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Database: UniProt
Entry: A0A1F5LYZ1_9EURO
LinkDB: A0A1F5LYZ1_9EURO
Original site: A0A1F5LYZ1_9EURO 
ID   A0A1F5LYZ1_9EURO        Unreviewed;      1046 AA.
AC   A0A1F5LYZ1;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OGE58325.1};
GN   ORFNames=PENARI_c001G00107 {ECO:0000313|EMBL:OGE58325.1};
OS   Penicillium arizonense.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=1835702 {ECO:0000313|EMBL:OGE58325.1, ECO:0000313|Proteomes:UP000177622};
RN   [1] {ECO:0000313|EMBL:OGE58325.1, ECO:0000313|Proteomes:UP000177622}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 141311 {ECO:0000313|EMBL:OGE58325.1,
RC   ECO:0000313|Proteomes:UP000177622};
RX   PubMed=27739446; DOI=10.1038/srep35112;
RA   Grijseels S., Nielsen J.C., Randelovic M., Nielsen J., Nielsen K.F.,
RA   Workman M., Frisvad J.C.;
RT   "Penicillium arizonense, a new, genome sequenced fungal species, reveals a
RT   high chemical diversity in secreted metabolites.";
RL   Sci. Rep. 6:35112-35112(2016).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:OGE58325.1}.
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DR   EMBL; LXJU01000001; OGE58325.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F5LYZ1; -.
DR   STRING; 1835702.A0A1F5LYZ1; -.
DR   OrthoDB; 2321389at2759; -.
DR   Proteomes; UP000177622; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR   Gene3D; 6.10.140.2220; -; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   InterPro; IPR002893; Znf_MYND.
DR   PANTHER; PTHR45641:SF1; NEPHROCYSTIN-3; 1.
DR   PANTHER; PTHR45641; TETRATRICOPEPTIDE REPEAT PROTEIN (AFU_ORTHOLOGUE AFUA_6G03870); 1.
DR   Pfam; PF13424; TPR_12; 2.
DR   SMART; SM00355; ZnF_C2H2; 2.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 1.
DR   SUPFAM; SSF144232; HIT/MYND zinc finger-like; 1.
DR   SUPFAM; SSF48452; TPR-like; 2.
DR   PROSITE; PS01360; ZF_MYND_1; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000177622};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Sporulation {ECO:0000256|ARBA:ARBA00022969};
KW   TPR repeat {ECO:0000256|ARBA:ARBA00022803};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          10..30
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS00028"
FT   DOMAIN          129..149
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS00028"
FT   DOMAIN          840..877
FT                   /note="MYND-type"
FT                   /evidence="ECO:0000259|PROSITE:PS01360"
FT   REGION          169..201
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          268..298
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          337..359
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        171..194
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        275..298
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        342..359
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1046 AA;  117828 MW;  513A0AF3C869FC29 CRC64;
     MDAVMSAQQC KHCEKIFFNR SLWQEHYDWH TTIQLQLGRS ARRQPVNQSE SGSDTIDQIN
     TLVSRLQLQS DDIGRKGRPE SLMEDEGKES NLLPTQAQME QYLQKAIADF PPYEGGGIEK
     VVSEPTIKCP DCDICFYTQY ELEEHYLWHD DIHLRHHIER RVERMKEQRG GSQAWNDTGA
     YISDSVTEPP QRVQNPWNRK GGFPQYDGDV VAISFLSEED LEMRYAPDGV LKDLSKDTTH
     LRLSSGVSNK IDDSATQKKR SLRKSLKNML GGRSEDTFRS PSPQSQRTSL GNSPNVSSVR
     GLGNIDVQEH MEWQLFYLHS RSDWVLTHDR SQHVEMHAAG DQRTHGNSQS RISSPPNRLS
     PEELQARFES LMGEIADYAK HNFVENIAGL ESIISEFTAA EVPSKTYLEK LHAWFNNEQK
     QAAFTNSEIK ALSGLPVLGY GSPSRILARD HVGRPRLITG QDLSRITCHA IGPPRGSLDV
     VRMALGRRGE AALARGRIGD AERAYTEMFR AMRALYGDEQ LQFILLVHLA SNVYKKNGNM
     SNAAGMYMQG LRCSQRLYGL KSVNNFTMMT NLAIYYEDIG RLDDAAALYR RSLRGRINAG
     EKEDALMNIQ ELSTVYWKMG KNPDALRFIE EAYTGYTQVV GPDHRMTQLT LNNLAAFHFR
     AGSIERARSL LGSALPAMTR VLGLDDPVTW GSVCNFVMYY EDSNFPPAIT QVIEQYMAQN
     TPASLNVLKG IGDHYGKNGL IRKAMETYRA LHGKRMALLG PSHPETWSSL YAYAYALDRL
     GETGEALKQY RLLVSQPQAR SLLPRSQVEG SQAAVQELSR KQAALDKEKV EWGLTTAQKC
     SRQVCSNSTL RFCSDCSLVR FCSPACQRED KSHHGACIPS VTLTESTFTI VENPQDKSSV
     VREADFLFTQ LQLPRRPRCE SARDVFINPK NFTTIRISKQ PSHILSFQAN PGLDLRFMIH
     RSTPFEWLTP TTSNMLCMLS DVEDSFIVVT PGESMMKGLV AARDKVFGTE SGNLDIPDQD
     LVEFARTVAA GDEQFVLGFM VTEWAL
//
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