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Database: UniProt
Entry: A0A1V6TBD2_9EURO
LinkDB: A0A1V6TBD2_9EURO
Original site: A0A1V6TBD2_9EURO 
ID   A0A1V6TBD2_9EURO        Unreviewed;      1673 AA.
AC   A0A1V6TBD2;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=PH domain-containing protein {ECO:0000259|PROSITE:PS50003};
GN   ORFNames=PENSTE_c008G05208 {ECO:0000313|EMBL:OQE23685.1};
OS   Penicillium steckii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=303698 {ECO:0000313|EMBL:OQE23685.1, ECO:0000313|Proteomes:UP000191285};
RN   [1] {ECO:0000313|Proteomes:UP000191285}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 24891 {ECO:0000313|Proteomes:UP000191285};
RX   PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA   Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA   Frisvad J.C., Workman M., Nielsen J.;
RT   "Global analysis of biosynthetic gene clusters reveals vast potential of
RT   secondary metabolite production in Penicillium species.";
RL   Nat. Microbiol. 2:17044-17044(2017).
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:OQE23685.1}.
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DR   EMBL; MLKD01000008; OQE23685.1; -; Genomic_DNA.
DR   STRING; 303698.A0A1V6TBD2; -.
DR   OrthoDB; 1368013at2759; -.
DR   Proteomes; UP000191285; Unassembled WGS sequence.
DR   GO; GO:0005938; C:cell cortex; IEA:InterPro.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
DR   GO; GO:0032065; P:maintenance of protein location in cell cortex; IEA:InterPro.
DR   CDD; cd13365; PH_PLC_plant-like; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR024774; PH_dom-Mcp5-type.
DR   InterPro; IPR001849; PH_domain.
DR   PANTHER; PTHR28190; NUCLEAR MIGRATION PROTEIN NUM1; 1.
DR   PANTHER; PTHR28190:SF1; NUCLEAR MIGRATION PROTEIN NUM1; 1.
DR   Pfam; PF12814; Mcp5_PH; 1.
DR   SMART; SM00233; PH; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000191285}.
FT   DOMAIN          1385..1496
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          132..183
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          267..293
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          354..397
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          440..819
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1123..1142
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1158..1179
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1228..1269
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1283..1347
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1518..1622
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1649..1673
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          55..123
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          202..236
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        139..183
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        440..477
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        484..498
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        543..587
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        609..628
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        647..670
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        696..714
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        735..768
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1237..1264
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1319..1347
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1522..1609
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1673 AA;  182285 MW;  05C456C34FC0BEE5 CRC64;
     MSTSNTGANS SLASMMEDPF VSNAGHNAAP RETHRYSSFD TQLFSLNASS PAQAKRALEA
     HLVETERRLE EASKLGQALI DQQRELSEQL KEVEQQQDEG EMGPELRKRL ADLEQEYNEI
     GRESTRAFLG PKRLAGGSED VPSSTTPFDQ KSPISPALFA GQATNSPSKV SVPSRKQRNQ
     PSNRVHDIEF ATEISTSLLA QVRQLQALLA EREESLKSVN LEKSRLELEA EGYAQRIRAL
     DDSEQRYKDE NWALETQTHE LMAAVRDATE REQKLTTSLD TSSSEKNAVE RELEELRQTN
     ARLLEDHAAA QKSNDSEVHL LRRNLNAGDL EKSALHKKLE ELTSQNQELA KAVAMRIRQH
     ESQGTRDLPD DMNGDEPEQT TPDNSPPPSP NKFTPRHNHL ESETLKSSLG HAHRMIQNLK
     STIHREKTEK IELKRMLQDA RDEVEQRRRE SAAPNGTKKS LKKKDDSFRK PARPDLLGAG
     RKETSMVELH DTDWDDEAGQ ISPSRSVAMN GARNHSGARS PDEPSDVYQT ATEAEDGFET
     ANERATATES EAFQTGVESM ADDSSDSADL TETENNVQTT PRNRVSSSIV MAKARDRTSY
     HSSASTSDDD ETDSGFPSPS QMSVSRPRVR SKRSILRRIR PSGEAPMAST SRPSSSRNSP
     ATSFEQEPMP QEGQSLFAEL QELEGGDEEE EEGATSQAST PRMQATSGSR RPSDISLGNV
     AKPVMVDSGM MTDPWEPQAN GSQVPVPIVA ETTSSGSPTS PQRTQTSERG VDSDSETPKQ
     VSSGTQWTPL KGPVADADHL INVPTPPKMA WDERSGAQQV EAGTQAELPQ MDLAAISSQE
     TIPLVPNWPT LEVSYFVGDE TVPVKQELPE PEIPEMNLSS ISSQITEPVM ATVPEPKPVI
     VEPVKELPDL SLSSLFTYST EPIQARLPEP EPVVEVPEVI SPEFGLSILS TQHTEPVEPR
     HPEPAPAPEP IIIPAPIPEP VIPELTLSML DPSSTEPIAP KLVEIPEPEP LPEPVIPEYT
     LSMLDSTSTE PIAPKLVEIP VPEPLPEPVI PKLSISWLDP ASTAPVVPKP IVAPNPPTPS
     LSILSSVSTH PVKHVTPIAP LMAELGIQTD PIDEPKAAAA LALASEENEP VEAARDLDAT
     SANDHRTSIG LALSDMSGNA LPQSATEKPG FVSSDQGSQT ILSSKQIDQI LVERESSRPI
     SSADSKSKEA AAIGAGVAVA GAGAAASFAT PKLRPRPQGQ SARSTTPGQH RPDSSTSQTS
     GLSAHPPLPA DHREAILAAE KKSIDVPPSS PGVMGPPLAP ASAYRMNVQG PRTPGDQGPR
     PGSTRTVSTQ ARMRRSSQSQ MSRRSSVSSF ASEIEERFNM NPHAGPMPHG YGPNTDPRMI
     QAITQTMIGE FLWKYTRKTG SGNMSSTRHR RYFWVHPYTR TLYWSDQDPQ TAGKSQLKTK
     SVPIEAVKVL ADDNPYPPGL HCRSLEVVSP GRRVRFTATT SQRHETWFNA LSYLLLRETN
     ENCEENDNSV TLDDIDEFNP GFRSASRQTG RMSLASHNSR RQAPKQQRAA SAMSMRSTGT
     QGRASPAFSS PGVTSTLQVP EEGQQRSSSR LSTILTGSIR GSIASMKGRQ GQAGSVHDGS
     LRAQDSVETF NHDAEDDDRL ENVRACCDGK HDVGSLSRTS RFSPRVDRSH SHH
//
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