ID   A0A1J9QIA3_9EURO        Unreviewed;      1025 AA.
AC   A0A1J9QIA3;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   13-SEP-2023, entry version 25.
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=AJ78_04128 {ECO:0000313|EMBL:OJD15636.1};
OS   Emergomyces pasteurianus Ep9510.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Emergomyces.
OX   NCBI_TaxID=1447872 {ECO:0000313|EMBL:OJD15636.1, ECO:0000313|Proteomes:UP000182235};
RN   [1] {ECO:0000313|EMBL:OJD15636.1, ECO:0000313|Proteomes:UP000182235}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 9510 {ECO:0000313|EMBL:OJD15636.1,
RC   ECO:0000313|Proteomes:UP000182235};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C.A., Munoz J.F., Imamovic A., Priest M.E., Young S., Clay O.K.,
RA   McEwen J.G.;
RT   "Emmonsia species relationships and genome sequence.";
RL   Submitted (JUL-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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OJD15636.1}.
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DR   EMBL; LGRN01000145; OJD15636.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1J9QIA3; -.
DR   STRING; 1447872.A0A1J9QIA3; -.
DR   VEuPathDB; FungiDB:AJ78_04128; -.
DR   OrthoDB; 198429at2759; -.
DR   Proteomes; UP000182235; 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   GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
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:UP000182235};
KW   RNA-binding {ECO:0000256|RuleBase:RU365006}.
FT   DOMAIN          301..470
FT                   /note="Beta-Casp"
FT                   /evidence="ECO:0000259|SMART:SM01027"
FT   REGION          361..393
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          546..580
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          654..747
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          879..910
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        561..580
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        690..713
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1025 AA;  110549 MW;  0A356B4C63BC8278 CRC64;
     MFTFTPLLGA QSSSSRAVQS ILELDGGVKI LVDVGWDENF DTSALAELEK QIPTLSLVLL
     THATPSHIGA FAHCCKTFPL FTQIPIYATS PVIALGRTLL QDLYASAPLA ATFLPKNTVV
     DSSPSSPVPP EAAIATETTN ADHYGSSGIL LPPPTSEEIA RYFSLIHPLK YSQPHQPLPS
     PFSPPLNGLT LTAYNAGHTV GGTIWHIQHG MESIIYAVDW NQARENVIAG AAWFGGSGAS
     GTEVVEQLRK PTALVCSTKG GDKLALSGGR KRRDDLLFDM IRSSFSKGGT VLIPTDTSAR
     ALELAYVLEH AWRESAETAD GEDPLKSGEL YLAGKKAHGT MRLARSMLEW MDEGIVREFE
     ASHGGDHVPG GGKGRPDGPN QRNPAAPIPD KRGDGAFKSL GPFTFKHLKI VERKTKLDKI
     LGSNTPKVIL TSDTSLNWGY SKQVLQKLAT GPENLIILTE SFSVSANRQM VGNGQPRSSL
     AHEIWSIYED RKDGVASEKA ASGELLEQVH SGGRLLTVTD VEKTPPNAND LLVYQQYLAT
     RRQLQNTAQG RGDSGLATTA DALDDGSSSS SSEDSDSEQQ GKVLNFSVSL AHSNRNKLGL
     SDADLGVNIL LRRKNVHDYD VRGKKGRERM FPYVAPKKRG DEYGEFIRPE EYLRAEEREE
     AEMQTQRGPD GRIQTRPGQK RRWGDVSASG KQSAIASNKR QHISSSSRDV QDSSGALALP
     AGFDINGTED ASASEEEAED QPVEGPSKAT FTYSTLELNA RIAFVDFSGL HDKRSLEMLI
     PLIQPRKLIL TAGLKEETMA LAAGCRSLLA AKAGIELGSP SQSDVDIFTP VLGETVDASV
     DTNAWMVKLS SALVKRLKWQ NVRNLGVVAL IGELRGPEPT ADDKDASGVS QKKQRMLPDN
     AASGEKDKQE QLVPKKDVFP LLDLLPVHMA AATRSVTRPL HVGDLRLADL RKLMQSSGHT
     AEFRGEGTLL IDGFVAVRKS GTGKIEIEGA AQSALSNPSA MKRDEGSFLA VKRKIYEGLA
     IVAGG
//