ID A0A2G5SUE9_9PELO Unreviewed; 549 AA.
AC A0A2G5SUE9;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:PIC18559.1};
GN Name=Cni-mig-23 {ECO:0000313|EMBL:PIC18559.1};
GN Synonyms=Cnig_chr_X.g24408 {ECO:0000313|EMBL:PIC18559.1};
GN ORFNames=B9Z55_024408 {ECO:0000313|EMBL:PIC18559.1};
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:PIC18559.1, 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 -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family.
CC {ECO:0000256|ARBA:ARBA00009283, ECO:0000256|RuleBase:RU003833}.
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:PIC18559.1}.
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DR EMBL; PDUG01000006; PIC18559.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5SUE9; -.
DR STRING; 1611254.A0A2G5SUE9; -.
DR Proteomes; UP000230233; Chromosome x.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
DR Gene3D; 3.30.420.40; -; 1.
DR Gene3D; 3.30.420.150; Exopolyphosphatase. Domain 2; 1.
DR InterPro; IPR000407; GDA1_CD39_NTPase.
DR PANTHER; PTHR11782; ADENOSINE/GUANOSINE DIPHOSPHATASE; 1.
DR PANTHER; PTHR11782:SF121; NUCLEOSIDE-DIPHOSPHATASE MIG-23; 1.
DR Pfam; PF01150; GDA1_CD39; 1.
DR PROSITE; PS01238; GDA1_CD39_NTPASE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PIRSR:PIRSR600407-2};
KW Hydrolase {ECO:0000256|RuleBase:RU003833};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR600407-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000230233};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT ACT_SITE 174
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-1"
FT BINDING 217..221
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-2"
SQ SEQUENCE 549 AA; 62088 MW; DA9604201C123017 CRC64;
MRVSRRFTIL AITAMIFLSL IICIYAVAAH TTVNVILQEQ ERSYGVICDA GSTGTRLFVY
NWVSTSDSEL IQIEPVIYDN KPVMKKISPG LSTFGTKPDE AAEYLRPLME LAELHIPEDK
RPYTPVFIFA TAGMRLIPDE QKEAVLTNLR TELPKITSMQ VLKEHIRIIE GKWEGIYSWI
AVNYALGKFN RTFTPDFPGT SPGQQRSKTV GMIDMGGASA QIAFELPDND DFNSINVENI
NLGCREDDSL FRYKLFVTTF LGYGVNEGIR KYEKTLMAKL KDLNGTVIQD DCMPLNLHKT
VTMENGEKFV RRGTGNWDTC AAEVKKLLNP ETSSEVCKAE AAKCYFGAVP APNIPLSNVE
MYGFSEYWYS THDVLGLGGQ YNAENIAKKS EQYCGQRWST IQAASKKNLY PRADEERLKT
QCFKSAWITS VLHDGFSVDK THNKFQSVST IAGQEVQWAL GAMIYHMRFF PLRDSTRNLI
VKETHSASES LWAPLFFLSA VFCLFVLVCA KEHSLLCFDD KRRGPFGITR SQYSYKILKD
NTTFYKDIA
//
