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Database: UniProt
Entry: A0A094HDG4_9PEZI
LinkDB: A0A094HDG4_9PEZI
Original site: A0A094HDG4_9PEZI 
ID   A0A094HDG4_9PEZI        Unreviewed;       268 AA.
AC   A0A094HDG4;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=adenylate kinase {ECO:0000256|ARBA:ARBA00012955};
DE            EC=2.7.4.3 {ECO:0000256|ARBA:ARBA00012955};
DE   Flags: Fragment;
GN   ORFNames=V502_06855 {ECO:0000313|EMBL:KFZ12947.1};
OS   Pseudogymnoascus sp. VKM F-4520 (FW-2644).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420915 {ECO:0000313|EMBL:KFZ12947.1, ECO:0000313|Proteomes:UP000029308};
RN   [1] {ECO:0000313|EMBL:KFZ12947.1, ECO:0000313|Proteomes:UP000029308}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4520 (FW-2644) {ECO:0000313|Proteomes:UP000029308};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the adenylate kinase family.
CC       {ECO:0000256|ARBA:ARBA00007220, ECO:0000256|RuleBase:RU003330}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KFZ12947.1}.
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DR   EMBL; JPKE01002508; KFZ12947.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094HDG4; -.
DR   STRING; 1420915.A0A094HDG4; -.
DR   HOGENOM; CLU_032354_1_1_1; -.
DR   OrthoDB; 167111at2759; -.
DR   Proteomes; UP000029308; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IEA:InterPro.
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   HAMAP; MF_03169; Adenylate_kinase_AK3; 1.
DR   InterPro; IPR000850; Adenylat/UMP-CMP_kin.
DR   InterPro; IPR033690; Adenylat_kinase_CS.
DR   InterPro; IPR007862; Adenylate_kinase_lid-dom.
DR   InterPro; IPR036193; ADK_active_lid_dom_sf.
DR   InterPro; IPR028586; AK3/Ak4_mitochondrial.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR23359:SF22; 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; SSF57774; Microbial and mitochondrial ADK, insert 'zinc finger' domain; 1.
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   Reference proteome {ECO:0000313|Proteomes:UP000029308};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003330}.
FT   DOMAIN          177..212
FT                   /note="Adenylate kinase active site lid"
FT                   /evidence="ECO:0000259|Pfam:PF05191"
FT   NON_TER         268
FT                   /evidence="ECO:0000313|EMBL:KFZ12947.1"
SQ   SEQUENCE   268 AA;  29213 MW;  11095B191BAE6987 CRC64;
     MKLAKAARII LVGAPGVGKG TQSTRLLTAF PQLSAISSGD LLRTHVQNRT PLGIRAESAI
     KAGSLVPDAM ILRLILAELK DRGWLFPGRP APYSLNSSSS AGGEDSAFVA GGMLDTPSLL
     ASFPEPRTCD EPGSSFILDG FPRTAEQAVQ LDNLVPINMV VHLDTPFSVI MDRIAGRWVH
     APSGRSYNTS FNAPRVPGRD DVTGEKLTKR ADDDEGVWLE RLEKFKETSE PLLEHYARKG
     VLWRVGGQTS DEITPKLHKE FARRFAVR
//
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