ID A0A0D1YNF0_9EURO Unreviewed; 942 AA.
AC A0A0D1YNF0;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=PV08_03789 {ECO:0000313|EMBL:KIW16601.1};
OS Exophiala spinifera.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=91928 {ECO:0000313|EMBL:KIW16601.1, ECO:0000313|Proteomes:UP000053328};
RN [1] {ECO:0000313|EMBL:KIW16601.1, ECO:0000313|Proteomes:UP000053328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 89968 {ECO:0000313|EMBL:KIW16601.1,
RC ECO:0000313|Proteomes:UP000053328};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala spinifera CBS89968.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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; KN847494; KIW16601.1; -; Genomic_DNA.
DR RefSeq; XP_016236817.1; XM_016378140.1.
DR AlphaFoldDB; A0A0D1YNF0; -.
DR STRING; 91928.A0A0D1YNF0; -.
DR GeneID; 27330872; -.
DR VEuPathDB; FungiDB:PV08_03789; -.
DR HOGENOM; CLU_002227_3_0_1; -.
DR OrthoDB; 198429at2759; -.
DR Proteomes; UP000053328; 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 InterPro; IPR011108; RMMBL.
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 Pfam; PF07521; RMMBL; 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:UP000053328};
KW RNA-binding {ECO:0000256|RuleBase:RU365006}.
FT DOMAIN 283..423
FT /note="Beta-Casp"
FT /evidence="ECO:0000259|SMART:SM01027"
FT REGION 335..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 500..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 603..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 803..837
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..523
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..642
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 654..668
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 805..821
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 822..837
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 942 AA; 103324 MW; 7DEE4CC0CCE2E1CA CRC64;
MFTFTPLLGA QSNSRSSQSI LELDGGVKIL VDVGWDERFD TRQLAEIEKH ASTLSFILLT
HATTSHVGAF AHCCKHIPIF SQIPVYATPP VIAFGRTLLQ DLYSSNPVAA TFIPGSGSPE
DDSSVDDKSR SNILRQAPTF EEINKFFTLI TPLKYSQPHQ PTPSHFSAPI EGLTLTAYNS
GHTLGGTIWH IQYGMESIVY AVDWNQAREN VIAGAAWFGG VGGAEVIEQL RKPTALVCSS
VGAARAGLAG GRKARDDALL GHIKSSIAKN GTVLIPTDSS ARVLELAWIL EKAWTDPVLK
GAKVYLASRS ANATLRHARS LLEWMDDSIV REFEEEDENQ TQSRRRNGSK QINGTSKSSR
PFELENIKIV ERKSQFERLL KAEGPRVILA SDVSLDWGFS RSLLEHMVQR PENLVLLTEK
AEMRPGSLSP SQVFWTWFEQ RQDGVALEKT LDGEQLEQVH SGGRMLKLRH AEKASLSTQE
SQRYQQYMAT QRQIQDSLAA NEQDQGGVDD NLDDESSTSS EEESEDEQQG RVLNVSSALG
HGARNKVALS DEDLGINILL RKKGVYDYDV RNKRGRNAVF PYTHTRRRGD EFGDFIKPED
FLREEEKEEQ EAQTDSKSMA LLGQKRKWSE ADNAREMHQK RPRQGGPASA ADSGDESESD
ESDEEGQMEI EGPQGPAKIV FSTSEVTVNA RLAFVDFAGL HDQRSLQMLI PLIGPKKLIL
TSGNPSDTLA LASDCKELLG VKAAGVEEET STEIFTPQEG QTIDASVDTN AWVVKLSREL
AKTLRWQNVK NMGVVTIQGQ LKAEGEQKAD VEDDPQSKKQ KIDTEASSQT TPQPGLSIQP
VLDVLPASLA ASTRSVSQAI HVGDLRLAEL RRIIAMDGHT AEFRGEGTLL VDGMIAVKKV
GSGRIIVEGA PLGVTAMSTS TADNFTRVKQ KVYEGLAVVA AG
//
