ID A0A2T7EP75_9POAL Unreviewed; 738 AA.
AC A0A2T7EP75;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 13-SEP-2023, entry version 15.
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=GQ55_2G125800 {ECO:0000313|EMBL:PUZ69629.1};
OS Panicum hallii var. hallii.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Panicodae; Paniceae; Panicinae; Panicum;
OC Panicum sect. Panicum.
OX NCBI_TaxID=1504633 {ECO:0000313|EMBL:PUZ69629.1, ECO:0000313|Proteomes:UP000244336};
RN [1] {ECO:0000313|EMBL:PUZ69629.1, ECO:0000313|Proteomes:UP000244336}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. HAL2 {ECO:0000313|Proteomes:UP000244336};
RA Lovell J., Jenkins J., Lowry D., Mamidi S., Sreedasyam A., Weng X.,
RA Barry K., Bonette J., Campitelli B., Daum C., Gordon S., Gould B.,
RA Lipzen A., MacQueen A., Palacio-Mejia J., Plott C., Shakirov E., Shu S.,
RA Yoshinaga Y., Zane M., Rokhsar D., Grimwood J., Schmutz J., Juenger T.;
RT "WGS assembly of Panicum hallii var. hallii HAL2.";
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}.
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DR EMBL; CM009750; PUZ69629.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T7EP75; -.
DR STRING; 1504633.A0A2T7EP75; -.
DR EnsemblPlants; PUZ69629; PUZ69629; GQ55_2G125800.
DR Gramene; PUZ69629; PUZ69629; GQ55_2G125800.
DR Proteomes; UP000244336; Chromosome 2.
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 SMART; SM00849; Lactamase_B; 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:UP000244336};
KW RNA-binding {ECO:0000256|RuleBase:RU365006}.
FT DOMAIN 17..222
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|SMART:SM00849"
FT DOMAIN 242..366
FT /note="Beta-Casp"
FT /evidence="ECO:0000259|SMART:SM01027"
FT REGION 417..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..443
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 738 AA; 81574 MW; 60CCFD2A1FBD3FD2 CRC64;
MGTSVQVTPL SGAYGEGPLC YLLAVDGFRF LLDCGWTDLC DTSQLQPLAK VAPTIDAVLL
SHPDMMHLGA LPYAMKHLGL SAPVYATEPV FRLGLLTMYD HFLSRWQVSD FDLFTLDDVD
AAFQNVVRLK YSQNYLLNDK GEGIVIAPHV AGHLLGGTVW KITKDGEDVV YAVDFNHRKE
MHLNGTVLGS FVRPAVLITD AYNALNNQGY RKKQDQDFID SLVKVLASGG SVLLPVDTAG
RVLELLLILD KYWGDRRLEY PIYFLTNVST STIDYVKSFL EWMGDQIAKS FESSRANAFL
LKKVTLIINK EELEKLGDTP KQVVLASMAS LEVGFSHDIF VEMANEARNL VLFTEKGQFG
TLARMLQVDP PPKAVKVTMS KRIPLVGDEL KAYEEEQERI KKEEAIKASL VKEEELKASH
GSNAKASDPM AIDASSSHKS AKAGSHFGGN NDILIDGFVP PSTSVAPMFP FFENTAEWDD
FGEVINPDDY TMKQEETDSA LMLGPGDGLD GKIDDGSARL LLDSTPSKVI SNEMTVQVKC
SLVYMDFEGR SDGRSVKSVI AHVAPLKLVL VHGSAESTEH LKMHCAKNLD SHVYAPQIEE
TIDVTSDLCA YKVQLSEKLM SNIICKKLGE HEIAWVDAEV GKEDEKLVLL PPSSAPPPHK
PVLVGDLKLS DFKQFLENKG WQVEFSGGAL RCGEHITVRK IGDSQKGSTG SQQIVIEGPL
CEDYYKIREH LYLQFYLL
//
