ID A0A2J6Q464_9HELO Unreviewed; 1327 AA.
AC A0A2J6Q464;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Cyclin-domain-containing protein {ECO:0000313|EMBL:PMD21036.1};
GN ORFNames=NA56DRAFT_748961 {ECO:0000313|EMBL:PMD21036.1};
OS Hyaloscypha hepaticicola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Hyaloscyphaceae; Hyaloscypha.
OX NCBI_TaxID=2082293 {ECO:0000313|EMBL:PMD21036.1, ECO:0000313|Proteomes:UP000235672};
RN [1] {ECO:0000313|EMBL:PMD21036.1, ECO:0000313|Proteomes:UP000235672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 7357 {ECO:0000313|EMBL:PMD21036.1,
RC ECO:0000313|Proteomes:UP000235672};
RG DOE Joint Genome Institute;
RA Martino E., Morin E., Grelet G., Kuo A., Kohler A., Daghino S., Barry K.,
RA Choi C., Cichocki N., Clum A., Copeland A., Hainaut M., Haridas S.,
RA Labutti K., Lindquist E., Lipzen A., Khouja H.-R., Murat C., Ohm R.,
RA Olson A., Spatafora J., Veneault-Fourrey C., Henrissat B., Grigoriev I.,
RA Martin F., Perotto S.;
RT "A degradative enzymes factory behind the ericoid mycorrhizal symbiosis.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812}.
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DR EMBL; KZ613482; PMD21036.1; -; Genomic_DNA.
DR STRING; 1745343.A0A2J6Q464; -.
DR OrthoDB; 2291769at2759; -.
DR Proteomes; UP000235672; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0019901; F:protein kinase binding; IEA:InterPro.
DR GO; GO:0004737; F:pyruvate decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR CDD; cd20558; CYCLIN_ScPCL7-like; 1.
DR CDD; cd07035; TPP_PYR_POX_like; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR Gene3D; 1.10.472.10; Cyclin-like; 1.
DR Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR InterPro; IPR013922; Cyclin_PHO80-like.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR18968:SF164; PYRUVATE DECARBOXYLASE; 1.
DR PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 1.
DR Pfam; PF08613; Cyclin; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF00205; TPP_enzyme_M; 1.
DR Pfam; PF02776; TPP_enzyme_N; 1.
DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000235672}.
FT DOMAIN 5..136
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 208..314
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 416..579
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT REGION 732..755
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 790..815
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1026..1046
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1106..1128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1106..1127
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1327 AA; 144904 MW; ED3D2879868F6A87 CRC64;
MVYTASFAFF ESLWEAGITH VFVNLGSDHP SIIEAIVKGQ NEKKGNFPRI ITCPNEMVAL
SMADGYARLT RKPQCVIVHV DVGTQGLGAA VHNASCGRAP VLIFAGLSPY TIEGEMRGSR
TEYIHWIQDV PDQKQIVAQY CRYSGEIKTG KNVKQMVNRA LQFARSDPAG PVYLCGAREV
MEEDIEPYKL DQGYWNPVEP AGLSETAVKR ISEALVEAKE PLIVTGYSGR NHDTVPALVK
LANTVKGIRV LDTGGSDMCF PADHRAWLGL RYGIEESIRT ADVIVVIDCD VPWINTQCKP
AEVAKIFHID VDPLKKQMPV FYLNAVARYF ADSYEAITQL TNYISSSPLS QQLSSQEFTK
KWDLLGESHS KRLAAIAAAS EPKSDNTFGT GYLCRTLRKL VPVDTIWAIE AVTNTAFVAD
NIQATFPGSW INCGGGGLGW SGGGTLGIKL ATEYENGPGK GKFVVQIVGD GTFLFSVPGS
VYWISKRYKI PVLTIVLNNK GWNAPRKSLL LVHPDGLGSK ATNEELNISF APSPDYAGIA
KAAAGGDLFA EKVSKTSDLE DVLRRAVESV KNGTTAVVDA QVVSGYGEAA SSFGNTSNSI
RMTWSTTQEL WLEAPVSPLG GWLIFVYQFA STSTAPHLIS SHLTTLLPSP DLLHAQQFQV
DVRQLLAWPR SDLLCLRAAF LLITRIEGCI PYQPSYGAGR RSGPKAPPFK GLACASRPVL
VWRGVGVFDI KARGPKQSPE GQNRRRQVGQ QEAWPSFPTK VVKAKQAGAA GQKSNTVSKA
RAYALPCCRT VPKSKRESDP QHQRQPAAQH PSDSLPPIHL QWEIHCISVG SRDIHVQLLR
VSSFYHCPLS APGSKPPAPS KAPVLPFRHS LKAKTAGDPR DLGTTANLSL AAGVTEYSPY
NYFEVPPESS PPTAFVRHLT EFPTSPHREY APLEAVQKAS TAVAEAWVKK TLRTSTTYRI
IRIIQFLSNT LRRLLHTSSE YAMSPTRSVT GVCVAASSPP EVKPYIHDSA DTFTYILPPR
PNPSADAGLS VKVPGDESDT PPSPNSLDVF TIGPVTALKL LCAGIEALVR VTGDIPPTPP
STNSTPPNMR GMQAEKENII RSNSWKNLAD LNQRPRTPSS SSGGSEDIDG VSFKKAAVGK
SNRAPIEPYI IIGDNAEPLN VQHSAITRKF YSKHPPPISL EDYLMRIHKF CPMSTAVYLA
TSYYIHKLAV DERAIPVTRR NCHRLLLAGL RVAMKALEDL SYPHSRFSKV GGVSESELAR
LEISFCFLTN FEFKTNKETL LDHAIALREI SSLQGAMNFI PRLPLKAKIR SNVAVQETVF
EVTADAC
//
