ID Q1CWL9_MYXXD Unreviewed; 502 AA.
AC Q1CWL9;
DT 11-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 109.
DE SubName: Full=HAD superfamily (Subfamily IG) hydrolase, 5'-nucleotidase {ECO:0000313|EMBL:ABF87462.1};
GN OrderedLocusNames=MXAN_7091 {ECO:0000313|EMBL:ABF87462.1};
OS Myxococcus xanthus (strain DK1622).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Myxococcaceae; Myxococcus.
OX NCBI_TaxID=246197 {ECO:0000313|EMBL:ABF87462.1, ECO:0000313|Proteomes:UP000002402};
RN [1] {ECO:0000313|EMBL:ABF87462.1, ECO:0000313|Proteomes:UP000002402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DK1622 {ECO:0000313|Proteomes:UP000002402};
RX PubMed=17015832; DOI=10.1073/pnas.0607335103;
RA Goldman B.S., Nierman W.C., Kaiser D., Slater S.C., Durkin A.S.,
RA Eisen J.A., Ronning C.M., Barbazuk W.B., Blanchard M., Field C.,
RA Halling C., Hinkle G., Iartchuk O., Kim H.S., Mackenzie C., Madupu R.,
RA Miller N., Shvartsbeyn A., Sullivan S.A., Vaudin M., Wiegand R.,
RA Kaplan H.B.;
RT "Evolution of sensory complexity recorded in a myxobacterial genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15200-15205(2006).
CC -!- SIMILARITY: Belongs to the 5'(3')-deoxyribonucleotidase family.
CC {ECO:0000256|ARBA:ARBA00009589}.
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DR EMBL; CP000113; ABF87462.1; -; Genomic_DNA.
DR RefSeq; WP_011557010.1; NC_008095.1.
DR AlphaFoldDB; Q1CWL9; -.
DR STRING; 246197.MXAN_7091; -.
DR EnsemblBacteria; ABF87462; ABF87462; MXAN_7091.
DR GeneID; 41364266; -.
DR KEGG; mxa:MXAN_7091; -.
DR eggNOG; COG1196; Bacteria.
DR HOGENOM; CLU_017845_4_1_7; -.
DR OrthoDB; 1488958at2; -.
DR Proteomes; UP000002402; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd07522; HAD_cN-II; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR008380; HAD-SF_hydro_IG_5-nucl.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR016695; Pur_nucleotidase.
DR NCBIfam; TIGR02244; HAD-IG-Ncltidse; 1.
DR PANTHER; PTHR12103; 5'-NUCLEOTIDASE DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR12103:SF22; HAD-SUPERFAMILY HYDROLASE, SUBFAMILY IG, 5'-NUCLEOTIDASE; 1.
DR Pfam; PF05761; 5_nucleotid; 1.
DR PIRSF; PIRSF017434; Purine_5'-nucleotidase; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ABF87462.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000002402}.
FT REGION 475..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 502 AA; 56841 MW; E5D25BD8B6E29EEF CRC64;
MSTFIPGPPP ERGLFCNRTL NLRAIKAVGY DMDYTLIHYH VEAWERRAYE HIRDRLVEQG
WPVADLSFDP ELSMRGLIID TEKGNLLKAN RFGFVKKALH GTQAMSFEAQ RDEYARTIID
LHEQRWVFLN TLFSLSEACI YAQLVDRLDA GQLPGPMGYS DLYEHVRKNL DATHMQGRLK
AEIIADPERY VIDDPETPLA LLDQRNAGKK LLLITNSEWA YTEPMMHFAF DRHLPEGMTW
RQLFDVVIVS ARKPEFFTTR SSLFEVVESS GEALLRPHTG PFKPGTPYFG GSAVELERHL
GMSGDQILYV GDHMFGDVHV TKNVLRWRTA LILRELEDEV RSIASFRATE TRLAERMVVK
ERLEAESCQI RLELQRRRFQ YGPRTDTPSE TELVARLATL RTELEALDAE LGPLARAATE
LSNPIWGLLT RAGNDKSHLA RQVERYADIY TSRVSNFLFA TPFVYLRSPR GSLPHDPSLP
GGTPVFGASE AGGGMSGTDG GE
//
