ID W2TDI2_NECAM Unreviewed; 692 AA.
AC W2TDI2;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
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=NECAME_10049 {ECO:0000313|EMBL:ETN79077.1};
OS Necator americanus (Human hookworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae; Bunostominae;
OC Necator.
OX NCBI_TaxID=51031 {ECO:0000313|EMBL:ETN79077.1, ECO:0000313|Proteomes:UP000053676};
RN [1] {ECO:0000313|Proteomes:UP000053676}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24441737; DOI=10.1038/ng.2875;
RA Tang Y.T., Gao X., Rosa B.A., Abubucker S., Hallsworth-Pepin K., Martin J.,
RA Tyagi R., Heizer E., Zhang X., Bhonagiri-Palsikar V., Minx P., Warren W.C.,
RA Wang Q., Zhan B., Hotez P.J., Sternberg P.W., Dougall A., Gaze S.T.,
RA Mulvenna J., Sotillo J., Ranganathan S., Rabelo E.M., Wilson R.K.,
RA Felgner P.L., Bethony J., Hawdon J.M., Gasser R.B., Loukas A., Mitreva M.;
RT "Genome of the human hookworm Necator americanus.";
RL Nat. Genet. 46:261-269(2014).
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; KI659662; ETN79077.1; -; Genomic_DNA.
DR RefSeq; XP_013301304.1; XM_013445850.1.
DR AlphaFoldDB; W2TDI2; -.
DR STRING; 51031.W2TDI2; -.
DR EnsemblMetazoa; NECAME_10049; NECAME_10049; NECAME_10049.
DR GeneID; 25350078; -.
DR KEGG; nai:NECAME_10049; -.
DR CTD; 25350078; -.
DR OMA; YVLEHAW; -.
DR OrthoDB; 198429at2759; -.
DR Proteomes; UP000053676; 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 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; 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; 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|RuleBase:RU365006};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU365006};
KW Reference proteome {ECO:0000313|Proteomes:UP000053676};
KW RNA-binding {ECO:0000256|RuleBase:RU365006}.
FT DOMAIN 150..239
FT /note="Beta-Casp"
FT /evidence="ECO:0000259|SMART:SM01027"
FT REGION 277..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 323..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..303
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 692 AA; 78202 MW; C3F07B505AFE2623 CRC64;
MGMMFMYDWI NSLMSVENFE LFTLDDVDVA FDRIQKLKFN QTVPLRGDSQ IKITAMPAGH
MIGGAMWRIT RHDEEDIIYA VDYNHKKERH LNGCSFDTIL RPYLLITDSL NAMYTQPRRK
ERDEQLVTTI LKTVRQNGDC VIVIDTAGRV LEIAHLLDQL WANTQSGLQK YNLVMMSHVA
ASVVEFAKSQ VEWMSDKVLN GIDMECGYSR ELFLDWCGDS RNSFIITGRS SERTLCSKLI
YMAECLATNS RTNRIVALEV KKRVRLEGAE LEAYKKKKAQ KDKEEARRRL EEQERRQAEL
RGYDSDDDDE MIASALAAVE TLRTKKTREE EQAAAAAGRG GDKVLKTPTP MIIDVEPKEE
ITEEGDMKSE AEPCAIPGLT MATLKIREEA LNEAPAFVPT GPKLPTRKRR PWDVYGEKYR
PEDYTVSKLR VHLPVPQEII KEADDPTANM AVPIVDDAPT KCITVIEKIE VSCNVEYIEF
EGRSDGESLK KLIAQMKPKQ LILVHGSGQS TRHLAQHCYD NNIAQGHIFT PSVGEVVDAT
VASHIYRILL NDELFESLEF IKVKDADLAW IDAQITARPS EVGVEREDGM EVDEQAADAH
LGDQHVDKCM LSALSGEAPF RDVVYVNDPK LSEMKQLLLN MGFAAEFSSG VLYIGGVISI
RRNEAGRFHI EGCVGPLYLR LRDIILEQFM VL
//
