ID C9SPX8_VERA1 Unreviewed; 854 AA.
AC C9SPX8;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Guanylate kinase {ECO:0000313|EMBL:EEY20903.1};
GN ORFNames=VDBG_07013 {ECO:0000313|EMBL:EEY20903.1};
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).
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DR EMBL; DS985222; EEY20903.1; -; Genomic_DNA.
DR RefSeq; XP_003002442.1; XM_003002396.1.
DR AlphaFoldDB; C9SPX8; -.
DR STRING; 526221.C9SPX8; -.
DR GeneID; 9527436; -.
DR KEGG; val:VDBG_07013; -.
DR eggNOG; KOG0707; Eukaryota.
DR eggNOG; KOG2491; Eukaryota.
DR HOGENOM; CLU_017925_0_0_1; -.
DR OMA; MMGIMDD; -.
DR OrthoDB; 5490969at2759; -.
DR Proteomes; UP000008698; Unassembled WGS sequence.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00071; GMPK; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR008145; GK/Ca_channel_bsu.
DR InterPro; IPR008144; Guanylate_kin-like_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR021861; THO_THOC1.
DR PANTHER; PTHR13265:SF0; HPR1; 1.
DR PANTHER; PTHR13265; THO COMPLEX SUBUNIT 1; 1.
DR Pfam; PF11957; efThoc1; 1.
DR Pfam; PF00625; Guanylate_kin; 1.
DR SMART; SM00072; GuKc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:EEY20903.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008698};
KW Transferase {ECO:0000313|EMBL:EEY20903.1}.
FT DOMAIN 604..782
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000259|PROSITE:PS50052"
FT REGION 305..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 786..854
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 789..827
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 854 AA; 94655 MW; 0459F1155208EE27 CRC64;
MPGTIVSDGR VSTVADVSAV LSDLLDRARG TKPPTIEPAL QKSDLGNDID RITAIFADGR
GAEATESAAQ QSQDKIRQFA VIETAVRDLF KTLVFNTKIE SPEFVQLWNL FDIVSILSDN
GSCDPALLFW MVEELLDSQT IAGCRKIFDF LESRRERITS SHFKQKQLVI LRTCNELLRR
LSRAEDTAFC GRVFIFMFQS FPLGDRSSVN LRGEYHVENV TAYDQSAAPM DPDADKMEVE
KDAAAGPDAN KQSSQDGAVN ADALYPVFWS LQESFSQPKK LFDMTNLEGF KQGLEATVKA
FKVVQKEQGS RPPKAADSAV GGTKRKRNHD DQGDQSNAFN PKYLTSQDLF ELEISDLSFR
RNILVQAYII LEFLLSLSAK AKEKLATIKT QNKSVMYMDQ TLSEEDAKWA SDMKEAVEDG
LKQGSDGPHY HRMVETVLVR DRNWIRWKME GCPPIELPPL SPETWSKAQD ELYSITRNKR
MKPPMGSLPL DFMQDEDDEK ALDKLRAPDR YELPELGSFR RKIADDDFEI EMPTNDETKA
AAIESKASKS WRALRIAARS RLGLFDKISD PEKIDAIFGE IEDPDAVPEP EAAPEQKAVL
PTDQRPVVIS GPPGVGKSTT TDVLLSRQPG AFAKVVRHTT RKPQDGEVAG RDFLFVDKQT
FDMQRDGDAL IEYTTIDGDD YGTSRKTIDG IVASGKVPIL HMDQEARSFG FEARFVLLLP
PNQETMEARL TAAGEREDAV KATGAAVAPY LAEGSILKEG FDEVLVNEKL DATFKALETF
IYGAEQGVSE PEKTDEKPTE ETEAQTEHKL SEDAPAAAAD KNEDDAVMAD AAPAAEDPDK
AQEGLGEFKP SAAT
//