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Conserved domains on  [gi|1716978861|ref|XP_030050421|]
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nitric oxide-associated protein 1 [Microcaecilia unicolor]

Protein Classification

YqeH domain-containing protein( domain architecture ID 10111420)

YqeH domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YqeH cd01855
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH ...
 166-359 2.57e-58

Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH induces an excess initiation of DNA replication, suggesting that it negatively controls initiation of chromosome replication. The YqeH subfamily is common in eukaryotes and sporadically present in bacteria with probable acquisition by plants from chloroplasts. Proteins of the YqeH family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases.


:

Pssm-ID: 206748 [Multi-domain]  Cd Length: 191  Bit Score: 194.79  E-value: 2.57e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716978861 166 CQRCFLLQHYQRALRLQLPPDRFRQVLRSLRSrpSPALVLLMIDLLDLPGSlFLPDLPELLSlggsdRRPraLFLLGNKV 245
Cdd:cd01855     1 CQRCFKLKHYNKLLDVEIPDEDFLEILSTLLN--DNALVVHVVDIFDFPGS-LIPGLAELIG-----AKP--VILVGNKI 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716978861 246 DLLPadrPGHLRRLRERLLELSQAAGLPKPEDALLISAKTGYGVEGLISRLQRSWRYKGDVYLMGATNCGKSTLFNTLLL 325
Cdd:cd01855    71 DLLP---KDVKPNRLKQWVKKRLKIGGLKIKDVILVSAKKGWGVEELIEEIKKLAKYRGDVYVVGATNVGKSTLINALLK 147

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1716978861 326 SDYCKSKAPEVIDRATISPWPGTTLNLLKFPIIN 359
Cdd:cd01855   148 SNGGKVQAQALVQRLTVSPIPGTTLGLIKIPLGE 181
 
Name Accession Description Interval E-value
YqeH cd01855
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH ...
 166-359 2.57e-58

Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH induces an excess initiation of DNA replication, suggesting that it negatively controls initiation of chromosome replication. The YqeH subfamily is common in eukaryotes and sporadically present in bacteria with probable acquisition by plants from chloroplasts. Proteins of the YqeH family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases.


Pssm-ID: 206748 [Multi-domain]  Cd Length: 191  Bit Score: 194.79  E-value: 2.57e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716978861 166 CQRCFLLQHYQRALRLQLPPDRFRQVLRSLRSrpSPALVLLMIDLLDLPGSlFLPDLPELLSlggsdRRPraLFLLGNKV 245
Cdd:cd01855     1 CQRCFKLKHYNKLLDVEIPDEDFLEILSTLLN--DNALVVHVVDIFDFPGS-LIPGLAELIG-----AKP--VILVGNKI 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716978861 246 DLLPadrPGHLRRLRERLLELSQAAGLPKPEDALLISAKTGYGVEGLISRLQRSWRYKGDVYLMGATNCGKSTLFNTLLL 325
Cdd:cd01855    71 DLLP---KDVKPNRLKQWVKKRLKIGGLKIKDVILVSAKKGWGVEELIEEIKKLAKYRGDVYVVGATNVGKSTLINALLK 147

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1716978861 326 SDYCKSKAPEVIDRATISPWPGTTLNLLKFPIIN 359
Cdd:cd01855   148 SNGGKVQAQALVQRLTVSPIPGTTLGLIKIPLGE 181
RbgA COG1161
Ribosome biogenesis GTPase RbgA [Translation, ribosomal structure and biogenesis];
203-351 1.20e-09

Ribosome biogenesis GTPase RbgA [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440775 [Multi-domain]  Cd Length: 279  Bit Score: 59.74  E-value: 1.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716978861 203 LVLLMIDLLD--LPGSLFLPDLPELLSlggsdRRPRalFLLGNKVDLLPAD----------RPGHlrrlrerllelsqaa 270
Cdd:COG1161    23 LVDLVIEVVDarIPLSSRNPMLDELVG-----NKPR--LLVLNKADLADPSvtkqwlkyfeKQGV--------------- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716978861 271 glpkpeDALLISAKTGYGVEGLISRLQRSWRYKG------DVYLMGATNCGKSTLFNTLLlsdycKSKApevidrATISP 344
Cdd:COG1161    81 ------DALAISAKKGKGIKELIEAIRELAPEKGikrrpiRVMIVGIPNVGKSTLINRLA-----GKKV------AKTGN 143


                  ....*..
gi 1716978861 345 WPGTTLN 351
Cdd:COG1161   144 KPGVTKG 150
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 305-357 2.30e-06

50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.


Pssm-ID: 460387 [Multi-domain]  Cd Length: 113  Bit Score: 46.84  E-value: 2.30e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1716978861 305 DVYLMGATNCGKSTLFNTLLLSdyckskapevidRATISPWPGTTLNLLKFPI 357
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGA------------KAIVSDYPGTTRDPNEGRL 41
trmE PRK05291
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
203-298 5.36e-03

tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;


Pssm-ID: 235392 [Multi-domain]  Cd Length: 449  Bit Score: 39.71  E-value: 5.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716978861 203 LVLLMIDlldlpGSLFLPDLPELLSLggsDRRPRALFLLGNKVDLLPADrpghlrrlrerllelsqAAGLPKPEDALLIS 282
Cdd:PRK05291  297 LVLLVLD-----ASEPLTEEDDEILE---ELKDKPVIVVLNKADLTGEI-----------------DLEEENGKPVIRIS 351

                          90
                  ....*....|....*.
gi 1716978861 283 AKTGYGVEGLISRLQR 298
Cdd:PRK05291  352 AKTGEGIDELREAIKE 367
 
Name Accession Description Interval E-value
YqeH cd01855
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH ...
 166-359 2.57e-58

Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH induces an excess initiation of DNA replication, suggesting that it negatively controls initiation of chromosome replication. The YqeH subfamily is common in eukaryotes and sporadically present in bacteria with probable acquisition by plants from chloroplasts. Proteins of the YqeH family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases.


Pssm-ID: 206748 [Multi-domain]  Cd Length: 191  Bit Score: 194.79  E-value: 2.57e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716978861 166 CQRCFLLQHYQRALRLQLPPDRFRQVLRSLRSrpSPALVLLMIDLLDLPGSlFLPDLPELLSlggsdRRPraLFLLGNKV 245
Cdd:cd01855     1 CQRCFKLKHYNKLLDVEIPDEDFLEILSTLLN--DNALVVHVVDIFDFPGS-LIPGLAELIG-----AKP--VILVGNKI 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716978861 246 DLLPadrPGHLRRLRERLLELSQAAGLPKPEDALLISAKTGYGVEGLISRLQRSWRYKGDVYLMGATNCGKSTLFNTLLL 325
Cdd:cd01855    71 DLLP---KDVKPNRLKQWVKKRLKIGGLKIKDVILVSAKKGWGVEELIEEIKKLAKYRGDVYVVGATNVGKSTLINALLK 147

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1716978861 326 SDYCKSKAPEVIDRATISPWPGTTLNLLKFPIIN 359
Cdd:cd01855   148 SNGGKVQAQALVQRLTVSPIPGTTLGLIKIPLGE 181
RbgA COG1161
Ribosome biogenesis GTPase RbgA [Translation, ribosomal structure and biogenesis];
203-351 1.20e-09

Ribosome biogenesis GTPase RbgA [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440775 [Multi-domain]  Cd Length: 279  Bit Score: 59.74  E-value: 1.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716978861 203 LVLLMIDLLD--LPGSLFLPDLPELLSlggsdRRPRalFLLGNKVDLLPAD----------RPGHlrrlrerllelsqaa 270
Cdd:COG1161    23 LVDLVIEVVDarIPLSSRNPMLDELVG-----NKPR--LLVLNKADLADPSvtkqwlkyfeKQGV--------------- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716978861 271 glpkpeDALLISAKTGYGVEGLISRLQRSWRYKG------DVYLMGATNCGKSTLFNTLLlsdycKSKApevidrATISP 344
Cdd:COG1161    81 ------DALAISAKKGKGIKELIEAIRELAPEKGikrrpiRVMIVGIPNVGKSTLINRLA-----GKKV------AKTGN 143


                  ....*..
gi 1716978861 345 WPGTTLN 351
Cdd:COG1161   144 KPGVTKG 150
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 305-357 2.30e-06

50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.


Pssm-ID: 460387 [Multi-domain]  Cd Length: 113  Bit Score: 46.84  E-value: 2.30e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1716978861 305 DVYLMGATNCGKSTLFNTLLLSdyckskapevidRATISPWPGTTLNLLKFPI 357
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGA------------KAIVSDYPGTTRDPNEGRL 41
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
186-308 6.42e-05

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 44.20  E-value: 6.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716978861 186 DRFRQV----LRSLRSRpspALVLLMIDLlDLPGSL--FLPDLPELLSLGGSDRrpraLFLLGNKVDLLPADRpghlrrl 259
Cdd:COG1100    64 DEFRETrqfyARQLTGA---SLYLFVVDG-TREETLqsLYELLESLRRLGKKSP----IILVLNKIDLYDEEE------- 128

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1716978861 260 RERLLELSQAAGLPKPEDALLISAKTGYGVEGLISRLQRSWRYKGDVYL 308
Cdd:COG1100   129 IEDEERLKEALSEDNIVEVVATSAKTGEGVEELFAALAEILRGEGDSLD 177
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
 203-298 1.12e-03

trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in bacteria and eukaryotes. It controls modification of the uridine at the wobble position (U34) of tRNAs that read codons ending with A or G in the mixed codon family boxes. TrmE contains a GTPase domain that forms a canonical Ras-like fold. It functions a molecular switch GTPase, and apparently uses a conformational change associated with GTP hydrolysis to promote the tRNA modification reaction, in which the conserved cysteine in the C-terminal domain is thought to function as a catalytic residue. In bacteria that are able to survive in extremely low pH conditions, TrmE regulates glutamate-dependent acid resistance.


Pssm-ID: 206727 [Multi-domain]  Cd Length: 159  Bit Score: 40.17  E-value: 1.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716978861 203 LVLLMIDlldlPGSLFLPDLPELLSLGGSDRrpraLFLLGNKVDLLPADrpghlrrlrerllelsQAAGLPKPEDALLIS 282
Cdd:cd04164    85 LVLLVVD----ASEGLDEEDLEILELPAKKP----VIVVLNKSDLLSDA----------------EGISELNGKPIIAIS 140

                          90
                  ....*....|....*.
gi 1716978861 283 AKTGYGVEGLISRLQR 298
Cdd:cd04164   141 AKTGEGIDELKEALLE 156
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
 310-349 1.85e-03

trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in bacteria and eukaryotes. It controls modification of the uridine at the wobble position (U34) of tRNAs that read codons ending with A or G in the mixed codon family boxes. TrmE contains a GTPase domain that forms a canonical Ras-like fold. It functions a molecular switch GTPase, and apparently uses a conformational change associated with GTP hydrolysis to promote the tRNA modification reaction, in which the conserved cysteine in the C-terminal domain is thought to function as a catalytic residue. In bacteria that are able to survive in extremely low pH conditions, TrmE regulates glutamate-dependent acid resistance.


Pssm-ID: 206727 [Multi-domain]  Cd Length: 159  Bit Score: 39.40  E-value: 1.85e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1716978861 310 GATNCGKSTLFNTLLLSdyckskapeviDRATISPWPGTT 349
Cdd:cd04164    10 GKPNVGKSSLLNALAGR-----------DRAIVSDIAGTT 38
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 203-298 3.39e-03

Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.


Pssm-ID: 206648 [Multi-domain]  Cd Length: 161  Bit Score: 38.59  E-value: 3.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716978861 203 LVLLMIDLlDLPGSLFLPDLPELLSLGGSDRRpraLFLLGNKVDLLPADRPghlrrlreRLLELSQAAGLPKPEDALLIS 282
Cdd:cd00882    78 LILLVVDS-TDRESEEDAKLLILRRLRKEGIP---IILVGNKIDLLEEREV--------EELLRLEELAKILGVPVFEVS 145

                          90
                  ....*....|....*.
gi 1716978861 283 AKTGYGVEGLISRLQR 298
Cdd:cd00882   146 AKTGEGVDELFEKLIE 161
MnmE_helical pfam12631
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ...
 203-298 3.98e-03

MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An N-terminal domain, a helical domain and a GTPase domain which is nested within the helical domain. This family represents the helical domain.


Pssm-ID: 463649 [Multi-domain]  Cd Length: 326  Bit Score: 39.77  E-value: 3.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716978861 203 LVLLMIDlldlpGSLFLPDLPELLSLGGSDRRPraLFLLGNKVDLLPADrpghlrrlrerllelsQAAGLPKPEDALLIS 282
Cdd:pfam12631 176 LVLLVLD-----ASRPLDEEDLEILELLKDKKP--IIVVLNKSDLLGEI----------------DELEELKGKPVLAIS 232

                          90
                  ....*....|....*.
gi 1716978861 283 AKTGYGVEGLISRLQR 298
Cdd:pfam12631 233 AKTGEGLDELEEAIKE 248
YlqF_related_GTPase cd01849
Circularly permuted YlqF-related GTPases; These proteins are found in bacteria, eukaryotes, ...
 203-324 4.77e-03

Circularly permuted YlqF-related GTPases; These proteins are found in bacteria, eukaryotes, and archaea. They all exhibit a circular permutation of the GTPase signature motifs so that the order of the conserved G box motifs is G4-G5-G1-G2-G3, with G4 and G5 being permuted from the C-terminal region of proteins in the Ras superfamily to the N-terminus of YlqF-related GTPases.


Pssm-ID: 206746 [Multi-domain]  Cd Length: 146  Bit Score: 38.13  E-value: 4.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716978861 203 LVLLMIDLLDlPGSLFLPDLPELLSLGGSDrrpraLFLLGNKVDLLPADRPGHLRRLRERLlelsqaaglpKPEDALLIS 282
Cdd:cd01849     2 VVVEVVDARD-PLSSRNPDIEVLINEKNKK-----LIMVLNKADLVPKEVLRKWVAELSEL----------YGTKTFFIS 65

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1716978861 283 AKTGYGVEGLI-----SRLQRSWRYKGDVYLMGATNCGKSTLFNTLL 324
Cdd:cd01849    66 ATNGQGILKLKaeitkQKLKLKYKKGIRVGVVGLPNVGKSSFINALL 112
trmE PRK05291
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
203-298 5.36e-03

tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;


Pssm-ID: 235392 [Multi-domain]  Cd Length: 449  Bit Score: 39.71  E-value: 5.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716978861 203 LVLLMIDlldlpGSLFLPDLPELLSLggsDRRPRALFLLGNKVDLLPADrpghlrrlrerllelsqAAGLPKPEDALLIS 282
Cdd:PRK05291  297 LVLLVLD-----ASEPLTEEDDEILE---ELKDKPVIVVLNKADLTGEI-----------------DLEEENGKPVIRIS 351

                          90
                  ....*....|....*.
gi 1716978861 283 AKTGYGVEGLISRLQR 298
Cdd:PRK05291  352 AKTGEGIDELREAIKE 367
FeoB cd01879
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ...
 308-349 7.31e-03

Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) subfamily. E. coli has an iron(II) transport system, known as feo, which may make an important contribution to the iron supply of the cell under anaerobic conditions. FeoB has been identified as part of this transport system. FeoB is a large 700-800 amino acid integral membrane protein. The N terminus contains a P-loop motif suggesting that iron transport may be ATP dependent.


Pssm-ID: 206667 [Multi-domain]  Cd Length: 159  Bit Score: 37.82  E-value: 7.31e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1716978861 308 LMGATNCGKSTLFNTLllsdyCKSkapevidRATISPWPGTT 349
Cdd:cd01879     2 LVGNPNVGKTTLFNAL-----TGA-------RQKVGNWPGVT 31
 
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.
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