ID A0A0A2KZ26_PENIT Unreviewed; 1056 AA.
AC A0A0A2KZ26;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Male sterility, NAD-binding {ECO:0000313|EMBL:KGO73092.1};
GN ORFNames=PITC_098230 {ECO:0000313|EMBL:KGO73092.1};
OS Penicillium italicum (Blue mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=40296 {ECO:0000313|EMBL:KGO73092.1, ECO:0000313|Proteomes:UP000030104};
RN [1] {ECO:0000313|EMBL:KGO73092.1, ECO:0000313|Proteomes:UP000030104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHI-1 {ECO:0000313|EMBL:KGO73092.1,
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:KGO73092.1}.
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DR EMBL; JQGA01000840; KGO73092.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2KZ26; -.
DR STRING; 40296.A0A0A2KZ26; -.
DR HOGENOM; CLU_002220_2_1_1; -.
DR OMA; QCKLVTY; -.
DR OrthoDB; 2230730at2759; -.
DR PhylomeDB; A0A0A2KZ26; -.
DR Proteomes; UP000030104; Unassembled WGS sequence.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR013120; Far_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR009081; PP-bd_ACP.
DR PANTHER; PTHR43439:SF2; ENZYME, PUTATIVE (JCVI)-RELATED; 1.
DR PANTHER; PTHR43439; PHENYLACETATE-COENZYME A LIGASE; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF07993; NAD_binding_4; 1.
DR Pfam; PF00550; PP-binding; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000030104}.
FT DOMAIN 554..633
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1056 AA; 117012 MW; 88AEC8D6E3755C2B CRC64;
MGIQRGSQAA QAGPSSTINP LVQEFGSLQV LDDLIRLRAA DVVQCPILAY PRFDNDSASY
ENYTGKHMDA MIDQAVVKLI DDGFKQATQS PSIVALLTLS DLNMVITFFA LSRLGYTIMM
LSPRLSGEAC VSLLETVKCE SIIYGQSPNI RSTLGEILRR RLVTCRPMLS CSLYNKLQLP
SLVLNRNQNP EKVALILHSS GSTGTPKPLF LTHKAIMTHP LRGPGLSSFN TLPWYHLHGL
STALQAMWMR KTAYMWNASL PLTAEFVATA LEEAKPESVA AVPYMLQILI DDPRGVTALR
QCKLVTYGGA PCPDELGDRL VSEGVHFGGS FGLTEAGLVA ESISRPKGDP YWNYLKFFDN
IRSYVWMKPI SESDSLFECV YLAGHPALTT SNSNEPPGSF HSKDVFTPHP TIAGRWKYIS
RLDDRINLVN GEKVLPLPIE GHIKQHPFIH DAVVVGVGKA APGLLVLRAD EPEANRLSDD
KYLNAIWPTV QEANSQAEAF SQIPRNMVAI LPSDTKFART DKGSMIRAQV YQEHSELIES
LYSEKEQICG NLQLDVVETE RVLLQISDQE LGIPVSGVDA KFFSEGVDSL KAIHFRRLIL
QHFKFEKSQT PGPNVIFEAG CISQLARQIC ALQKGETLED VETGVSVMTQ LIEKYSVFER
HIPQPHVFSG PNSVLLTGAT GSIGAHVLYE LLNDDSISKV YCLTRRESPL EAILRTLTDK
DLFISSEQKA KIVAFNGCID QPDFGLSLDE STVRHMLNSV SLIIHTAWPV NFNLPLNEFE
PHIQGLYNLI QISLSVRRRE PAVMMFCSSV STALGSRSAE ISEEPVALDS AFMGYGQSKS
IGERIVSNAR RSGARAYSLR IGQVSGHSEK GLWNDSEALP LMIRSALTLG ALPELSQTCS
WLPVDKLAPI ILELARTCAT PSVFGESQAS SSAAVEYVDD SIFNLCNSRE FTWSSLLHAL
KDCGFQFEAV PFEEWLLRLR RSEARGEELV NPAVKLIHHY ETMHGKKSSL MQNGPKRFIT
EKAEKSSVTL RTGRLRIIDD GILRCYAQDW LARWRA
//
