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Database: UniProt
Entry: A0A0A2KTL9_PENIT
LinkDB: A0A0A2KTL9_PENIT
Original site: A0A0A2KTL9_PENIT 
ID   A0A0A2KTL9_PENIT        Unreviewed;       624 AA.
AC   A0A0A2KTL9;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=C2 calcium/lipid-binding domain, CaLB {ECO:0000313|EMBL:KGO67690.1};
GN   ORFNames=PITC_064530 {ECO:0000313|EMBL:KGO67690.1};
OS   Penicillium italicum (Blue mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=40296 {ECO:0000313|EMBL:KGO67690.1, ECO:0000313|Proteomes:UP000030104};
RN   [1] {ECO:0000313|EMBL:KGO67690.1, ECO:0000313|Proteomes:UP000030104}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PHI-1 {ECO:0000313|EMBL:KGO67690.1,
RC   ECO:0000313|Proteomes:UP000030104};
RX   PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA   Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA   Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT   "Genome, transcriptome, and functional analyses of Penicillium expansum
RT   provide new insights into secondary metabolism and pathogenicity.";
RL   Mol. Plant Microbe Interact. 28:232-248(2015).
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:KGO67690.1}.
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DR   EMBL; JQGA01001270; KGO67690.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A2KTL9; -.
DR   STRING; 40296.A0A0A2KTL9; -.
DR   HOGENOM; CLU_022666_2_0_1; -.
DR   OMA; SRYNFQA; -.
DR   OrthoDB; 2459226at2759; -.
DR   PhylomeDB; A0A0A2KTL9; -.
DR   Proteomes; UP000030104; Unassembled WGS sequence.
DR   CDD; cd04041; C2A_fungal; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 1.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR037767; C2A_Mug190-like.
DR   PANTHER; PTHR47800; C2 DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR47800:SF5; FER-1-LIKE PROTEIN 6; 1.
DR   Pfam; PF00168; C2; 1.
DR   SMART; SM00239; C2; 1.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR   PROSITE; PS50004; C2; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000030104}.
FT   DOMAIN          38..169
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   REGION          395..463
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          538..566
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          584..624
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        402..423
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        435..454
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        605..624
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   624 AA;  70906 MW;  39BB7D7873612CBE CRC64;
     MDDSQPQSLH VHPIDKYGPK FVEKADKIHR RVTMNDDSKP AGGFDATPIP HAPPGYTLKI
     TFHRAEDLPV ADFGSFSSDP YVSAHMVVDL PTRHKQDPDL RFRTPTIRKD MNPKWECEWI
     VANVPASGFQ LKCHLMDEDP ADHDDKLGIA FIDVPTLSED WAGFKQQSFK VKKRFGSKRV
     YVFTNISAFA TGHRKESWLV VSIECLGKTP GTEGGQVYTI GPNHWFKHFS PLIGRLAGIK
     DQVQSKDGSG KSISRYNFQA IEMQLTGPIP AELYHRYVEF KPFVAGMFQA QSLRGRILHK
     ALHHQHQRIY NFDRTTLHGS FQTPCRELAQ KFLEFAHYGQ GGRIFTYVLT LDGQLRFTET
     GKEFGIDMLS KHTMHSDVSI YIAYSGEFFL RRRKHRHRRN SPEGRAERAE NAENAENAEN
     AENAERAESS TVPTDEFPVE EDEDHNEGED LDQTEEGIPI STNPADYELF IDNDSGTYRP
     NAEKLPLLQE FISSNFPGLH VTTLDCQADA ERMGNLKNEQ REFKKNAGNI ITFLQQSSAS
     SLSISSSEED ELNERSGQSK QRGDLLQRVH EMRDLRGQVM RWVEADEKPD GHKHKHRHLS
     TRERPVSTGA ITTDPKNGKS QHAI
//
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