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Database: UniProt
Entry: A0A094C098_9PEZI
LinkDB: A0A094C098_9PEZI
Original site: A0A094C098_9PEZI 
ID   A0A094C098_9PEZI        Unreviewed;      1032 AA.
AC   A0A094C098;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   22-FEB-2023, entry version 32.
DE   RecName: Full=mRNA 3'-end-processing protein RNA14 {ECO:0000256|RuleBase:RU369035};
GN   ORFNames=V492_01589 {ECO:0000313|EMBL:KFY16072.1};
OS   Pseudogymnoascus sp. VKM F-4246.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420902 {ECO:0000313|EMBL:KFY16072.1, ECO:0000313|Proteomes:UP000029299};
RN   [1] {ECO:0000313|EMBL:KFY16072.1, ECO:0000313|Proteomes:UP000029299}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4246 {ECO:0000313|EMBL:KFY16072.1,
RC   ECO:0000313|Proteomes:UP000029299};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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:KFY16072.1}.
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DR   EMBL; JPJU01000412; KFY16072.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094C098; -.
DR   STRING; 1420902.A0A094C098; -.
DR   HOGENOM; CLU_007630_1_1_1; -.
DR   Proteomes; UP000029299; 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; 6.
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:UP000029299}.
FT   DOMAIN          691..1016
FT                   /note="Suppressor of forked"
FT                   /evidence="ECO:0000259|Pfam:PF05843"
FT   REGION          51..242
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          879..972
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        51..78
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        79..93
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        115..131
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        165..180
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        194..233
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        924..941
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1032 AA;  115815 MW;  0B7FE5A964329299 CRC64;
     MISSLPQTKA VSANKQQALN YLPYLFTYPF EDTSESMAEE DAEIALLHQM QSGQESVSWG
     QGTDDTEEGV GATNTENSDQ PVKEEEKDFS DDQVLRALSP SDALSDGEEY NPESANPVPS
     HTTTSLAGTG PPSRASPARK PKTIGGFLAD DSDDEDDVEI ATSKSELLQP PTNGPTRSVS
     KSPLHLEAVP QDSAAQTPVP NVDTPNALGD GEQTSGGVSN QAFTPNVPAT ATAPISGASL
     PKARLPHDRV GILEDRIKED PRGDLDAWLS LITEHRNRNK LDDARVVYDR FFKVFPMAAD
     IWVAYAEMEL GIDNFFAAEQ IFGKSLLTVP HVQLWSVYLN YIRRRNDLTN DVTGSARATI
     SQAYDFVLAN VGIDRDSGKI WQEYIQFIRS APGQIGGSSW QDQQKMDQMR KAYQRAVCVP
     MSNVNALWKE YDQFEMSLNK ITGRKFLQEK SPSYMTARSA NTAMENITRN LVRTNLPRLP
     PALGFEGDTE YLEQVGLWRQ WINWEQEDPL VFKDEDIQAY KQRIVYVYKH AVMALRFWPE
     IWVEAAEWSF NNGMDKEGND FLSQGIAANP ESCLLAFKQA DRLETVLPME EGEEGLASRG
     AAVRAPYNTL LDALYDLIKK LKSRENAELA RIQESAMLDS SINSALDRAD DDEDDTDRLL
     KEAKESARDN QLKAVKQGYH MQSELTQRTL SFAWIALMRA MRRVQGKGKV GAAVGGSRQI
     LSDARVKGKI LSDVYIASAL IEHNVYKDPA GTKIFEKGAK LFPEDDVFIL EYLKHLLSIG
     DTTNARAVFE TSVNRLTQKP ETVSKAKPLY IFFHKYESDY GELSQINRLE QRMADLFPED
     QRLARFSSRY SSERFDPTVV RLIISPVAQM RPKSIMQSIE EPISVQPSPR PQYREISPRP
     QPRQEVNPIP AYLQPTNSPK RPLGGEESDN ESGRPRKLVR GESPLKGAAG RRLDQQKRMQ
     QTHGGVQQWQ SNGPAQFMIP RDITFLLSII PRAETYNATL FNAEAMVRLL DKTPIPDYST
     WKASRDQAPR YY
//
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