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Database: UniProt
Entry: A0A2H3J625_9EURO
LinkDB: A0A2H3J625_9EURO
Original site: A0A2H3J625_9EURO 
ID   A0A2H3J625_9EURO        Unreviewed;      1731 AA.
AC   A0A2H3J625;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=Pre-mRNA-processing protein 45 {ECO:0000256|ARBA:ARBA00022160};
GN   ORFNames=PENO1_015980 {ECO:0000313|EMBL:PCH06707.1};
OS   Penicillium occitanis (nom. inval.).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=290292 {ECO:0000313|EMBL:PCH06707.1, ECO:0000313|Proteomes:UP000218381};
RN   [1] {ECO:0000313|EMBL:PCH06707.1, ECO:0000313|Proteomes:UP000218381}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CL100 {ECO:0000313|EMBL:PCH06707.1,
RC   ECO:0000313|Proteomes:UP000218381};
RX   PubMed=28951729; DOI=10.3389/fmicb.2017.01627;
RA   Bravo-Ruiz G., Sassi A.H., Marcet-Houben M., Di Pietro A., Gargouri A.,
RA   Gabaldon T., Roncero M.I.G.;
RT   "Regulatory Mechanisms of a Highly Pectinolytic Mutant of Penicillium
RT   occitanis and Functional Analysis of a Candidate Gene in the Plant Pathogen
RT   Fusarium oxysporum.";
RL   Front. Microbiol. 8:1627-1627(2017).
CC   -!- SIMILARITY: Belongs to the SNW family. {ECO:0000256|ARBA:ARBA00010197}.
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:PCH06707.1}.
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DR   EMBL; NPFK01000025; PCH06707.1; -; Genomic_DNA.
DR   STRING; 290292.A0A2H3J625; -.
DR   OrthoDB; 5490078at2759; -.
DR   Proteomes; UP000218381; Unassembled WGS sequence.
DR   GO; GO:0005681; C:spliceosomal complex; IEA:InterPro.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IEA:InterPro.
DR   CDD; cd06257; DnaJ; 1.
DR   Gene3D; 1.10.287.110; DnaJ domain; 1.
DR   InterPro; IPR024586; DnaJ-like_C11_C.
DR   InterPro; IPR001623; DnaJ_domain.
DR   InterPro; IPR036869; J_dom_sf.
DR   InterPro; IPR017862; SKI-int_prot_SKIP.
DR   InterPro; IPR004015; SKI-int_prot_SKIP_SNW-dom.
DR   PANTHER; PTHR12096; NUCLEAR PROTEIN SKIP-RELATED; 1.
DR   PANTHER; PTHR12096:SF0; SNW DOMAIN-CONTAINING PROTEIN 1; 1.
DR   Pfam; PF00226; DnaJ; 1.
DR   Pfam; PF11875; DnaJ-like_C11_C; 1.
DR   Pfam; PF02731; SKIP_SNW; 1.
DR   PRINTS; PR00625; JDOMAIN.
DR   SMART; SM00271; DnaJ; 1.
DR   SUPFAM; SSF46565; Chaperone J-domain; 1.
DR   PROSITE; PS50076; DNAJ_2; 1.
PE   3: Inferred from homology;
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW   Reference proteome {ECO:0000313|Proteomes:UP000218381};
KW   Stress response {ECO:0000313|EMBL:PCH06707.1}.
FT   DOMAIN          40..109
FT                   /note="J"
FT                   /evidence="ECO:0000259|PROSITE:PS50076"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          231..252
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          830..907
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          919..1097
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1155..1174
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1359..1393
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1458..1558
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1666..1731
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        12..27
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        838..867
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        919..941
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        942..972
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        973..1006
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1007..1039
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1048..1064
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1458..1498
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1499..1524
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1525..1558
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1666..1684
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1708..1731
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1731 AA;  192006 MW;  F22820E4E156B1EE CRC64;
     MASSRVGKSR PNGNFHNDDD ASTDLDKDYE RLMRYPEKVD YYSLLGLSRY PPPTDSQLQS
     AYHNLSLSLH PDKQPAHLVE SANAQFRLVQ EAYKILSDPK KRIVYDLEGE EGVQREWSAS
     GPMAARMENE DSGLGQVGPR AMSPAEFRRW FIARMKAKER TALNRMVGAK SSVSVTIDAS
     SLISPGEEEG EVDFNFPPPK LRVSRFVLGY SFKTALPDFA GAWTWFSGRQ KDTEEETSAE
     SENVEEESGF PPEVTFHANV SGAIRPSKQA FRLPTPDGGT EVVKIDGPPF LGAATFNLGA
     TINHQFTTAG LLAVPQSKFD LRSLLEGASV GGTVTILPAR ALALHMEKQV YPFPNSKPFT
     VLVKSNIPSN VNHFMPNITA SIVRQFGSKK FGTVSYSTGS HLTWSSFMRG FLSPFMDMSL
     DPRLEPMLVN DGSLQLQYTS LSSPTAEEVS NDPDLAKSTE NEVWQWGFAA TPAQAQLSLT
     YGRTFFADRL EDVPRSEWNL DGYHPTIPLP DRRGVRVEVE AAVDLDGDMA WGITASRRVA
     KFTNMGLGVS LRDARGLVLS LSWRRLGQSI RVPILICPLD LANAEISAMA VIVPWLTYIG
     VEFGYIRPRE RRRRREAIIR KRKQLKAQLS ARKKESAQQI ELMSDLTRRR QAREEDKGGL
     VVEKAEYGYF PPENAKHAES EVIDVTIPVA AQVDKSQLFI SKNTIRFQII GFYDPAPLLT
     KTLKVWYTFR GQRHYAEAKD GEDLACPRRE HMLISDDLLT MNFPYLAVFV AIALSQTMST
     RQSSPESHTE IIATRRSSKL TKCAPELASI ASSRIGVVVG VPTPSKRVVD GEETIQNVKA
     ANRENTMSAP LPYGVTRTTG NTNAEDSNSD RGGRRRRQEG PSSNQNGGGR SNDDRPARGG
     KQGKDVGVQT TDSLLNLGAG ASVLGSGNQQ DNQGKGKNKK NNNQDNNQKD DNQDKKQDTN
     EGTNEGTNKD KNQENNNKQQ NNNGGKKNKN KNKNNKGNSN QDCPQEESSK VNDRSDETKD
     EAKDKGKGKA KDDSKPQDSG TNNKKNVHFS ENENKEKETE PEESGGTSEW PAADEAPSEW
     ETNTGDDSAA AAGALEWNNE ATEIANIDCK NSRFQTKDRN PNTRQAITSR SLQRRHRTHI
     LTMASVASGL FKSLPKPKYT GEDEEIPSHA QQRGPRVLGA GALDESQIVL RRTGPPPYGN
     RTGWRPRAPE DFGDGGAFPE ILVAQYPLDM GRKGGQTTSN ALAVQVDGEG KVKYDAIARR
     GHSDNRIVHA SFKDLIPLRQ RVDMGEISLD RPSQEEVAEQ MEKTKDALAK LVTGAVAAQK
     PKNVRGGQRA DPTFVRYTPA NQMGDTSRKN DRIMKIMERQ QDPMEPPKFK HKKIPRGPPS
     PPPPVMHSPP RKLTAEDQEA WKIPPPVSNW KNPKGYTVPL DKRLAADGRG LQDVTINDKF
     AQFAEALFTA DRHAREEVQQ RAQMQQKLAE KEKAQKEEHL RQLAQKAREQ RSTAASSRRE
     SRARSFSGSR SPSPAYSSRS VSPSDDESAA REREQARRER RQEAERQLRQ SRMGTERRIQ
     MMAREQNRDI SEKVALGLAK PTQTTESMYD SRLFNQTSGM STGFNEDNPY DKPLFAAQDA
     ISSIYRPRAQ ADDEYDEDAA AGEMNKIQKS GRFEVLGRAK EGFRGAAEAE ARDGPVEFEK
     DTADPFGIDS MIADVTGGGA SAGKKRYGIQ QADRDEDGGR GSKRARVDEE D
//
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