ID C9SMS3_VERA1 Unreviewed; 365 AA.
AC C9SMS3;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=ATP-grasp domain-containing protein {ECO:0000259|PROSITE:PS50975};
GN ORFNames=VDBG_06197 {ECO:0000313|EMBL:EEY20088.1};
OS Verticillium alfalfae (strain VaMs.102 / ATCC MYA-4576 / FGSC 10136)
OS (Verticillium wilt of alfalfa) (Verticillium albo-atrum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=526221 {ECO:0000313|Proteomes:UP000008698};
RN [1] {ECO:0000313|Proteomes:UP000008698}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VaMs.102 / ATCC MYA-4576 / FGSC 10136
RC {ECO:0000313|Proteomes:UP000008698};
RX PubMed=21829347; DOI=10.1371/journal.ppat.1002137;
RA Klosterman S.J., Subbarao K.V., Kang S., Veronese P., Gold S.E.,
RA Thomma B.P.H.J., Chen Z., Henrissat B., Lee Y.-H., Park J.,
RA Garcia-Pedrajas M.D., Barbara D.J., Anchieta A., de Jonge R., Santhanam P.,
RA Maruthachalam K., Atallah Z., Amyotte S.G., Paz Z., Inderbitzin P.,
RA Hayes R.J., Heiman D.I., Young S., Zeng Q., Engels R., Galagan J.,
RA Cuomo C.A., Dobinson K.F., Ma L.-J.;
RT "Comparative genomics yields insights into niche adaptation of plant
RT vascular wilt pathogens.";
RL PLoS Pathog. 7:E1002137-E1002137(2011).
CC -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC {ECO:0000256|ARBA:ARBA00010871}.
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DR EMBL; DS985220; EEY20088.1; -; Genomic_DNA.
DR RefSeq; XP_003003755.1; XM_003003709.1.
DR AlphaFoldDB; C9SMS3; -.
DR STRING; 526221.C9SMS3; -.
DR GeneID; 9534938; -.
DR KEGG; val:VDBG_06197; -.
DR eggNOG; ENOG502QPTY; Eukaryota.
DR HOGENOM; CLU_784577_0_0_1; -.
DR OMA; HGVKLCH; -.
DR OrthoDB; 5473129at2759; -.
DR Proteomes; UP000008698; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008716; F:D-alanine-D-alanine ligase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR011095; Dala_Dala_lig_C.
DR PANTHER; PTHR23132; D-ALANINE--D-ALANINE LIGASE; 1.
DR PANTHER; PTHR23132:SF0; D-ALANINE-D-ALANINE LIGASE FAMILY; 1.
DR Pfam; PF07478; Dala_Dala_lig_C; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Reference proteome {ECO:0000313|Proteomes:UP000008698}.
FT DOMAIN 137..351
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 365 AA; 39914 MW; 5EF4181442A1CCE5 CRC64;
MSVENEQRAK PRVAVLYQTT EPPVIDGTRK PMKPGGYQDS GADIGYALSL SDEVEVITQS
SDPVPEQHAG WCFPDTEEGI LQAIERGATH LWANTILFAS HPIQVSTKVG KHQNYLRVVG
QGPLLVEKYD NKDYVNDLLR RLGGFTMPRA WSLPSGPITL SDIDDCIYPL VVKPARGRGS
YGVKVCKDAS ELISHAESLR SEGLNLVMVE EYLAGEEATV TVMPPSLDRL GYLALPVVTR
FNHQDGIAPY NGTVAVSTNS RAVVGSDDPA YEVISRECEN VARVLGVTGA IRIDVRRYGP
SDPRFVIFDV NMKPNITGPG RPGREDQACL SLLAAGGLGW DYQRLLKEIL GTAVLLTKHR
SLHPR
//
