ID A0A0A2KPG1_PENIT Unreviewed; 987 AA.
AC A0A0A2KPG1;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Molybdenum cofactor biosynthesis, MoeB {ECO:0000313|EMBL:KGO68863.1};
GN ORFNames=PITC_078040 {ECO:0000313|EMBL:KGO68863.1};
OS Penicillium italicum (Blue mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=40296 {ECO:0000313|EMBL:KGO68863.1, ECO:0000313|Proteomes:UP000030104};
RN [1] {ECO:0000313|EMBL:KGO68863.1, ECO:0000313|Proteomes:UP000030104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHI-1 {ECO:0000313|EMBL:KGO68863.1,
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:KGO68863.1}.
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DR EMBL; JQGA01001176; KGO68863.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2KPG1; -.
DR STRING; 40296.A0A0A2KPG1; -.
DR HOGENOM; CLU_012412_0_0_1; -.
DR OMA; SKWWQEL; -.
DR OrthoDB; 10004at2759; -.
DR PhylomeDB; A0A0A2KPG1; -.
DR Proteomes; UP000030104; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR CDD; cd00144; MPP_PPP_family; 1.
DR CDD; cd00755; YgdL_like; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR PANTHER; PTHR43267; TRNA THREONYLCARBAMOYLADENOSINE DEHYDRATASE; 1.
DR PANTHER; PTHR43267:SF2; TRNA THREONYLCARBAMOYLADENOSINE DEHYDRATASE 1-RELATED; 1.
DR Pfam; PF00149; Metallophos; 1.
DR Pfam; PF00899; ThiF; 1.
DR SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000030104}.
FT DOMAIN 163..424
FT /note="THIF-type NAD/FAD binding fold"
FT /evidence="ECO:0000259|Pfam:PF00899"
FT DOMAIN 731..902
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
FT REGION 23..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 563..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 618..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..51
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..600
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..637
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 987 AA; 108132 MW; 39C4FD82E654F667 CRC64;
MASPSSKWWQ ELTDADLDYG FDSDEMDTRY NESDRNTSHE NKSEPRDNQN TDDKGVIASM
SSWLHRQAGS SHGQLATAAV VSGAAVAGAI FGYQSYKRKE AVHDLKASIP SIDDFHPAEM
LTDFGAASKG IQLSKEDERS AALARRAQQG DYDDDLILEQ LARNRVFLGD EGLAKLRSSF
VVVVGCGGVG SHAAASLARS GVSKIRLIDF DQVTLSSLNR HALATLADVG TPKVQTIRRR
LEQIAPWVAF DCRNELYGKA ASEDLLGPWS LTHDGEGRRP DFVLDCIDNI TSKVELLHYC
HSNSLPVISS MGAGCKSDPT RVVVGDISLS TDDPLSRSTR RRLKLLGVSS GVAAVFSTEK
PGPGKATLLP LPEDEFTKGQ VGELGVLPDF RARILPVLGT MPAVFGYTVA NHVICTITGY
PLDYNMGAKG REKLYDSILS TLLNLHERMI RQVTGQDTVG LRAPLSKDDI AFAVEEVYRG
KSAISGLSNR LALIPWQTPA HGWNIDLSLE KEGQKSIPME INDMVCMTKE EALHHEKEVL
KGGKKVEEVY DETVLQRVNL RRREAEESMA SRNSYPQDFE SNSADDDFPP TTSHHASYSN
QFPQYSRPLI DSARNAWQTR APEGSQHASS SPADDIKSPG WSQMASAPRF RHMLIFGALS
IFAWIGWRML LSPRLQEQIS LNPTSKAGMV GLLGANSYPQ FDGFVQIRTL DPDLVPGDLT
KVETGESSRK RLIIVGDVHG CKEELVQLLE KVSFNQKGGD HLIFVGDLIN KGPDSTGVVD
LAREYSASSV RGNHEDRILL LRQKMLKTKT LTTPDDKKYS GFSSRELGER ALARSLSDEQ
VQWLEECPVI LNVGQVPGMG QVVVVHAGLV PGIELEKQDP SSVMTMRTID LDTHVPSPKK
KGTNWAETFD KHQSKLNSTL ESSAEDPLAK AMTVVYGHDA STSLSIRTFT KGLDSGCVKG
GKLTALVIED GGKQSIAQVS CRDYLKE
//
