ID A0A2J6QLY7_9HELO Unreviewed; 211 AA.
AC A0A2J6QLY7;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 13-SEP-2023, entry version 19.
DE RecName: Full=guanylate kinase {ECO:0000256|ARBA:ARBA00012961};
DE EC=2.7.4.8 {ECO:0000256|ARBA:ARBA00012961};
GN ORFNames=NA56DRAFT_641006 {ECO:0000313|EMBL:PMD27284.1};
OS Hyaloscypha hepaticicola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Hyaloscyphaceae; Hyaloscypha.
OX NCBI_TaxID=2082293 {ECO:0000313|EMBL:PMD27284.1, ECO:0000313|Proteomes:UP000235672};
RN [1] {ECO:0000313|EMBL:PMD27284.1, ECO:0000313|Proteomes:UP000235672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 7357 {ECO:0000313|EMBL:PMD27284.1,
RC ECO:0000313|Proteomes:UP000235672};
RG DOE Joint Genome Institute;
RA Martino E., Morin E., Grelet G., Kuo A., Kohler A., Daghino S., Barry K.,
RA Choi C., Cichocki N., Clum A., Copeland A., Hainaut M., Haridas S.,
RA Labutti K., Lindquist E., Lipzen A., Khouja H.-R., Murat C., Ohm R.,
RA Olson A., Spatafora J., Veneault-Fourrey C., Henrissat B., Grigoriev I.,
RA Martin F., Perotto S.;
RT "A degradative enzymes factory behind the ericoid mycorrhizal symbiosis.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the guanylate kinase family.
CC {ECO:0000256|ARBA:ARBA00005790}.
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DR EMBL; KZ613466; PMD27284.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2J6QLY7; -.
DR STRING; 1745343.A0A2J6QLY7; -.
DR OrthoDB; 324675at2759; -.
DR Proteomes; UP000235672; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004385; F:guanylate kinase activity; IEA:UniProtKB-EC.
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 HAMAP; MF_00328; Guanylate_kinase; 1.
DR InterPro; IPR008145; GK/Ca_channel_bsu.
DR InterPro; IPR008144; Guanylate_kin-like_dom.
DR InterPro; IPR017665; Guanylate_kinase.
DR InterPro; IPR020590; Guanylate_kinase_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR03263; guanyl_kin; 1.
DR PANTHER; PTHR23117:SF13; GUANYLATE KINASE; 1.
DR PANTHER; PTHR23117; GUANYLATE KINASE-RELATED; 1.
DR Pfam; PF00625; Guanylate_kin; 1.
DR SMART; SM00072; GuKc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:PMD27284.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000235672};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 8..190
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000259|PROSITE:PS50052"
FT REGION 192..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 211 AA; 23647 MW; E5F5791DD4F8418D CRC64;
MAPVPTDLRP IVISGPSGVG KGTLYKLLLE RHPSIFATSV SHTTRDPRPG EKRGVDYYYI
TMAEFEKMIE EKAFVEHAKF GGNRYGTSKR TIGELTASGR VVVLDIEMEG VKQIKNSHIE
ARYVFIAPPS MEVLEQRLRG RGTEKEDSIQ KRLAQARNEL EYSETPGVHD LTIVNDDLEN
AYTELEEFVF QKRTQDQGAK DEGAAGESVQ D
//
