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Entry: A0A1B9H2F8_9TREE
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ID   A0A1B9H2F8_9TREE        Unreviewed;       447 AA.
AC   A0A1B9H2F8;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=adenylate kinase {ECO:0000256|ARBA:ARBA00012955};
DE            EC=2.7.4.3 {ECO:0000256|ARBA:ARBA00012955};
GN   ORFNames=I316_00575 {ECO:0000313|EMBL:OCF37453.1};
OS   Kwoniella heveanensis BCC8398.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Kwoniella.
OX   NCBI_TaxID=1296120 {ECO:0000313|EMBL:OCF37453.1, ECO:0000313|Proteomes:UP000092666};
RN   [1] {ECO:0000313|EMBL:OCF37453.1, ECO:0000313|Proteomes:UP000092666}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCC8398 {ECO:0000313|EMBL:OCF37453.1,
RC   ECO:0000313|Proteomes:UP000092666};
RG   The Broad Institute Genome Sequencing Platform;
RA   Cuomo C., Litvintseva A., Chen Y., Heitman J., Sun S., Springer D.,
RA   Dromer F., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A.,
RA   Alvarado L., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA   Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA   Murphy C., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Cryptococcus heveanensis BCC8398.";
RL   Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000092666}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCC8398 {ECO:0000313|Proteomes:UP000092666};
RA   Cuomo C., Litvintseva A., Heitman J., Chen Y., Sun S., Springer D.,
RA   Dromer F., Young S., Zeng Q., Chapman S., Gujja S., Saif S., Birren B.;
RT   "Evolution of pathogenesis and genome organization in the Tremellales.";
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the adenylate kinase family.
CC       {ECO:0000256|ARBA:ARBA00007220, ECO:0000256|RuleBase:RU003330}.
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DR   EMBL; KV700122; OCF37453.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1B9H2F8; -.
DR   STRING; 1296120.A0A1B9H2F8; -.
DR   Proteomes; UP000092666; 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; IPR006259; Adenyl_kin_sub.
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   NCBIfam; TIGR01351; adk; 1.
DR   PANTHER; PTHR23359:SF22; GTP:AMP PHOSPHOTRANSFERASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR23359; NUCLEOTIDE KINASE; 1.
DR   Pfam; PF00406; ADK; 1.
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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:UP000092666};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003330}.
FT   DOMAIN          231..266
FT                   /note="Adenylate kinase active site lid"
FT                   /evidence="ECO:0000259|Pfam:PF05191"
FT   REGION          32..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          315..365
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          406..447
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        317..359
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   447 AA;  48657 MW;  3FE614DD34FBDEB5 CRC64;
     MLVALRPLTG TRLTSAAPSS SSCNALRYLS TTVRRRQPVS STPRRGKPSS TSSATAGTTA
     EAVGAAATQT LETISDSFHS IAQKFKSAVE HSHSEQYEGV EERGLRMLVF GKPGSGKNPS
     YVCSLVRDYD IAFVSTGDVL RKEIAAKSDV GQKAEAIVAS GGLVSDELML EIIKAELDRL
     HGKSWIIDGF PRTLHQGELL DKVLNEENRP LNMIVHLNVP DSVIMARIAA RWVHLPSGRV
     YNTTYSAPKV AGKDDVTGEP LTKRPDDTPE TFSKRLHAYY ESTAPLLEYF AKTYPSSLFS
     LSGSSSDEVL IAAGLKSAPS PTQTQTQTEN LNKSETTNQD SSTDLNRSPS KSAPSPTPTD
     VVDPNLKPFA ELKFTPKTDS AQSLAALDQL WPQLVSLIEP FNLRRKPAED LTDEEVKEVR
     KEADDLKDPG EVDMGDKKGG KRTVQRE
//
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