ID A8P7L9_COPC7 Unreviewed; 857 AA.
AC A8P7L9;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 2.
DT 24-JAN-2024, entry version 66.
DE RecName: Full=mRNA 3'-end-processing protein RNA14 {ECO:0000256|RuleBase:RU369035};
GN ORFNames=CC1G_11088 {ECO:0000313|EMBL:EAU82402.2};
OS Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003)
OS (Inky cap fungus) (Hormographiella aspergillata).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Psathyrellaceae; Coprinopsis.
OX NCBI_TaxID=240176 {ECO:0000313|EMBL:EAU82402.2, ECO:0000313|Proteomes:UP000001861};
RN [1] {ECO:0000313|EMBL:EAU82402.2, ECO:0000313|Proteomes:UP000001861}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003
RC {ECO:0000313|Proteomes:UP000001861};
RX PubMed=20547848; DOI=10.1073/pnas.1003391107;
RA Stajich J.E., Wilke S.K., Ahren D., Au C.H., Birren B.W., Borodovsky M.,
RA Burns C., Canback B., Casselton L.A., Cheng C.K., Deng J., Dietrich F.S.,
RA Fargo D.C., Farman M.L., Gathman A.C., Goldberg J., Guigo R., Hoegger P.J.,
RA Hooker J.B., Huggins A., James T.Y., Kamada T., Kilaru S., Kodira C.,
RA Kues U., Kupfer D., Kwan H.S., Lomsadze A., Li W., Lilly W.W., Ma L.J.,
RA Mackey A.J., Manning G., Martin F., Muraguchi H., Natvig D.O.,
RA Palmerini H., Ramesh M.A., Rehmeyer C.J., Roe B.A., Shenoy N., Stanke M.,
RA Ter-Hovhannisyan V., Tunlid A., Velagapudi R., Vision T.J., Zeng Q.,
RA Zolan M.E., Pukkila P.J.;
RT "Insights into evolution of multicellular fungi from the assembled
RT chromosomes of the mushroom Coprinopsis cinerea (Coprinus cinereus).";
RL Proc. Natl. Acad. Sci. U.S.A. 107:11889-11894(2010).
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|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:EAU82402.2}.
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DR EMBL; AACS02000005; EAU82402.2; -; Genomic_DNA.
DR RefSeq; XP_001839388.2; XM_001839336.2.
DR AlphaFoldDB; A8P7L9; -.
DR STRING; 240176.A8P7L9; -.
DR GeneID; 6016002; -.
DR KEGG; cci:CC1G_11088; -.
DR VEuPathDB; FungiDB:CC1G_11088; -.
DR eggNOG; KOG1914; Eukaryota.
DR HOGENOM; CLU_007630_0_0_1; -.
DR InParanoid; A8P7L9; -.
DR OMA; VQLWSVY; -.
DR OrthoDB; 23291at2759; -.
DR Proteomes; UP000001861; 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; 7.
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:UP000001861}.
FT DOMAIN 447..796
FT /note="Suppressor of forked"
FT /evidence="ECO:0000259|Pfam:PF05843"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 615..774
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 792..857
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 615..639
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 652..735
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 857 AA; 96650 MW; 61F57451FA2C648B CRC64;
MDEPQNDEHS FQGEATQPTE EIIAALNASN ASEQSNPPQS EFDGLFSKLS ENPYDPDGWR
RLIDLANESG EITKIQQAYN ELLKHYPNTS AAQIAYINHF LNKEDTFTEA EQLFIKFLRT
SPSVDLWKFY LTYVRRRNVG PATRDIVRKS YEFALQHVGQ DKESGEIWND YIQFLKAGET
SSTWEEQQKM DALRKVYHRA VQIPLDNVER LWSELETFEM NLNKITAKKF MSDLSPAHMQ
ARTTLRQLSN HMNGLYPPSS SNNDLFLPSQ PKFDAAERSL VGKWKAYLKW EESNPLELED
KDKQTFITRL QGVYRKAVIR MRFYAEIWFM AYTWTNSVGK TDEALAILKA GMEAVPSSFL
LTFAYAEAME LKKDFAEVHS AYEKLLSVLV KELEALEKST ANANTNGTQQ NGSNPNNTND
TSFNSQSSDD KPPKNSELQE KRTEYGLVYI MYMRFARRTE GLAALRRVFA KARRDRFSPW
EVYEACALME YHCFDDKNVA SRIFEKGLEQ FGDEIDYVLR YLGFLISIND GNNARALFER
VITTFSPERA RPLWERWARY EYQYGDLESA LKLEKRIAEV YPTDPPIKRF AQRHMYLGTD
AIAARDLGFS MAKRAGTSAS SSNNSLGRTE TSGSLLTGLG PSNAAKRPAS PDNYRNPKRD
DKGGDYGAGH KRARGPASPA REREIPPPRD RDRDVQMRDR DRGDRGDRWN DRGRRGSPGP
GGWDRDRDDR DGGRGRGGPA GGGRDGGRDY PRGPPEPQIP PLVSWFMGEL PPAASFDGPI
FKTDDLMKAF KQAQIPAAAP AGGHGGPAAP MGPPHSTAGR NRSPAPTYPQ HRGGGRPPPD
YGPYQGPGGG RAAGRRY
//
