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Database: UniProt
Entry: A0A182H7P4_AEDAL
LinkDB: A0A182H7P4_AEDAL
Original site: A0A182H7P4_AEDAL 
ID   A0A182H7P4_AEDAL        Unreviewed;       779 AA.
AC   A0A182H7P4;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 41.
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=RP20_CCG023536 {ECO:0000313|EMBL:KXJ70452.1};
OS   Aedes albopictus (Asian tiger mosquito) (Stegomyia albopicta).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Culicinae; Aedini; Aedes; Stegomyia.
OX   NCBI_TaxID=7160 {ECO:0000313|EMBL:KXJ70452.1};
RN   [1] {ECO:0000313|EMBL:KXJ70452.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Foshan {ECO:0000313|EMBL:KXJ70452.1};
RC   TISSUE=Whole organism {ECO:0000313|EMBL:KXJ70452.1};
RX   PubMed=26483478; DOI=10.1073/pnas.1516410112;
RA   Chen X.G., Jiang X., Gu J., Xu M., Wu Y., Deng Y., Zhang C., Bonizzoni M.,
RA   Dermauw W., Vontas J., Armbruster P., Huang X., Yang Y., Zhang H., He W.,
RA   Peng H., Liu Y., Wu K., Chen J., Lirakis M., Topalis P., Van Leeuwen T.,
RA   Hall A.B., Jiang X., Thorpe C., Mueller R.L., Sun C., Waterhouse R.M.,
RA   Yan G., Tu Z.J., Fang X., James A.A.;
RT   "Genome sequence of the Asian Tiger mosquito, Aedes albopictus, reveals
RT   insights into its biology, genetics, and evolution.";
RL   Proc. Natl. Acad. Sci. U.S.A. 112:E5907-E5915(2015).
RN   [2] {ECO:0000313|EMBL:KXJ70452.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Foshan {ECO:0000313|EMBL:KXJ70452.1};
RC   TISSUE=Whole organism {ECO:0000313|EMBL:KXJ70452.1};
RA   Xiang T., Song Y., Huang L., Wang B., Wu P.;
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; KQ566020; KXJ70452.1; -; Genomic_DNA.
DR   RefSeq; XP_019528071.1; XM_019672526.2.
DR   RefSeq; XP_019931255.1; XM_020075696.1.
DR   AlphaFoldDB; A0A182H7P4; -.
DR   STRING; 7160.A0A182H7P4; -.
DR   GeneID; 109400054; -.
DR   GeneID; 109621621; -.
DR   KEGG; aalb:109400054; -.
DR   KEGG; aalb:109621621; -.
DR   VEuPathDB; VectorBase:AALC636_011995; -.
DR   VEuPathDB; VectorBase:AALC636_016520; -.
DR   VEuPathDB; VectorBase:AALF023536; -.
DR   VEuPathDB; VectorBase:AALFPA_042226; -.
DR   VEuPathDB; VectorBase:AALFPA_057746; -.
DR   VEuPathDB; VectorBase:AALFPA_058209; -.
DR   OMA; YVLEHAW; -.
DR   OrthoDB; 198429at2759; -.
DR   Proteomes; UP000249989; 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:UP000249989};
KW   RNA-binding {ECO:0000256|RuleBase:RU365006}.
SQ   SEQUENCE   779 AA;  87849 MW;  35DE63EE07B3D55A CRC64;
     MTSIIKLHAI SGAMDESPPC YILQVDEVRF LLDCGWDEKF DPNFIKELKK YVHTIDAVLL
     SYPDGLHLGA LPYLVGKLGL NCPIYATIPV YKMGQMFMYD LFMSHYNMYD FDLFTLDDVD
     AAFDRIIQLK YNQSVSLKGK GYGITITPLP AGHLIGGTIW KVMKVGEEDI VYATDFNHKK
     ERHLNGCELE KLQRPSLLIT DAYNAKYQQA RRRARDEKFM TNILQTLRNN GNVLVTVDTA
     GRVLELAHML DQLWKNKESG LMAYSLALLN NVSYNVVEFA KSQIEWMSDK LMKSFEGARN
     NPFQFKHLRL CHTMADLAKV PSPKVVLASS ADMESGFSRE LFVQWASNAN NSIIITCRSS
     PGTLSRDLIE NGGNGRKIEL DVRRRVELEG AELEEYMRTE GEKHNRSIIK SDMDLDSSSD
     SDDELEMSVI TGKHDIVVRP EGRSHTGFFK SSKKQYAMFP FHEEKIKFDE YGEIIQPDDY
     KMIDLGPDGG FEDNKENQIK PEDIKKEKGE ELSVLDKPTK CISSRKLVEI NAQVQFIDFE
     GRSDGESMLK ILSQLRPRRV VVIRGSPQNT AHIAEHCQLN IGARVFTPNR GEVIDATTET
     HIYQVRLTEA LISQLEFQKG KDAEVAWVDA QIVIRNKQFS AQGAEDDVSG PLSGMTNNAT
     TNNAIAAAAA AASDTPMDVD QVEGGDDKSD RQILTLEPMK NEELPAHNSV FINELKLIDF
     KQILMKANIN SEFSGGVLWC SNGTVALRRV DTGKVTVEGC LSEEYYKIRE LLYEQYAIV
//
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