ID A0A0V1BMT6_TRISP Unreviewed; 1132 AA.
AC A0A0V1BMT6;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
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 Name=Cpsf2 {ECO:0000313|EMBL:KRY38523.1};
GN ORFNames=T01_12036 {ECO:0000313|EMBL:KRY38523.1};
OS Trichinella spiralis (Trichina worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6334 {ECO:0000313|EMBL:KRY38523.1, ECO:0000313|Proteomes:UP000054776};
RN [1] {ECO:0000313|EMBL:KRY38523.1, ECO:0000313|Proteomes:UP000054776}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS3 {ECO:0000313|EMBL:KRY38523.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
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}.
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:KRY38523.1}.
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DR EMBL; JYDH01000024; KRY38523.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1BMT6; -.
DR STRING; 6334.A0A0V1BMT6; -.
DR eggNOG; KOG1135; Eukaryota.
DR eggNOG; KOG2404; Eukaryota.
DR InParanoid; A0A0V1BMT6; -.
DR Proteomes; UP000054776; Unassembled WGS sequence.
DR GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1.
DR Gene3D; 3.90.700.10; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
DR InterPro; IPR022712; Beta_Casp.
DR InterPro; IPR027075; CPSF2.
DR InterPro; IPR025069; Cpsf2_C.
DR InterPro; IPR035639; CPSF2_MBL.
DR InterPro; IPR003953; FAD-binding_2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR InterPro; IPR011108; RMMBL.
DR InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
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; PF00890; FAD_binding_2; 2.
DR Pfam; PF16661; Lactamase_B_6; 1.
DR Pfam; PF07521; RMMBL; 1.
DR SMART; SM01027; Beta-Casp; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
PE 3: Inferred from homology;
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664,
KW ECO:0000256|RuleBase:RU365006};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU365006};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000054776};
KW RNA-binding {ECO:0000256|RuleBase:RU365006}.
FT DOMAIN 243..380
FT /note="Beta-Casp"
FT /evidence="ECO:0000259|SMART:SM01027"
FT REGION 439..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1132 AA; 126959 MW; 4D3592128BED3E4C CRC64;
MTSLIRFEAL SGVMDDSPPC YVLEVGEFHF MLDCGWDSSF NMDFIERAQK WAPRIDAVLL
SYPDIAHIGA LPYLVGKCGL SCPIYATVPV YRMGQMFLYD WYQSFQNYED FQIFSLDDVD
QVFDKVLQVK YNQQVSMKGR GHGLQIVPLP AGHMIGGTIW RITKMGEEEI VYAVDFNHKK
ERHLNGCPLE SIARPNLLIT DAYMCGTALL RRKFRDEALL STILKTLRSG GNVLIVVDTA
GRVLELVQLL DQLWHNAEAG LLLYSLIFMN SVAFNVVEFA KSQVEWMSER MLRMFEEGRS
NPFQFRHAQL CHSLAELTRL RSPKVLSFRD AFFSDKVVLA SQPDLDSGFS RELFLDWCID
AKNCIILTSR ARIGSLCSKL IEMVSSPERI GTKQITVQVK RRVRLEGHEL DEFRVKKREQ
EQQATKLRLE QHRRRSRVDV VSLDDEDSDD EEKKSDAAAN EFPYDISYTA QGPDYWYNRA
ESYRRFPKYP HFEKRIKFDD YGEVIHAKSY LQLETKVRMV DLMRDRMGED QENGVATPGE
VQDIPTKCIQ FVQTVEVFAQ LEFIDFEGRT DVDSLKKILQ MSKPKQIILV HGMAEQTEKL
ANYCRKSLNM AEDKVFTPRL GDLVDATIES HMYQLKLTDA LLNSLKFIHV KDVEIAWVNG
LIKHNCSEEE TEDQKIAAMD VDEEKNAENA VDIGSDNIPY LDLLPSSEIP SHDAVFVGDP
KLSDLKQALM LDGFQAEFSH GVLVVNNVLS IRKRADGQLH VEGIVCKDYY AIRDQFHANY
FFYICIVVLH SCLMVETEPR HVIVVGSGLA GLSAALAAFN QGSRVTVLEG EPNIGGNSAK
ATSGINGCNT STQRVNGVQD NAKLFYSDTM KAGHGINDMQ LVDLLTKSSA DAIDRLTEIG
VDLSDLVIDP EQPDAGTKFL AAEALRGSGA LLLDHSGQRF ANELGPRDYL TGRIESQCKQ
SKDVGRKTAY MLLNDEAVDL FGRPSFEFYW KKKNFFTKAD NVEQLAKLLN VEAELVNATL
KEYAEAADGA RDDPFGKTVF PVIFDPGRPI YVARITPVIH YTMGGLKIDI HSQVLREDGS
KISGLYAAGE VSGGVHGANR LGGNSLLECA VFGAIAGKYA ATVPVGAQAG DL
//
