ID A0A0A2L176_PENIT Unreviewed; 1038 AA.
AC A0A0A2L176;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 03-MAY-2023, entry version 32.
DE RecName: Full=mRNA 3'-end-processing protein RNA14 {ECO:0000256|RuleBase:RU369035};
GN ORFNames=PITC_061860 {ECO:0000313|EMBL:KGO72958.1};
OS Penicillium italicum (Blue mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=40296 {ECO:0000313|EMBL:KGO72958.1, ECO:0000313|Proteomes:UP000030104};
RN [1] {ECO:0000313|EMBL:KGO72958.1, ECO:0000313|Proteomes:UP000030104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHI-1 {ECO:0000313|EMBL:KGO72958.1,
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 -!- FUNCTION: Component of the cleavage factor IA (CFIA) complex, which is
CC involved in the endonucleolytic cleavage during polyadenylation-
CC dependent pre-mRNA 3'-end formation. {ECO:0000256|ARBA:ARBA00002863,
CC ECO:0000256|RuleBase:RU369035}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU369035}.
CC Cytoplasm {ECO:0000256|RuleBase:RU369035}. Note=Nucleus and/or
CC cytoplasm. {ECO:0000256|RuleBase:RU369035}.
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:KGO72958.1}.
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DR EMBL; JQGA01000847; KGO72958.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2L176; -.
DR STRING; 40296.A0A0A2L176; -.
DR HOGENOM; CLU_007630_1_1_1; -.
DR OMA; VQLWSVY; -.
DR OrthoDB; 23291at2759; -.
DR PhylomeDB; A0A0A2L176; -.
DR Proteomes; UP000030104; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0006378; P:mRNA polyadenylation; IEA:UniProtKB-UniRule.
DR Gene3D; 1.25.40.1040; -; 1.
DR InterPro; IPR003107; HAT.
DR InterPro; IPR045243; Rna14-like.
DR InterPro; IPR008847; Suf.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR19980:SF0; CLEAVAGE STIMULATION FACTOR SUBUNIT 3; 1.
DR PANTHER; PTHR19980; RNA CLEAVAGE STIMULATION FACTOR; 1.
DR Pfam; PF05843; Suf; 1.
DR SMART; SM00386; HAT; 5.
DR SUPFAM; SSF48452; TPR-like; 2.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|RuleBase:RU369035};
KW mRNA processing {ECO:0000256|RuleBase:RU369035};
KW Nucleus {ECO:0000256|RuleBase:RU369035};
KW Reference proteome {ECO:0000313|Proteomes:UP000030104}.
FT DOMAIN 686..988
FT /note="Suppressor of forked"
FT /evidence="ECO:0000259|Pfam:PF05843"
FT REGION 1..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 638..659
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 887..949
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 896..914
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 927..946
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1038 AA; 115805 MW; 57B1E8147D9F367B CRC64;
MADDEAEAAF FQAQALNTDS QSPTVEQEGD NSEAESDDYD PSLALGDQFS VSLPETKQPD
AGSADAAPSD ETEHSIPNPT VASDADVASD VEAGQTSDSP DPSQNPSRVE SSTPVPASAA
EAQPKTRTIG GFEVDDDEDD EGDAEYEPPA VLGGEDVNAM PVTMSEDPNS GDAMQNTSPN
VSSHQAEQTP ASGPDVANSS YSPDLVLNID PSSVPGQSHW AAQDLQSATM QNSTVPTSVP
DSPASKGRLA HDRVGLLEDR IREDPRGDIP AWLELIAEHR GRNRLDSARE TYERFLKLFP
MAADQWVAYA SMESELNEFF RLEQIFNRTL LTTPSVQLWS VYLDYIRRRN PLTTDASGEA
RKTISSAYDM AIQYVGMDKD SGNIWTDYIE FIRSGPGIVG GSGWQDQQKM DLLRKAYQRA
IGVPTQAVNT LWKEYDQFEM NLNKLTGRKF LQEHSPSYMT ARSSYTELQN ITRNLIRTSL
PPLPPVPGSE GDVEYSAQAD IWKRWIAWEK EDPLVLKEED LAAYKSRVVY FYKQALMALA
FLPEMWFDAA EFCFLNDMED AGTEFLKNGI DANPESCLLT FKRADRLEVT SDSEQDSAKR
AAKVREPYDK LLDALYELIN KARNQETQDV SRIEAYFAPQ NAESQPQNED EDDPEAKQRE
AAKIAQIDAV RKAHSVQINI ISKTVSFAWI SLMRSMRRIQ GKGKPGEMAG SRQIFAEARR
RGRITSDVYI ASALMEYHCY KDPAATKIFE RGAKLFPEDE HFALEYLKHL LDINDTINAR
AVFETTVRKL TSNPENVHKA KPIFSFLHEY EFRYGDLTQV INLENRMREL YPEDPALEQF
ANRYSNTNFD PTSVQLILSP SQTKPKTTMP GIPAEPHGSP MARYMDTSLN SPKRPYPTDE
YDEDSGRPRK FVRAESPMKS AQARRLDQPK RVQQLNGQTT SYRPQGSPAP LPREVVNLLS
ILPSAAAYNI TRLSPEKMID LLRHVEVPSD ISQIQIPQTA HGPGGGQTPG LNPYSGKIIV
YLSHNNTLTH MSSPGGYR
//
