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Conserved domains on  [gi|495027916|ref|YP_007969877|]
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protein 2A2 [avihepatovirus A1]

Protein Classification

P-loop NTPase family protein( domain architecture ID 1562424)

P-loop NTPase (nucleoside triphosphate hydrolase) family protein contains two conserved sequence signatures, the Walker A motif (the P-loop proper) and Walker B motif which bind, respectively, the beta and gamma phosphate moieties of the bound nucleotide (typically ATP or GTP), and a Mg(2+) cation

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
2-167 6.32e-26

P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.


The actual alignment was detected with superfamily member cd01852:

Pssm-ID: 476819 [Multi-domain]  Cd Length: 201  Bit Score: 101.07  E-value: 6.32e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495027916   2 ILVVGKSGSGKSRLCNVLAGVELFESKLSPRSVTMVHQVETVDIEGKKVTIVDSP------ETPNY-------------D 62
Cdd:cd01852    3 LVLVGKTGNGKSATGNTILGRKVFESKLSASGVTKTCQKESAVWDGRRVNVIDTPglfdtsVSPEQlskeiirclslsaP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495027916  63 GPiSAFFYLIEAGRFTAEDKEYIQMMRKRF-PGFEKSTILILNRADELKtDDDIRNWVKTSGE-LDSLVRACGGRIAKFH 140
Cdd:cd01852   83 GP-HAFLLVVPLGRFTEEEEQAVEELQELFgEKVLDHTIVLFTRGDDLE-GGSLEDYLEDSCEaLKRLLEKCGGRYVAFN 160
                        170       180
                 ....*....|....*....|....*..
gi 495027916 141 rhkiNRAKLLEKAATLPEFVSHLPRLV 167
Cdd:cd01852  161 ----NKAKGREQEQQVKELLAKVEEMV 183
 
Name Accession Description Interval E-value
AIG1 cd01852
AvrRpt2-Induced Gene 1 (AIG1); This group represents Arabidoposis protein AIG1 ...
2-167 6.32e-26

AvrRpt2-Induced Gene 1 (AIG1); This group represents Arabidoposis protein AIG1 (avrRpt2-induced gene 1) that appears to be involved in plant resistance to bacteria. The Arabidopsis disease resistance gene RPS2 is involved in recognition of bacterial pathogens carrying the avirulence gene avrRpt2. AIG1 exhibits RPS2- and avrRpt1-dependent induction early after infection with Pseudomonas syringae carrying avrRpt2. This subfamily also includes IAN-4 protein, which has GTP-binding activity and shares sequence homology with a novel family of putative GTP-binding proteins: the immuno-associated nucleotide (IAN) family. The evolutionary conservation of the IAN family provides a unique example of a plant pathogen response gene conserved in animals. The IAN/IMAP subfamily has been proposed to regulate apoptosis in vertebrates and angiosperm plants, particularly in relation to cancer, diabetes, and infections. The human IAN genes were renamed GIMAP (GTPase of the immunity associated proteins).


Pssm-ID: 206651 [Multi-domain]  Cd Length: 201  Bit Score: 101.07  E-value: 6.32e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495027916   2 ILVVGKSGSGKSRLCNVLAGVELFESKLSPRSVTMVHQVETVDIEGKKVTIVDSP------ETPNY-------------D 62
Cdd:cd01852    3 LVLVGKTGNGKSATGNTILGRKVFESKLSASGVTKTCQKESAVWDGRRVNVIDTPglfdtsVSPEQlskeiirclslsaP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495027916  63 GPiSAFFYLIEAGRFTAEDKEYIQMMRKRF-PGFEKSTILILNRADELKtDDDIRNWVKTSGE-LDSLVRACGGRIAKFH 140
Cdd:cd01852   83 GP-HAFLLVVPLGRFTEEEEQAVEELQELFgEKVLDHTIVLFTRGDDLE-GGSLEDYLEDSCEaLKRLLEKCGGRYVAFN 160
                        170       180
                 ....*....|....*....|....*..
gi 495027916 141 rhkiNRAKLLEKAATLPEFVSHLPRLV 167
Cdd:cd01852  161 ----NKAKGREQEQQVKELLAKVEEMV 183
AIG1 pfam04548
AIG1 family; Arabidopsis protein AIG1 appears to be involved in plant resistance to bacteria.
2-167 5.31e-14

AIG1 family; Arabidopsis protein AIG1 appears to be involved in plant resistance to bacteria.


Pssm-ID: 398307 [Multi-domain]  Cd Length: 200  Bit Score: 69.17  E-value: 5.31e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495027916    2 ILVVGKSGSGKSRLCNVLAGVELFESKLSPRSVTMVHQVETVDIEGKKVTIVDSP-----ETPNYD-------------G 63
Cdd:pfam04548   3 IVLVGKTGNGKSATGNSILGRKAFESKLRAQGVTKTCQLVSRTWDGRIINVIDTPglfdlSVSNDFiskeiirclllaeP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495027916   64 PISAFFYLIEAGRFTAEDKEYIQMMRKRF-PGFEKSTILILNRADELKTDDdirnwvktsgeLDSLVRACggrIAKFHRH 142
Cdd:pfam04548  83 GPHAVLLVLSLGRFTEEEEQALRTLQELFgSKILDYMIVVFTRKDDLEDDS-----------LDDYLSDG---CPEFLKE 148
                         170       180
                  ....*....|....*....|....*
gi 495027916  143 KINRAKLLEKAATLPEFVSHLPRLV 167
Cdd:pfam04548 149 VLRTADGEEKEEQVQQLLALVEAIV 173
YeeP COG3596
Predicted GTPase [General function prediction only];
2-109 3.28e-09

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 56.70  E-value: 3.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495027916   2 ILVVGKSGSGKSRLCNVLAGVELFE-SKLSPrsVTM---VHQVETVDIEGkkVTIVDSP---ETPNYDGPISA------- 67
Cdd:COG3596   42 IALVGKTGAGKSSLINALFGAEVAEvGVGRP--CTReiqRYRLESDGLPG--LVLLDTPglgEVNERDREYRElrellpe 117
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 495027916  68 ---FFYLIEAG-RFTAEDKEYIQMMRKRFPGfeKSTILILNRADEL 109
Cdd:COG3596  118 adlILWVVKADdRALATDEEFLQALRAQYPD--PPVLVVLTQVDRL 161
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
2-56 4.78e-04

small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this model include Ras, RhoA, Rab11, translation elongation factor G, translation initiation factor IF-2, tetratcycline resistance protein TetM, CDC42, Era, ADP-ribosylation factors, tdhF, and many others. In some proteins the domain occurs more than once.This model recognizes a large number of small GTP-binding proteins and related domains in larger proteins. Note that the alpha chains of heterotrimeric G proteins are larger proteins in which the NKXD motif is separated from the GxxxxGK[ST] motif (P-loop) by a long insert and are not easily detected by this model. [Unknown function, General]


Pssm-ID: 272973 [Multi-domain]  Cd Length: 162  Bit Score: 40.05  E-value: 4.78e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 495027916    2 ILVVGKSGSGKSRLCNVLAGVELFESKLSPR-SVTMVHQVETVDIEGKKVTIVDSP 56
Cdd:TIGR00231   4 IVIVGHPNVGKSTLLNSLLGNKGSITEYYPGtTRNYVTTVIEEDGKTYKFNLLDTA 59
 
Name Accession Description Interval E-value
AIG1 cd01852
AvrRpt2-Induced Gene 1 (AIG1); This group represents Arabidoposis protein AIG1 ...
2-167 6.32e-26

AvrRpt2-Induced Gene 1 (AIG1); This group represents Arabidoposis protein AIG1 (avrRpt2-induced gene 1) that appears to be involved in plant resistance to bacteria. The Arabidopsis disease resistance gene RPS2 is involved in recognition of bacterial pathogens carrying the avirulence gene avrRpt2. AIG1 exhibits RPS2- and avrRpt1-dependent induction early after infection with Pseudomonas syringae carrying avrRpt2. This subfamily also includes IAN-4 protein, which has GTP-binding activity and shares sequence homology with a novel family of putative GTP-binding proteins: the immuno-associated nucleotide (IAN) family. The evolutionary conservation of the IAN family provides a unique example of a plant pathogen response gene conserved in animals. The IAN/IMAP subfamily has been proposed to regulate apoptosis in vertebrates and angiosperm plants, particularly in relation to cancer, diabetes, and infections. The human IAN genes were renamed GIMAP (GTPase of the immunity associated proteins).


Pssm-ID: 206651 [Multi-domain]  Cd Length: 201  Bit Score: 101.07  E-value: 6.32e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495027916   2 ILVVGKSGSGKSRLCNVLAGVELFESKLSPRSVTMVHQVETVDIEGKKVTIVDSP------ETPNY-------------D 62
Cdd:cd01852    3 LVLVGKTGNGKSATGNTILGRKVFESKLSASGVTKTCQKESAVWDGRRVNVIDTPglfdtsVSPEQlskeiirclslsaP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495027916  63 GPiSAFFYLIEAGRFTAEDKEYIQMMRKRF-PGFEKSTILILNRADELKtDDDIRNWVKTSGE-LDSLVRACGGRIAKFH 140
Cdd:cd01852   83 GP-HAFLLVVPLGRFTEEEEQAVEELQELFgEKVLDHTIVLFTRGDDLE-GGSLEDYLEDSCEaLKRLLEKCGGRYVAFN 160
                        170       180
                 ....*....|....*....|....*..
gi 495027916 141 rhkiNRAKLLEKAATLPEFVSHLPRLV 167
Cdd:cd01852  161 ----NKAKGREQEQQVKELLAKVEEMV 183
AIG1 pfam04548
AIG1 family; Arabidopsis protein AIG1 appears to be involved in plant resistance to bacteria.
2-167 5.31e-14

AIG1 family; Arabidopsis protein AIG1 appears to be involved in plant resistance to bacteria.


Pssm-ID: 398307 [Multi-domain]  Cd Length: 200  Bit Score: 69.17  E-value: 5.31e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495027916    2 ILVVGKSGSGKSRLCNVLAGVELFESKLSPRSVTMVHQVETVDIEGKKVTIVDSP-----ETPNYD-------------G 63
Cdd:pfam04548   3 IVLVGKTGNGKSATGNSILGRKAFESKLRAQGVTKTCQLVSRTWDGRIINVIDTPglfdlSVSNDFiskeiirclllaeP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495027916   64 PISAFFYLIEAGRFTAEDKEYIQMMRKRF-PGFEKSTILILNRADELKTDDdirnwvktsgeLDSLVRACggrIAKFHRH 142
Cdd:pfam04548  83 GPHAVLLVLSLGRFTEEEEQALRTLQELFgSKILDYMIVVFTRKDDLEDDS-----------LDDYLSDG---CPEFLKE 148
                         170       180
                  ....*....|....*....|....*
gi 495027916  143 KINRAKLLEKAATLPEFVSHLPRLV 167
Cdd:pfam04548 149 VLRTADGEEKEEQVQQLLALVEAIV 173
YeeP COG3596
Predicted GTPase [General function prediction only];
2-109 3.28e-09

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 56.70  E-value: 3.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495027916   2 ILVVGKSGSGKSRLCNVLAGVELFE-SKLSPrsVTM---VHQVETVDIEGkkVTIVDSP---ETPNYDGPISA------- 67
Cdd:COG3596   42 IALVGKTGAGKSSLINALFGAEVAEvGVGRP--CTReiqRYRLESDGLPG--LVLLDTPglgEVNERDREYRElrellpe 117
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 495027916  68 ---FFYLIEAG-RFTAEDKEYIQMMRKRFPGfeKSTILILNRADEL 109
Cdd:COG3596  118 adlILWVVKADdRALATDEEFLQALRAQYPD--PPVLVVLTQVDRL 161
p47_IIGP_like cd04104
p47 GTPase family includes IGTP, TGTP/Mg21, IRG-47, GTPI, LRG-47, and IIGP1; The p47 GTPase ...
2-92 1.45e-06

p47 GTPase family includes IGTP, TGTP/Mg21, IRG-47, GTPI, LRG-47, and IIGP1; The p47 GTPase family consists of several highly homologous proteins, including IGTP, TGTP/Mg21, IRG-47, GTPI, LRG-47, and IIGP1. They are found in higher eukaryotes where they play a role in immune resistance against intracellular pathogens. p47 proteins exist at low resting levels in mouse cells, but are strongly induced by Type II interferon (IFN-gamma). ITGP is critical for resistance to Toxoplasma gondii infection and in involved in inhibition of Coxsackievirus-B3-induced apoptosis. TGTP was shown to limit vesicular stomatitis virus (VSV) infection of fibroblasts in vitro. IRG-47 is involved in resistance to T. gondii infection. LRG-47 has been implicated in resistance to T. gondii, Listeria monocytogenes, Leishmania, and mycobacterial infections. IIGP1 has been shown to localize to the ER and to the Golgi membranes in IFN-induced cells and inflamed tissues. In macrophages, IIGP1 interacts with hook3, a microtubule binding protein that participates in the organization of the cis-Golgi compartment.


Pssm-ID: 206690  Cd Length: 197  Bit Score: 47.71  E-value: 1.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495027916   2 ILVVGKSGSGKSRLCNVLAGVELFESKLSPRSVtmvhqVETVdiegKKVTIVDSPETPN---YDGP-ISA---------- 67
Cdd:cd04104    4 IAVTGESGAGKSSFINALRGIGHEEEGAAPTGV-----VETT----MKRTPYPHPKFPNvtlWDLPgIGStafppddyle 74
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 495027916  68 --------FFYLIEAGRFTAED---KEYIQMMRKRF 92
Cdd:cd04104   75 emkfseydFFIIISSTRFSSNDvklAKAIQMMGKKF 110
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
2-105 1.58e-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: 46.07  E-value: 1.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495027916    2 ILVVGKSGSGKSRLCNVLAGVelfESKLSPRS-VTMVHQVETVDIEGKKVTIVDSP----ETPNYDGPISAFFYLIEA-- 74
Cdd:pfam01926   2 VALVGRPNVGKSTLINALTGA---KAIVSDYPgTTRDPNEGRLELKGKQIILVDTPglieGASEGEGLGRAFLAIIEAdl 78
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 495027916   75 --------GRFTAEDKEYIQMMRKRfpgfEKSTILILNR 105
Cdd:pfam01926  79 ilfvvdseEGITPLDEELLELLREN----KKPIILVLNK 113
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
2-163 3.95e-06

Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The dynamin family of large mechanochemical GTPases includes the classical dynamins and dynamin-like proteins (DLPs) that are found throughout the Eukarya. This family also includes bacterial DLPs. These proteins catalyze membrane fission during clathrin-mediated endocytosis. Dynamin consists of five domains; an N-terminal G domain that binds and hydrolyzes GTP, a middle domain (MD) involved in self-assembly and oligomerization, a pleckstrin homology (PH) domain responsible for interactions with the plasma membrane, GED, which is also involved in self-assembly, and a proline arginine rich domain (PRD) that interacts with SH3 domains on accessory proteins. To date, three vertebrate dynamin genes have been identified; dynamin 1, which is brain specific, mediates uptake of synaptic vesicles in presynaptic terminals; dynamin-2 is expressed ubiquitously and similarly participates in membrane fission; mutations in the MD, PH and GED domains of dynamin 2 have been linked to human diseases such as Charcot-Marie-Tooth peripheral neuropathy and rare forms of centronuclear myopathy. Dynamin 3 participates in megakaryocyte progenitor amplification, and is also involved in cytoplasmic enlargement and the formation of the demarcation membrane system. This family also includes mitofusins (MFN1 and MFN2 in mammals) that are involved in mitochondrial fusion. Dynamin oligomerizes into helical structures around the neck of budding vesicles in a GTP hydrolysis-dependent manner.


Pssm-ID: 206739 [Multi-domain]  Cd Length: 180  Bit Score: 46.39  E-value: 3.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495027916   2 ILVVGKSGSGKSRLCNVLAGVELFESKLSPrsVTMVHQVETVDIEgKKVTIVDSP-----------ETPNYDGPISAFFY 70
Cdd:cd09912    3 LAVVGEFSAGKSTLLNALLGEEVLPTGVTP--TTAVITVLRYGLL-KGVVLVDTPglnstiehhteITESFLPRADAVIF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495027916  71 LIEAGR-FTAEDKEYIQMMRKRfpgFEKSTILILNRADELkTDDDIRNWVKTSGELDSLVRACGGRIAKF-------HRH 142
Cdd:cd09912   80 VLSADQpLTESEREFLKEILKW---SGKKIFFVLNKIDLL-SEEELEEVLEYSREELGVLELGGGEPRIFpvsakeaLEA 155
                        170       180
                 ....*....|....*....|.
gi 495027916 143 KINRAKLLEKAATLPEFVSHL 163
Cdd:cd09912  156 RLQGDEELLEQSGFEELEEHL 176
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
3-113 4.71e-06

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: 45.91  E-value: 4.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495027916   3 LVVGKSGSGKSRLCNVLAGVELFE-SKLSPRSVTMVHQVETVDIEGKKVTIVDSPETPNYDGPISAFFYLIEAGR----- 76
Cdd:cd00882    1 VVVGRGGVGKSSLLNALLGGEVGEvSDVPGTTRDPDVYVKELDKGKVKLVLVDTPGLDEFGGLGREELARLLLRGadlil 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 495027916  77 --FTAEDKEYIQMMR----KRFPGFEKSTILILNRADELKTDD 113
Cdd:cd00882   81 lvVDSTDRESEEDAKllilRRLRKEGIPIILVGNKIDLLEERE 123
CDC_Septin cd01850
CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated ...
2-61 2.57e-05

CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated with diverse processes in dividing and non-dividing cells. They were first discovered in the budding yeast S. cerevisiae as a set of genes (CDC3, CDC10, CDC11 and CDC12) required for normal bud morphology. Septins are also present in metazoan cells, where they are required for cytokinesis in some systems, and implicated in a variety of other processes involving organization of the cell cortex and exocytosis. In humans, 12 septin genes generate dozens of polypeptides, many of which comprise heterooligomeric complexes. Since septin mutants are commonly defective in cytokinesis and formation of the neck formation of the neck filaments/septin rings, septins have been considered to be the primary constituents of the neck filaments. Septins belong to the GTPase superfamily for their conserved GTPase motifs and enzymatic activities.


Pssm-ID: 206649  Cd Length: 275  Bit Score: 44.84  E-value: 2.57e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495027916   2 ILVVGKSGSGKSRLCNVLAGVELFESKLSPRSVTMVH-----QVETVDIEGK----KVTIVDspeTPNY 61
Cdd:cd01850    7 IMVVGESGLGKSTFINTLFGTKLYPSKYPPAPGEHITktveiKISKAELEENgvklKLTVID---TPGF 72
YfjP cd11383
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ...
3-108 3.80e-05

YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several uncharacterized bacterial GTPases that are similar to Era. They generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain.


Pssm-ID: 206743 [Multi-domain]  Cd Length: 140  Bit Score: 42.71  E-value: 3.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495027916   3 LVVGKSGSGKSRLCNVLAGVELfeSKLSPRSVTMVhQVETVD--IEGKKVTIVDSPETPnydgpisaffyliEAGRFtae 80
Cdd:cd11383    1 GLMGKTGAGKSSLCNALFGTEV--AAVGDRRPTTR-AAQAYVwqTGGDGLVLLDLPGVG-------------ERGRR--- 61
                         90       100
                 ....*....|....*....|....*...
gi 495027916  81 DKEYIQMMRKRFPgfEKSTILILNRADE 108
Cdd:cd11383   62 DREYEELYRRLLP--EADLVLWLLDADD 87
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
2-56 4.78e-04

small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this model include Ras, RhoA, Rab11, translation elongation factor G, translation initiation factor IF-2, tetratcycline resistance protein TetM, CDC42, Era, ADP-ribosylation factors, tdhF, and many others. In some proteins the domain occurs more than once.This model recognizes a large number of small GTP-binding proteins and related domains in larger proteins. Note that the alpha chains of heterotrimeric G proteins are larger proteins in which the NKXD motif is separated from the GxxxxGK[ST] motif (P-loop) by a long insert and are not easily detected by this model. [Unknown function, General]


Pssm-ID: 272973 [Multi-domain]  Cd Length: 162  Bit Score: 40.05  E-value: 4.78e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 495027916    2 ILVVGKSGSGKSRLCNVLAGVELFESKLSPR-SVTMVHQVETVDIEGKKVTIVDSP 56
Cdd:TIGR00231   4 IVIVGHPNVGKSTLLNSLLGNKGSITEYYPGtTRNYVTTVIEEDGKTYKFNLLDTA 59
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
4-116 9.28e-04

E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family includes several distinct subfamilies (TrmE/ThdF, FeoB, YihA (EngB), Era, and EngA/YfgK) that generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. TrmE is ubiquitous in bacteria and is a widespread mitochondrial protein in eukaryotes, but is absent from archaea. The yeast member of TrmE family, MSS1, is involved in mitochondrial translation; bacterial members are often present in translation-related operons. FeoB represents an unusual adaptation of GTPases for high-affinity iron (II) transport. YihA (EngB) family of GTPases is typified by the E. coli YihA, which is an essential protein involved in cell division control. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain. EngA and its orthologs are composed of two GTPase domains and, since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family.


Pssm-ID: 206646 [Multi-domain]  Cd Length: 161  Bit Score: 39.15  E-value: 9.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495027916   4 VVGKSGSGKSRLCNVLAGVELFESKLSPRSVTMVHQVETVDIEGKKVTIVDspeTPNYD---GPISAFFYL--------- 71
Cdd:cd00880    2 IFGRPNVGKSSLLNALLGQNVGIVSPIPGTTRDPVRKEWELLPLGPVVLID---TPGLDeegGLGRERVEEarqvadrad 78
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 495027916  72 -----IEAGRFTAEDKEYIQMMRKRfpgfEKSTILILNRADELKTDDDIR 116
Cdd:cd00880   79 lvllvVDSDLTPVEEEAKLGLLRER----GKPVLLVLNKIDLVPESEEEE 124
IIGP pfam05049
Interferon-inducible GTPase (IIGP); Interferon-inducible GTPase (IIGP) is thought to play a ...
2-92 1.91e-03

Interferon-inducible GTPase (IIGP); Interferon-inducible GTPase (IIGP) is thought to play a role in in intracellular defence. IIGP is predominantly associated with the Golgi apparatus and also localizes to the endoplasmic reticulum and exerts a distinct role in IFN-induced intracellular membrane trafficking or processing.


Pssm-ID: 461536 [Multi-domain]  Cd Length: 375  Bit Score: 39.39  E-value: 1.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495027916    2 ILVVGKSGSGKSRLCNVLAGVELFESKLSPRSVtmvhqVETVdiegKKVTIVDSPETPN---YDGP-ISA---------- 67
Cdd:pfam05049  38 IAVTGDSGNGKSSFINALRGIGHEEDGSAPTGV-----VETT----MKRTPYSHPHFPNvvlWDLPgLGAtnftvesyle 108
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 495027916   68 --------FFYLIEAGRFTAEDKEY---IQMMRKRF 92
Cdd:pfam05049 109 emkfseydFFIIISSERFSLNDVKLakaIQRMGKRF 144
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
2-118 5.64e-03

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 36.88  E-value: 5.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495027916   2 ILVVGKSGSGKSRLCNVLAGVELFESK-LSPRSVTMVHQVETVDIEGKKVTIVDSP-------ETPNYDGPI---SAFFY 70
Cdd:COG1100    6 IVVVGTGGVGKTSLVNRLVGDIFSLEKyLSTNGVTIDKKELKLDGLDVDLVIWDTPgqdefreTRQFYARQLtgaSLYLF 85
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 495027916  71 LIEAGR---FTAEdKEYIQMMRKRFPGFEksTILILNRADELkTDDDIRNW 118
Cdd:COG1100   86 VVDGTReetLQSL-YELLESLRRLGKKSP--IILVLNKIDLY-DEEEIEDE 132
Septin pfam00735
Septin; Members of this family include CDC3, CDC10, CDC11 and CDC12/Septin. Members of this ...
2-56 6.02e-03

Septin; Members of this family include CDC3, CDC10, CDC11 and CDC12/Septin. Members of this family bind GTP. As regards the septins, these are polypeptides of 30-65kDa with three characteriztic GTPase motifs (G-1, G-3 and G-4) that are similar to those of the Ras family. The G-4 motif is strictly conserved with a unique septin consensus of AKAD. Most septins are thought to have at least one coiled-coil region, which in some cases is necessary for intermolecular interactions that allow septins to polymerize to form rod-shaped complexes. In turn, these are arranged into tandem arrays to form filaments. They are multifunctional proteins, with roles in cytokinesis, sporulation, germ cell development, exocytosis and apoptosis.


Pssm-ID: 395596  Cd Length: 272  Bit Score: 37.66  E-value: 6.02e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495027916    2 ILVVGKSGSGKSRLCNVLAGVELFESKLSP-RSVTMVHQVE----TVDIEGKKV----TIVDSP 56
Cdd:pfam00735   6 LMVVGESGLGKTTFINTLFLTDLYRARGIPgPSEKIKKTVEikayTVEIEEDGVklnlTVIDTP 69
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
2-23 8.06e-03

First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.


Pssm-ID: 213192 [Multi-domain]  Cd Length: 211  Bit Score: 36.68  E-value: 8.06e-03
                         10        20
                 ....*....|....*....|..
gi 495027916   2 ILVVGKSGSGKSRLCNVLAGVE 23
Cdd:cd03225   30 VLIVGPNGSGKSTLLRLLNGLL 51
 
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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