ID A0A2T7NWN8_POMCA Unreviewed; 533 AA.
AC A0A2T7NWN8;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
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=C0Q70_13242 {ECO:0000313|EMBL:PVD25584.1};
OS Pomacea canaliculata (Golden apple snail).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Architaenioglossa; Ampullarioidea; Ampullariidae; Pomacea.
OX NCBI_TaxID=400727 {ECO:0000313|EMBL:PVD25584.1, ECO:0000313|Proteomes:UP000245119};
RN [1] {ECO:0000313|EMBL:PVD25584.1, ECO:0000313|Proteomes:UP000245119}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SZHN2017 {ECO:0000313|EMBL:PVD25584.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:PVD25584.1};
RA Liu C., Liu B., Ren Y., Zhang Y., Wang H., Li S., Jiang F., Yin L.,
RA Zhang G., Qian W., Fan W.;
RT "The genome of golden apple snail Pomacea canaliculata provides insight
RT into stress tolerance and invasive adaptation.";
RL Submitted (APR-2018) 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:PVD25584.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; PZQS01000008; PVD25584.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T7NWN8; -.
DR STRING; 400727.A0A2T7NWN8; -.
DR Proteomes; UP000245119; Miscellaneous, Linkage group lg8.
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 Gene3D; 3.40.50.10890; -; 1.
DR InterPro; IPR022712; Beta_Casp.
DR InterPro; IPR027075; CPSF2.
DR InterPro; IPR025069; Cpsf2_C.
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; 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|RuleBase:RU365006};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU365006};
KW Reference proteome {ECO:0000313|Proteomes:UP000245119};
KW RNA-binding {ECO:0000256|RuleBase:RU365006}.
FT DOMAIN 17..142
FT /note="Beta-Casp"
FT /evidence="ECO:0000259|SMART:SM01027"
FT REGION 416..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 533 AA; 60426 MW; 343FAA8B7C2F5889 CRC64;
MRNDGNVLIA TDTAGRMLEL AQLLDQMWRN TESGLTTYSL ALLNNVSFNV VEFAKSQVEW
MSDKIMRAFE DNRNNPFQFK HLKLCHNLAE LARVPEPKVV LASTPDLQSG YSRDLFVAWC
GNSKNSIILT SRTSPGTLTR WLIENQEAKT VTLEIRRRIK LDGAELEEYV KRKQDQEQED
IRRKVELALK GDVDSSDESE TEMEVDSFYT SGVKGKHDLM RKAENKSRTG FFKQAKKAYP
MFLFQEEKLK WDEYGEVIRP EDYIIADPVP ADEEKSKEVW SPLTCFCLFT SREVPTKCVS
STVTLDINAN VLYIDFEGRS DGDSIRRYLT QIKPRQLVLI HGPEEATSSL ADYCHTANAV
QGRVFCPSVG DVIDATTERH IYQVRLRDQL ASSLNFAKAR DIELAWIDGQ IDMSAGRTDT
SAMSEGKGQE SMDTKDNKEE EEEPVAELVP TLYPLPPSQV QPHTAVFVNE PKLSDFKLVL
INAGIPCEFV AGVLICNNVV AVRRESGRIQ VEGTLCPDYF KVRELLYEQY AIV
//
