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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//