ID A0A2G5ULN8_9PELO Unreviewed; 1020 AA.
AC A0A2G5ULN8;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 08-NOV-2023, entry version 21.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:PIC40429.1};
GN Name=Cnig_chr_III.g11774 {ECO:0000313|EMBL:PIC40429.1};
GN ORFNames=B9Z55_011774 {ECO:0000313|EMBL:PIC40429.1};
OS Caenorhabditis nigoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=1611254 {ECO:0000313|EMBL:PIC40429.1, ECO:0000313|Proteomes:UP000230233};
RN [1] {ECO:0000313|Proteomes:UP000230233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JU1422 {ECO:0000313|Proteomes:UP000230233};
RA Yin D., Schwarz E.M., Thomas C.G., Felde R.L., Korf I.F., Cutter A.D.,
RA Schartner C.M., Ralston E.J., Meyer B.J., Haag E.S.;
RT "Rapid genome shrinkage in a self-fertile nematode reveals novel sperm
RT competition proteins.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the ANKZF1/VMS1 family.
CC {ECO:0000256|ARBA:ARBA00009262}.
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:PIC40429.1}.
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DR EMBL; PDUG01000003; PIC40429.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5ULN8; -.
DR STRING; 1611254.A0A2G5ULN8; -.
DR Proteomes; UP000230233; Chromosome iii.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032012; P:regulation of ARF protein signal transduction; IEA:InterPro.
DR CDD; cd01252; PH_GRP1-like; 1.
DR CDD; cd00171; Sec7; 1.
DR Gene3D; 1.10.220.20; -; 1.
DR Gene3D; 1.10.1000.11; Arf Nucleotide-binding Site Opener,domain 2; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR047139; ANKZ1/VMS1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR023394; Sec7_C_sf.
DR InterPro; IPR000904; Sec7_dom.
DR InterPro; IPR035999; Sec7_dom_sf.
DR InterPro; IPR041540; VATC.
DR InterPro; IPR041175; VLRF1/Vms1.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR16036; ANKYRIN REPEAT AND ZINC FINGER DOMAIN-CONTAINING PROTEIN 1; 1.
DR PANTHER; PTHR16036:SF2; ANKYRIN REPEAT AND ZINC FINGER DOMAIN-CONTAINING PROTEIN 1; 1.
DR Pfam; PF18826; bVLRF1; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF01369; Sec7; 1.
DR Pfam; PF18716; VATC; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00222; Sec7; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF48425; Sec7 domain; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50190; SEC7; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 3: Inferred from homology;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Reference proteome {ECO:0000313|Proteomes:UP000230233};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 53..239
FT /note="SEC7"
FT /evidence="ECO:0000259|PROSITE:PS50190"
FT DOMAIN 261..380
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 499..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 749..772
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 897..948
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 713..740
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 908..948
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1020 AA; 117674 MW; D4C21336ABF61E09 CRC64;
MSSRYSERNG PSESEKMTLP KVRKRKAQLV DEIEALKNEV REVDEELDQV YYTHPKSKDY
QKIVVNGRKK FNQDPWKALD WLASRNVVAK DPQALALWMK AGEGLSKSAI GEILGDNRPF
ALETLDKFTR EHRLHDVPIV PALRQYLFSF RLPGESQKIN RILEKFAEIY ALQNPSYGNA
DQAHTVAYSC IMVNTLLHNP NVKDKPTLEK YIEMNEQLLE SGAITIEQLT EVYESVSITQ
FKIPDEVSST GKGSVNDILL HAEREGWLFK QSSNPLFSGA LSWKKRWFVL SENCLYYFDQ
MTDKEPKGII TLANVGIRKV EAPTRPFMFE IYSLSDGQIK ACKTEQDGRL VEGRHSIYRI
CAVNDEDMRS WINAISRMMA PQQQMMTRPK TPKIMVLTLK SLEFMNGVEA FRIEENEEIS
GGKVAEKESV SVETDAGMAL MLEWKMRLSE DSDMCTTCQC SVDFQDRSAI LEHYQSLFHR
TNVLRKAKNL PIFEEEDFDG TEKDDHDLTQ SSQTPSTTVE SDDEEFDALL LPANRAFFVR
DDHVFSIPRN ILHVDETDVT NSTFLRPFNC TIILWNGGHF AAAVFENDRI AAQKSFHRYV
ARAKQGGVQS QHDSGGKGAA KSAGAQLRRY NEQKMKEEIQ QMVRDWSQHL QKTPLVFIRC
ATYHRSVFFE ANADLYPRDA RIRTIPFETK RPTKDEVEET WRRLQEVRPH GTNSEFRSEM
EEIREKRKEL ARKVAGKKRK DGGLSMICEW SDHDDESKDE QSDKKAKKTQ QIRVRAMRKS
EDVVQQIQWP GLDDEWRQKT YNLIRQDDAN SLREHVESLN EDVRNEAIDY LRNAKIPPNR
SHFLHVSAAN SAKNCLKYLL DDVQCDSGAK DGAGLPPYSS SANAEIKSIF IDYRSKNDPS
GANWGRTHIP EPKKKVELTE EQEKEKAEKQ REKKQRQKAR ERTKKEEQKQ IELENAECQK
YREMSERERR AQAVERRLAG LPPIMRCHQC GRQLPPTPFQ YSHFNFCSTD CVAGHRKANP
//
