ID A0A168PLB9_ABSGL Unreviewed; 412 AA.
AC A0A168PLB9;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Nudix hydrolase domain-containing protein {ECO:0000259|PROSITE:PS51462};
GN Name=ABSGL_08388.1 scaffold 10128 {ECO:0000313|EMBL:SAM02585.1};
OS Absidia glauca (Pin mould).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Cunninghamellaceae; Absidia.
OX NCBI_TaxID=4829 {ECO:0000313|EMBL:SAM02585.1};
RN [1] {ECO:0000313|EMBL:SAM02585.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101.48 {ECO:0000313|EMBL:SAM02585.1};
RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA Babar A., Rosenke K.;
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the CWC25 family.
CC {ECO:0000256|ARBA:ARBA00006695}.
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DR EMBL; LT553932; SAM02585.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A168PLB9; -.
DR STRING; 4829.A0A168PLB9; -.
DR InParanoid; A0A168PLB9; -.
DR OrthoDB; 3035837at2759; -.
DR Proteomes; UP000078561; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0016462; F:pyrophosphatase activity; IEA:InterPro.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR CDD; cd04666; Nudix_Hydrolase_9; 1.
DR Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1.
DR InterPro; IPR019339; CIR_N_dom.
DR InterPro; IPR022209; CWC25.
DR InterPro; IPR047198; DDP-like_NUDIX.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR020084; NUDIX_hydrolase_CS.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR PANTHER; PTHR16196; CELL CYCLE CONTROL PROTEIN CWF25; 1.
DR PANTHER; PTHR16196:SF0; PRE-MRNA-SPLICING FACTOR CWC25 HOMOLOG; 1.
DR Pfam; PF10197; Cir_N; 1.
DR Pfam; PF12542; CWC25; 1.
DR Pfam; PF00293; NUDIX; 1.
DR SMART; SM01083; Cir_N; 1.
DR SUPFAM; SSF55811; Nudix; 1.
DR PROSITE; PS51462; NUDIX; 1.
DR PROSITE; PS00893; NUDIX_BOX; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW mRNA splicing {ECO:0000256|ARBA:ARBA00023187};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000078561};
KW Spliceosome {ECO:0000256|ARBA:ARBA00022728};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 235..252
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 279..403
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS51462"
FT REGION 67..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..82
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..207
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..231
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 412 AA; 47502 MW; 710846836C35E4BB CRC64;
MGHSANAICM LCIGGGDLNL KKSWHPSTFK NQERLWKQEK KHAEEQTKIE QMKKELQEER
QLLELQRLQE DSGSRKRSDR LDWMYAAPSS NGPKAGGSEM EDFLLGKKNV DDLLRNKAAN
ETTTTDADER FALTNSNANT ERDIQAKIRE DPLFAIKQKQ QSALKSIIDN PILMKKLKKD
KKDKKSKKKD IKEHHHRHHH RSSSPTHDSG RRRHTSHSST SDHRKRSSRD SDERAVFALF
SSFLLVSLFL LAPPPLMSFS PFGSQARTGR ENQTYDDHYA RQVAGCLPID TKNQRVLLVQ
SSKHDHVWPK GGWENDETVE QAAARETYEE GGVYGDIVGL IGDYLDYDKF GQPKTHFWLY
EMHITQVLDQ WPEMRQRRWF TFDEAMHVLR FKPIMQKALQ QSSFGKNSSA AS
//
