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Conserved domains on  [gi|2652668330|ref|WP_326714207|]
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MULTISPECIES: ATP/GTP-binding protein [Streptomyces]

Protein Classification

GTP-binding protein( domain architecture ID 10006198)

GTP-binding protein similar to mutual gliding-mobilty protein MglA, a GTPase that is critical for single-cell (A) gliding, type IV pili-mediated (S) gliding and development of Myxococcus xanthus

CATH:  3.30.450.30
EC:  3.6.5.-
Gene Ontology:  GO:0005525|GO:0003924
PubMed:  11152757
SCOP:  3002022

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
Srp102 COG2229
Signal recognition particle receptor subunit beta, a GTPase [Intracellular trafficking, ...
10-196 1.12e-79

Signal recognition particle receptor subunit beta, a GTPase [Intracellular trafficking, secretion, and vesicular transport];


:

Pssm-ID: 441830 [Multi-domain]  Cd Length: 189  Bit Score: 235.49  E-value: 1.12e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2652668330  10 NADNSALALKILVAGGFGVGKTTLVGAVSEIRPLRTEELLSELGqhvddtgaVERKTTTTVAMDFGRITIRSDLSLYLFG 89
Cdd:COG2229     5 NVAAREITVKIVYAGPFGAGKTTFVRSISEIEPLSTEGRLTDAS--------LETKTTTTVAFDFGRLTLGDGLRLHLFG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2652668330  90 TPGQDRFWFLWDELSQGALGAVVLADTRRLEDSFPA--VDYFEHR--HIPFVVAVNCFTNARTYGALEVSRALDLDRGTP 165
Cdd:COG2229    77 TPGQVRFDFMWDILLRGADGVVFLADSRRLEDSFNAesLDFFEERleKLPFVVAVNKRDLPDALSLEELREALDLGPDVP 156
                         170       180       190
                  ....*....|....*....|....*....|.
gi 2652668330 166 VVLCDARDRDSGKEVLIRLVEYAGRMHTARL 196
Cdd:COG2229   157 VVEADARDGESVKETLIALLELVLARLDARA 187
 
Name Accession Description Interval E-value
Srp102 COG2229
Signal recognition particle receptor subunit beta, a GTPase [Intracellular trafficking, ...
10-196 1.12e-79

Signal recognition particle receptor subunit beta, a GTPase [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 441830 [Multi-domain]  Cd Length: 189  Bit Score: 235.49  E-value: 1.12e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2652668330  10 NADNSALALKILVAGGFGVGKTTLVGAVSEIRPLRTEELLSELGqhvddtgaVERKTTTTVAMDFGRITIRSDLSLYLFG 89
Cdd:COG2229     5 NVAAREITVKIVYAGPFGAGKTTFVRSISEIEPLSTEGRLTDAS--------LETKTTTTVAFDFGRLTLGDGLRLHLFG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2652668330  90 TPGQDRFWFLWDELSQGALGAVVLADTRRLEDSFPA--VDYFEHR--HIPFVVAVNCFTNARTYGALEVSRALDLDRGTP 165
Cdd:COG2229    77 TPGQVRFDFMWDILLRGADGVVFLADSRRLEDSFNAesLDFFEERleKLPFVVAVNKRDLPDALSLEELREALDLGPDVP 156
                         170       180       190
                  ....*....|....*....|....*....|.
gi 2652668330 166 VVLCDARDRDSGKEVLIRLVEYAGRMHTARL 196
Cdd:COG2229   157 VVEADARDGESVKETLIALLELVLARLDARA 187
ATP_bind_1 pfam03029
Conserved hypothetical ATP binding protein; Members of this family are found in a range of ...
22-188 1.72e-40

Conserved hypothetical ATP binding protein; Members of this family are found in a range of archaea and eukaryotes and have hypothesized ATP binding activity.


Pssm-ID: 397252 [Multi-domain]  Cd Length: 238  Bit Score: 137.50  E-value: 1.72e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2652668330  22 VAGGFGVGKTTLVGAVSEIRPLR-----------------------TEELLSELGQHVDDtgAVERKTTTTVAMDFGRIT 78
Cdd:pfam03029   1 VVGPAGSGKTTFVGALSEILPLRgrpvyvvnldpaaenlpypadidIRELITVADVMEDY--GLGPNGALTVAMDFGRIT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2652668330  79 -------IRSDLSLYLFGTPGQDRFWFLWDELSQ--------GALGAVVLADTRRLEDsfpAVDYFEHRH---------- 133
Cdd:pfam03029  79 ldwldeeLKREDDYYLFDTPGQIELFTHWDSLAIivealesrGALGAVYLVDTRRLTD---PTDFFSGLLyalsimlrlg 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2652668330 134 IPFVVAVNCFTNARTYGALE-------------------------VSRALDLDRGTPVVLCDARDRDSGKEVLIRLVEYA 188
Cdd:pfam03029 156 LPFVVALNKFDLLSLEFALKwftdpedlqlllelddgkyrklneaIREALDLFYLVPVFLPDARERGESMEDLLTLIDEA 235
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
21-186 8.15e-10

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: 55.16  E-value: 8.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2652668330  21 LVAGGFGVGKTTLVGAVseirplrteellseLGQHVddtGAVERKTTTTVAMDFGRITIRSDL-SLYLFGTPGQDRFWFL 99
Cdd:cd00882     1 VVVGRGGVGKSSLLNAL--------------LGGEV---GEVSDVPGTTRDPDVYVKELDKGKvKLVLVDTPGLDEFGGL 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2652668330 100 WDE-----LSQGALGAVVLADTRRLEdSFPAVDYFEHRH-----IPFVVAVNCF--TNARTYGALEVSRALDLDRGTPVV 167
Cdd:cd00882    64 GREelarlLLRGADLILLVVDSTDRE-SEEDAKLLILRRlrkegIPIILVGNKIdlLEEREVEELLRLEELAKILGVPVF 142
                         170
                  ....*....|....*....
gi 2652668330 168 LCDARDRDSGKEVLIRLVE 186
Cdd:cd00882   143 EVSAKTGEGVDELFEKLIE 161
PLN03118 PLN03118
Rab family protein; Provisional
1-120 6.40e-04

Rab family protein; Provisional


Pssm-ID: 215587 [Multi-domain]  Cd Length: 211  Bit Score: 39.27  E-value: 6.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2652668330   1 MASEHSEETNADnsaLALKILVAGGFGVGKTTLvgavseirplrteeLLSELGQHVDDTGAverktttTVAMDF--GRIT 78
Cdd:PLN03118    1 MGSSSGQSSGYD---LSFKILLIGDSGVGKSSL--------------LVSFISSSVEDLAP-------TIGVDFkiKQLT 56
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2652668330  79 IRSD-LSLYLFGTPGQDRFWFLWDELSQGALGAVVLADTRRLE 120
Cdd:PLN03118   57 VGGKrLKLTIWDTAGQERFRTLTSSYYRNAQGIILVYDVTRRE 99
 
Name Accession Description Interval E-value
Srp102 COG2229
Signal recognition particle receptor subunit beta, a GTPase [Intracellular trafficking, ...
10-196 1.12e-79

Signal recognition particle receptor subunit beta, a GTPase [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 441830 [Multi-domain]  Cd Length: 189  Bit Score: 235.49  E-value: 1.12e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2652668330  10 NADNSALALKILVAGGFGVGKTTLVGAVSEIRPLRTEELLSELGqhvddtgaVERKTTTTVAMDFGRITIRSDLSLYLFG 89
Cdd:COG2229     5 NVAAREITVKIVYAGPFGAGKTTFVRSISEIEPLSTEGRLTDAS--------LETKTTTTVAFDFGRLTLGDGLRLHLFG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2652668330  90 TPGQDRFWFLWDELSQGALGAVVLADTRRLEDSFPA--VDYFEHR--HIPFVVAVNCFTNARTYGALEVSRALDLDRGTP 165
Cdd:COG2229    77 TPGQVRFDFMWDILLRGADGVVFLADSRRLEDSFNAesLDFFEERleKLPFVVAVNKRDLPDALSLEELREALDLGPDVP 156
                         170       180       190
                  ....*....|....*....|....*....|.
gi 2652668330 166 VVLCDARDRDSGKEVLIRLVEYAGRMHTARL 196
Cdd:COG2229   157 VVEADARDGESVKETLIALLELVLARLDARA 187
ATP_bind_1 pfam03029
Conserved hypothetical ATP binding protein; Members of this family are found in a range of ...
22-188 1.72e-40

Conserved hypothetical ATP binding protein; Members of this family are found in a range of archaea and eukaryotes and have hypothesized ATP binding activity.


Pssm-ID: 397252 [Multi-domain]  Cd Length: 238  Bit Score: 137.50  E-value: 1.72e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2652668330  22 VAGGFGVGKTTLVGAVSEIRPLR-----------------------TEELLSELGQHVDDtgAVERKTTTTVAMDFGRIT 78
Cdd:pfam03029   1 VVGPAGSGKTTFVGALSEILPLRgrpvyvvnldpaaenlpypadidIRELITVADVMEDY--GLGPNGALTVAMDFGRIT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2652668330  79 -------IRSDLSLYLFGTPGQDRFWFLWDELSQ--------GALGAVVLADTRRLEDsfpAVDYFEHRH---------- 133
Cdd:pfam03029  79 ldwldeeLKREDDYYLFDTPGQIELFTHWDSLAIivealesrGALGAVYLVDTRRLTD---PTDFFSGLLyalsimlrlg 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2652668330 134 IPFVVAVNCFTNARTYGALE-------------------------VSRALDLDRGTPVVLCDARDRDSGKEVLIRLVEYA 188
Cdd:pfam03029 156 LPFVVALNKFDLLSLEFALKwftdpedlqlllelddgkyrklneaIREALDLFYLVPVFLPDARERGESMEDLLTLIDEA 235
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
21-186 8.15e-10

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: 55.16  E-value: 8.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2652668330  21 LVAGGFGVGKTTLVGAVseirplrteellseLGQHVddtGAVERKTTTTVAMDFGRITIRSDL-SLYLFGTPGQDRFWFL 99
Cdd:cd00882     1 VVVGRGGVGKSSLLNAL--------------LGGEV---GEVSDVPGTTRDPDVYVKELDKGKvKLVLVDTPGLDEFGGL 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2652668330 100 WDE-----LSQGALGAVVLADTRRLEdSFPAVDYFEHRH-----IPFVVAVNCF--TNARTYGALEVSRALDLDRGTPVV 167
Cdd:cd00882    64 GREelarlLLRGADLILLVVDSTDRE-SEEDAKLLILRRlrkegIPIILVGNKIdlLEEREVEELLRLEELAKILGVPVF 142
                         170
                  ....*....|....*....
gi 2652668330 168 LCDARDRDSGKEVLIRLVE 186
Cdd:cd00882   143 EVSAKTGEGVDELFEKLIE 161
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
18-190 7.96e-06

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 44.59  E-value: 7.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2652668330  18 LKILVAGGFGVGKTTLVGAVseirplrteellseLGQHVDdtgAVERKTTTTVAMDFGRITIRS-DLSLYLFGTPGQDRF 96
Cdd:COG1100     4 KKIVVVGTGGVGKTSLVNRL--------------VGDIFS---LEKYLSTNGVTIDKKELKLDGlDVDLVIWDTPGQDEF 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2652668330  97 ----WFLWDELsQGALGAVVLADTRRLEDSFPAVDYFEH-----RHIPFVVAVN---CFTNARTYGALEVSRALDLDRGT 164
Cdd:COG1100    67 retrQFYARQL-TGASLYLFVVDGTREETLQSLYELLESlrrlgKKSPIILVLNkidLYDEEEIEDEERLKEALSEDNIV 145
                         170       180
                  ....*....|....*....|....*.
gi 2652668330 165 PVVLCDARDRDSGKEVLIRLVEYAGR 190
Cdd:COG1100   146 EVVATSAKTGEGVEELFAALAEILRG 171
Rab cd00154
Ras-related in brain (Rab) family of small guanosine triphosphatases (GTPases); Rab GTPases ...
18-128 1.65e-04

Ras-related in brain (Rab) family of small guanosine triphosphatases (GTPases); Rab GTPases form the largest family within the Ras superfamily. There are at least 60 Rab genes in the human genome, and a number of Rab GTPases are conserved from yeast to humans. Rab GTPases are small, monomeric proteins that function as molecular switches to regulate vesicle trafficking pathways. The different Rab GTPases are localized to the cytosolic face of specific intracellular membranes, where they regulate distinct steps in membrane traffic pathways. In the GTP-bound form, Rab GTPases recruit specific sets of effector proteins onto membranes. Through their effectors, Rab GTPases regulate vesicle formation, actin- and tubulin-dependent vesicle movement, and membrane fusion. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which mask C-terminal lipid binding and promote cytosolic localization. While most unicellular organisms possess 5-20 Rab members, several have been found to possess 60 or more Rabs; for many of these Rab isoforms, homologous proteins are not found in other organisms. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Since crystal structures often lack C-terminal residues, the lipid modification site is not available for annotation in many of the CDs in the hierarchy, but is included where possible.


Pssm-ID: 206640 [Multi-domain]  Cd Length: 159  Bit Score: 40.52  E-value: 1.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2652668330  18 LKILVAGGFGVGKTTLvgavseirplrteellseLGQHVDDTgaVERKTTTTVAMDFGRITIRSD---LSLYLFGTPGQD 94
Cdd:cd00154     1 FKIVLIGDSGVGKTSL------------------LLRFVDNK--FSENYKSTIGVDFKSKTIEVDgkkVKLQIWDTAGQE 60
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2652668330  95 RFWFLWDELSQGALGAVVLAD-TRRleDSFPAVDY 128
Cdd:cd00154    61 RFRSITSSYYRGAHGAILVYDvTNR--ESFENLDK 93
Rab18 cd01863
Rab GTPase family 18 (Rab18); Rab18 subfamily. Mammalian Rab18 is implicated in endocytic ...
18-128 2.04e-04

Rab GTPase family 18 (Rab18); Rab18 subfamily. Mammalian Rab18 is implicated in endocytic transport and is expressed most highly in polarized epithelial cells. However, trypanosomal Rab, TbRAB18, is upregulated in the BSF (Blood Stream Form) stage and localized predominantly to elements of the Golgi complex. In human and mouse cells, Rab18 has been identified in lipid droplets, organelles that store neutral lipids. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206656 [Multi-domain]  Cd Length: 161  Bit Score: 39.99  E-value: 2.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2652668330  18 LKILVAGGFGVGKTTLvgavseirplrteeLLSelgqHVDDTgaVERKTTTTVAMDFGRITIRSD---LSLYLFGTPGQD 94
Cdd:cd01863     1 LKILLIGDSGVGKSSL--------------LLR----FTDDT--FDEDLSSTIGVDFKVKTVTVDgkkVKLAIWDTAGQE 60
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2652668330  95 RFWFLWDELSQGALGAVVLAD-TRRleDSFPAVDY 128
Cdd:cd01863    61 RFRTLTSSYYRGAQGVILVYDvTRR--DTFDNLDT 93
PLN03118 PLN03118
Rab family protein; Provisional
1-120 6.40e-04

Rab family protein; Provisional


Pssm-ID: 215587 [Multi-domain]  Cd Length: 211  Bit Score: 39.27  E-value: 6.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2652668330   1 MASEHSEETNADnsaLALKILVAGGFGVGKTTLvgavseirplrteeLLSELGQHVDDTGAverktttTVAMDF--GRIT 78
Cdd:PLN03118    1 MGSSSGQSSGYD---LSFKILLIGDSGVGKSSL--------------LVSFISSSVEDLAP-------TIGVDFkiKQLT 56
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2652668330  79 IRSD-LSLYLFGTPGQDRFWFLWDELSQGALGAVVLADTRRLE 120
Cdd:PLN03118   57 VGGKrLKLTIWDTAGQERFRTLTSSYYRNAQGIILVYDVTRRE 99
 
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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