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Database: UniProt
Entry: R7S3I5_PUNST
LinkDB: R7S3I5_PUNST
Original site: R7S3I5_PUNST 
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
//
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