CFT1_NEUCR
ID CFT1_NEUCR Reviewed; 1487 AA.
AC Q7SEY2;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-MAR-2014, sequence version 3.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Protein cft1;
DE AltName: Full=Cleavage factor two protein 1;
DE AltName: Full=Polyadenylation factor 3;
GN Name=paa-3; Synonyms=cft1; ORFNames=NCU02082;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
CC -!- FUNCTION: RNA-binding component of the cleavage and polyadenylation
CC factor (CPF) complex, which plays a key role in polyadenylation-
CC dependent pre-mRNA 3'-end formation and cooperates with cleavage
CC factors including the CFIA complex and hrp1/CFIB. Involved in poly(A)
CC site recognition. May be involved in coupling transcription termination
CC and mRNA 3'-end formation (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CFT1 family. {ECO:0000305}.
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DR EMBL; CM002236; EAA35373.3; -; Genomic_DNA.
DR RefSeq; XP_964609.3; XM_959516.3.
DR AlphaFoldDB; Q7SEY2; -.
DR SMR; Q7SEY2; -.
DR STRING; 5141.EFNCRP00000001333; -.
DR EnsemblFungi; EAA35373; EAA35373; NCU02082.
DR GeneID; 3880749; -.
DR KEGG; ncr:NCU02082; -.
DR VEuPathDB; FungiDB:NCU02082; -.
DR HOGENOM; CLU_002414_2_1_1; -.
DR InParanoid; Q7SEY2; -.
DR Proteomes; UP000001805; Chromosome 1, Linkage Group I.
DR GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006378; P:mRNA polyadenylation; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR004871; Cleavage/polyA-sp_fac_asu_C.
DR InterPro; IPR018846; Cleavage/polyA-sp_fac_asu_N.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR Pfam; PF03178; CPSF_A; 1.
DR Pfam; PF10433; MMS1_N; 1.
PE 3: Inferred from homology;
KW mRNA processing; Nucleus; Reference proteome; RNA-binding.
FT CHAIN 1..1487
FT /note="Protein cft1"
FT /id="PRO_0000290633"
FT REGION 486..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..506
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1487 AA; 160921 MW; 9158CA575E0EEF6A CRC64;
MQCYTELTPP TAVTHSVTLQ LVPGQGTNLA VAKASLLQIF KTKVVSAEID TYATLNGTNT
SSKAAAAGRY DSRLVNDDDG FEASFLGGDN IAARADRANS AKLVLVAEVT LPGTMTGLAR
IKKPSGSSSG GADCLLLSFR DARLSLVEWN VERNTLETVS IHYYEKEELV GSPWVAPLHQ
YPTLLVADPA SRCAALKFSE RNLAILPFKQ PDEDMDMDNW DEELDGPRPK KDLSGAVANG
ASTIEDTPYS PSFVLRLSKL EASLLHPVHL AFLHEYRDPT IGVLSSTKTA SNSLGHKDHF
TYMVFTLDLQ QRASTTILAV NGLPQDLFRV VALPAPVGGA LLVGANELIH IDQSGKSNGI
AVNPLTKQTT SFSLVDQADL DLRLEGCAID VLAAELGEFL LILNDGRLGL ITFRIDGRTV
SGLSIKMIAP EAGGSVIQSR VTSLSRMGRS TMFVGSEEGD SVLLGWTRRQ GQTQKRKSRL
QDADLDLDLD DEDLEDDDDD DLYGEESASP EQAMSAAKAI KSGDLNFRIH DRLLSIAPIQ
KMTYGQPVTL PDSEEERNSE GVRSDLQLVC AVGRGKASAL AIMNLAIQPK IIGRFEFPEA
RGFWTVCAKK PIPKTLVGDK GPMNNDYDTS GQYHKFMIVA KVDLDGYETS DVYALTAAGF
ESLTGTEFEP AAGFTVEAGT MGKDSRILQV LKSEVRCYDG DLGLSQIVPM LDEETGAEPR
VRTASIADPF LLLIRDDFSV FIAEMSPKLL ELEEVEKEDQ ILTSTKWLAG CLYTDTSGVF
ADETVGKGTK DNILMFLLST SGVLYIYRLP DLTKPVYVAE GLSYIPPGLS ADYAARKGTA
KESVAEILVA DLGDTTHKSP YLILRHANDD LTLYQPYRLK ATAGQPFSKS LFFQKVPNST
FAKAPEEKPA DDDEPHNAQR FLPMRRCSNI SGYSTVFLPG SSPSFILKTA KSSPRVLSLQ
GSGVQAMSSF HTEGCEHGFI YADTNGIARV TQIPTDSSYA ELGLSVKKIP IGVDTQSVAY
HPPTQAYVVG CNDVEPFELP KDDDYHKEWA RENITFKPMV DRGVLKLLSG ITWTVIDTVE
MEPCETVLCV ETLNLEVSES TNERKQLIAV GTALIKGEDL PTRGRVYVFD IADVIPEPGK
PETSKKLKLV AKEDIPRGAV TALSEVGTQG LMLVAQGQKC MVRGLKEDGT LLPVAFMDMN
CYVTSVKELP GTGLCLMADA FKGVWFTGYT EEPYKMMLFG KSSTRMEVLN ADFLPDGKEL
YIVASDADGH IHILQFDPEH PKSLQGHLLL HRTTFNTGAH HPTSSLLLPA VYPNPSSLSS
NSEENSPHIL LLASPTGVLA TLRPLQENAY RRLSSLAVQL TNGLPHPAGL NPKGYRLPSP
SASASMQLPG VDAGIGRNIV DGKILERFLE LGTGKRQEMA GRAGYVVGTG AHGVNPAGSG
KMMGGGGGLS LGGLRLNGLH GQEGGMEWEE VRGELGVVLG WSGLGYF