ID A0A139HPH9_9PEZI Unreviewed; 807 AA.
AC A0A139HPH9;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=HpcH/HpaI aldolase/citrate lyase domain-containing protein {ECO:0000259|Pfam:PF03328};
GN ORFNames=AC578_7900 {ECO:0000313|EMBL:KXT04303.1};
OS Pseudocercospora eumusae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX NCBI_TaxID=321146 {ECO:0000313|EMBL:KXT04303.1, ECO:0000313|Proteomes:UP000070133};
RN [1] {ECO:0000313|EMBL:KXT04303.1, ECO:0000313|Proteomes:UP000070133}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 114824 {ECO:0000313|EMBL:KXT04303.1,
RC ECO:0000313|Proteomes:UP000070133};
RA Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT link between parallel evolutionary changes in Pseudocercospora fijiensis
RT and Pseudocercospora eumusae and increased virulence on the banana host.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the HpcH/HpaI aldolase family.
CC {ECO:0000256|ARBA:ARBA00005568}.
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:KXT04303.1}.
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DR EMBL; LFZN01000022; KXT04303.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A139HPH9; -.
DR STRING; 321146.A0A139HPH9; -.
DR OrthoDB; 2785075at2759; -.
DR Proteomes; UP000070133; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR InterPro; IPR005000; Aldolase/citrate-lyase_domain.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR PANTHER; PTHR30502; 2-KETO-3-DEOXY-L-RHAMNONATE ALDOLASE; 1.
DR PANTHER; PTHR30502:SF0; PHOSPHOENOLPYRUVATE CARBOXYLASE FAMILY PROTEIN; 1.
DR Pfam; PF03328; HpcH_HpaI; 1.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Reference proteome {ECO:0000313|Proteomes:UP000070133}.
FT DOMAIN 33..246
FT /note="HpcH/HpaI aldolase/citrate lyase"
FT /evidence="ECO:0000259|Pfam:PF03328"
FT REGION 414..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 666..686
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..442
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..476
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..502
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 668..686
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 807 AA; 88246 MW; 9FC74D23258EB79C CRC64;
MQAANRLQKA LKSGGPSLGG WQMLPGANLS RAIARTPGLD WICVDTEHGN ISDAEMHESV
AAIAACGVSP VVRLPDGQHW MIKRALDAGA HGIIIPLLQS VEDARNVVKF SKFPPNGNRG
LGSPFAMEKF AEQVSNPKEI SISQYFQEAN SSIVVIVQIE TASALEQIDQ IAAVPGIDVC
FIGPVDLGNS IGHPPENIGV YAPELENAIS KIHAATQAAG KWTAIYTGSG EQAKRYVNLG
FNMVNTMNDV GAIRASFAHA AAAAAVKQKP LMRPRVVDFG VTLIAYCALS TTFTKQLAKL
KLDLNAPNYF PQPFLPQRRR ARLLNSMCFI DIIHYICGGE DQILVERCVL PSLCIPHVRR
TLHSTTVCEL CGRAWELSAL TEEAYEAVTT PLIESRQANG GYFGYFMQSQ PARPLLCQPQ
TPPSSDEIEV HELSRKQSPK VVNDRPKMST NTTGPAQHAQ ESDSPAKASK DVTSTSFDAK
APEPVDEKLM PADGKPIAED DRRPKFDWKG ALSTLATSAV GIATFPGSGT AAMRVNYYQR
LITEQAIDAL PKEAQRVLFV QLTILALNTD SSLGTPSSNI ENYKRGIQFV LRMLGGKDIG
SGEPQPSLSS VTDPDRQAEI MTLAVQLAEL FDKHGLLHVC PDVFRGTWEG DFDDEDLEFE
QEMKSHFQRL QNEPAPSPSP ENTPSVSDTQ IIVTVEALTK LQSRYPDLFA LDTKYLELLA
EKANLEACVI ESKDDLSKLR KVVEDEAGVM RGQSELKRIY GAADNVRTAI GRHADELKEF
IDIKSELCEV EIKIAVHLAE KKIRTEL
//