ID T5A6K3_OPHSC Unreviewed; 723 AA.
AC T5A6K3;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=Cleavage and polyadenylation specificity factor subunit 2 {ECO:0000256|RuleBase:RU365006};
DE AltName: Full=Cleavage and polyadenylation specificity factor 100 kDa subunit {ECO:0000256|RuleBase:RU365006};
GN ORFNames=OCS_03194 {ECO:0000313|EMBL:EQL01100.1};
OS Ophiocordyceps sinensis (strain Co18 / CGMCC 3.14243) (Yarsagumba
OS caterpillar fungus) (Hirsutella sinensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX NCBI_TaxID=911162 {ECO:0000313|EMBL:EQL01100.1, ECO:0000313|Proteomes:UP000019374};
RN [1] {ECO:0000313|EMBL:EQL01100.1, ECO:0000313|Proteomes:UP000019374}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Co18 / CGMCC 3.14243 {ECO:0000313|Proteomes:UP000019374};
RC TISSUE=Fruit-body {ECO:0000313|EMBL:EQL01100.1};
RX DOI=10.1007/s11434-013-5929-5;
RA Hu X., Zhang Y., Xiao G., Zheng P., Xia Y., Zhang X., St Leger R.J.,
RA Liu X., Wang C.;
RT "Genome survey uncovers the secrets of sex and lifestyle in caterpillar
RT fungus.";
RL Chin. Sci. Bull. 58:2846-2854(2013).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU365006}.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. RNA-
CC metabolizing metallo-beta-lactamase-like family. CPSF2/YSH1 subfamily.
CC {ECO:0000256|RuleBase:RU365006}.
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DR EMBL; KE652592; EQL01100.1; -; Genomic_DNA.
DR AlphaFoldDB; T5A6K3; -.
DR eggNOG; KOG1135; Eukaryota.
DR HOGENOM; CLU_002227_3_0_1; -.
DR Proteomes; UP000019374; Unassembled WGS sequence.
DR GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006378; P:mRNA polyadenylation; IEA:InterPro.
DR CDD; cd16293; CPSF2-like_MBL-fold; 1.
DR Gene3D; 3.40.50.10890; -; 1.
DR Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1.
DR InterPro; IPR022712; Beta_Casp.
DR InterPro; IPR027075; CPSF2.
DR InterPro; IPR025069; Cpsf2_C.
DR InterPro; IPR035639; CPSF2_MBL.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR PANTHER; PTHR45922; CLEAVAGE AND POLYADENYLATION SPECIFICITY FACTOR SUBUNIT 2; 1.
DR PANTHER; PTHR45922:SF1; CLEAVAGE AND POLYADENYLATION SPECIFICITY FACTOR SUBUNIT 2; 1.
DR Pfam; PF10996; Beta-Casp; 1.
DR Pfam; PF13299; CPSF100_C; 1.
DR Pfam; PF16661; Lactamase_B_6; 1.
DR SMART; SM01027; Beta-Casp; 1.
DR SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
PE 3: Inferred from homology;
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664,
KW ECO:0000256|RuleBase:RU365006};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU365006};
KW Reference proteome {ECO:0000313|Proteomes:UP000019374};
KW RNA-binding {ECO:0000256|RuleBase:RU365006}.
FT DOMAIN 286..443
FT /note="Beta-Casp"
FT /evidence="ECO:0000259|SMART:SM01027"
FT REGION 509..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 723 AA; 78843 MW; C5CBD976E1D7BEA5 CRC64;
MFTFCPLQGA LSESTASQSL LELDGGVKVL VDLGWDESFD VEKLAELEKQ VPTLSLILLT
HATVSHLAAY VHCCKNFPLF TRVPAYATRP VIDLGRSLTQ DLYSSTPTAC TTISQSSLSE
LAYAYSQTAS TASTAQNLLL QSPTPDDIAR YFSLIQPLKY SQPHQPLPSP FSPPLNGLTI
TAYNAGHTLG GTIWHIQHGL ESIVYAVDWN QARENVFAGA AWLDGAAGGG AEVIEQLRKP
TALICSSRVA QAGGRIKRDE SLIDTIKACV SKGGTVLIPV DSSARVLEMA YFLEHAWRLD
ASSKGGNLRS AKLYLAGRNM SSTMRYARSM LEWMDNNIVQ EFEACAEGQR RANGANDRKE
AGPFDFKHLR LLERKAQITK LLSRVSHHGE SEGRVILASD SSMEWGFSKD LIKGLAGDSR
NLVILTDRPS MAKDGNESVA RTLWEWWRER RDGVSVEQTA GGDQLEMVYG GGRELQLRQA
ARQALEGDEL AVYQQWLVTQ RQLQATQHTG GAAALEASAD VDDASSDSSS DSEDDDGQQQ
GKALTVSATM GQAGRKNVVL KDEDLGINVL MKKKGVYDFD SRGKRGRERS FPLAVRRKRN
DDFGELIRPE DYLRAEEKDE DNADGGNVAA VDDKLGKKRK WGDPLHVGDL RLADLRRAMQ
GAGHGAEFRG EGMLVVDGSV VVRKTTEGRV EVESVGVPAG ARRNTVFAVK RAIYEGLAVV
AGA
//