NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2017541163|emb|CAG0948310|]
View 

partial Bifunctional glutamine synthetase adenylyltransferase/adenylyl-removing enzyme, partial [Geobacteraceae bacterium]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
GlnE1 super family cl34250
Glutamine synthetase adenylyltransferase [Posttranslational modification, protein turnover, ...
 1-146 7.16e-24

Glutamine synthetase adenylyltransferase [Posttranslational modification, protein turnover, chaperones];


The actual alignment was detected with superfamily member COG1391:

Pssm-ID: 441001 [Multi-domain]  Cd Length: 948  Bit Score: 96.36  E-value: 7.16e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541163   1 RTRMEVELAKEKEGSYNIKTGRGGIVDIEFMVQYLQLRHGVNLPEIRSTN-TLLALKAMRLCGVLTEVESATLQSGYkfl 79
Cdd:COG1391   829 REKMRAELGSKSAGRFDLKQDRGGIVDIEFIVQYLVLAHAHEHPELLRNSdNIRLLEALAEAGLLPAEDAEALADAY--- 905

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2017541163  80 rrlenrlrlihdysindlggpREYLDKLAR-RLGYDPKLRHPGDLlmreyEETTEAIRGIYERILGGE 146
Cdd:COG1391   906 ---------------------RLLRRLQHRlRLQEQPARVPPDEL-----EAERAAVRALWQRVFGEP 947
 
Name Accession Description Interval E-value
GlnE1 COG1391
Glutamine synthetase adenylyltransferase [Posttranslational modification, protein turnover, ...
 1-146 7.16e-24

Glutamine synthetase adenylyltransferase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441001 [Multi-domain]  Cd Length: 948  Bit Score: 96.36  E-value: 7.16e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541163   1 RTRMEVELAKEKEGSYNIKTGRGGIVDIEFMVQYLQLRHGVNLPEIRSTN-TLLALKAMRLCGVLTEVESATLQSGYkfl 79
Cdd:COG1391   829 REKMRAELGSKSAGRFDLKQDRGGIVDIEFIVQYLVLAHAHEHPELLRNSdNIRLLEALAEAGLLPAEDAEALADAY--- 905

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2017541163  80 rrlenrlrlihdysindlggpREYLDKLAR-RLGYDPKLRHPGDLlmreyEETTEAIRGIYERILGGE 146
Cdd:COG1391   906 ---------------------RLLRRLQHRlRLQEQPARVPPDEL-----EAERAAVRALWQRVFGEP 947
PRK14109 PRK14109
bifunctional [glutamine synthetase] adenylyltransferase/[glutamine synthetase] ...
 19-146 2.22e-12

bifunctional [glutamine synthetase] adenylyltransferase/[glutamine synthetase]-adenylyl-L-tyrosine phosphorylase;


Pssm-ID: 237613 [Multi-domain]  Cd Length: 1007  Bit Score: 63.33  E-value: 2.22e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541163   19 KTGRGGIVDIEFMVQYLQLRHGVNLPEIRSTNTLLALKAMRLCGVLTEVESATLQSGYKFLRRLENRLRLIHDYSINDLG 98
Cdd:PRK14109   883 KLGRGGLSDVEWTVQLLQLQHAHEVPALRTTSTLEALDAAAAAGLLSEEDAELLREAWLLATRARNALVLVRGRPTDQLP 962

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 2017541163   99 GPREYLDKLARRLGYDPKlrHPGDLLmREYEETTEAIRGIYERILGGE 146
Cdd:PRK14109   963 GDGRDLAAVARALGYPPG--DGGEFL-DDYLRVTRRARAVVERVFYGE 1007
GlnD_UR_UTase pfam08335
GlnD PII-uridylyltransferase; This is a family of bifunctional uridylyl-removing enzymes ...
 17-143 2.60e-11

GlnD PII-uridylyltransferase; This is a family of bifunctional uridylyl-removing enzymes/uridylyltransferases (UR/UTases, GlnD) that are responsible for the modification (EC:2.7.7.59) of the regulatory protein P-II, or GlnB (pfam00543). In response to nitrogen limitation, these transferases catalyze the uridylylation of the PII protein, which in turn stimulates deadenylylation of glutamine synthetase (GlnA). Deadenylylated glutamine synthetase is the more active form of the enzyme. Moreover, uridylylated PII can act together with NtrB and NtrC to increase transcription of genes in the sigma54 regulon, which include glnA and other nitrogen-level controlled genes. It has also been suggested that the product of the glnD gene is involved in other physiological functions such as control of iron metabolism in certain species. The region described in this family is found in many of its members to be C-terminal to a nucleotidyltransferase domain (pfam01909), and N-terminal to an HD domain (pfam01966) and two ACT domains (pfam01842).


Pssm-ID: 462432 [Multi-domain]  Cd Length: 140  Bit Score: 57.59  E-value: 2.60e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541163  17 NIKTGRGGIVDIEFMVQYLQLRHgvnlpeirstnTLLALKAMRLCGVLTEVESATLQSGYKFLRRLENRLRLIHDYSIND 96
Cdd:pfam08335  27 NIKLGPGGLRDIEFIVWIAQLIF-----------TLRALEELVELGLLTREEARELRRAYRFLRRVRHRLHLLADRQTDR 95

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2017541163  97 LggPREYLDKLARRLGYDPKLRHPGDLLMREYEETTEAIRGIYERIL 143
Cdd:pfam08335  96 L--PFDLQRRLARALGYARDGWLAVERFMRRLFRHAHRVSRLFEILL 140
 
Name Accession Description Interval E-value
GlnE1 COG1391
Glutamine synthetase adenylyltransferase [Posttranslational modification, protein turnover, ...
 1-146 7.16e-24

Glutamine synthetase adenylyltransferase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441001 [Multi-domain]  Cd Length: 948  Bit Score: 96.36  E-value: 7.16e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541163   1 RTRMEVELAKEKEGSYNIKTGRGGIVDIEFMVQYLQLRHGVNLPEIRSTN-TLLALKAMRLCGVLTEVESATLQSGYkfl 79
Cdd:COG1391   829 REKMRAELGSKSAGRFDLKQDRGGIVDIEFIVQYLVLAHAHEHPELLRNSdNIRLLEALAEAGLLPAEDAEALADAY--- 905

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2017541163  80 rrlenrlrlihdysindlggpREYLDKLAR-RLGYDPKLRHPGDLlmreyEETTEAIRGIYERILGGE 146
Cdd:COG1391   906 ---------------------RLLRRLQHRlRLQEQPARVPPDEL-----EAERAAVRALWQRVFGEP 947
PRK14109 PRK14109
bifunctional [glutamine synthetase] adenylyltransferase/[glutamine synthetase] ...
 19-146 2.22e-12

bifunctional [glutamine synthetase] adenylyltransferase/[glutamine synthetase]-adenylyl-L-tyrosine phosphorylase;


Pssm-ID: 237613 [Multi-domain]  Cd Length: 1007  Bit Score: 63.33  E-value: 2.22e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541163   19 KTGRGGIVDIEFMVQYLQLRHGVNLPEIRSTNTLLALKAMRLCGVLTEVESATLQSGYKFLRRLENRLRLIHDYSINDLG 98
Cdd:PRK14109   883 KLGRGGLSDVEWTVQLLQLQHAHEVPALRTTSTLEALDAAAAAGLLSEEDAELLREAWLLATRARNALVLVRGRPTDQLP 962

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 2017541163   99 GPREYLDKLARRLGYDPKlrHPGDLLmREYEETTEAIRGIYERILGGE 146
Cdd:PRK14109   963 GDGRDLAAVARALGYPPG--DGGEFL-DDYLRVTRRARAVVERVFYGE 1007
PRK11072 PRK11072
bifunctional [glutamate--ammonia ligase]-adenylyl-L-tyrosine phosphorylase/ ...
 1-78 4.68e-12

bifunctional [glutamate--ammonia ligase]-adenylyl-L-tyrosine phosphorylase/[glutamate--ammonia-ligase] adenylyltransferase;


Pssm-ID: 236836 [Multi-domain]  Cd Length: 943  Bit Score: 62.54  E-value: 4.68e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2017541163   1 RTRMEVELAKEKEGSYNIKTGRGGIVDIEFMVQYLQLRHGVNLPE-IRSTNTLLALKAMRLCGVLTEVESATLQSGYKF 78
Cdd:PRK11072  827 REKMRDHLGNKTRDRFDLKQDRGGIVDIEFIAQYLVLAHAHEHPElTRWSDNVRILELLAELGLMSEEEAEALTDAYRT 905
PRK14108 PRK14108
bifunctional [glutamine synthetase] adenylyltransferase/[glutamine synthetase] ...
 4-145 5.98e-12

bifunctional [glutamine synthetase] adenylyltransferase/[glutamine synthetase]-adenylyl-L-tyrosine phosphorylase;


Pssm-ID: 237612 [Multi-domain]  Cd Length: 986  Bit Score: 62.33  E-value: 5.98e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541163   4 MEVELAKEK--EGSYNIKTGRGGIVDIEFMVQYLQLRHGVNLPEIRSTNTLLALK-AMRLcgVLTEVESATLQSGYKFLr 80
Cdd:PRK14108  847 MRRLIAQEKppRDIWDLKLAPGGIVDLEFIAQYLQLVHAAKGPDILGVSTAEVLDnLGRL--LLDPADADILREAARLY- 923

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2017541163  81 rlenrlrliHDYS------INDLGGPREYLDKLAR---RLGYDPKLRHpgdlLMREYEETTEAIRGIYERILGG 145
Cdd:PRK14108  924 ---------TNLSqilrlcVSDKFDPDDAPPGLLDllcRAGDAPDFSR----LEAELKETQKEVRAIFDRLLKA 984
GlnD_UR_UTase pfam08335
GlnD PII-uridylyltransferase; This is a family of bifunctional uridylyl-removing enzymes ...
 17-143 2.60e-11

GlnD PII-uridylyltransferase; This is a family of bifunctional uridylyl-removing enzymes/uridylyltransferases (UR/UTases, GlnD) that are responsible for the modification (EC:2.7.7.59) of the regulatory protein P-II, or GlnB (pfam00543). In response to nitrogen limitation, these transferases catalyze the uridylylation of the PII protein, which in turn stimulates deadenylylation of glutamine synthetase (GlnA). Deadenylylated glutamine synthetase is the more active form of the enzyme. Moreover, uridylylated PII can act together with NtrB and NtrC to increase transcription of genes in the sigma54 regulon, which include glnA and other nitrogen-level controlled genes. It has also been suggested that the product of the glnD gene is involved in other physiological functions such as control of iron metabolism in certain species. The region described in this family is found in many of its members to be C-terminal to a nucleotidyltransferase domain (pfam01909), and N-terminal to an HD domain (pfam01966) and two ACT domains (pfam01842).


Pssm-ID: 462432 [Multi-domain]  Cd Length: 140  Bit Score: 57.59  E-value: 2.60e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541163  17 NIKTGRGGIVDIEFMVQYLQLRHgvnlpeirstnTLLALKAMRLCGVLTEVESATLQSGYKFLRRLENRLRLIHDYSIND 96
Cdd:pfam08335  27 NIKLGPGGLRDIEFIVWIAQLIF-----------TLRALEELVELGLLTREEARELRRAYRFLRRVRHRLHLLADRQTDR 95

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2017541163  97 LggPREYLDKLARRLGYDPKLRHPGDLLMREYEETTEAIRGIYERIL 143
Cdd:pfam08335  96 L--PFDLQRRLARALGYARDGWLAVERFMRRLFRHAHRVSRLFEILL 140
GlnE1 COG1391
Glutamine synthetase adenylyltransferase [Posttranslational modification, protein turnover, ...
 12-152 9.17e-10

Glutamine synthetase adenylyltransferase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441001 [Multi-domain]  Cd Length: 948  Bit Score: 55.91  E-value: 9.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541163  12 KEGSYNIKTGRGGIVDIEFMVQYLQLRHGVNLPEIRSTNTLLALKAMRLCGVLTEVESATLQSGYKFLRRLENRLRLIHD 91
Cdd:COG1391   316 RGLGDNIKLGRGGIREIEFIVQTFQLIRGGREPELRQRSTLEALDALAELGLLPAEAADELAEAYRFLRRVEHRLQMLDD 395

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2017541163  92 YSINDLGGPREYLDKLARRLGYDPKlrhpgDLLMREYEETTEAIRGIYERILGGENPGREP 152
Cdd:COG1391   396 QQTHTLPEDEEDRARLARAMGFADW-----AAFLAALDAHRQRVHRHFAALFGDPEELSSE 451
PRK11072 PRK11072
bifunctional [glutamate--ammonia ligase]-adenylyl-L-tyrosine phosphorylase/ ...
 17-81 2.06e-09

bifunctional [glutamate--ammonia ligase]-adenylyl-L-tyrosine phosphorylase/[glutamate--ammonia-ligase] adenylyltransferase;


Pssm-ID: 236836 [Multi-domain]  Cd Length: 943  Bit Score: 54.84  E-value: 2.06e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2017541163  17 NIKTGRGGIVDIEFMVQYLQLRHGVNLPEIRSTNTLLALKAMRLCGVLTEVESATLQSGYKFLRR 81
Cdd:PRK11072  315 NIKLGAGGIREIEFIVQVFQLIRGGREPSLQQRSLLEVLDALAELGLLPEEQVAELRDAYLFLRR 379
PRK14109 PRK14109
bifunctional [glutamine synthetase] adenylyltransferase/[glutamine synthetase] ...
 1-57 3.65e-09

bifunctional [glutamine synthetase] adenylyltransferase/[glutamine synthetase]-adenylyl-L-tyrosine phosphorylase;


Pssm-ID: 237613 [Multi-domain]  Cd Length: 1007  Bit Score: 54.08  E-value: 3.65e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2017541163    1 RTRMEvELAKEKEGSYNIKTGRGGIVDIEFMVQYLQLRHGVNLPEIRSTNTLLALKA 57
Cdd:PRK14109   356 RRRVE-DLIPAAERDRELKLGPGGLRDVEFAVQLLQLVHGRSDESLRVRSTLDALAA 411
PRK14108 PRK14108
bifunctional [glutamine synthetase] adenylyltransferase/[glutamine synthetase] ...
 16-114 6.72e-09

bifunctional [glutamine synthetase] adenylyltransferase/[glutamine synthetase]-adenylyl-L-tyrosine phosphorylase;


Pssm-ID: 237612 [Multi-domain]  Cd Length: 986  Bit Score: 53.47  E-value: 6.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541163  16 YNIKTGRGGIVDIEFMVQYLQLRHGVNLPEIRSTNTLLALKAMRLCGVLTEVESATLQSGYKFLRRLENRLRLIHDYSIN 95
Cdd:PRK14108  346 HNVKLGRGGIREIEFFVQTQQLIAGGRFPELRGRQTLEALAELAERGWITAQARDELTEAYWFLRDVEHRIQMVADEQTH 425

                          90
                  ....*....|....*....
gi 2017541163  96 DLGGPREYLDKLARRLGYD 114
Cdd:PRK14108  426 LLPEDDEALERFARMMGYE 444
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH