ID   A0A087SAB4_AUXPR        Unreviewed;       828 AA.
AC   A0A087SAB4;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Cleavage and polyadenylation specificity factor subunit 3 {ECO:0000313|EMBL:KFM22668.1};
GN   ORFNames=F751_0464 {ECO:0000313|EMBL:KFM22668.1};
OS   Auxenochlorella protothecoides (Green microalga) (Chlorella
OS   protothecoides).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC   Chlorellales; Chlorellaceae; Auxenochlorella.
OX   NCBI_TaxID=3075 {ECO:0000313|EMBL:KFM22668.1, ECO:0000313|Proteomes:UP000028924};
RN   [1] {ECO:0000313|EMBL:KFM22668.1, ECO:0000313|Proteomes:UP000028924}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0710 {ECO:0000313|EMBL:KFM22668.1,
RC   ECO:0000313|Proteomes:UP000028924};
RX   PubMed=25012212; DOI=10.1186/1471-2164-15-582;
RA   Gao C., Wang Y., Shen Y., Yan D., He X., Dai J., Wu Q.;
RT   "Oil accumulation mechanisms of the oleaginous microalga Chlorella
RT   protothecoides revealed through its genome, transcriptomes, and
RT   proteomes.";
RL   BMC Genomics 15:582-582(2014).
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; KL662079; KFM22668.1; -; Genomic_DNA.
DR   RefSeq; XP_011395524.1; XM_011397222.1.
DR   AlphaFoldDB; A0A087SAB4; -.
DR   STRING; 3075.A0A087SAB4; -.
DR   GeneID; 23611855; -.
DR   KEGG; apro:F751_0464; -.
DR   eggNOG; KOG1137; Eukaryota.
DR   OrthoDB; 169081at2759; -.
DR   Proteomes; UP000028924; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   CDD; cd16292; CPSF3-like_MBL-fold; 1.
DR   Gene3D; 3.40.50.10890; -; 1.
DR   Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 2.
DR   InterPro; IPR022712; Beta_Casp.
DR   InterPro; IPR021718; CPSF73-100_C.
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; PF16661; Lactamase_B_6; 2.
DR   Pfam; PF07521; RMMBL; 1.
DR   SMART; SM01027; Beta-Casp; 1.
DR   SMART; SM00849; Lactamase_B; 2.
DR   SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 2.
PE   4: Predicted;
KW   mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028924}.
FT   DOMAIN          39..229
FT                   /note="Metallo-beta-lactamase"
FT                   /evidence="ECO:0000259|SMART:SM00849"
FT   DOMAIN          232..459
FT                   /note="Metallo-beta-lactamase"
FT                   /evidence="ECO:0000259|SMART:SM00849"
FT   DOMAIN          471..592
FT                   /note="Beta-Casp"
FT                   /evidence="ECO:0000259|SMART:SM01027"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   828 AA;  86958 MW;  AE1EAD718309FDB4 CRC64;
     MTVAAGPSEA VPAPPADAAP TTPTSHVEII PLGAAQEVGR SCVIVRFAGK TVMLDCGVHP
     GFSGLASLPF FDVIDMSSVD VMLVTHFHLD HSAAVPYVVG HTNFRGTILM THATKAITST
     LLRDFVKVSK GGAGESGVQG SRGLGGFGRG DAGLYTEADL DASLERTHVI NFQQTLCVNG
     IGITAYRAGH VLGAAMFMVE IAGQRILYTD AAPTTPTSHV EIIPLGAAQE VGRSCVIVRF
     AGKTVMLDCG VHPGFSGLAS LPFFDVIDMS SVDVMLVTHF HLDHSAAVPY VVGHTNFRGT
     ILMTHATKAI TSTLLRDFVK VSKGGAGESG VQGSRGLGGF GRGDAGLYTE ADLDASLERT
     HVINFQQTLC VNGIGITAYR AGHVLGAAMF MVEIAGQRIL YTGDYSRVPD RHMPAADTPS
     PPPHIVIVES TYGVSRHLPR AERESRFLQR IHTAVARGGR VLLPVVALGR AQELLLILEE
     HWAAHPELHG VPIYQASGLA KRAISVYQTY IEMMNADIQA AFAVANPFAF RHVTHLRSAR
     AFDDVGACVV MATPSMLQSG VSRDLFEAWC GDARNLVVIA DFAVQGTLAR EILAGPAEVL
     TRAGARVPLR CQVDAISFSA HADFPQTSGF LDTLAPPHVV LVRLALELLF EGVHGAGDLA
     LVSSDQGATA NDREGAPVAP QILRVGEAVT VSYDPASAPG RLTLEWQGGP GADAVADAVV
     AVVLGAGPAP PPRLSRLDAA RAEALRGGDG EALALVEAEL VEALLSAQFG PAATDPETGL
     TFLEVDGAHV LVDCKSRGVR CADAGLKARV ERAITRLEAA MRACPLEG
//