ID A0A2H3IHD3_9EURO Unreviewed; 1379 AA.
AC A0A2H3IHD3;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=PENO1_083050 {ECO:0000313|EMBL:PCG93544.1};
OS Penicillium occitanis (nom. inval.).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=290292 {ECO:0000313|EMBL:PCG93544.1, ECO:0000313|Proteomes:UP000218381};
RN [1] {ECO:0000313|EMBL:PCG93544.1, ECO:0000313|Proteomes:UP000218381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL100 {ECO:0000313|EMBL:PCG93544.1,
RC ECO:0000313|Proteomes:UP000218381};
RX PubMed=28951729; DOI=10.3389/fmicb.2017.01627;
RA Bravo-Ruiz G., Sassi A.H., Marcet-Houben M., Di Pietro A., Gargouri A.,
RA Gabaldon T., Roncero M.I.G.;
RT "Regulatory Mechanisms of a Highly Pectinolytic Mutant of Penicillium
RT occitanis and Functional Analysis of a Candidate Gene in the Plant Pathogen
RT Fusarium oxysporum.";
RL Front. Microbiol. 8:1627-1627(2017).
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 -!- 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:PCG93544.1}.
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DR EMBL; NPFK01000313; PCG93544.1; -; Genomic_DNA.
DR STRING; 290292.A0A2H3IHD3; -.
DR OrthoDB; 149432at2759; -.
DR Proteomes; UP000218381; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR Gene3D; 1.10.150.910; -; 1.
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:UP000218381}.
FT DOMAIN 97..701
FT /note="Cleavage/polyadenylation specificity factor A
FT subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10433"
FT DOMAIN 1004..1344
FT /note="Cleavage/polyadenylation specificity factor A
FT subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03178"
FT REGION 184..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..212
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1379 AA; 150174 MW; 2B3EB393EB4C4A65 CRC64;
MQCYTEVLPP SGVTHAVSAP FTSATAQNLI VVKTSLLQIY TLVTERATAS LPENGQQAAE
GVKNEATKLH LQAEYDLYGT VTDISPVKIL KSRSGGDALL LSFRNAKLSL IEWNPETQGI
STVSIHYYEK EDITLSPWVP DLSQCDSHLT VDPSSRCALL NFGVRNLAIL PFHQTGDELV
MDEYDPDMDM DDFTTQEENK KPSTDSKRTD GDHQTPYAAS FVLPLTALDP TLIHPIGLTF
LHEYREPTFG ILYSPIATSA ALLEERKDVV VYSVFTLDLE QRASTPLLSI AKLPSDLLHI
MALPAPVGGA LLIGPNELIH IDQSGKASAV AVNEFAKQVS AFPMVDQSDL GLRLEGSVVE
VINNESGDIL LTLSTGELVL IHFKIDGRSV SGFVVSPIPA VSGGDAVSAA ASCAVALGSG
KVFIGSEDAE SVLLDCYVPS AASKKSKKDD RYHFDEEMND EEDDDIYEDD LYSSAPKEAV
DKAVSDGKAS ESYTFKAIDR LLSLGPLRAV TVGKPASRDS DVTDAQQSVN DLELAAAYGS
GRSGGVALLQ RTLHLDNVFI LDGEPADSVW NIHTSNTTPG HGNSDEANPS YVIVARANPP
ENEETVVYAV NEGNLELFNA PDVNPNGDST IDIGTLAGNS RVVQVLTGEV RIYDTNLGMA
QIYPVWDEDE GDERIAVSAS FADPYLLIIR DDSSVLLLHS DESGDLDELT KPETVSSQSW
LCGCVYTDKH GVFEEGSTTE TTYMFLLNRE CKLFVFRLPT MEVVSVTEGV DYVSSILSPD
PPTRRLNSRE TIAELLVADL GELPTVSPYL IIRTATDDLI IYKPFRESSN EEKSGSLKYI
KETNHFLPKV PLEAATSASQ QRTPGLRRLS DIGGYSAVVM SGASPSLIVR TSKSLPHVHS
IQNDFIRGIS SFDSVGCEKG LVYVDNERVI RTCQLHNNTQ LDFSWPIRRI PLNEQVDHLA
YSTASGTYVV GTTLEQDFKL PDDDELHPEW ATEEISLPPK VAHGSIKLLN PKTWKVIDSH
TFGPAERITA VENINLEISE KTGKRKDMIV VGTTYAKGED IAARGNLYVF DVIDVVPDPD
EPGTNLKLKL IGEESIRGAV TAVSGIGGQG FMIVAQGQKC MVRGLKDDGS LLPVAFIDVQ
CYVSVIKELK GTGMCLIGDA LKGLWFTGYS EEPYKMTLFG KDLDELEVVT ADFLPDGKKL
YILVADSDCN LHVLQYDPED PKSSNGDRLL NRCKFHMGHF ASTLTLLPRT AVSSELAIMS
SDTMDIDSYT PLHQALITTQ SGSMALVTSL SEESYRRLSA LQSQLSNTLE HPCGLNPRAY
RAVESDGVVG RGMIDGKLLM RWLDLSRSRK LEIAGRVGAD EWEIRADLEA VSGAGLGYL
//
