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Database: UniProt
Entry: A0A2V0NNX7_9CHLO
LinkDB: A0A2V0NNX7_9CHLO
Original site: A0A2V0NNX7_9CHLO 
ID   A0A2V0NNX7_9CHLO        Unreviewed;       253 AA.
AC   A0A2V0NNX7;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   28-JUN-2023, entry version 19.
DE   RecName: Full=Cleavage and polyadenylation specificity factor subunit 5 {ECO:0000256|ARBA:ARBA00016266};
GN   ORFNames=Rsub_02171 {ECO:0000313|EMBL:GBF89294.1};
OS   Raphidocelis subcapitata.
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Sphaeropleales; Selenastraceae; Raphidocelis.
OX   NCBI_TaxID=307507 {ECO:0000313|EMBL:GBF89294.1, ECO:0000313|Proteomes:UP000247498};
RN   [1] {ECO:0000313|EMBL:GBF89294.1, ECO:0000313|Proteomes:UP000247498}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-35 {ECO:0000313|EMBL:GBF89294.1,
RC   ECO:0000313|Proteomes:UP000247498};
RX   PubMed=29795299; DOI=10.1038/s41598-018-26331-6;
RA   Suzuki S., Yamaguchi H., Nakajima N., Kawachi M.;
RT   "Raphidocelis subcapitata (=Pseudokirchneriella subcapitata) provides an
RT   insight into genome evolution and environmental adaptations in the
RT   Sphaeropleales.";
RL   Sci. Rep. 8:8058-8058(2018).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the Nudix hydrolase family. CPSF5 subfamily.
CC       {ECO:0000256|ARBA:ARBA00009710}.
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:GBF89294.1}.
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DR   EMBL; BDRX01000009; GBF89294.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2V0NNX7; -.
DR   STRING; 307507.A0A2V0NNX7; -.
DR   InParanoid; A0A2V0NNX7; -.
DR   Proteomes; UP000247498; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005849; C:mRNA cleavage factor complex; IEA:InterPro.
DR   GO; GO:0003729; F:mRNA binding; IEA:InterPro.
DR   GO; GO:0006378; P:mRNA polyadenylation; IEA:InterPro.
DR   Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1.
DR   InterPro; IPR016706; Cleav_polyA_spec_factor_su5.
DR   InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR   InterPro; IPR000086; NUDIX_hydrolase_dom.
DR   PANTHER; PTHR13047:SF0; CLEAVAGE AND POLYADENYLATION SPECIFICITY FACTOR SUBUNIT 5; 1.
DR   PANTHER; PTHR13047; PRE-MRNA CLEAVAGE FACTOR IM, 25KD SUBUNIT; 1.
DR   Pfam; PF13869; NUDIX_2; 1.
DR   SUPFAM; SSF55811; Nudix; 1.
DR   PROSITE; PS51462; NUDIX; 1.
PE   3: Inferred from homology;
KW   mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000247498};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT   DOMAIN          46..174
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000259|PROSITE:PS51462"
FT   REGION          210..253
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   253 AA;  28798 MW;  C3C2571054A8A733 CRC64;
     MLRPSYAHAV YPVDGYKFGH KPAKQEKEGG PPERLARLRA KFEREGLRRS VDAVLLVQQH
     GHPHVLLLQL GNSGLFKLPG GKLKPGEDEI EGLRRKLVTY LSPDDPNLVT PWEIGECVGT
     WWRPNYDTVL YPYLSPHVTR PKEVRRLYIA PLLDRSCFAV PRNYKLVAVP LFELYDNAAR
     FGPVLASIPQ MLCRFRLNIV GGSGAAKLLG GGQPQQQAQQ PQPAQQPYQQ QQQAYPQQQQ
     QQQQQQQQPY QQY
//
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