ID A0A0D1ZWJ2_9EURO Unreviewed; 1359 AA.
AC A0A0D1ZWJ2;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Protein CFT1 {ECO:0000256|ARBA:ARBA00039443};
DE AltName: Full=Cleavage factor two protein 1 {ECO:0000256|ARBA:ARBA00041264};
DE AltName: Full=Protein cft1 {ECO:0000256|ARBA:ARBA00039187};
GN ORFNames=PV08_04228 {ECO:0000313|EMBL:KIW17037.1};
OS Exophiala spinifera.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=91928 {ECO:0000313|EMBL:KIW17037.1, ECO:0000313|Proteomes:UP000053328};
RN [1] {ECO:0000313|EMBL:KIW17037.1, ECO:0000313|Proteomes:UP000053328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 89968 {ECO:0000313|EMBL:KIW17037.1,
RC ECO:0000313|Proteomes:UP000053328};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala spinifera CBS89968.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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 NAB4/CFIB. Involved in poly(A)
CC site recognition. May be involved in coupling transcription termination
CC and mRNA 3'-end formation. {ECO:0000256|ARBA:ARBA00037232}.
CC -!- SIMILARITY: Belongs to the CFT1 family.
CC {ECO:0000256|ARBA:ARBA00038304}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KN847494; KIW17037.1; -; Genomic_DNA.
DR RefSeq; XP_016237253.1; XM_016378576.1.
DR STRING; 91928.A0A0D1ZWJ2; -.
DR GeneID; 27331311; -.
DR VEuPathDB; FungiDB:PV08_04228; -.
DR HOGENOM; CLU_002414_2_1_1; -.
DR OrthoDB; 149432at2759; -.
DR Proteomes; UP000053328; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 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 PANTHER; PTHR10644:SF2; CLEAVAGE AND POLYADENYLATION SPECIFICITY FACTOR SUBUNIT 1; 1.
DR PANTHER; PTHR10644; DNA REPAIR/RNA PROCESSING CPSF FAMILY; 1.
DR Pfam; PF03178; CPSF_A; 1.
DR Pfam; PF10433; MMS1_N; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000053328}.
FT DOMAIN 89..683
FT /note="Cleavage/polyadenylation specificity factor A
FT subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10433"
FT DOMAIN 981..1323
FT /note="Cleavage/polyadenylation specificity factor A
FT subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03178"
FT REGION 169..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 424..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 487..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..450
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..503
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1359 AA; 148275 MW; 7D559CBCB4712639 CRC64;
MQCYTELLPP SGVTHSLSAS FTSAKAENLI VARTSLLQVF QYKHLDHGTK LILVAEYNLA
GTVTSLGKVR TADSKSGGDA VLVAFLDAKL SLIEWDPTLH SISTLSIHYY EQHDIQSAPW
QPDLADCVSR LSIDPSSRCA AYNFGVSNLA IIPFHQTGDD LAMDDFDDLD HDEKGHHTPT
KNPDGTMNGH SSPYSPSFVL PLTVLDPGLF HPVDIAFLHE YRDPTIGIVY STMARSSNMS
AERRDVTIYA VYALDLDQKA STTLQSVQKL PNDIYCILAL PPPVGGALLV GGNELIHVDQ
GGKASAVAVN EFAKDASSFP MTDHSEYRLK LEGCRIEHLG NAAGDMLIIL STGDLVLLTF
RMDGRSVTGI SLRRIAEGQM QGLQLNAASC TANLGPSCLF IGGEDCDSVV VSLARKSGQL
KRVQSRIKSE TDGFEPDGDE DDLDDEDDLY GEIYSGANGH NSADASGQNL RVMDRLPSIA
PINSFALGSK KRKRDDTDTS EESQSQQHEL AVAYGKGHAG GIAFLSRQLT PKVTKRFKFE
GANGLWCLAS KQAPSEGGQT LDDLVIVSQY TSEGLGLSSL CRLNGGNLDP VPDSEFDEMA
GPTVSISQLH TSGHTIQVLP TEIRVYDSKF ALSQIFPIVD EDDGQLAKAV KTTFAEPYLA
VIRDDRVMTL LKADKAGELD EVELPEMLQD KAVLSASLYQ DHHDFFQTSR FYDNAGSPGP
ILSIFTTDGH FCLLSLPNIS LRVFQCDSLP FLPTYLMQDL QIPKHWRNKD DIGEILLADL
GNMTDRRPFL AVRNLTGDVI LYEPFAIPDI AGSFKFRKVM TKSAEDLDDQ GEEEGEESSL
GPMQVVPNVG SRAAIFVPGA HSWIILREAS TLPRVYELNL PGTNSLVGAH TPLCPQGLAF
LDGQQHVCFG QLPDSTMIGQ SDWSVNRVPL GQDISSIAYF EPSDSYVLAI NYGIDFQLPQ
DDEWHPEWQT ETTSFLPSSI QSSLKLMSSV SHSIISQYHF DACERVLCVK TLNLEISEET
HERKDMIVVG TAIVKGENVT TRGNIYIFDV VDVVPEPGVA ESDLKLKLIT KEDVRGAVSA
ICDIGSQGFL LAAQGQKCMV RGLKEDMSIL PVAFLDMRYY VHVAKELRGT GLCILGDAFS
GLWLTGYSEE PYKLQIIGRD LENPPVLAAE FLPDGKQLFI VSADEDGTLR VLQYDPENPK
AERGTKLLLR STFNAGTLPT QMSLLPPRTT GAVVAGGDAD MDLDGGGRMA NFSRILVATQ
SGSLCMITPL PESAYRRLST LQNTLLATLD FQPCSLNPRA YRKVETDGIG GRGIIDGNLV
KRWWETSTQQ RVASADKAGG SVWEVRADME LISGGDLTF
//