ID R7YQE5_CONA1 Unreviewed; 972 AA.
AC R7YQE5;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 13-SEP-2023, entry version 40.
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=W97_03129 {ECO:0000313|EMBL:EON63901.1};
OS Coniosporium apollinis (strain CBS 100218) (Rock-inhabiting black yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Coniosporium.
OX NCBI_TaxID=1168221 {ECO:0000313|EMBL:EON63901.1, ECO:0000313|Proteomes:UP000016924};
RN [1] {ECO:0000313|Proteomes:UP000016924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 100218 {ECO:0000313|Proteomes:UP000016924};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Gorbushina A., Noack S., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The genome sequence of Coniosporium apollinis CBS 100218.";
RL Submitted (JUN-2012) 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; JH767565; EON63901.1; -; Genomic_DNA.
DR RefSeq; XP_007779218.1; XM_007781028.1.
DR AlphaFoldDB; R7YQE5; -.
DR STRING; 1168221.R7YQE5; -.
DR GeneID; 19900440; -.
DR eggNOG; KOG1135; Eukaryota.
DR HOGENOM; CLU_002227_3_0_1; -.
DR OMA; YVLEHAW; -.
DR OrthoDB; 198429at2759; -.
DR Proteomes; UP000016924; 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; 3.60.15.10; 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:UP000016924};
KW RNA-binding {ECO:0000256|RuleBase:RU365006}.
FT DOMAIN 285..454
FT /note="Beta-Casp"
FT /evidence="ECO:0000259|SMART:SM01027"
FT REGION 344..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 515..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 618..710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 849..870
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..372
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..537
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..657
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 671..685
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 849..869
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 972 AA; 106032 MW; C26D933F2A1C86C0 CRC64;
MFNFTPLLGA QSTSAASQSL LELDGGIKIL VDVGWDESFD AEKLKELERQ IPTLSIILLT
HATTAHLGAF VHCCKHFPLF KRIPIYATTP VISLGRTLLQ DVYSSTPLAA SIIPEAALSE
SAYSCPSART GGVPNILLQP PTADEIAKYF SLINPLKYSQ SHQPLPSPFS PPLNGLTVTA
YGAGHTLGGT IWHIQHGLES IVYSVDWNQS RENVFPGAEW LSETGAEVKE QLRRPTALVC
SSKGAERVAP PGGRKRRDDT LLSMIRDTVS NGGTVLIPTD SSARVLELAY LLENAWQAAH
TGDGLEALKE SKLYLAGRTG GATMRYVRSM LEWMNESIVR DFETASGAQG SQGHRRTRSR
GGAADGERSG KDQSKSVNAP FDFKHLKLLE RKSQLRRMLS QTSPRVILAS DSSLEWGFSK
DAILMVAKDR RNLIVLTERP SRPHQRRDGL AGSLFEIYKG KAGTGANLET DTATVVDMEG
RDLAVELVET AALAGNEVPL YQQYLARQRQ LHNTMQPGQG ASLETSADVV DDRSSTTSTT
SEDSDEERQG KVLNVSAAMN HSRHKLGLSD QELGINILIR GKLIHDYDVR GKKGRETMFP
FVAKRRRADD FGDVIRPEDY IRQEEKDEVN GEAQRDGEPK KENALGQKRK WDDVGTKSGL
NGHRTSNGVN KRRKKNEDQP KEQRDAASNG TEVSDNEDFE SSDEEGDVKT AEGPLKVTIT
KQIMTFECKI GYIDFAGLHD KRSLQMLIPL IRPRKLILVA GEKEETLALA ADCRKLLSPG
SETTSESSFE VLTPAIGTTV DASVDTNAWT LKLSHHLARR LHWQNVRGLG VVAITGLLES
ESAEDEALQK NAKKKQKMTT GEKEDSESST PILDVVPASM AGATRSVAQP LHVGDLRLAD
LRKLMQASGL TAEFRGEGTL LVNGMVAVRK TGTGKIEVDG GGVSVLGSNQ TDGTFNKVKR
KIYEGLAVVA GG
//
