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Database: UniProt
Entry: A0A139HAD4_9PEZI
LinkDB: A0A139HAD4_9PEZI
Original site: A0A139HAD4_9PEZI 
ID   A0A139HAD4_9PEZI        Unreviewed;       590 AA.
AC   A0A139HAD4;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   22-FEB-2023, entry version 19.
DE   RecName: Full=Pre-mRNA-processing protein 45 {ECO:0000256|ARBA:ARBA00022160, ECO:0000256|RuleBase:RU367140};
GN   ORFNames=AC578_6747 {ECO:0000313|EMBL:KXS99338.1};
OS   Pseudocercospora eumusae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX   NCBI_TaxID=321146 {ECO:0000313|EMBL:KXS99338.1, ECO:0000313|Proteomes:UP000070133};
RN   [1] {ECO:0000313|EMBL:KXS99338.1, ECO:0000313|Proteomes:UP000070133}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 114824 {ECO:0000313|EMBL:KXS99338.1,
RC   ECO:0000313|Proteomes:UP000070133};
RA   Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT   "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT   link between parallel evolutionary changes in Pseudocercospora fijiensis
RT   and Pseudocercospora eumusae and increased virulence on the banana host.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in pre-mRNA splicing.
CC       {ECO:0000256|RuleBase:RU367140}.
CC   -!- SUBUNIT: Associated with the spliceosome.
CC       {ECO:0000256|RuleBase:RU367140}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU367140}.
CC   -!- SIMILARITY: Belongs to the SNW family. {ECO:0000256|ARBA:ARBA00010197,
CC       ECO:0000256|RuleBase:RU367140}.
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:KXS99338.1}.
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DR   EMBL; LFZN01000094; KXS99338.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A139HAD4; -.
DR   STRING; 321146.A0A139HAD4; -.
DR   OrthoDB; 5490078at2759; -.
DR   Proteomes; UP000070133; Unassembled WGS sequence.
DR   GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IEA:InterPro.
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; PF02731; SKIP_SNW; 1.
PE   3: Inferred from homology;
KW   mRNA processing {ECO:0000256|RuleBase:RU367140};
KW   mRNA splicing {ECO:0000256|RuleBase:RU367140};
KW   Nucleus {ECO:0000256|RuleBase:RU367140};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070133};
KW   Spliceosome {ECO:0000256|RuleBase:RU367140}.
FT   DOMAIN          193..351
FT                   /note="SKI-interacting protein SKIP SNW"
FT                   /evidence="ECO:0000259|Pfam:PF02731"
FT   REGION          1..99
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          171..256
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          311..430
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          497..590
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        208..232
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        311..370
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        371..388
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        389..430
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        574..590
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   590 AA;  65654 MW;  F6F6A2AB6356F09B CRC64;
     MSLAGSRASL LSALPKPKYT GEDEELPTHT QQKGPRVVGA RELESSQLVV KRSGPPPYGQ
     RSGWRPRNVE DFGDGGAFPE VPMAQYPLDM GRKNQPSTSN ALALQVDNEG KVKYDAIARR
     GHGEKRIVHA SFKDLIPLRQ RADVGDISLE RPSEEEVQAS KERTQKALQG LVDGTLAAQK
     PKNVKGTTRP EPTFVRYTPA NQMGDNSKKP DRIMKIVARQ QDPMEPPKHK IKKIPRGPPS
     PPPPVMHSPP RKLTAEDQEA WKIPPPVSNW KNPKGYTVPL DKRLAADGRG LQDVTINDKF
     AQFAEALHTA DRHAREEVQQ RHRMQQRLAE KEKEAQEEHL RQLAMKARED KAAAATQRRG
     ADRGRSRSRS VDSRSSYSSY SSRSGSRSRS RSGGRDGDRD RREREKQRAE RKQEAKREMA
     RKNMGHERKM QMMAREQNRD IGEKVALGLA KPTQSKEAMY DSRLFNQSSG FAAGFNEDQA
     YDKPLFADRD ALNSIYRPTV GDEDDGEDGG ETLEKIQGTK RFDTLGRAPK SGFKGTETAE
     ARSGPVQFER DRGDDPFGIE AGIAAASGGS KRVADDDGGG KSKRARVDDE
//
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