ID A0A183C5Q9_GLOPA Unreviewed; 1029 AA.
AC A0A183C5Q9;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=PDZ domain-containing protein {ECO:0000313|WBParaSite:GPLIN_000820400};
OS Globodera pallida (Potato cyst nematode).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Tylenchomorpha; Tylenchoidea; Heteroderidae; Heteroderinae;
OC Globodera.
OX NCBI_TaxID=36090 {ECO:0000313|Proteomes:UP000050741, ECO:0000313|WBParaSite:GPLIN_000820400};
RN [1] {ECO:0000313|Proteomes:UP000050741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lindley {ECO:0000313|Proteomes:UP000050741};
RA Aslett M.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000050741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lindley {ECO:0000313|Proteomes:UP000050741};
RA Cotton J.A., Lilley C.J., Jones L.M., Kikuchi T., Reid A.J., Thorpe P.,
RA Tsai I.J., Beasley H., Blok V., Cock P.J.A., Van den Akker S.E.,
RA Holroyd N., Hunt M., Mantelin S., Naghra H., Pain A., Palomares-Rius J.E.,
RA Zarowiecki M., Berriman M., Jones J.T., Urwin P.E.;
RT "The genome and life-stage specific transcriptomes of Globodera pallida
RT elucidate key aspects of plant parasitism by a cyst nematode.";
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|WBParaSite:GPLIN_000820400}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR AlphaFoldDB; A0A183C5Q9; -.
DR WBParaSite; GPLIN_000820400; GPLIN_000820400; GPLIN_000820400.
DR Proteomes; UP000050741; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd00992; PDZ_signaling; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 1.10.167.10; Regulator of G-protein Signalling 4, domain 2; 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR015212; RGS-like_dom.
DR InterPro; IPR036305; RGS_sf.
DR InterPro; IPR044926; RGS_subdomain_2.
DR PANTHER; PTHR45872; RHO GUANINE NUCLEOTIDE EXCHANGE FACTOR 2, ISOFORM D; 1.
DR PANTHER; PTHR45872:SF2; RHO GUANINE NUCLEOTIDE EXCHANGE FACTOR 2, ISOFORM D; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF17820; PDZ_6; 1.
DR Pfam; PF09128; RGS-like; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF48097; Regulator of G-protein signaling, RGS; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 101..163
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 699..749
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 295..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 426..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 838..861
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 920..984
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..369
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 838..860
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1029 AA; 111820 MW; CBBB7C9C599464E9 CRC64;
MSRWSIISEE SSSNSSATNH TPSIPEFSRQ CRRFSPPTST ATAAGDGDAA QPIKKAATDG
GAAANCLQNI SATVDMAPPV VQQLSETLQQ QQQQQKMTER CVLVARQPDG YGLTVNGEYP
VKVAAVKHNG AAHLAGVRAG DRILKVNGMP VTAQNFQEVI KMISGGYNLA LTLLGPAAMA
ASSWDDFDKL FPVQHQQTPV VQCPQSPPAA MIITGGNNNS GQKIEMLNDP NWRQRCANDL
FRALQRERAN LEASMHRSDK QQQQHIIGPA GGGIKLERAL GRISQLERKL NALSPLLNNN
NNNNNNGRIE HADNNNFNTY QQQQQQTRRR RRGTNAGKCG GGTEKRVSLC SAAESGGSEQ
QSNKTFPPSS MRVAPPKSAA TAAVVAAKVE PIRSWVETGG MHYIHQQQQQ TTTAADLLLM
GDELEEAQEE EDEGRNSDLG SNDDPVGPFS NLQELKSHPA ALAIFLTHLM NTPNPGSLLF
YLITDAFPSS SVKDQRRFAY EIFSTFLIPG APLQLPNIAQ RDIQIIDKVL RTICGSQQPP
EGTDQLRKLF ISTRTRAVSQ INEQLADFRR RGQPFEPVDG VDSVLLDSLT SRADRGAELR
LAGRLLFKTL QNLAKSSTSA PFACIPDFEN IERRTLALIM SIATLIKVVF CLRTSNSSLE
KLLDKCPTFL MPTSKHSGAG TSMFKMLASS AKQKFQLKDH QFLLQPVLLT VHCYQCREAV
WGVNPQAYFC QNCDVVVHKN CTSQLTDHCW PTQQQKAKTG LHHHHHQRQP SASVSTLSLL
NTVNAPLHPS STTRLKHAGG ATTAAGVHYK GVGESVSTYA QSLGGHDSVY SVSILNFPKQ
QRPKRSSPKS SLSLTPPLGR SVHSTALDMK AGSKEGSSID KHGNDLIPPY EHEMMIDADH
HHHPPQHQQM IGTISPAKMH QPKMESLDSS SSPPSSTAML PPPVFSTRFE RIAPPDVPPS
VAPDSAATQS ATKTHRTPRG PCKIGATDHI DGFGHLHASK QQLGTRCDYG INNNDAGGGG
IGSANTISQ
//
