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Conserved domains on  [gi|30681303|ref|NP_850553|]
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P-loop containing nucleoside triphosphate hydrolases superfamily protein [Arabidopsis thaliana]

Protein Classification

SpoIIIAA family protein( domain architecture ID 10790452)

SpoIIIAA family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SpoIIIAA COG3854
Stage III sporulation protein SpoIIIAA [Cell cycle control, cell division, chromosome ...
 96-368 8.48e-102

Stage III sporulation protein SpoIIIAA [Cell cycle control, cell division, chromosome partitioning];


:

Pssm-ID: 443063  Cd Length: 309  Bit Score: 309.39  E-value: 8.48e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681303  96 ELDAFLEILPPATRKELVKH--EAIEELIEVVMDLGRKPLARFPSGDWVISEQ-PVTHQDLELAVSKVGDFS-------- 164
Cdd:COG3854   1 DLEEILAILPPTIREALEKLpdPVLDKLEEIRLRLGRPLELRFPGGEYFLSEAyPVTREDLERTLNRISNYSlyaleeel 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681303 165 --------DDNRSGIDRSLHRISAIRNRKLQVIGLTCRVGRVVSGSAEIIRDLIEGGG---SILVIGSPGVGKTTLIREI 233
Cdd:COG3854  81 rqgyitipGGHRVGIAGTVVRESGIVKRIKDISGLNIRIAREVKGTADPILPYIISGGriyNTLIISPPGCGKTTLLRDI 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681303 234 ARMLADE----HRKRVVIVDTSNEIGGD-GDVPHSGIGRarRMQVPNVNLQHDVMIEAVENHMPETIIIDEIGTELEALA 308
Cdd:COG3854 161 ARVLSDGllgfPGKRVGVVDERSEIAGCyGGIPQPDIGI--RTDVLDGCPKAEGMIMAIRSMSPEVIVVDEIGREEDAEA 238

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30681303 309 ASTIAQRGVQLVATAHGMTIDNIIKNPSLQILIGGI---ESVTLGDEEArkRKVQKTILERKG 368
Cdd:COG3854 239 LREAANAGVQLIATAHGNSLEDLLKRPTLSDLIGGGvfeRYVTLSRREG--PGTVETILDRKA 299
 
Name Accession Description Interval E-value
SpoIIIAA COG3854
Stage III sporulation protein SpoIIIAA [Cell cycle control, cell division, chromosome ...
 96-368 8.48e-102

Stage III sporulation protein SpoIIIAA [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443063  Cd Length: 309  Bit Score: 309.39  E-value: 8.48e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681303  96 ELDAFLEILPPATRKELVKH--EAIEELIEVVMDLGRKPLARFPSGDWVISEQ-PVTHQDLELAVSKVGDFS-------- 164
Cdd:COG3854   1 DLEEILAILPPTIREALEKLpdPVLDKLEEIRLRLGRPLELRFPGGEYFLSEAyPVTREDLERTLNRISNYSlyaleeel 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681303 165 --------DDNRSGIDRSLHRISAIRNRKLQVIGLTCRVGRVVSGSAEIIRDLIEGGG---SILVIGSPGVGKTTLIREI 233
Cdd:COG3854  81 rqgyitipGGHRVGIAGTVVRESGIVKRIKDISGLNIRIAREVKGTADPILPYIISGGriyNTLIISPPGCGKTTLLRDI 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681303 234 ARMLADE----HRKRVVIVDTSNEIGGD-GDVPHSGIGRarRMQVPNVNLQHDVMIEAVENHMPETIIIDEIGTELEALA 308
Cdd:COG3854 161 ARVLSDGllgfPGKRVGVVDERSEIAGCyGGIPQPDIGI--RTDVLDGCPKAEGMIMAIRSMSPEVIVVDEIGREEDAEA 238

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30681303 309 ASTIAQRGVQLVATAHGMTIDNIIKNPSLQILIGGI---ESVTLGDEEArkRKVQKTILERKG 368
Cdd:COG3854 239 LREAANAGVQLIATAHGNSLEDLLKRPTLSDLIGGGvfeRYVTLSRREG--PGTVETILDRKA 299
spore_III_AA TIGR02858
stage III sporulation protein AA; Members of this protein are the stage III sporulation ...
 177-341 7.51e-18

stage III sporulation protein AA; Members of this protein are the stage III sporulation protein AA, encoded by one of several genes in the spoIIIA locus. It seems that this protein is found in a species if and only if that species is capable of endospore formation. [Cellular processes, Sporulation and germination]


Pssm-ID: 274324  Cd Length: 270  Bit Score: 83.55  E-value: 7.51e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681303   177 RISAIRNrklqVIGLTCRVGRVVSGSAE-IIRDLIEGGG--SILVIGSPGVGKTTLIREIARMLADEHRK------RVVI 247
Cdd:TIGR02858  76 KVKTIKN----VSSLNIRIAREKLGAADkLLPYLVRNNRvlNTLIISPPQCGKTTLLRDLARILSTGISQlglrgkKVGI 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681303   248 VDTSNEIGG--DGdVPHSGIGRarRMQVPNVNLQHDVMIEAVENHMPETIIIDEIGTELEALAASTIAQRGVQLVATAHG 325
Cdd:TIGR02858 152 VDERSEIAGcvNG-VPQHDVGI--RTDVLDGCPKAEGMMMLIRSMSPDVIVVDEIGREEDVEALLEALHAGVSIIATAHG 228

                         170
                  ....*....|....*.
gi 30681303   326 MTIDNIIKNPSLQILI 341
Cdd:TIGR02858 229 RDVEDLYKRPVFKELI 244
Spore_III_AA pfam19568
Sporulation stage III, protein AA;
191-341 3.84e-11

Sporulation stage III, protein AA;


Pssm-ID: 437400  Cd Length: 306  Bit Score: 64.43  E-value: 3.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681303   191 LTCRVGRVVSGSAEIIRDLIEGGGSI---LVIGSPGVGKTTLIREIARMLADEHRKR----VVIVDTSNEIGG-DGDVPH 262
Cdd:pfam19568 119 LNIRLAHEVRGCADGVMPYIWCNEEVrhtLIISPPRCGKTTLLRDMIRQISDGNQYVpgvtVGVVDERSELGAcYLGVPQ 198

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30681303   263 SGIGRarRMQVPNVNLQHDVMIEAVENHMPETIIIDEIGTELEALAASTIAQRGVQLVATAHGMTIDNIIKNPSLQILI 341
Cdd:pfam19568 199 NDLGR--RTDILDCCPKAEGMIMLIRSMSPTVVAVDEIGGQEDIEALEYAMNCGCTIIATVHGACMEDISNRPVLRRLI 275
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 213-328 1.96e-09

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 56.23  E-value: 1.96e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681303    213 GGSILVIGSPGVGKTTLIREIARMLADEHrKRVVIVDTSNEIGGDGDVPHsGIGRARRMQVPNVNLQHDVMIEAVENHMP 292
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPG-GGVIYIDGEDILEEVLDQLL-LIIVGGKKASGSGELRLRLALALARKLKP 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 30681303    293 ETIIIDEIGT-------------ELEALAASTIAQRGVQLVATAHGMTI 328
Cdd:smart00382  80 DVLILDEITSlldaeqealllllEELRLLLLLKSEKNLTVILTTNDEKD 128
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 213-302 1.30e-08

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 54.07  E-value: 1.30e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681303 213 GGSILVIGSPGVGKTTLIREIARMLAdEHRKRVVIVDTSNEIGGDGDVPHSGIGRARRMQvpnvnlqhdvmiEAVENHMP 292
Cdd:cd00009  19 PKNLLLYGPPGTGKTTLARAIANELF-RPGAPFLYLNASDLLEGLVVAELFGHFLVRLLF------------ELAEKAKP 85

                        90
                ....*....|
gi 30681303 293 ETIIIDEIGT 302
Cdd:cd00009  86 GVLFIDEIDS 95
PRK13894 PRK13894
conjugal transfer ATPase TrbB; Provisional
 180-254 3.22e-05

conjugal transfer ATPase TrbB; Provisional


Pssm-ID: 184377  Cd Length: 319  Bit Score: 46.27  E-value: 3.22e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30681303  180 AIRNRKLQVIGLTCRV--GRVVSGSAEIIRDLIEGGGSILVIGSPGVGKTTLIREIAR-MLADEHRKRVVIVDTSNEI 254
Cdd:PRK13894 113 AIRKKAVAIFTLDQYVerGIMTAAQREAIIAAVRAHRNILVIGGTGSGKTTLVNAIINeMVIQDPTERVFIIEDTGEI 190
 
Name Accession Description Interval E-value
SpoIIIAA COG3854
Stage III sporulation protein SpoIIIAA [Cell cycle control, cell division, chromosome ...
 96-368 8.48e-102

Stage III sporulation protein SpoIIIAA [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443063  Cd Length: 309  Bit Score: 309.39  E-value: 8.48e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681303  96 ELDAFLEILPPATRKELVKH--EAIEELIEVVMDLGRKPLARFPSGDWVISEQ-PVTHQDLELAVSKVGDFS-------- 164
Cdd:COG3854   1 DLEEILAILPPTIREALEKLpdPVLDKLEEIRLRLGRPLELRFPGGEYFLSEAyPVTREDLERTLNRISNYSlyaleeel 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681303 165 --------DDNRSGIDRSLHRISAIRNRKLQVIGLTCRVGRVVSGSAEIIRDLIEGGG---SILVIGSPGVGKTTLIREI 233
Cdd:COG3854  81 rqgyitipGGHRVGIAGTVVRESGIVKRIKDISGLNIRIAREVKGTADPILPYIISGGriyNTLIISPPGCGKTTLLRDI 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681303 234 ARMLADE----HRKRVVIVDTSNEIGGD-GDVPHSGIGRarRMQVPNVNLQHDVMIEAVENHMPETIIIDEIGTELEALA 308
Cdd:COG3854 161 ARVLSDGllgfPGKRVGVVDERSEIAGCyGGIPQPDIGI--RTDVLDGCPKAEGMIMAIRSMSPEVIVVDEIGREEDAEA 238

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30681303 309 ASTIAQRGVQLVATAHGMTIDNIIKNPSLQILIGGI---ESVTLGDEEArkRKVQKTILERKG 368
Cdd:COG3854 239 LREAANAGVQLIATAHGNSLEDLLKRPTLSDLIGGGvfeRYVTLSRREG--PGTVETILDRKA 299
spore_III_AA TIGR02858
stage III sporulation protein AA; Members of this protein are the stage III sporulation ...
 177-341 7.51e-18

stage III sporulation protein AA; Members of this protein are the stage III sporulation protein AA, encoded by one of several genes in the spoIIIA locus. It seems that this protein is found in a species if and only if that species is capable of endospore formation. [Cellular processes, Sporulation and germination]


Pssm-ID: 274324  Cd Length: 270  Bit Score: 83.55  E-value: 7.51e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681303   177 RISAIRNrklqVIGLTCRVGRVVSGSAE-IIRDLIEGGG--SILVIGSPGVGKTTLIREIARMLADEHRK------RVVI 247
Cdd:TIGR02858  76 KVKTIKN----VSSLNIRIAREKLGAADkLLPYLVRNNRvlNTLIISPPQCGKTTLLRDLARILSTGISQlglrgkKVGI 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681303   248 VDTSNEIGG--DGdVPHSGIGRarRMQVPNVNLQHDVMIEAVENHMPETIIIDEIGTELEALAASTIAQRGVQLVATAHG 325
Cdd:TIGR02858 152 VDERSEIAGcvNG-VPQHDVGI--RTDVLDGCPKAEGMMMLIRSMSPDVIVVDEIGREEDVEALLEALHAGVSIIATAHG 228

                         170
                  ....*....|....*.
gi 30681303   326 MTIDNIIKNPSLQILI 341
Cdd:TIGR02858 229 RDVEDLYKRPVFKELI 244
Spore_III_AA pfam19568
Sporulation stage III, protein AA;
191-341 3.84e-11

Sporulation stage III, protein AA;


Pssm-ID: 437400  Cd Length: 306  Bit Score: 64.43  E-value: 3.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681303   191 LTCRVGRVVSGSAEIIRDLIEGGGSI---LVIGSPGVGKTTLIREIARMLADEHRKR----VVIVDTSNEIGG-DGDVPH 262
Cdd:pfam19568 119 LNIRLAHEVRGCADGVMPYIWCNEEVrhtLIISPPRCGKTTLLRDMIRQISDGNQYVpgvtVGVVDERSELGAcYLGVPQ 198

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30681303   263 SGIGRarRMQVPNVNLQHDVMIEAVENHMPETIIIDEIGTELEALAASTIAQRGVQLVATAHGMTIDNIIKNPSLQILI 341
Cdd:pfam19568 199 NDLGR--RTDILDCCPKAEGMIMLIRSMSPTVVAVDEIGGQEDIEALEYAMNCGCTIIATVHGACMEDISNRPVLRRLI 275
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 213-328 1.96e-09

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 56.23  E-value: 1.96e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681303    213 GGSILVIGSPGVGKTTLIREIARMLADEHrKRVVIVDTSNEIGGDGDVPHsGIGRARRMQVPNVNLQHDVMIEAVENHMP 292
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPG-GGVIYIDGEDILEEVLDQLL-LIIVGGKKASGSGELRLRLALALARKLKP 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 30681303    293 ETIIIDEIGT-------------ELEALAASTIAQRGVQLVATAHGMTI 328
Cdd:smart00382  80 DVLILDEITSlldaeqealllllEELRLLLLLKSEKNLTVILTTNDEKD 128
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 213-302 1.30e-08

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 54.07  E-value: 1.30e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681303 213 GGSILVIGSPGVGKTTLIREIARMLAdEHRKRVVIVDTSNEIGGDGDVPHSGIGRARRMQvpnvnlqhdvmiEAVENHMP 292
Cdd:cd00009  19 PKNLLLYGPPGTGKTTLARAIANELF-RPGAPFLYLNASDLLEGLVVAELFGHFLVRLLF------------ELAEKAKP 85

                        90
                ....*....|
gi 30681303 293 ETIIIDEIGT 302
Cdd:cd00009  86 GVLFIDEIDS 95
RadA_SMS_N cd01121
bacterial RadA DNA repair protein; Sms or bacterial RadA is a DNA repair protein that plays a ...
 197-314 6.32e-08

bacterial RadA DNA repair protein; Sms or bacterial RadA is a DNA repair protein that plays a role in recombination and recombinational repair of DNA damaged by UV radiation, X-rays, and chemical agent and is responsible for the stabilization or processing of branched DNA molecules.


Pssm-ID: 410866 [Multi-domain]  Cd Length: 268  Bit Score: 54.07  E-value: 6.32e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681303 197 RVVSGSAEIIRDLieGGG-----SILVIGSPGVGKTTLIREIARMLADEHRKrVVIV---DTSNEIGgdgdvphsgiGRA 268
Cdd:cd01121  63 RISTGIGELDRVL--GGGlvpgsVVLIGGDPGIGKSTLLLQVAARLAQRGGK-VLYVsgeESLSQIK----------LRA 129

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 30681303 269 RRMQVPNVNLQ------HDVMIEAVENHMPETIIIDEIGT----ELEAlAASTIAQ 314
Cdd:cd01121 130 ERLGLGSDNLYllaetnLEAILAEIEELKPSLVVIDSIQTvyspELTS-SPGSVSQ 184
RecA-like_Thep1 cd19482
RecA-like domain of the nucleoside-triphosphatase THEP1 family; This family represents the ...
 216-301 4.97e-06

RecA-like domain of the nucleoside-triphosphatase THEP1 family; This family represents the THEP1 family ATPase domain. It includes nucleoside-triphosphatase THEP 1 from Aquifex aeolicus (aaTHEP1) a nucleoside-phosphatase, with activity towards ATP, GTP, CTP, TTP and UTP; and which may hydrolyze nucleoside diphosphates with lower efficiency. The catalytic function of aaTHEP1 remains unclear, it may be a DNA/RNA modifying enzyme. Human THEP1 (hsTHEP1) may have a general function in many human tissues, as it is widely expressed in most examined tissues (such as in brain, heart, lymph node, skin, pancreas); it is especially highly expressed in embryonic and various tumor tissues. This family belongs to the RecA-like NTPase superfamily which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410890 [Multi-domain]  Cd Length: 164  Bit Score: 46.83  E-value: 4.97e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681303 216 ILVIGSPGVGKTTLIREIARMLAD--------------EHRKRV--VIVDTSNeiGGDGDVPHSGIGRARRMQVPnVNLQ 279
Cdd:cd19482   1 IFITGPPGVGKTTLVLKVAELLKEsglkvggfytpevrEGGKRIgfKIVDLAS--GERGWLARVGAGSPKVGKYG-VDVD 77

                        90       100
                ....*....|....*....|....*.
gi 30681303 280 H--DVMIEAVENHMPET--IIIDEIG 301
Cdd:cd19482  78 EleEIAVPALRRALEEAdvIIIDEIG 103
AAA_22 pfam13401
AAA domain;
211-300 1.53e-05

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 44.64  E-value: 1.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681303   211 EGGGSILVIGSPGVGKTTLIREIARMLaDEHRKRVVIVDTSNEIGGDGDVPH--SGIGRARRMQVPNVNLQHDVMIEAVE 288
Cdd:pfam13401   3 FGAGILVLTGESGTGKTTLLRRLLEQL-PEVRDSVVFVDLPSGTSPKDLLRAllRALGLPLSGRLSKEELLAALQQLLLA 81

                          90
                  ....*....|..
gi 30681303   289 NHMPETIIIDEI 300
Cdd:pfam13401  82 LAVAVVLIIDEA 93
NTPase_1 pfam03266
NTPase; This domain is found across all species from bacteria to human, and the function was ...
 216-324 2.03e-05

NTPase; This domain is found across all species from bacteria to human, and the function was determined first in a hyperthermophilic bacterium to be an NTPase. The structure of one member-sequence represents a variation of the RecA fold, and implies that the function might be that of a DNA/RNA modifying enzyme. The sequence carries both a Walker A and Walker B motif which together are characteriztic of ATPases or GTPases. The protein exhibits an increased expression profile in human liver cholangiocarcinoma when compared to normal tissue.


Pssm-ID: 460869  Cd Length: 168  Bit Score: 44.92  E-value: 2.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681303   216 ILVIGSPGVGKTTLIREIARMLAD--------------EHRKRV--VIVDTSNEIGGdgdvPHSGIGRARRMQV--PNVN 277
Cdd:pfam03266   2 IFITGPPGVGKTTLVLKVAELLKSsgvkvggfytpevrEGGRRIgfKIVDLASGEEG----WLARVGAVSGPRVgkYVVN 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 30681303   278 LQH--DVMIEAVENHMPET--IIIDEIGT-ELEAL----AASTIAQRGVQLVATAH 324
Cdd:pfam03266  78 VESfeEIAVPALRRALEEAdlIIIDEIGPmELKSKkfreAVREVLDSGKPVLAVIH 133
PRK13894 PRK13894
conjugal transfer ATPase TrbB; Provisional
 180-254 3.22e-05

conjugal transfer ATPase TrbB; Provisional


Pssm-ID: 184377  Cd Length: 319  Bit Score: 46.27  E-value: 3.22e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30681303  180 AIRNRKLQVIGLTCRV--GRVVSGSAEIIRDLIEGGGSILVIGSPGVGKTTLIREIAR-MLADEHRKRVVIVDTSNEI 254
Cdd:PRK13894 113 AIRKKAVAIFTLDQYVerGIMTAAQREAIIAAVRAHRNILVIGGTGSGKTTLVNAIINeMVIQDPTERVFIIEDTGEI 190
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
203-300 8.85e-05

Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 44.84  E-value: 8.85e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681303 203 AEIIRDLIEGGGS--ILVIGSPGVGKTTLIREIARMLADEHRKRVVIVDT------------------SNEIGGDGDVPH 262
Cdd:COG1474  39 ASALRPALRGERPsnVLIYGPTGTGKTAVAKYVLEELEEEAEERGVDVRVvyvncrqastryrvlsriLEELGSGEDIPS 118

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 30681303 263 SGIGRarrmqvpnvnlqhDVMIEAVENHMPET-----IIIDEI 300
Cdd:COG1474 119 TGLST-------------DELFDRLYEALDERdgvlvVVLDEI 148
THEP1 COG1618
Nucleoside-triphosphatase THEP1 [Nucleotide transport and metabolism];
216-301 2.00e-04

Nucleoside-triphosphatase THEP1 [Nucleotide transport and metabolism];


Pssm-ID: 441225 [Multi-domain]  Cd Length: 175  Bit Score: 42.20  E-value: 2.00e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681303 216 ILVIGSPGVGKTTLIREIARMLAD--------------EHRKRV--VIVDTSNeiGGDGDVPHSGIGRARRMQVPNVNLQ 279
Cdd:COG1618   3 IFITGRPGVGKTTLLLKVVEELRDeglrvggfitpevrEGGRRVgfKLVDLAT--GEEAILASVDIDSGPRVGKYGVDPE 80

                        90       100
                ....*....|....*....|....*.
gi 30681303 280 --HDVMIEAVENHMPET--IIIDEIG 301
Cdd:COG1618  81 alEAIAVEALERALEEAdlIVIDEIG 106
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 194-237 2.24e-04

MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 440478 [Multi-domain]  Cd Length: 292  Bit Score: 43.23  E-value: 2.24e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 30681303 194 RVGRVVSGSAEIIRDLIEG---GGSILVIGSPGVGKTTLIREIARML 237
Cdd:COG0714   9 EIGKVYVGQEELIELVLIAllaGGHLLLEGVPGVGKTTLAKALARAL 55
ExeA COG3267
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ...
 203-299 3.10e-04

Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 442498 [Multi-domain]  Cd Length: 261  Bit Score: 42.85  E-value: 3.10e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681303 203 AEIIRDLIEGGGSILVIGSPGVGKTTLIREIARMLaDEHRKRVVIVDTS-------NEIGGDGDVPHSGIGRARRMQvpn 275
Cdd:COG3267  33 ARLEYALAQGGGFVVLTGEVGTGKTTLLRRLLERL-PDDVKVAYIPNPQlspaellRAIADELGLEPKGASKADLLR--- 108

                        90       100
                ....*....|....*....|....
gi 30681303 276 vnLQHDVMIEAVENHMPETIIIDE 299
Cdd:COG3267 109 --QLQEFLLELAAAGRRVVLIIDE 130
SRP54 smart00962
SRP54-type protein, GTPase domain; This entry represents the GTPase domain of the 54 kDa SRP54 ...
 216-250 3.92e-04

SRP54-type protein, GTPase domain; This entry represents the GTPase domain of the 54 kDa SRP54 component, a GTP-binding protein that interacts with the signal sequence when it emerges from the ribosome. SRP54 of the signal recognition particle has a three-domain structure: an N-terminal helical bundle domain, a GTPase domain, and the M-domain that binds the 7s RNA and also binds the signal sequence. The extreme C-terminal region is glycine-rich and lower in complexity and poorly conserved between species. The GTPase domain is evolutionary related to P-loop NTPase domains found in a variety of other proteins.


Pssm-ID: 214940  Cd Length: 197  Bit Score: 41.63  E-value: 3.92e-04
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 30681303    216 ILVIGSPGVGKTTLIREIARMLADEHRKRVVIV--DT 250
Cdd:smart00962   4 ILLVGPNGVGKTTTIAKLAARLKLKGGKKVLLVaaDT 40
PRK13695 PRK13695
NTPase;
216-301 4.04e-04

NTPase;


Pssm-ID: 237475  Cd Length: 174  Bit Score: 41.44  E-value: 4.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681303  216 ILVIGSPGVGKTTLIREIARMLAD--------------EHRKRV--VIVDT-SNEIGGDGDVPHSGIGRARRMQVpNVNL 278
Cdd:PRK13695   3 IGITGPPGVGKTTLVLKIAELLKEegykvggfyteevrEGGKRIgfKIIDLdTGEEGILARVGFPSRPRVGKYVV-NLED 81

                         90       100
                 ....*....|....*....|....*
gi 30681303  279 QHDVMIEAVENHMPET--IIIDEIG 301
Cdd:PRK13695  82 LERIGIPALERALEEAdvIIIDEIG 106
type_II_IV_secretion_ATPases cd19477
type II/type IV hexameric secretion ATPases; RecA-like NTPases. This family includes the NTP ...
 206-398 5.98e-04

type II/type IV hexameric secretion ATPases; RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410885 [Multi-domain]  Cd Length: 168  Bit Score: 40.84  E-value: 5.98e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681303 206 IRDLIEGGGSILVIGSPGVGKTTLIREIARMLADEhrKRVVIVDTSNEIGGDgdvPHSGIGrarRMQVpNVNLQHDVMIE 285
Cdd:cd19477   3 IKDGIAIGKNVIVCGGTGSGKTTYIKSILEFIPKE--ERIISIEDTEEIVFK---HHKNYT---QLFF-GGNITSADCLK 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681303 286 AVENHMPETIIIDEIgtelealaASTIAQRGVQLVATAHGMTIDNIIKNPSlqiliggIESVTLGDEEARKRKVQKTILE 365
Cdd:cd19477  74 SCLRQRPDRIILGEL--------RSSEAYDFYNVLCSGHKGTLTTLHAGSS-------EEAFIRLAN*SSSNSAARNIKF 138

                       170       180       190
                ....*....|....*....|....*....|...
gi 30681303 366 RKGPPTFTCAVEMIsrtecrVHQRLDVTVDAIL 398
Cdd:cd19477 139 ESLIEGFKDLIDGI------VHINHHKQCDEFY 165
AAA_18 pfam13238
AAA domain;
216-306 9.60e-04

AAA domain;


Pssm-ID: 433052 [Multi-domain]  Cd Length: 128  Bit Score: 39.33  E-value: 9.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681303   216 ILVIGSPGVGKTTLIREIARMLADEHrkRVVIVDTSNEIGGDGDVPHSGIGRARRMQVPNVnlqHDVMIEAVENHMPETI 295
Cdd:pfam13238   1 ILITGTPGVGKTTLAKELSKRLGFGD--NVRDLALENGLVLGDDPETRESKRLDEDKLDRL---LDLLEENAALEEGGNL 75

                          90
                  ....*....|.
gi 30681303   296 IIDEIGTELEA 306
Cdd:pfam13238  76 IIDGHLAELEP 86
FlhF COG1419
Flagellar biosynthesis GTPase FlhF [Cell motility];
207-250 1.06e-03

Flagellar biosynthesis GTPase FlhF [Cell motility];


Pssm-ID: 441029 [Multi-domain]  Cd Length: 361  Bit Score: 41.39  E-value: 1.06e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 30681303 207 RDLIEGGGSILVIGSPGVGKTTLIREIARMLADEHRKRVVIV--DT 250
Cdd:COG1419 158 DPLLDEGGVIALVGPTGVGKTTTIAKLAARFVLRGKKKVALIttDT 203
TrwB_TraG_TraD_VirD4 cd01127
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are ...
 216-343 1.27e-03

TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are bacterial conjugation proteins involved in type IV secretion (T4S) systems, versatile bacterial secretion systems mediating transport of protein and/or DNA. They are present in gram-negative and gram-positive bacteria, as well as archaea. They form hexameric rings and belong to the RecA-like NTPases superfamily, which also includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases.


Pssm-ID: 410871 [Multi-domain]  Cd Length: 144  Bit Score: 39.51  E-value: 1.27e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681303 216 ILVIGSPGVGKTTLIREIARMLAdEHRKRVVIVDTSNE---IGGDGDVPHSGIGRARRMQVPNVNLQHDVMIEAVENHmP 292
Cdd:cd01127   2 TLVLGTTGSGKTTSIVIPLLDQA-ARGGSVIITDPKGElflVIPDRDDSFAALRALFFNQLFRALTELASLSPGRLPR-R 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30681303 293 ETIIIDEIGT-----ELEALAA---------STIAQRGVQLVATAHGMTIDNIIKNPSLQILIGG 343
Cdd:cd01127  80 VWFILDEFANlgripNLPNLLAtgrkrgisvVLILQSLAQLEAVYGKDGAQTILGNCNTKLYLGT 144
HypB COG0378
Hydrogenase/urease maturation factor HypB, Ni2+-binding GTPase [Posttranslational modification, ...
 203-242 1.42e-03

Hydrogenase/urease maturation factor HypB, Ni2+-binding GTPase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440147 [Multi-domain]  Cd Length: 200  Bit Score: 40.04  E-value: 1.42e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 30681303 203 AEIIRDLIEGGG--SILVIGSPGVGKTTLIREIARMLADEHR 242
Cdd:COG0378   1 AAENRALFAEKGvlAVNLMGSPGSGKTTLLEKTIRALKDRLR 42
DEXSc_Pif1_like cd18037
DEAD-box helicase domain of Pif1; Pif1 and other members of this family are RecD-like ...
 208-300 2.74e-03

DEAD-box helicase domain of Pif1; Pif1 and other members of this family are RecD-like helicases involved in maintaining genome stability through unwinding double-stranded DNAs (dsDNAs), DNA/RNA hybrids, and G quadruplex (G4) structures. The members of Pif1 helicase subfamily studied so far all appear to contribute to telomere maintenance. Pif1 is a member of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350795 [Multi-domain]  Cd Length: 183  Bit Score: 39.15  E-value: 2.74e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681303 208 DLIEGGGSILVIGSPGVGKTTLIREIARMLAdEHRKRVVIVDT----SNEIGgdGDVPHS--GIGrarRMQVPNVNLQHD 281
Cdd:cd18037   7 DLVLDGKNVFFTGSAGTGKSYLLRRIIRALP-SRPKRVAVTAStgiaACNIG--GTTLHSfaGIG---LGSEPAEDLLER 80

                        90       100
                ....*....|....*....|..
gi 30681303 282 VMIE-AVENH--MPETIIIDEI 300
Cdd:cd18037  81 VKRSpYLVQRwrKCDVLIIDEI 102
flhF PRK05703
flagellar biosynthesis protein FlhF;
208-250 3.17e-03

flagellar biosynthesis protein FlhF;


Pssm-ID: 235570 [Multi-domain]  Cd Length: 424  Bit Score: 40.26  E-value: 3.17e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 30681303  208 DLIEGGGSILVIGSPGVGKTTLIREIA-RMLADEHRKRVVIV--DT 250
Cdd:PRK05703 216 DILKQGGVVALVGPTGVGKTTTLAKLAaRYALLYGKKKVALItlDT 261
PRK06835 PRK06835
DNA replication protein DnaC; Validated
 204-304 3.43e-03

DNA replication protein DnaC; Validated


Pssm-ID: 235871 [Multi-domain]  Cd Length: 329  Bit Score: 39.88  E-value: 3.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681303  204 EIIRDLIEG----GGSILVIGSPGVGKTTLIREIARMLADehRKRVVIVDTSNEIggdgdvphSGIGRARRMQvPNVNLQ 279
Cdd:PRK06835 170 EKCKNFIENfdknNENLLFYGNTGTGKTFLSNCIAKELLD--RGKSVIYRTADEL--------IEILREIRFN-NDKELE 238

                         90       100
                 ....*....|....*....|....*..
gi 30681303  280 --HDVMIEAvenhmpETIIIDEIGTEL 304
Cdd:PRK06835 239 evYDLLINC------DLLIIDDLGTEK 259
AAA_24 pfam13479
AAA domain; This AAA domain is found in a wide variety of presumed phage proteins.
 215-308 3.77e-03

AAA domain; This AAA domain is found in a wide variety of presumed phage proteins.


Pssm-ID: 433243  Cd Length: 199  Bit Score: 38.85  E-value: 3.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681303   215 SILVIGSPGVGKTTLIREIarmladehrKRVVIVDTSneiGGDGDVphsgigRARRMQVPNVNLQHDVMIEAV------E 288
Cdd:pfam13479   4 KILIYGPSGIGKTTFAKTL---------PKPLFLDTE---KGSKAL------DGDRFPDIVIRDSWQDFLDAIdeltaaE 65

                          90       100
                  ....*....|....*....|
gi 30681303   289 NHMPETIIIDEIgTELEALA 308
Cdd:pfam13479  66 LADYKTIVIDTV-DWLERLC 84
RepA COG3598
RecA-family ATPase [Replication, recombination and repair];
205-298 3.85e-03

RecA-family ATPase [Replication, recombination and repair];


Pssm-ID: 442817 [Multi-domain]  Cd Length: 313  Bit Score: 39.50  E-value: 3.85e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681303 205 IIRDLIEGGGSILVIGSPGVGKTTLIREIARMLA--------DEHRKRVVIVDT----------SNEIGGDGDVPHSGIG 266
Cdd:COG3598   5 LVPGLLPEGGVTLLAGPPGTGKSFLALQLAAAVAaggpwlgrRVPPGKVLYLAAeddrgelrrrLKALGADLGLPFADLD 84

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 30681303 267 RARRMQVPNVNLQH----DVMIEAVENHMPETIIID 298
Cdd:COG3598  85 GRLRLLSLAGDLDDtddlEALERAIEEEGPDLVVID 120
MMAA-like cd03114
methylmalonic aciduria associated protein; Methylmalonyl Co-A mutase-associated GTPase MeaB ...
 202-256 5.24e-03

methylmalonic aciduria associated protein; Methylmalonyl Co-A mutase-associated GTPase MeaB and its human homolog, methylmalonic aciduria associated protein (MMAA) are metallochaperones that function as a G-protein chaperone that assists AdoCbl cofactor delivery to the methylmalonyl-CoA mutase (MCM) and reactivation of the enzyme during catalysis. A member of the family, Escherichia coli ArgK, was previously thought to be a membrane ATPase which is required for transporting arginine, ornithine and lysine into the cells by the arginine and ornithine (AO system) and lysine, arginine and ornithine (LAO) transport systems.


Pssm-ID: 349768  Cd Length: 252  Bit Score: 38.71  E-value: 5.24e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 30681303 202 SAEIIRDLIEGGGSILVI---GSPGVGKTTLIREIARML-ADEHRKRVVIVDTSNEIGG 256
Cdd:cd03114  32 AQELLDALLPQAGRAFRVgitGPPGAGKSTLIEALGRLLrEQGHRVAVLAVDPSSPRSG 90
VirB11-like_ATPase cd01130
Type IV secretory pathway component VirB11-like; Type IV secretory pathway component VirB11, ...
 203-254 5.37e-03

Type IV secretory pathway component VirB11-like; Type IV secretory pathway component VirB11, and related ATPases. The homohexamer, VirB11 is one of eleven Vir (virulence) proteins, which are required for T-pilus biogenesis and virulence in the transfer of T-DNA from the bacterial Ti (tumor-inducing)-plasmid into plant cells. The pilus is a fibrous cell surface organelle, which mediates adhesion between bacteria during conjugative transfer or between bacteria and host eukaryotic cells during infection. VirB11-related ATPases include Sulfolobus acidocaldarius FlaI, which plays key roles in archaellum (archaeal flagellum) assembly and motility functions, and the pilus assembly proteins CpaF/TadA and TrbB. This alignment contains the C-terminal domain, which is the ATPase.


Pssm-ID: 410874 [Multi-domain]  Cd Length: 177  Bit Score: 37.90  E-value: 5.37e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 30681303 203 AEIIRDLIEGGGSILVIGSPGVGKTTLIreiaRMLADE--HRKRVVIVDTSNEI 254
Cdd:cd01130   2 AAFLRLAVRARKNILISGGTGSGKTTLL----NALLSFipPDERIVTIEDTREL 51
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 90-249 5.55e-03

Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 443989 [Multi-domain]  Cd Length: 358  Bit Score: 39.33  E-value: 5.55e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681303  90 TAPPTVELDAFLEILPPATRKELVKHEAIEELIEVVMDLGRKPLARFPSGDWVISEQPVTHQDLELAVSKvGDFSDDNRS 169
Cdd:COG4963   6 RPLPRISIQAFCESAALAALIEAAAEDRRLALAAVAVASGGAAAAAAAYLSAPTPNLILLEALSESAALL-ADVLPLSPD 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681303 170 GIDRSLHRISAIRNRklqvigltcRVGRVVSgsaeiirdliegggsilVIG-SPGVGKTTLIREIARMLADEHRKRVVIV 248
Cdd:COG4963  85 ELRAALARLLDPGAA---------RRGRVIA-----------------VVGaKGGVGATTLAVNLAWALARESGRRVLLV 138


                .
gi 30681303 249 D 249
Cdd:COG4963 139 D 139
flhF PRK14723
flagellar biosynthesis regulator FlhF; Provisional
 208-332 6.12e-03

flagellar biosynthesis regulator FlhF; Provisional


Pssm-ID: 237802 [Multi-domain]  Cd Length: 767  Bit Score: 39.40  E-value: 6.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681303  208 DLIEGGGSILVIGSPGVGK-TTLIREIARMLADEHRKRVVIVDTSN-EIGGDGDVPHSGigraRRMQVP-----NVNLQH 280
Cdd:PRK14723 180 ALLAQGGVLALVGPTGVGKtTTTAKLAARCVAREGADQLALLTTDSfRIGALEQLRIYG----RILGVPvhavkDAADLR 255

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30681303  281 DVMIEAVENHMpetIIIDEIG--------TELEALAAStiAQRGVQ----LVATAHGMTIDNII 332
Cdd:PRK14723 256 FALAALGDKHL---VLIDTVGmsqrdrnvSEQIAMLCG--VGRPVRrlllLNAASHGDTLNEVV 314
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
 184-241 6.73e-03

AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.


Pssm-ID: 433025 [Multi-domain]  Cd Length: 167  Bit Score: 37.48  E-value: 6.73e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 30681303   184 RKLQVIGLTCRVGRVVSGSaeiirdliegGGSILVIGSPGVGKTTLIREIARMLADEH 241
Cdd:pfam13191   5 REEELEQLLDALDRVRSGR----------PPSVLLTGEAGTGKTTLLRELLRALERDG 52
VirB11 COG0630
Type IV secretory pathway ATPase VirB11/Archaellum biosynthesis ATPase ArlI/FlaI [Cell ...
 209-325 7.21e-03

Type IV secretory pathway ATPase VirB11/Archaellum biosynthesis ATPase ArlI/FlaI [Cell motility, Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 440395 [Multi-domain]  Cd Length: 462  Bit Score: 38.91  E-value: 7.21e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681303 209 LIEGGGSILVIGSPGVGKTTLIREIArMLADEHRKRVVIVDTSnEIggdgDVPH----SGIGR-ARRMQVPNVNLQhDVM 283
Cdd:COG0630 286 LLENGKSVLVAGGTASGKTTLLNALL-SFIPPDAKIVTIEDTR-EL----NLPHenwiSLVTReSFGGEEGDVTMF-DLL 358

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 30681303 284 IEAVEnHMPETIIIDEIGTElEALAAstiaqrgVQLVATAHG 325
Cdd:COG0630 359 KAALR-QRPDYIVVGEVRGE-EAYTL-------FQAMATGHG 391
GPN2 cd17871
GPN-loop GTPase 2; GPN-loop GTPase 2 (GPN2) is a small GTPase required for proper localization ...
 217-253 8.43e-03

GPN-loop GTPase 2; GPN-loop GTPase 2 (GPN2) is a small GTPase required for proper localization of RNA polymerase II and III (RNAPII and RNAPIII). It forms heterodimers with GPN1 or GPN3.


Pssm-ID: 349780  Cd Length: 196  Bit Score: 37.90  E-value: 8.43e-03
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 30681303 217 LVIGSPGVGKTTLIREIARMLADEHRKrVVIV--DTSNE 253
Cdd:cd17871   4 VVIGPPGSGKTTYCKGMQQFLSALGRK-VAVVnlDPANE 41
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 205-237 9.31e-03

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 38.53  E-value: 9.31e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 30681303  205 IIRDLIEGG--GSILVIGSPGVGKTTLIREIARML 237
Cdd:PRK13342  26 PLRRMIEAGrlSSMILWGPPGTGKTTLARIIAGAT 60
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
 214-251 9.52e-03

AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.


Pssm-ID: 400187 [Multi-domain]  Cd Length: 168  Bit Score: 37.17  E-value: 9.52e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 30681303   214 GSILVIGSPGVGKTTLIREIARMLADEhRKRVVIVDTS 251
Cdd:pfam07724   4 GSFLFLGPTGVGKTELAKALAELLFGD-ERALIRIDMS 40
 
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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