ID   A0A0W1AH82_9GAMM        Unreviewed;       911 AA.
AC   A0A0W1AH82;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Adenylyl transferase {ECO:0000313|EMBL:KTD80684.1};
GN   ORFNames=Lwor_0927 {ECO:0000313|EMBL:KTD80684.1};
OS   Legionella worsleiensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=45076 {ECO:0000313|EMBL:KTD80684.1, ECO:0000313|Proteomes:UP000054662};
RN   [1] {ECO:0000313|EMBL:KTD80684.1, ECO:0000313|Proteomes:UP000054662}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49508 {ECO:0000313|EMBL:KTD80684.1,
RC   ECO:0000313|Proteomes:UP000054662};
RA   Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA   Pupko T., Shuman H.A., Segal G.;
RT   "Genomic analysis of 38 Legionella species identifies large and diverse
RT   effector repertoires.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KTD80684.1}.
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DR   EMBL; LNZC01000009; KTD80684.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0W1AH82; -.
DR   STRING; 45076.Lwor_0927; -.
DR   PATRIC; fig|45076.6.peg.1009; -.
DR   OrthoDB; 9759366at2; -.
DR   Proteomes; UP000054662; Unassembled WGS sequence.
DR   GO; GO:0008882; F:[glutamate-ammonia-ligase] adenylyltransferase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   CDD; cd05401; NT_GlnE_GlnD_like; 2.
DR   Gene3D; 1.20.120.1510; -; 1.
DR   Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 2.
DR   Gene3D; 1.20.120.330; Nucleotidyltransferases domain 2; 2.
DR   InterPro; IPR023057; GlnE.
DR   InterPro; IPR005190; GlnE_rpt_dom.
DR   InterPro; IPR043519; NT_sf.
DR   InterPro; IPR013546; PII_UdlTrfase/GS_AdlTrfase.
DR   PANTHER; PTHR30621:SF0; BIFUNCTIONAL GLUTAMINE SYNTHETASE ADENYLYLTRANSFERASE_ADENYLYL-REMOVING ENZYME; 1.
DR   PANTHER; PTHR30621; GLUTAMINE SYNTHETASE ADENYLYLTRANSFERASE; 1.
DR   Pfam; PF08335; GlnD_UR_UTase; 2.
DR   Pfam; PF03710; GlnE; 2.
DR   SUPFAM; SSF81301; Nucleotidyltransferase; 2.
DR   SUPFAM; SSF81593; Nucleotidyltransferase substrate binding subunit/domain; 2.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054662};
KW   Transferase {ECO:0000313|EMBL:KTD80684.1}.
FT   DOMAIN          81..263
FT                   /note="Glutamate-ammonia ligase adenylyltransferase
FT                   repeated"
FT                   /evidence="ECO:0000259|Pfam:PF03710"
FT   DOMAIN          293..428
FT                   /note="PII-uridylyltransferase/Glutamine-synthetase
FT                   adenylyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF08335"
FT   DOMAIN          549..784
FT                   /note="Glutamate-ammonia ligase adenylyltransferase
FT                   repeated"
FT                   /evidence="ECO:0000259|Pfam:PF03710"
FT   DOMAIN          818..884
FT                   /note="PII-uridylyltransferase/Glutamine-synthetase
FT                   adenylyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF08335"
SQ   SEQUENCE   911 AA;  105197 MW;  D7548B4272CE85D0 CRC64;
     MMQNSRYSDL ISAKSWFIEK HTANINHPFK ESVEQLLLIS DYSCRYIKLL ELLLEEECIA
     LLCREDYFYA INELNLDTAQ PHFIKALRQF RNTHFLHLLV LERAEIASTE DVMRSWSDCA
     DAIILHALRY CQYTLSAQYG TPRNARGEEV DLFVLAMGKL GGRELNYSSD IDLIFAFDEV
     GFTDGDTVLT NQEFFSKVVQ QFIQLLQPVT PDGFVFRVDL RLRPYGDSGP LVSSLAAMET
     YYQEQGRDWE RYAMVKARVI TQSLNETVLW FDRLIIPFVY RRYVDFSVIE SLRSMKSMIE
     REVRLNPRLD DIKRGKGGIR EVEFIIQNVQ LIRGGRMPRL QVQNAMAALD VLKQEQLLPR
     CDALKQAYLF LRKLENALQS LGDQQTHSLP QEAIKQTQIT LAMGFTHWDD LLAKLHQYQR
     IVSNSFHSIL GKVEVYEDEK RVLANQLSNV WQGHVEQSMA INLLTSLGFA NAPHCYQMIH
     AFRHGSRCRR LPQGARIRLD RFMVMLLSEL THFPHTDEVL LQVMHLLEHI VGRSAYLALL
     TENPSVLKEL LFWLANSPFI TSLFVNQPFL LEVLLDHGEH WRPASRRQLE QMIAEQLAEV
     DECELKEERL RQFKLTHWLL AARSELNGTS KAVRMGQFLA DVAEVIVTQV MNIACQQLSL
     RNPEMAAIKK SFAIIAYGKL GSREMNYSSD LDLVFLHTAK PSEEALVTRL TQKIIHMLTT
     RTQSGVLYSV DTRLRPSGSA GLLVSPIDAF IEYQKAQAWT WEHQALLKAR IVFGNRKIKQ
     DFTRLKKTIL GLSREKTSLQ EEVLTMRAKI DQHQDSDLIK HSRGGLLDLE FLIQFLVLSA
     GDSGFAHHTH TLNQIEHLYL TKAITREQLN ILRRAYRYYH RVLHQKILQP GFDHAEGINE
     AVIEVCQEIY H
//