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Database: UniProt
Entry: A0A3N4HCK3_ASCIM
LinkDB: A0A3N4HCK3_ASCIM
Original site: A0A3N4HCK3_ASCIM 
ID   A0A3N4HCK3_ASCIM        Unreviewed;       253 AA.
AC   A0A3N4HCK3;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Adenylate kinase {ECO:0000313|EMBL:RPA72079.1};
GN   ORFNames=BJ508DRAFT_419657 {ECO:0000313|EMBL:RPA72079.1};
OS   Ascobolus immersus RN42.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC   Pezizales; Ascobolaceae; Ascobolus.
OX   NCBI_TaxID=1160509 {ECO:0000313|EMBL:RPA72079.1, ECO:0000313|Proteomes:UP000275078};
RN   [1] {ECO:0000313|EMBL:RPA72079.1, ECO:0000313|Proteomes:UP000275078}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RN42 {ECO:0000313|EMBL:RPA72079.1,
RC   ECO:0000313|Proteomes:UP000275078};
RX   PubMed=30420746; DOI=10.1038/s41559-018-0710-4;
RA   Murat C., Payen T., Noel B., Kuo A., Morin E., Chen J., Kohler A.,
RA   Krizsan K., Balestrini R., Da Silva C., Montanini B., Hainaut M.,
RA   Levati E., Barry K.W., Belfiori B., Cichocki N., Clum A., Dockter R.B.,
RA   Fauchery L., Guy J., Iotti M., Le Tacon F., Lindquist E.A., Lipzen A.,
RA   Malagnac F., Mello A., Molinier V., Miyauchi S., Poulain J., Riccioni C.,
RA   Rubini A., Sitrit Y., Splivallo R., Traeger S., Wang M., Zifcakova L.,
RA   Wipf D., Zambonelli A., Paolocci F., Nowrousian M., Ottonello S.,
RA   Baldrian P., Spatafora J.W., Henrissat B., Nagy L.G., Aury J.M.,
RA   Wincker P., Grigoriev I.V., Bonfante P., Martin F.M.;
RT   "Pezizomycetes genomes reveal the molecular basis of ectomycorrhizal
RT   truffle lifestyle.";
RL   Nat. Ecol. Evol. 2:1956-1965(2018).
CC   -!- SIMILARITY: Belongs to the adenylate kinase family.
CC       {ECO:0000256|ARBA:ARBA00007220, ECO:0000256|RuleBase:RU003330}.
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DR   EMBL; ML119881; RPA72079.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3N4HCK3; -.
DR   STRING; 1160509.A0A3N4HCK3; -.
DR   Proteomes; UP000275078; Unassembled WGS sequence.
DR   GO; GO:0004017; F:adenylate kinase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd01428; ADK; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_00235; Adenylate_kinase_Adk; 1.
DR   InterPro; IPR000850; Adenylat/UMP-CMP_kin.
DR   InterPro; IPR033690; Adenylat_kinase_CS.
DR   InterPro; IPR007862; Adenylate_kinase_lid-dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR23359:SF242; GTP:AMP PHOSPHOTRANSFERASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR23359; NUCLEOTIDE KINASE; 1.
DR   Pfam; PF00406; ADK; 2.
DR   Pfam; PF05191; ADK_lid; 1.
DR   PRINTS; PR00094; ADENYLTKNASE.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00113; ADENYLATE_KINASE; 1.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU003330};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000275078};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003330}.
FT   DOMAIN          160..200
FT                   /note="Adenylate kinase active site lid"
FT                   /evidence="ECO:0000259|Pfam:PF05191"
SQ   SEQUENCE   253 AA;  27772 MW;  59A1467B9390DBD4 CRC64;
     MSTTRTLTRA ARLILIGPPG CGKGTQTQRI LNTFPQISAL SAGDLLRENV RLRTPLGIRA
     ESVLREGRLL PDDTVTSLII SELATRGWIA GPGGEALAAG VVLGDRKASV SDDPASSFLL
     DGFPRTRGQA EGLSASGVSI NLAVQIDMPD RFILERFKDR MVHPASGRSY NLSWKNPPPK
     DADGNYLDEV TGEKLVKRDD DKEETVMRRL DTYKRNVEPL LEYYGRDGVL VTITGSESDK
     ITPEIFRVMD RFA
//
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