ID J9VFW9_CRYNH Unreviewed; 1066 AA.
AC J9VFW9;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 22-FEB-2023, entry version 48.
DE RecName: Full=mRNA 3'-end-processing protein RNA14 {ECO:0000256|RuleBase:RU369035};
GN ORFNames=CNAG_03761 {ECO:0000313|EMBL:AFR93267.1};
OS Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 /
OS CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=235443 {ECO:0000313|EMBL:AFR93267.1, ECO:0000313|Proteomes:UP000010091};
RN [1] {ECO:0000313|EMBL:AFR93267.1, ECO:0000313|Proteomes:UP000010091}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H99 / ATCC 208821 / CBS 10515 / FGSC 9487
RC {ECO:0000313|Proteomes:UP000010091};
RX PubMed=24743168; DOI=10.1371/journal.pgen.1004261;
RA Janbon G., Ormerod K.L., Paulet D., Byrnes E.J.III., Yadav V.,
RA Chatterjee G., Mullapudi N., Hon C.C., Billmyre R.B., Brunel F., Bahn Y.S.,
RA Chen W., Chen Y., Chow E.W., Coppee J.Y., Floyd-Averette A., Gaillardin C.,
RA Gerik K.J., Goldberg J., Gonzalez-Hilarion S., Gujja S., Hamlin J.L.,
RA Hsueh Y.P., Ianiri G., Jones S., Kodira C.D., Kozubowski L., Lam W.,
RA Marra M., Mesner L.D., Mieczkowski P.A., Moyrand F., Nielsen K., Proux C.,
RA Rossignol T., Schein J.E., Sun S., Wollschlaeger C., Wood I.A., Zeng Q.,
RA Neuveglise C., Newlon C.S., Perfect J.R., Lodge J.K., Idnurm A.,
RA Stajich J.E., Kronstad J.W., Sanyal K., Heitman J., Fraser J.A.,
RA Cuomo C.A., Dietrich F.S.;
RT "Analysis of the genome and transcriptome of Cryptococcus neoformans var.
RT grubii reveals complex RNA expression and microevolution leading to
RT virulence attenuation.";
RL PLoS Genet. 10:E1004261-E1004261(2014).
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; CP003821; AFR93267.1; -; Genomic_DNA.
DR RefSeq; XP_012047437.1; XM_012192047.1.
DR AlphaFoldDB; J9VFW9; -.
DR GeneID; 23887229; -.
DR KEGG; cng:CNAG_03761; -.
DR VEuPathDB; FungiDB:CNAG_03761; -.
DR HOGENOM; CLU_007630_0_0_1; -.
DR OrthoDB; 23291at2759; -.
DR Proteomes; UP000010091; Chromosome 2.
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; 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}.
FT DOMAIN 694..1024
FT /note="Suppressor of forked"
FT /evidence="ECO:0000259|Pfam:PF05843"
FT REGION 30..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 130..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 887..985
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1025..1066
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 917..945
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 946..968
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1026..1040
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1049..1066
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1066 AA; 116918 MW; 5052C60F7E248B18 CRC64;
MSHEHPADIV NQLQSIDSIQ QDLADTAAAV VDAASQSHPP QHAAQDQKSQ STLLDNAEAM
ESILESAIPP APGSSSTTAA SDAIGDNNLT ASGPPPISDT VVAPSAADDE IGDVIVVGVE
TPTTANAVEA VVNPVNNGDI PIESTEQSSE QPPEQSVEQS AEQSGEQPPE QPAVETPQAP
QPNSAAPAAA AIESIPTYLE ETQLEQIVQA PVPTAHTEPP TPVVDSKMEE KPLVEHVAWA
PPQGIHSDVF LPEGLTEYSP SVSQNGELIR SWRADPSNPT LLLSLFNWAV QKTEVEDARA
WYRVLAVDNP TAAQPLLALI NLELALSNFA EVEAIFASTL KGSAGITTAA DVSIWTAYLH
YIRRQNPLAE GSANAADVRS TITEAYEFAL RECGFDRESG DIWDEYIKFV ASGPATNQWD
TQAKNDNLRK IYQRAVCIPL NNIEALWKSY DTFESSLNKL TAKKYLAEKS PAYMTARTAL
RELRALSDPI PKPILPPYPT FTEQDRQIVS AWKACLRWEE GNPLVIENHD VLQSRIGYAL
RKCLGEMRHF AELWHYAASY YSKLGKQDEA AEILEAGVNA CPKSFLLTFA YAELQEERKA
FPTCHSLYTT LISKLNPEVD ELRQNVAREI EIARGPSIPG SEKAAAAAAV GDSIDVDGND
ISDIQRLVEE REQRGELVAQ RRGKDIEELM VGISVVWIMY MRFARRAEGI KAARGVFGKA
RKSPHLTWHV FEASALMEFH TNKDAAVAIR IFELGLKQFS EDVDYVIKYL QFLLSINDDN
NARALFERSA VRIMGDKARP LWDAWARYEY TYGDLSAVHK LEARFSEVFP EDAPLKRFAQ
RWSYNGIDQI AIRDLGFNRA RMGVAVPPVP AVAPALPPPT ASIPAPIAAP VPVQPPQESY
KRSAPDDIPP RRPSSAEFSR SPKRHRAQSP PRRYAERDDR PPPGRYRDSI PPVKAPSSIP
PPHLGAGPAY ATPPSGAYGG DKDRSGLEKP LAWFMAQLPN ARSFDGPVFR PDDIMKLFGG
LSLPGAGMPP APPPISRGPA PTPMQSRGYY EPERDRRYGG HRSGRY
//
