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Database: UniProt
Entry: A0A0L0H720_SPIPD
LinkDB: A0A0L0H720_SPIPD
Original site: A0A0L0H720_SPIPD 
ID   A0A0L0H720_SPIPD        Unreviewed;      1498 AA.
AC   A0A0L0H720;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   RecName: Full=adenylate kinase {ECO:0000256|ARBA:ARBA00012955};
DE            EC=2.7.4.3 {ECO:0000256|ARBA:ARBA00012955};
GN   ORFNames=SPPG_07966 {ECO:0000313|EMBL:KNC96759.1};
OS   Spizellomyces punctatus (strain DAOM BR117).
OC   Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC   Chytridiomycota incertae sedis; Chytridiomycetes; Spizellomycetales;
OC   Spizellomycetaceae; Spizellomyces.
OX   NCBI_TaxID=645134 {ECO:0000313|EMBL:KNC96759.1, ECO:0000313|Proteomes:UP000053201};
RN   [1] {ECO:0000313|EMBL:KNC96759.1, ECO:0000313|Proteomes:UP000053201}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DAOM BR117 {ECO:0000313|EMBL:KNC96759.1,
RC   ECO:0000313|Proteomes:UP000053201};
RG   The Broad Institute Genome Sequencing Platform;
RA   Russ C., Cuomo C., Shea T., Young S.K., Zeng Q., Koehrsen M., Haas B.,
RA   Borodovsky M., Guigo R., Alvarado L., Berlin A., Bochicchio J.,
RA   Borenstein D., Chapman S., Chen Z., Engels R., Freedman E., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C.,
RA   Jen D., Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A.,
RA   Saif S., Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., Walk T.,
RA   White J., Yandava C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA   Lang F.B.F., Roger A.J., Ruiz-Trillo I., Lander E., Nusbaum C.;
RT   "The Genome Sequence of Spizellomyces punctatus strain DAOM BR117.";
RL   Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=AMP + ATP = 2 ADP; Xref=Rhea:RHEA:12973, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.4.3;
CC         Evidence={ECO:0000256|ARBA:ARBA00000582};
CC   -!- SIMILARITY: Belongs to the adenylate kinase family.
CC       {ECO:0000256|ARBA:ARBA00007220}.
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DR   EMBL; KQ257467; KNC96759.1; -; Genomic_DNA.
DR   RefSeq; XP_016604799.1; XM_016756118.1.
DR   STRING; 645134.A0A0L0H720; -.
DR   GeneID; 27691149; -.
DR   VEuPathDB; FungiDB:SPPG_07966; -.
DR   eggNOG; KOG3078; Eukaryota.
DR   eggNOG; KOG3079; Eukaryota.
DR   InParanoid; A0A0L0H720; -.
DR   OMA; MESVCGT; -.
DR   OrthoDB; 52389at2759; -.
DR   Proteomes; UP000053201; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0019205; F:nucleobase-containing compound kinase activity; IEA:InterPro.
DR   GO; GO:0006139; P:nucleobase-containing compound metabolic process; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.890.10; cAMP-dependent protein kinase regulatory subunit, dimerization-anchoring domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR000850; Adenylat/UMP-CMP_kin.
DR   InterPro; IPR033690; Adenylat_kinase_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR23359:SF81; ADENYLATE KINASE 8; 1.
DR   PANTHER; PTHR23359; NUCLEOTIDE KINASE; 1.
DR   Pfam; PF00406; ADK; 3.
DR   PRINTS; PR00094; ADENYLTKNASE.
DR   SMART; SM00382; AAA; 3.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 4.
DR   PROSITE; PS00113; ADENYLATE_KINASE; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053201};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          23..303
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          436..615
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          1025..1158
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          173..245
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        205..229
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        230..244
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1498 AA;  165895 MW;  DF471D81FEDAB268 CRC64;
     MMGTVNEILS TLALPDTSTA IAPRPCYLIL GKPGAGKTTL ASRLAASLNA QWISPESLLL
     HALSNTASPW HKEIQSCLAS GGAVAPETLI AIVKDMIASQ ETDFQGYVLE GLPGNLTDSA
     QDMSLLTDLL NKRPAHHVPV LIQLNISDED LIRRRAAQWI DMETGIIYPG PQVVHSRERW
     AQGKGDEEDD DEDNEGGSES SGKNHDDEEE EDDDDDDEEN SEDDEDQQEE GETDRRREAK
     KPKTSLSDLV TNVQWPLIPM DVVDRLIKRP EDAPESVTAH LAAVSQYDSL LADFKRNYFD
     ANHTIELDAT QHPTVLYKNL MDRLHVLGYG VFTKAVLPKP LAPPDGGFKA GTTDQEIFKI
     FCSTQLEEGE PKREVGIWGK YCPVTYTRNN GQLVQVSSFD FCAAYKGQIY FFASQTDLQA
     FLSNPAKYLS TPPRLSPLHI SILGGPFSGK TTQSKLLAHL YGLVHVSLDE VFDEWCALSE
     EQGNKVWGTV FGQILRKCRL GKTIAPTLQV QVIQLVISKA FELKRYNGWI LDGFPRTMDQ
     MNAMIAADLN PHRTIVLEND INDETVRGRM MAFVSDPITG RPVTTSTTTN GMTPNAPSIL
     AYPNFDNLFN GFREDLANMT KTLSNVVTLP ADRGIQTVLS SIQGHMDPFL PKAVPLTPKM
     QAELPAQIPL GTTKDYCPVM LKQGILVKGD RNFTVKYQGQ YYHLTSEDAK TTFVTEPQTY
     IHSPLPPPRL IFLGPPGSGL DALIPALLST LSTPIPHIVF ETFVLSWAAM QGGAVKEEVE
     FMLQENGGIG AHVLTDVLKT LFYSEPYKTT GFILTSFPRT KLDCDTLLKY SLHVDAMVVL
     DCESSVALKR VVSRLRRGGV VDGVAVPHDA QAADDDDEEW EDKVLEEIEK HQSRISEITS
     TFSSQSSIPL FTIDASRPIR PVLASVKHDL RPFLEYRASL LGNAFKVTKK EAKVLLDLGV
     VVYSPFRKYC PVTLEKNRFL TRECTGTLPV VYGGCIYFLK DRNARTHFIQ NTTHYTALPP
     PPPLLRPHLT LVGPPKSGKT TLAKSIAQSF GLVYLDVETI VAGLAGFSGV SEQVKATLEA
     GLPLPDTLVT EAIRTITSCA MCQEKGWILD GYPITTAQAH LLESAGVVPH CVFVLDIPVE
     EGLKRGMVDW EIEAESPLPP LNTPTTLNQY SQVYETHISA IDTHYTTAYA NVTHLDALRS
     KWALKNLVVK AVQDVMVARQ EYFGRIGRGK AASITSTSIP LTHISTHLSP HLTYCPVSLH
     LHQTLIQPPS THMAEYKQQY YYLAGPSEQA LFLEDPELYI RTPLPAELPR VVTQEEVKAM
     FPKGFECGGY CPVALKEGGK GFASLVRGLP TLTALYAQKL YSFSTPTALA KFLATPHLYT
     SLTPPKKLPP PMTPIATHTL PIPGYIDQTL SETLVAALED LARKRPKYPY WTPEASAIEF
     LAVWLKGHNT KSSEWVRRGY SERLEGFLRS CEIIHSEERE RVEGIWKLRP IRRGGLES
//
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