ID A0A0N5BNB8_STREA Unreviewed; 974 AA.
AC A0A0N5BNB8;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 27.
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};
OS Strongyloides papillosus (Intestinal threadworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Strongyloides.
OX NCBI_TaxID=174720 {ECO:0000313|Proteomes:UP000046392, ECO:0000313|WBParaSite:SPAL_0000739700.1};
RN [1] {ECO:0000313|WBParaSite:SPAL_0000739700.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
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 AlphaFoldDB; A0A0N5BNB8; -.
DR STRING; 174720.A0A0N5BNB8; -.
DR WBParaSite; SPAL_0000739700.1; SPAL_0000739700.1; SPAL_0000739700.
DR Proteomes; UP000046392; Unplaced.
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; 3.40.50.10890; -; 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; IPR035639; CPSF2_MBL.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
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 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 RNA-binding {ECO:0000256|RuleBase:RU365006}.
FT DOMAIN 289..454
FT /note="Beta-Casp"
FT /evidence="ECO:0000259|SMART:SM01027"
FT REGION 509..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 671..701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 673..688
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 974 AA; 110042 MW; A17488B8230846B9 CRC64;
MSSSVKFTTL NDDPYGSYQA YILEIPPYTF LLDCGWDSKF NMTYFNSIAA YADKISAILI
SYPSISHLGA LPYLYSKCNI SNVPIYCTFP TVKLGILTLY DWIASLKQNS EFNLFDLEDV
DRVMEKVQKI KYSQLITINT LKGVNCQQFQ ISDNYNKTDG DIEIPLEKQV TIQALCSGHM
LGGSYWKISR MSDEDIIYAV DFNNKKERHL NGANFNAFIN TNVSNPSSST LSSATNIGTK
PLLFITSGVN AGYIPEKRRT RDEKFLSSSY ETLRNGGDVL VCVDTGGRML ELVNLLNSAW
SNNNIAINNN ANQDDARDTN ITNQYRYNFE PYALVILSNV GNSVLQTAVM NVEWMNDRFT
VDHTSSSILG NGTTEGINGT SMPTVSAFSY DNFNICNSLE ALDAIPQNKL ILVPSFDMEI
GFSRNLFYSF VEDPKNLVIL TNRSGDRNSL AGKLFRIVEG RNKEERGLGR SEETIDLDVK
LRVLLEGKEL EAYNQRKLDA EAEEARKKQE EIRRNQQLRE DEEQEEERNV LGMGKTETCG
GDEIENSEDF LSIDNIFKQN LPKGFKMELV DEEFNTTING ESKKLANKTL DYSSLEMEVD
VTKTEGEEDD DEDDYSSLIF PLGERNSEHE MMSYLPLKSY DQPWDDYGEV INPEEIIALD
PYRKAFASKE GVLENDDDDD ENDTHSVDDE MNDDLGGGSK KQRLAGMKLT KESLFPWTAA
PTKCISCNQT FHLNCQLTFI DFEGRVDGDS LEKIISQMSP KNLIIVNGYD QAVHKLMTLC
RDTVKIEGIV ENVKVGKGVE IIGDNKGKVV KMSKDLISRT NMIKIMNGQE WSWVEGVLES
KSVKDGDYHM SDIDDNNVTD DKENIEKDQE MNDITESENE SIAKNNESQL ILKPCTVTTS
KPHPVLYLNS PKLIDIKARF TAEGYNAVLY LNILHINGIA TIQKDDTGSV KIEGKYCMEY
FKIRDLLYNM FAII
//