ID A0AAD1ZMV1_9LAMI Unreviewed; 1078 AA.
AC A0AAD1ZMV1;
DT 29-MAY-2024, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2024, sequence version 1.
DT 28-JAN-2026, entry version 9.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CAI9770130.1};
GN ORFNames=FPE_LOCUS17763 {ECO:0000313|EMBL:CAI9770130.1};
OS Fraxinus pennsylvanica.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Oleaceae; Oleeae; Fraxinus.
OX NCBI_TaxID=56036 {ECO:0000313|EMBL:CAI9770130.1, ECO:0000313|Proteomes:UP000834106};
RN [1] {ECO:0000313|EMBL:CAI9770130.1}
RP NUCLEOTIDE SEQUENCE.
RA Huff M.;
RL Submitted (MAY-2023) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; OU503045; CAI9770130.1; -; Genomic_DNA.
DR AlphaFoldDB; A0AAD1ZMV1; -.
DR Proteomes; UP000834106; Chromosome 10.
DR GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IEA:TreeGrafter.
DR GO; GO:0004534; F:5'-3' RNA exonuclease activity; IEA:TreeGrafter.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:TreeGrafter.
DR GO; GO:0004521; F:RNA endonuclease activity; IEA:TreeGrafter.
DR GO; GO:0006398; P:mRNA 3'-end processing by stem-loop binding and cleavage; IEA:TreeGrafter.
DR CDD; cd10017; B3_DNA; 1.
DR CDD; cd16292; CPSF3-like_MBL-fold; 1.
DR FunFam; 3.60.15.10:FF:000001; Cleavage and polyadenylation specificity factor; 1.
DR FunFam; 3.40.50.10890:FF:000001; Cleavage and polyadenylation specificity factor subunit 3; 1.
DR Gene3D; 3.40.50.10890; -; 1.
DR Gene3D; 2.40.330.10; DNA-binding pseudobarrel domain; 3.
DR Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1.
DR InterPro; IPR003340; B3_DNA-bd.
DR InterPro; IPR022712; Beta_Casp.
DR InterPro; IPR021718; CPSF73-100_C.
DR InterPro; IPR015300; DNA-bd_pseudobarrel_sf.
DR InterPro; IPR050698; MBL.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR InterPro; IPR011108; RMMBL.
DR PANTHER; PTHR11203; CLEAVAGE AND POLYADENYLATION SPECIFICITY FACTOR FAMILY MEMBER; 1.
DR PANTHER; PTHR11203:SF11; CLEAVAGE AND POLYADENYLATION SPECIFICITY FACTOR SUBUNIT 3; 1.
DR Pfam; PF10996; Beta-Casp; 1.
DR Pfam; PF11718; CPSF73-100_C; 1.
DR Pfam; PF00753; Lactamase_B; 1.
DR Pfam; PF07521; RMMBL; 1.
DR SMART; SM01019; B3; 3.
DR SMART; SM01027; Beta-Casp; 1.
DR SMART; SM01098; CPSF73-100_C; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF101936; DNA-binding pseudobarrel domain; 3.
DR SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000834106};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 34..251
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|SMART:SM00849"
FT DOMAIN 256..377
FT /note="Beta-Casp"
FT /evidence="ECO:0000259|SMART:SM01027"
FT DOMAIN 484..688
FT /note="Pre-mRNA 3'-end-processing endonuclease
FT polyadenylation factor C-term"
FT /evidence="ECO:0000259|SMART:SM01098"
FT DOMAIN 725..832
FT /note="TF-B3"
FT /evidence="ECO:0000259|SMART:SM01019"
FT DOMAIN 853..960
FT /note="TF-B3"
FT /evidence="ECO:0000259|SMART:SM01019"
FT DOMAIN 973..1077
FT /note="TF-B3"
FT /evidence="ECO:0000259|SMART:SM01019"
SQ SEQUENCE 1078 AA; 122156 MW; C950A74AEC197E07 CRC64;
MASTGQPASS LKRSAMRDED QLIITPLGAG SEVGRSCVHM SYKGKVVMFD CGIHPGFSGM
SALPYFDEID PSLIDVLLIT HFHLDHAASL PYFLEKTTFK GRVFMTHATK AIYKLLLSDY
VKVSKVSVDD MLFDEQDILR SMDKIEVIDF HQTVEVNGIR FWCYTAGHVL GAAMFMVDIA
GVRVLYTGDY SREEDRHLRA AEIPQFSPDI CIIESTYGVQ LHEPRHIREK RFTDVIHSTV
TQGGRVLIPA FALGRAQELL LILDEYWSSH PDLHKVPIYY ASPLAKRCMA VYQTYTNAMN
EKIRNQFASS NPFDFKHIFP LKSIDEFNDT GPCVVMATPG GLQSGLSRQL FDKWCSDRKN
ACVLPGYVVE GTLAKTIINE PKEVTLMNGL TASLNMQVHY ISFSAHADYA QTSTFLKELM
PPNIILVHGE ANEMGRLKQK LLSVFADGNT KIITPKNCQS VEMYFNSQKM AKTIGKLAEK
RPSAGETVSG LLVKKGFTYQ IMAPEDLHVF SQLSTGNIIQ RITIPYSGAL AVIKYRLKQI
YESVESSTDE ESGVPTLLVH GQVTVKQESE NHLSVHWTAD PISDMVSDSI VALVLNVSRE
MPKLVVDSEP VVNKEEDTKK AEKIVDALLV SLFGDVKYGE DGKLVINVDG NVAQLDKESG
EVESENSGLK ERVKMAFRRI KSADKDPAPL SQSSRSSRKF DLCIQRMKRT TYYNDAAQMQ
DQWPIKKALT LSDVDITHPF LTLSRQQIET HILVYMTPQQ QEDLSTNGQV GFNAQDDDTG
DVYVMKLKWR GSYYNLIGKW GKVVRGKGLD VGQEIKLRWF NGCLHFSVPE QQVIAVPPTR
TVAAPLVQDH WPIKKVLTSS DVDTNHPFLP LPRRSVEDHI LVHWVPQERE ELRKEEQVSI
NARDYDTGEI HVMKLKWRGN YYNLIGGWAN IIRQKGLGIG QEIRLRWANN CLYFSVLVEQ
YVPTASGHDN WPIKKALTLS DVDTNHPFLT LPGKAVEDHI LFYWSQQARE QLRNEHQIRI
NARDDDTGDL YAMKLKWRRS YYNLIGKWGK IIREKRLQVG REIRVRWDNG CLIFSVPE
//
