ID R7S3I5_PUNST Unreviewed; 844 AA.
AC R7S3I5;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=mRNA 3'-end-processing protein RNA14 {ECO:0000256|RuleBase:RU369035};
GN ORFNames=PUNSTDRAFT_108487 {ECO:0000313|EMBL:EIN04357.1};
OS Punctularia strigosozonata (strain HHB-11173) (White-rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Corticiales; Punctulariaceae; Punctularia.
OX NCBI_TaxID=741275 {ECO:0000313|EMBL:EIN04357.1, ECO:0000313|Proteomes:UP000054196};
RN [1] {ECO:0000313|Proteomes:UP000054196}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB-11173 SS5 {ECO:0000313|Proteomes:UP000054196};
RX PubMed=22745431; DOI=10.1126/science.1221748;
RA Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT 31 fungal genomes.";
RL Science 336:1715-1719(2012).
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}.
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DR EMBL; JH687555; EIN04357.1; -; Genomic_DNA.
DR RefSeq; XP_007388500.1; XM_007388438.1.
DR AlphaFoldDB; R7S3I5; -.
DR GeneID; 18876168; -.
DR KEGG; psq:PUNSTDRAFT_108487; -.
DR eggNOG; KOG1914; Eukaryota.
DR HOGENOM; CLU_007630_0_0_1; -.
DR OMA; VQLWSVY; -.
DR OrthoDB; 23291at2759; -.
DR Proteomes; UP000054196; 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; -; 2.
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:UP000054196}.
FT DOMAIN 476..804
FT /note="Suppressor of forked"
FT /evidence="ECO:0000259|Pfam:PF05843"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 418..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 645..764
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 804..844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..457
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..661
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 676..736
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 750..764
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 809..834
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 844 AA; 95651 MW; 19F23639DC268A88 CRC64;
MLQDHSVLAS SQNSERIDSP ATSQQLQHSQ QDPSQSPWDV LFARLKDHPH NPEGWKKLVD
LAEAPGPNGV VQLDRVKATY DRLLETYPNT AGAQIAYINH YMQNGQQATV EQLFKRFLPT
SPAVELWRHY IGYVRRLHSG SDPGARKIVA DSYEYALRHI GQDKDAGEMW ADYVTFLKMA
QPTTPREEQE KNDAIRKAYH RAVKIPLENV ERLWSELESF ENGLNRTTAQ KFMTDLRPEH
MQARSVLRTL RGHLATLLPP PPPSGVSGRT SVWLPSVPTF DPAQRALVGA WKAYLKWEES
NPLALEEKDR AVLEARLRGV YRKAVVRMRY FGEIWFMAYT WAKGLTTGKQ DEPITWLEAG
IKANPASFLL NFAYAEAMEL KGDFAKVRTT FETFLNVLRA DLDSLKARID AVYPPAANGA
AAGADTTLAT DPNTSVGANT TMNSQNTQSS QGSTTSTPDE ESKRKELAEK RTEYGLVYIM
YMRFSRRAEG QMPWRLIFKK ARQDSWTPWE VYEAAALMEY HCSKDVAVAG RIFEKGEELF
GDEIEFVTRH LGFLISINDQ NNADALFKKA VTKFPADRAR PLWERWARYV YQFGDLPSSQ
ELERRFAEVY PNDPPIKRFA QRHIYLGTDA IAARDLGFAI ARQNNLSSNS SGSSVGKANP
DASSASMAPP PAKRGASPDG RRRDEPPPAK RQRGSPPPRD RERERERERE RERMERERDR
ERLERDRERE RERRAALAQM PPPPARRYAS PAGRERDHGK PHREVHVPPV ISWFVGTLPP
PAAFDGPVFK TDDLMSLFRN AIIPSSNSSS AGPPPPPLRD ASPHGMPPRR ARPPPDYTLG
GRRW
//