RACIARRSIY VPRRTTQWRS YSSAVSDDTL PLKGIRVLDM TRVLAGPYCT
QILGDLGADV IKIEHPVRGD DTRAWGPPYA TYTDGSEGPG ESAYYLGVNR NKKSIGLSFA
HKSGVEILHR LAKECDVLVE NYLPGSLKKY NMDYETLRSI NPKLIYASIT GYGQTGPYSN
RAGYDVMVEA EMGLMHITGS REGEPVKVGV AVTDLTTGLY TSNAIMAALL ARARTGKGQH
IDACLSDCQV ATLANIASSA LISGKKDSGR WGTAHPSIVP YRSYKTLDGD ILFGGGNDRL
FGVLCDRLGH PEWKTDPRFV TNSDRVKHRT DIDGLIEETV KQKTTQEWLE ILEGSGMPYA
AVNDIQGTLN HSHVQARGMV AEIDHPACGP IKLVNTPIKY SHATPGIRTP PPTLGQHTDE
ILGELLECSV LSKSTKATEQ LCTSTRIGDM SPHNGAPSSQ ASIETAPSSA HGTLHTTTTI
SGSPPSDSSR SISIGSSLGL PPSLPGRPSS IPSKRVEIPR LSAATTELLA RVTGNLKGPQ
QRNDNDKFVT WNPSTVTRTF ESQNSNSKMG KMRASSTIIE LPTAPFVYSN NVAPPAVPQA
ASPVPQGNAG DIVKPTNLPN LAPKPPSIIS VDASPASSGS PVPVNVDLKP TSSTPVNAVS
RQSASPIPVN IAPKPSTTPV GVNSAPTPLT ASIPAEPTAA IKIAPKPNGT LSDGAAPAST
SLPTTQQPQP AAKPKKPQAA AGSRQRKGAA NGNKRGKKRR RNNDSDGEDI IRAGDSSSDE
SDVAPTATQT KSGRLVNRPS LYVPAPSTPA VAKEVSNSVD ASDNAAVARK RKRIHRRGKD
AIIICLHCQR GHSPLSNSIV FCDECNAAWH QWCHDPPIGA DVVAVKEKEW FCRECRPVQI
SVIQPTVVQS NPNLTSGPLV PNYPLLSIPK GEVGAAEFSA DERRGFLSSL SHATLVELLM
TISDNNPILP MFPENMRDLQ SSKFAFRLPI SDAPTPSTSV SGNVSTSNDI RDSASASTEG
NKQNEDSAPE ATSSSITRRQ YEEISDDDSE YEFQEHRLYP RAGNGFRLSL NVDDMDIMRE
DPACPTFSYS LHGPAQVRAQ MNEIVPVWGT
//
