|
Name |
Accession |
Description |
Interval |
E-value |
| bpMoxR |
pfam20030 |
MoxR domain in the MoxR-vWA-beta-propeller ternary systems; Core MoxR component domain of the ... |
12-216 |
3.10e-132 |
|
MoxR domain in the MoxR-vWA-beta-propeller ternary systems; Core MoxR component domain of the MoxR-vWA-beta-propeller ternary systems, a class of NTP-dependent biological conflict systems.
Pssm-ID: 437862 [Multi-domain] Cd Length: 205 Bit Score: 376.97 E-value: 3.10e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100053960 12 DKLNDVLQRMKRTFVGKDDIIDLMGICLAGRENLFLFGPPGTAKSALVRELARQLDLKTFEYLLTRFTEPNELFGPFDIR 91
Cdd:pfam20030 1 RRLREVLRPLKTGFVGKDEIIDLLGLALVARENLFLLGPPGTAKSALVRRLAARLGGRYFEYLLTRFTEPNELFGPFDIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100053960 92 KLRDGDLVTNTEGMLPEASLVFLDELLNANSAILNSLLMALNEKIFRRGKETRILPVLTFIGASNHLPEDEALQALFDRF 171
Cdd:pfam20030 81 KLREGELVTNTEGMLPEASLVFLDELFNANSAILNSLLMVLNERIFRRGKETRKLPALMFVGASNHLPEDEALAALFDRF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1100053960 172 LIRVRCSNVDPVMLDSVLQAGWGLEQQTEQIREGIAADELRALQQ 216
Cdd:pfam20030 161 LLRVKCDNVPPDQLEAVLAAGWKLERRPVTTRPSIAAAEIRELQQ 205
|
|
| PRK13531 |
PRK13531 |
regulatory ATPase RavA; Provisional |
43-280 |
1.67e-42 |
|
regulatory ATPase RavA; Provisional
Pssm-ID: 184118 [Multi-domain] Cd Length: 498 Bit Score: 155.17 E-value: 1.67e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100053960 43 ENLFLFGPPGTAKSALVREL--ARQlDLKTFEYLLTRFTEPNELFGPFDIRKLRD-GDLVTNTEGMLPEASLVFLDELLN 119
Cdd:PRK13531 40 ESVFLLGPPGIAKSLIARRLkfAFQ-NARAFEYLMTRFSTPEEVFGPLSIQALKDeGRYQRLTSGYLPEAEIVFLDEIWK 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100053960 120 ANSAILNSLLMALNEKIFRRGKETRILPVLTFIGASNHLPE-DEALQALFDRFLIRVRCSNV-DPVMLDSVLqagwgLEQ 197
Cdd:PRK13531 119 AGPAILNTLLTAINERRFRNGAHEEKIPMRLLVTASNELPEaDSSLEALYDRMLIRLWLDKVqDKANFRSML-----TSQ 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100053960 198 QTEQ---IREG--IAADELRALQQLNTTIDLNDVRPEyisLIQQLRN------AGVQISDRRAVKLQRLIAASALLCKRD 266
Cdd:PRK13531 194 QDENdnpVPASlqITDEEYQQWQKEIGKITLPDHVFE---LIFQLRQqldalpNAPYVSDRRWKKAIRLLQASAFFSGRD 270
|
250
....*....|....*
gi 1100053960 267 KALLSDLWILRY-IW 280
Cdd:PRK13531 271 AIAPIDLILLKDcLW 285
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
15-273 |
3.96e-14 |
|
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: 72.12 E-value: 3.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100053960 15 NDVLQRMKRTFVGKDDIIDLMGICLAGRENLFLFGPPGTAKSALVRELARQLDLKtfeylLTR--FTE------------ 80
Cdd:COG0714 4 ARLRAEIGKVYVGQEELIELVLIALLAGGHLLLEGVPGVGKTTLAKALARALGLP-----FIRiqFTPdllpsdilgtyi 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100053960 81 PNELFGPFDIRKlrdGDLVTNtegmlpeasLVFLDELLNANSAILNSLLMALNEKIFRRGKETRILPVLTF-IGASN--- 156
Cdd:COG0714 79 YDQQTGEFEFRP---GPLFAN---------VLLADEINRAPPKTQSALLEAMEERQVTIPGGTYKLPEPFLvIATQNpie 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100053960 157 -----HLPEdealqALFDRFLIRVRCSNVDPVMLDSVLQAGWGleQQTEQIREGIAADELRALQQLNTTIDLNDVRPEYI 231
Cdd:COG0714 147 qegtyPLPE-----AQLDRFLLKLYIGYPDAEEEREILRRHTG--RHLAEVEPVLSPEELLALQELVRQVHVSEAVLDYI 219
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1100053960 232 -SLIQQLRN-AGVQI--SDRRAVKLQRLIAASALLCKRDKALLSDL 273
Cdd:COG0714 220 vDLVRATREhPDLRKgpSPRASIALLRAARALALLDGRDYVTPDDV 265
|
|
| AAA_lid_8 |
pfam17868 |
AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ... |
231-293 |
5.34e-11 |
|
AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains.
Pssm-ID: 465541 Cd Length: 72 Bit Score: 57.96 E-value: 5.34e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100053960 231 ISLIQQLRN------AGVQISDRRAVKLQRLIAASALLCKRDKALLSDLWILRY-IWDTEEQIEIIAGIV 293
Cdd:pfam17868 3 IDLIYDIRNkldeeeENIYVSDRRWKKIVKLLKASAYLNGRDEVNLSDLLLLKHcLWNKPEDREKVRKII 72
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
37-176 |
6.66e-11 |
|
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: 60.24 E-value: 6.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100053960 37 ICLAGRENLFLFGPPGTAKSALVRELARQLDLKTFEYLLTRFTepnELFGPFDIRKLRDGDLVTNTEGMLPEA--SLVFL 114
Cdd:cd00009 14 LELPPPKNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNAS---DLLEGLVVAELFGHFLVRLLFELAEKAkpGVLFI 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1100053960 115 DELLNANSAILNSLLMALNEKIFRRGKETRILpvltFIGASNHLPEDEALQALFDRFLIRVR 176
Cdd:cd00009 91 DEIDSLSRGAQNALLRVLETLNDLRIDRENVR----VIGATNRPLLGDLDRALYDRLDIRIV 148
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
42-170 |
4.21e-06 |
|
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: 46.21 E-value: 4.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100053960 42 RENLFLFGPPGTAKSALVRELARQLDLKTFEYLLTRfTEPNELFGPFDIRKLRDGDLVTNTEGML-----------PEAS 110
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYID-GEDILEEVLDQLLLIIVGGKKASGSGELrlrlalalarkLKPD 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1100053960 111 LVFLDELLNANSAILNSLLMALNEkiFRRGKETRILPVLTFIGASNHLPE--DEALQALFDR 170
Cdd:smart00382 81 VLILDEITSLLDAEQEALLLLLEE--LRLLLLLKSEKNLTVILTTNDEKDlgPALLRRRFDR 140
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| bpMoxR |
pfam20030 |
MoxR domain in the MoxR-vWA-beta-propeller ternary systems; Core MoxR component domain of the ... |
12-216 |
3.10e-132 |
|
MoxR domain in the MoxR-vWA-beta-propeller ternary systems; Core MoxR component domain of the MoxR-vWA-beta-propeller ternary systems, a class of NTP-dependent biological conflict systems.
Pssm-ID: 437862 [Multi-domain] Cd Length: 205 Bit Score: 376.97 E-value: 3.10e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100053960 12 DKLNDVLQRMKRTFVGKDDIIDLMGICLAGRENLFLFGPPGTAKSALVRELARQLDLKTFEYLLTRFTEPNELFGPFDIR 91
Cdd:pfam20030 1 RRLREVLRPLKTGFVGKDEIIDLLGLALVARENLFLLGPPGTAKSALVRRLAARLGGRYFEYLLTRFTEPNELFGPFDIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100053960 92 KLRDGDLVTNTEGMLPEASLVFLDELLNANSAILNSLLMALNEKIFRRGKETRILPVLTFIGASNHLPEDEALQALFDRF 171
Cdd:pfam20030 81 KLREGELVTNTEGMLPEASLVFLDELFNANSAILNSLLMVLNERIFRRGKETRKLPALMFVGASNHLPEDEALAALFDRF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1100053960 172 LIRVRCSNVDPVMLDSVLQAGWGLEQQTEQIREGIAADELRALQQ 216
Cdd:pfam20030 161 LLRVKCDNVPPDQLEAVLAAGWKLERRPVTTRPSIAAAEIRELQQ 205
|
|
| PRK13531 |
PRK13531 |
regulatory ATPase RavA; Provisional |
43-280 |
1.67e-42 |
|
regulatory ATPase RavA; Provisional
Pssm-ID: 184118 [Multi-domain] Cd Length: 498 Bit Score: 155.17 E-value: 1.67e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100053960 43 ENLFLFGPPGTAKSALVREL--ARQlDLKTFEYLLTRFTEPNELFGPFDIRKLRD-GDLVTNTEGMLPEASLVFLDELLN 119
Cdd:PRK13531 40 ESVFLLGPPGIAKSLIARRLkfAFQ-NARAFEYLMTRFSTPEEVFGPLSIQALKDeGRYQRLTSGYLPEAEIVFLDEIWK 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100053960 120 ANSAILNSLLMALNEKIFRRGKETRILPVLTFIGASNHLPE-DEALQALFDRFLIRVRCSNV-DPVMLDSVLqagwgLEQ 197
Cdd:PRK13531 119 AGPAILNTLLTAINERRFRNGAHEEKIPMRLLVTASNELPEaDSSLEALYDRMLIRLWLDKVqDKANFRSML-----TSQ 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100053960 198 QTEQ---IREG--IAADELRALQQLNTTIDLNDVRPEyisLIQQLRN------AGVQISDRRAVKLQRLIAASALLCKRD 266
Cdd:PRK13531 194 QDENdnpVPASlqITDEEYQQWQKEIGKITLPDHVFE---LIFQLRQqldalpNAPYVSDRRWKKAIRLLQASAFFSGRD 270
|
250
....*....|....*
gi 1100053960 267 KALLSDLWILRY-IW 280
Cdd:PRK13531 271 AIAPIDLILLKDcLW 285
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
44-171 |
5.62e-25 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 98.52 E-value: 5.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100053960 44 NLFLFGPPGTAKSALVRELARQLD-LKTFEYLLTRFTEPNELFGPFDIR----KLRDGDLVTNTEgmlpEASLVFLDELL 118
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSnRPVFYVQLTRDTTEEDLFGRRNIDpggaSWVDGPLVRAAR----EGEIAVLDEIN 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1100053960 119 NANSAILNSLLMALNEKIFRRGKETRILPV----LTFIGASNHLPED--EALQALFDRF 171
Cdd:pfam07728 77 RANPDVLNSLLSLLDERRLLLPDGGELVKAapdgFRLIATMNPLDRGlnELSPALRSRF 135
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
15-273 |
3.96e-14 |
|
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: 72.12 E-value: 3.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100053960 15 NDVLQRMKRTFVGKDDIIDLMGICLAGRENLFLFGPPGTAKSALVRELARQLDLKtfeylLTR--FTE------------ 80
Cdd:COG0714 4 ARLRAEIGKVYVGQEELIELVLIALLAGGHLLLEGVPGVGKTTLAKALARALGLP-----FIRiqFTPdllpsdilgtyi 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100053960 81 PNELFGPFDIRKlrdGDLVTNtegmlpeasLVFLDELLNANSAILNSLLMALNEKIFRRGKETRILPVLTF-IGASN--- 156
Cdd:COG0714 79 YDQQTGEFEFRP---GPLFAN---------VLLADEINRAPPKTQSALLEAMEERQVTIPGGTYKLPEPFLvIATQNpie 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100053960 157 -----HLPEdealqALFDRFLIRVRCSNVDPVMLDSVLQAGWGleQQTEQIREGIAADELRALQQLNTTIDLNDVRPEYI 231
Cdd:COG0714 147 qegtyPLPE-----AQLDRFLLKLYIGYPDAEEEREILRRHTG--RHLAEVEPVLSPEELLALQELVRQVHVSEAVLDYI 219
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1100053960 232 -SLIQQLRN-AGVQI--SDRRAVKLQRLIAASALLCKRDKALLSDL 273
Cdd:COG0714 220 vDLVRATREhPDLRKgpSPRASIALLRAARALALLDGRDYVTPDDV 265
|
|
| AAA_lid_8 |
pfam17868 |
AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ... |
231-293 |
5.34e-11 |
|
AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains.
Pssm-ID: 465541 Cd Length: 72 Bit Score: 57.96 E-value: 5.34e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100053960 231 ISLIQQLRN------AGVQISDRRAVKLQRLIAASALLCKRDKALLSDLWILRY-IWDTEEQIEIIAGIV 293
Cdd:pfam17868 3 IDLIYDIRNkldeeeENIYVSDRRWKKIVKLLKASAYLNGRDEVNLSDLLLLKHcLWNKPEDREKVRKII 72
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
37-176 |
6.66e-11 |
|
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: 60.24 E-value: 6.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100053960 37 ICLAGRENLFLFGPPGTAKSALVRELARQLDLKTFEYLLTRFTepnELFGPFDIRKLRDGDLVTNTEGMLPEA--SLVFL 114
Cdd:cd00009 14 LELPPPKNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNAS---DLLEGLVVAELFGHFLVRLLFELAEKAkpGVLFI 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1100053960 115 DELLNANSAILNSLLMALNEKIFRRGKETRILpvltFIGASNHLPEDEALQALFDRFLIRVR 176
Cdd:cd00009 91 DEIDSLSRGAQNALLRVLETLNDLRIDRENVR----VIGATNRPLLGDLDRALYDRLDIRIV 148
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
45-172 |
3.46e-07 |
|
ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.
Pssm-ID: 459627 [Multi-domain] Cd Length: 130 Bit Score: 48.74 E-value: 3.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100053960 45 LFLFGPPGTAKSALVRELARQLDLKTFEYLLTRFTEPNELFGPFDIRklrdgDLVTNTEGMLPeaSLVFLDEL----LNA 120
Cdd:pfam00004 1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLR-----ELFEAAKKLAP--CVIFIDEIdalaGSR 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1100053960 121 NSAILNSLLMALNEKIFRRGKETRILPVLTFIGASNHLPE-DEALQALFDRFL 172
Cdd:pfam00004 74 GSGGDSESRRVVNQLLTELDGFTSSNSKVIVIAATNRPDKlDPALLGRFDRII 126
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
42-170 |
4.21e-06 |
|
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: 46.21 E-value: 4.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100053960 42 RENLFLFGPPGTAKSALVRELARQLDLKTFEYLLTRfTEPNELFGPFDIRKLRDGDLVTNTEGML-----------PEAS 110
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYID-GEDILEEVLDQLLLIIVGGKKASGSGELrlrlalalarkLKPD 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1100053960 111 LVFLDELLNANSAILNSLLMALNEkiFRRGKETRILPVLTFIGASNHLPE--DEALQALFDR 170
Cdd:smart00382 81 VLILDEITSLLDAEQEALLLLLEE--LRLLLLLKSEKNLTVILTTNDEKDlgPALLRRRFDR 140
|
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
24-170 |
5.49e-05 |
|
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: 43.26 E-value: 5.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100053960 24 TFVGKDDII----DLMGICLAGR-ENLFLFGPPGTAKSALVRELARQLDLKTFEYLLTRFTEPN------ELFGPFDIRK 92
Cdd:pfam13191 1 RLVGREEELeqllDALDRVRSGRpPSVLLTGEAGTGKTTLLRELLRALERDGGYFLRGKCDENLpyspllEALTREGLLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100053960 93 LRDGDLVTNTEGMLPEASLVFLDELLNANSAILNSLLMALNEKIFRRGKETRilPVLTFIGASNHLPED--EALQALFDR 170
Cdd:pfam13191 81 QLLDELESSLLEAWRAALLEALAPVPELPGDLAERLLDLLLRLLDLLARGER--PLVLVLDDLQWADEAslQLLAALLRL 158
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
44-165 |
2.01e-03 |
|
proteases similar to RecA; 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: 410889 [Multi-domain] Cd Length: 158 Bit Score: 38.42 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100053960 44 NLFLFGPPGTAKSALVRELARQLDLKTFEYLLTRFTEPNELFGPFDIRKLRDGdlvtnTEGMLPeaSLVFLDELlnansa 123
Cdd:cd19481 28 GILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFER-----ARRLAP--CILFIDEI------ 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1100053960 124 ilnsllmalnEKIFRR-------GKETRILPVL-------------TFIGASNHLPE-DEALQ 165
Cdd:cd19481 95 ----------DAIGRKrdssgesGELRRVLNQLlteldgvnsrskvLVIAATNRPDLlDPALL 147
|
|
| AAA_7 |
pfam12775 |
P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 ... |
34-74 |
5.90e-03 |
|
P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. Cytoplasmic dynein-2 (dynein-2) performs intraflagellar transport and is associated with human skeletal ciliopathies. Dyneins share a conserved motor domain that couples cycles of ATP hydrolysis with conformational changes to produce movement. Structural analysis reveal that the motor's ring consists of six AAA+ domains (ATPases associated with various cellular activities (AAA1-AAA6). This is the third nucleotide binding sites in the dynein motor. However, AAA3 has lost the catalytic residues necessary for ATP hydrolysis (the Walker B glutamate, the arginine finger, sensor-I and sensor-II motifs).
Pssm-ID: 463698 [Multi-domain] Cd Length: 179 Bit Score: 37.37 E-value: 5.90e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1100053960 34 LMGICLAGRENLFLFGPPGTAKSALVRELARQLDLKTFEYL 74
Cdd:pfam12775 23 LLDLLLKNGKPVLLVGPTGTGKTVIIQNLLRKLDKEKYLPL 63
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
44-171 |
7.39e-03 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 37.56 E-value: 7.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100053960 44 NLFLFGPPGTAKSALVRELARQLDLktfEYLLTRFTepnELFGPFdirklrDGDLVTNTEGMLPEAS----LVFLDEL-- 117
Cdd:COG1223 37 KILFYGPPGTGKTMLAEALAGELKL---PLLTVRLD---SLIGSY------LGETARNLRKLFDFARrapcVIFFDEFda 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1100053960 118 -------LNAN---SAILNSLLMALNEkiFRRGketrilpVLTfIGASNHLpedEAL-QALFDRF 171
Cdd:COG1223 105 iakdrgdQNDVgevKRVVNALLQELDG--LPSG-------SVV-IAATNHP---ELLdSALWRRF 156
|
|
| |
