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Database: UniProt
Entry: A0A135LIT2_PENPA
LinkDB: A0A135LIT2_PENPA
Original site: A0A135LIT2_PENPA 
ID   A0A135LIT2_PENPA        Unreviewed;      1016 AA.
AC   A0A135LIT2;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   03-MAY-2023, entry version 25.
DE   RecName: Full=mRNA 3'-end-processing protein RNA14 {ECO:0000256|RuleBase:RU369035};
GN   ORFNames=PGRI_027190 {ECO:0000313|EMBL:KXG48849.1};
OS   Penicillium patulum (Penicillium griseofulvum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=5078 {ECO:0000313|EMBL:KXG48849.1, ECO:0000313|Proteomes:UP000070168};
RN   [1] {ECO:0000313|EMBL:KXG48849.1, ECO:0000313|Proteomes:UP000070168}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PG3 {ECO:0000313|EMBL:KXG48849.1,
RC   ECO:0000313|Proteomes:UP000070168};
RX   PubMed=26729047; DOI=10.1186/s12864-015-2347-x;
RA   Banani H., Marcet-Houben M., Ballester A.R., Abbruscato P.,
RA   Gonzalez-Candelas L., Gabaldon T., Spadaro D.;
RT   "Genome sequencing and secondary metabolism of the postharvest pathogen
RT   Penicillium griseofulvum.";
RL   BMC Genomics 17:19-19(2016).
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:KXG48849.1}.
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DR   EMBL; LHQR01000065; KXG48849.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A135LIT2; -.
DR   STRING; 5078.A0A135LIT2; -.
DR   OMA; VQLWSVY; -.
DR   OrthoDB; 23291at2759; -.
DR   Proteomes; UP000070168; 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:UP000070168}.
FT   DOMAIN          684..986
FT                   /note="Suppressor of forked"
FT                   /evidence="ECO:0000259|Pfam:PF05843"
FT   REGION          1..251
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          635..658
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          860..947
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          996..1016
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        11..25
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        92..108
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        165..242
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        860..893
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        894..912
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        925..944
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1016 AA;  113381 MW;  EBB2D86E2A0EF4CF CRC64;
     MADDEAENAF FQAQALNTDS QPPIEEQEGD NSDAESDDYD PSLALGDQYS ASFSESKQPD
     AGLADPSPSD ETDDSIPNPT VTSDADVAPD VNADASQTSD SPDLSQNPPP AQSSTPVPAS
     AAEAQPKTRT IGGFEVDEDE DDEGDAEYEP PAVLGGEDVT AMPVTMSEDP SSGNAMQNTS
     PDVSSHQAEQ GPASGPAANS SYSPVPVPNI DPSSVPGQSH WSAQELQSAT MQNSTVPTSV
     PDSPASKGRL AHDRVGMLED RIREDPRGDI PAWLELIAEH RGRSRLDSAR ETYERFLKLF
     PMAADQWVAY ATMESELNEF FRLEQIFNRT LLTTPSVQLW SVYLDYIRRR NPLTSDEARK
     TISSAYDMAI QYVGMDKDSG NIWTDYIEFI RSGPGIVGGS GWQDQQKMDL LRKAYQRAIG
     VPTQAVNTLW KEYDQFEMNL NKLTGRKFLQ EHSPSYMTAR SSYTELQNIT RDLIRTSLPP
     MPPVPGSEGD VEFATQVDIW KRWIAWEKED PLVLKEDDPA AYKSRVVYFY KQALMALTFL
     PEMWFDAAEF CFLNDMEDAG TEFLKNGIDA NPESCLLTFK RADRLEVTSD SEHDSAKRAA
     KVREPYDKLL NALYDLINKA RDQETQDVSR IEAYYTPQNV EGQPQSEDEG DPEAKEREAA
     KTAQIDAVRK AHSVQINIIS KTLSFAWISL MRSMRRIQGK GKPGEVAGSR QIFAEARRRG
     RITSDVYIAS ALMEYHCYKD PAATKIFERG AKLFPEDEHF ALEYLKHLLD INDTINARAV
     FETTVRKLTS NPENVQKAKP IFSFLHEYES RYGDLTQVIN LENRMRELYP ADPTLDQFAN
     RYSDSTFDPT SVRLILSPSQ TRPKTTMPGI STETHGSPMA RYMDTSLNSP KRSYPTDDYD
     EDSGRPRKFV RAESPMKSVQ ARRLDQPKRV QQLNGQSTSY RPQGSPAPLP REVVNLLSIL
     PSAAAYNITR LSPEKTIDLL RHIDIPSDIS QIQIPQAVHG SGGGQTPGMN PYSGYR
//
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