|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13531 |
PRK13531 |
regulatory ATPase RavA; Provisional |
1-497 |
0e+00 |
|
regulatory ATPase RavA; Provisional
Pssm-ID: 184118 [Multi-domain] Cd Length: 498 Bit Score: 1009.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012417618 1 MAHSQLLAERIARLSNALEKGLYERHHAIRLCLLAALCGESVFLLGPPGIAKSLIARRLKFAFQHARAFEYLMTRFSTPE 80
Cdd:PRK13531 1 MAHPHLLAERISRLSSALEKGLYERSHAIRLCLLAALSGESVFLLGPPGIAKSLIARRLKFAFQNARAFEYLMTRFSTPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012417618 81 EVFGPLSIQALKDEGRYQRLIKGYLPDAEIVFLDEIWKAGPAILNTLLTAINERRFRNGDSEEKIPMRLLVTASNELPEA 160
Cdd:PRK13531 81 EVFGPLSIQALKDEGRYQRLTSGYLPEAEIVFLDEIWKAGPAILNTLLTAINERRFRNGAHEEKIPMRLLVTASNELPEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012417618 161 DSGLEALYDRMLIRLWLDNVHEKQNFRSLLTHQQDENQNPVAESLCITDEEYLEWQQGISKVSLPDDVFELIFQLRQQLE 240
Cdd:PRK13531 161 DSSLEALYDRMLIRLWLDKVQDKANFRSMLTSQQDENDNPVPASLQITDEEYQQWQKEIGKITLPDHVFELIFQLRQQLD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012417618 241 NQPEAPYISDRRWKKAIHLLQASAFYSGRNAIVPIDLILLKDCLWHDVGSMKLLDHELDNLITQQAWQQQPMLFKLQQIN 320
Cdd:PRK13531 241 ALPNAPYVSDRRWKKAIRLLQASAFFSGRDAIAPIDLILLKDCLWHDAQSLNLLQQQLEQLMTEHAWQQQGMLTRLGAIV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012417618 321 ARRLALQQQQSVEQAIRLEKHGGMFSRKPHYELPESLANDALTLMLQKPLTLHEMQVTHITLAREALHHWLQKGGDVRGK 400
Cdd:PRK13531 321 QRRLQLQQQQSDKTALTVIKQGGMFSRKPHYQLPVNLTASTLTLLLQKPLKLHDMEVNHITFERSALEQWLQKGGEIRGK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012417618 401 LNGIGFAQTLDLHVDGNDCLTLRDVSLQATRLMLPGKPQQGLPEEIVLALDELETQLRGQRTLFSQHHRCLFISDDWLAR 480
Cdd:PRK13531 401 LNGIGFAQKLNLEVDSAQHLVVRDVSLQGSTLALPGSSAEGLPGEIKQQLEELESDWRQQHTLFSEQQPCLFIPSDWLAR 480
|
490
....*....|....*..
gi 1012417618 481 VEESLQQVADQLKQARQ 497
Cdd:PRK13531 481 IEASLQQVGEQIRQAQQ 497
|
|
| bpMoxR |
pfam20030 |
MoxR domain in the MoxR-vWA-beta-propeller ternary systems; Core MoxR component domain of the ... |
9-217 |
6.08e-54 |
|
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: 180.13 E-value: 6.08e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012417618 9 ERIARLSNALEKGLYERHHAIRLCLLAALCGESVFLLGPPGIAKSLIARRLKFAFqHARAFEYLMTRFSTPEEVFGPLSI 88
Cdd:pfam20030 1 RRLREVLRPLKTGFVGKDEIIDLLGLALVARENLFLLGPPGTAKSALVRRLAARL-GGRYFEYLLTRFTEPNELFGPFDI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012417618 89 QALKdEGRYQRLIKGYLPDAEIVFLDEIWKAGPAILNTLLTAINERRFRNGDSEEKIPMRLLVTASNELPEaDSGLEALY 168
Cdd:pfam20030 80 RKLR-EGELVTNTEGMLPEASLVFLDELFNANSAILNSLLMVLNERIFRRGKETRKLPALMFVGASNHLPE-DEALAALF 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1012417618 169 DRMLIRLWLDNVHEKQNFRSLLTHQQDEnQNPVAESLCITDEEYLEWQQ 217
Cdd:pfam20030 158 DRFLLRVKCDNVPPDQLEAVLAAGWKLE-RRPVTTRPSIAAAEIRELQQ 205
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
12-286 |
1.36e-12 |
|
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: 68.27 E-value: 1.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012417618 12 ARLSNALEKGLYERHHAIRLCLLAALCGESVFLLGPPGIAKSLIARRLkfafqhARAFEYLMTRF-----STPEEVFGpL 86
Cdd:COG0714 4 ARLRAEIGKVYVGQEELIELVLIALLAGGHLLLEGVPGVGKTTLAKAL------ARALGLPFIRIqftpdLLPSDILG-T 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012417618 87 SIqALKDEGRyQRLIKGYLPdAEIVFLDEIWKAGPAILNTLLTAINERRFRNGDSEEKIPMRLLVTA-SN--------EL 157
Cdd:COG0714 77 YI-YDQQTGE-FEFRPGPLF-ANVLLADEINRAPPKTQSALLEAMEERQVTIPGGTYKLPEPFLVIAtQNpieqegtyPL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012417618 158 PeadsglEALYDRMLIRLWLDnVHEKQNFRSLLTHQQDENQNPVAEslCITDEEYLEWQQGISKVSLPDDVFELIFQLRQ 237
Cdd:COG0714 154 P------EAQLDRFLLKLYIG-YPDAEEEREILRRHTGRHLAEVEP--VLSPEELLALQELVRQVHVSEAVLDYIVDLVR 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1012417618 238 QLENQPEAPY-ISDRRWKKAIHLLQASAFYSGRNAIVPIDLI-LLKDCLWH 286
Cdd:COG0714 225 ATREHPDLRKgPSPRASIALLRAARALALLDGRDYVTPDDVKaVAGPVLKH 275
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
23-175 |
1.29e-06 |
|
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: 47.91 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012417618 23 YERHHAIRLcLLAALCGES---VFLLGPPGIAKSLIARRL-KFAFQHARAFEYL-MTRFSTPEEVfgplsiqALKDEGRY 97
Cdd:cd00009 1 VGQEEAIEA-LREALELPPpknLLLYGPPGTGKTTLARAIaNELFRPGAPFLYLnASDLLEGLVV-------AELFGHFL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012417618 98 QRLIKGYLPDAE--IVFLDEIWKAGPAILNTLLTAINERRFRNGDSEEkipmRLLVTASNElPEADSGLEALYDRMLIRL 175
Cdd:cd00009 73 VRLLFELAEKAKpgVLFIDEIDSLSRGAQNALLRVLETLNDLRIDREN----VRVIGATNR-PLLGDLDRALYDRLDIRI 147
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13531 |
PRK13531 |
regulatory ATPase RavA; Provisional |
1-497 |
0e+00 |
|
regulatory ATPase RavA; Provisional
Pssm-ID: 184118 [Multi-domain] Cd Length: 498 Bit Score: 1009.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012417618 1 MAHSQLLAERIARLSNALEKGLYERHHAIRLCLLAALCGESVFLLGPPGIAKSLIARRLKFAFQHARAFEYLMTRFSTPE 80
Cdd:PRK13531 1 MAHPHLLAERISRLSSALEKGLYERSHAIRLCLLAALSGESVFLLGPPGIAKSLIARRLKFAFQNARAFEYLMTRFSTPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012417618 81 EVFGPLSIQALKDEGRYQRLIKGYLPDAEIVFLDEIWKAGPAILNTLLTAINERRFRNGDSEEKIPMRLLVTASNELPEA 160
Cdd:PRK13531 81 EVFGPLSIQALKDEGRYQRLTSGYLPEAEIVFLDEIWKAGPAILNTLLTAINERRFRNGAHEEKIPMRLLVTASNELPEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012417618 161 DSGLEALYDRMLIRLWLDNVHEKQNFRSLLTHQQDENQNPVAESLCITDEEYLEWQQGISKVSLPDDVFELIFQLRQQLE 240
Cdd:PRK13531 161 DSSLEALYDRMLIRLWLDKVQDKANFRSMLTSQQDENDNPVPASLQITDEEYQQWQKEIGKITLPDHVFELIFQLRQQLD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012417618 241 NQPEAPYISDRRWKKAIHLLQASAFYSGRNAIVPIDLILLKDCLWHDVGSMKLLDHELDNLITQQAWQQQPMLFKLQQIN 320
Cdd:PRK13531 241 ALPNAPYVSDRRWKKAIRLLQASAFFSGRDAIAPIDLILLKDCLWHDAQSLNLLQQQLEQLMTEHAWQQQGMLTRLGAIV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012417618 321 ARRLALQQQQSVEQAIRLEKHGGMFSRKPHYELPESLANDALTLMLQKPLTLHEMQVTHITLAREALHHWLQKGGDVRGK 400
Cdd:PRK13531 321 QRRLQLQQQQSDKTALTVIKQGGMFSRKPHYQLPVNLTASTLTLLLQKPLKLHDMEVNHITFERSALEQWLQKGGEIRGK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012417618 401 LNGIGFAQTLDLHVDGNDCLTLRDVSLQATRLMLPGKPQQGLPEEIVLALDELETQLRGQRTLFSQHHRCLFISDDWLAR 480
Cdd:PRK13531 401 LNGIGFAQKLNLEVDSAQHLVVRDVSLQGSTLALPGSSAEGLPGEIKQQLEELESDWRQQHTLFSEQQPCLFIPSDWLAR 480
|
490
....*....|....*..
gi 1012417618 481 VEESLQQVADQLKQARQ 497
Cdd:PRK13531 481 IEASLQQVGEQIRQAQQ 497
|
|
| bpMoxR |
pfam20030 |
MoxR domain in the MoxR-vWA-beta-propeller ternary systems; Core MoxR component domain of the ... |
9-217 |
6.08e-54 |
|
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: 180.13 E-value: 6.08e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012417618 9 ERIARLSNALEKGLYERHHAIRLCLLAALCGESVFLLGPPGIAKSLIARRLKFAFqHARAFEYLMTRFSTPEEVFGPLSI 88
Cdd:pfam20030 1 RRLREVLRPLKTGFVGKDEIIDLLGLALVARENLFLLGPPGTAKSALVRRLAARL-GGRYFEYLLTRFTEPNELFGPFDI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012417618 89 QALKdEGRYQRLIKGYLPDAEIVFLDEIWKAGPAILNTLLTAINERRFRNGDSEEKIPMRLLVTASNELPEaDSGLEALY 168
Cdd:pfam20030 80 RKLR-EGELVTNTEGMLPEASLVFLDELFNANSAILNSLLMVLNERIFRRGKETRKLPALMFVGASNHLPE-DEALAALF 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1012417618 169 DRMLIRLWLDNVHEKQNFRSLLTHQQDEnQNPVAESLCITDEEYLEWQQ 217
Cdd:pfam20030 158 DRFLLRVKCDNVPPDQLEAVLAAGWKLE-RRPVTTRPSIAAAEIRELQQ 205
|
|
| LARA_dom |
pfam20265 |
ATPase, RavA, LARA domain; This is the LARA (LdcI Associating domain of RavA) domain of ... |
334-437 |
7.95e-39 |
|
ATPase, RavA, LARA domain; This is the LARA (LdcI Associating domain of RavA) domain of bacterial regulatory ATPase RavA (Regulatory ATPase variant A). It adopts an unique fold which consists of a compact antiparallel beta-barrel- like structure formed by six beta-strands and one alpha-helix. This domain mediates the interaction between RavA and LdcI (inducible lysine decarboxylase) which form a cage-like complex proposed to assist assembly of specific respiratory complexes in E. coli.
Pssm-ID: 466415 Cd Length: 104 Bit Score: 136.66 E-value: 7.95e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012417618 334 QAIRLEKHGGMFSRKPHYELPESLANDALTLMLQKPLTLHEMQVTHITLAREALHHWLQKGGDVRGKLNGIGFAQTLDLH 413
Cdd:pfam20265 1 QALDVEKAKGLFGRKPQYSLPDNLTLEKLTLLLQSPLSLHDIEVRHVYVERDELEKWLNKGGEIYGKLNGIGFLQRLDFE 80
|
90 100
....*....|....*....|....
gi 1012417618 414 VDGNDCLTLRDVSLQATRLMLPGK 437
Cdd:pfam20265 81 VDAQNQLVIRDISNRSSLLALPGK 104
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
41-171 |
2.05e-29 |
|
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: 112.39 E-value: 2.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012417618 41 SVFLLGPPGIAKSLIARRLKFAFQHARAFEYLMTRFSTPEEVFGPLSIQALKDEGRYQRLIKGYLPdAEIVFLDEIWKAG 120
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSNRPVFYVQLTRDTTEEDLFGRRNIDPGGASWVDGPLVRAARE-GEIAVLDEINRAN 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1012417618 121 PAILNTLLTAINERRFR--NGDSEEKIPM--RLLVTASNELP-EADSGLEALYDRM 171
Cdd:pfam07728 80 PDVLNSLLSLLDERRLLlpDGGELVKAAPdgFRLIATMNPLDrGLNELSPALRSRF 135
|
|
| AAA_lid_8 |
pfam17868 |
AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ... |
227-285 |
3.93e-18 |
|
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: 78.38 E-value: 3.93e-18
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1012417618 227 DVFELIFQLRQQLENQPEAPYISDRRWKKAIHLLQASAFYSGRNAIVPIDLILLKDCLW 285
Cdd:pfam17868 1 EVIDLIYDIRNKLDEEEENIYVSDRRWKKIVKLLKASAYLNGRDEVNLSDLLLLKHCLW 59
|
|
| ATPase_RavA_C |
pfam12592 |
ATPase, RavA, C-terminal; This domain is found at the C-terminal of bacterial regulatory ... |
443-497 |
1.93e-15 |
|
ATPase, RavA, C-terminal; This domain is found at the C-terminal of bacterial regulatory ATPase RavA (Regulatory ATPase variant A) and is the second subdomain that forms the discontinuous triple helical domain. RavA forms an hexamer in which the triple helical domain mediates the lateral interactions between neighbouring RavA monomers.
Pssm-ID: 432657 Cd Length: 55 Bit Score: 70.44 E-value: 1.93e-15
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1012417618 443 PEEIVLALDELETQLRGQRTLFSQHHRCLFISDDWLARVEESLQQVADQLKQARQ 497
Cdd:pfam12592 1 PEEWLEQLEALEQELRQQRRLFHQHQPHLFIEPEWLARIEASLQQVTEQLEQLQQ 55
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
12-286 |
1.36e-12 |
|
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: 68.27 E-value: 1.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012417618 12 ARLSNALEKGLYERHHAIRLCLLAALCGESVFLLGPPGIAKSLIARRLkfafqhARAFEYLMTRF-----STPEEVFGpL 86
Cdd:COG0714 4 ARLRAEIGKVYVGQEELIELVLIALLAGGHLLLEGVPGVGKTTLAKAL------ARALGLPFIRIqftpdLLPSDILG-T 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012417618 87 SIqALKDEGRyQRLIKGYLPdAEIVFLDEIWKAGPAILNTLLTAINERRFRNGDSEEKIPMRLLVTA-SN--------EL 157
Cdd:COG0714 77 YI-YDQQTGE-FEFRPGPLF-ANVLLADEINRAPPKTQSALLEAMEERQVTIPGGTYKLPEPFLVIAtQNpieqegtyPL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012417618 158 PeadsglEALYDRMLIRLWLDnVHEKQNFRSLLTHQQDENQNPVAEslCITDEEYLEWQQGISKVSLPDDVFELIFQLRQ 237
Cdd:COG0714 154 P------EAQLDRFLLKLYIG-YPDAEEEREILRRHTGRHLAEVEP--VLSPEELLALQELVRQVHVSEAVLDYIVDLVR 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1012417618 238 QLENQPEAPY-ISDRRWKKAIHLLQASAFYSGRNAIVPIDLI-LLKDCLWH 286
Cdd:COG0714 225 ATREHPDLRKgPSPRASIALLRAARALALLDGRDYVTPDDVKaVAGPVLKH 275
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
23-175 |
1.29e-06 |
|
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: 47.91 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012417618 23 YERHHAIRLcLLAALCGES---VFLLGPPGIAKSLIARRL-KFAFQHARAFEYL-MTRFSTPEEVfgplsiqALKDEGRY 97
Cdd:cd00009 1 VGQEEAIEA-LREALELPPpknLLLYGPPGTGKTTLARAIaNELFRPGAPFLYLnASDLLEGLVV-------AELFGHFL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012417618 98 QRLIKGYLPDAE--IVFLDEIWKAGPAILNTLLTAINERRFRNGDSEEkipmRLLVTASNElPEADSGLEALYDRMLIRL 175
Cdd:cd00009 73 VRLLFELAEKAKpgVLFIDEIDSLSRGAQNALLRVLETLNDLRIDREN----VRVIGATNR-PLLGDLDRALYDRLDIRI 147
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
18-159 |
2.94e-04 |
|
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and eukaryotic Heat shock protein 104 (Hsp104) are ATP-dependent molecular chaperones and essential proteins of the heat-shock response. ClpB/Hsp104 ATPases, in concert with the DnaK/Hsp70 chaperone system, disaggregate and reactivate aggregated proteins. This RecA-like_ClpB_Hsp104_like subfamily belongs to the RecA-like NTPase family 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: 410907 [Multi-domain] Cd Length: 178 Bit Score: 41.78 E-value: 2.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012417618 18 LEKGLYER----HHAIRLcLLAALCGE-----------SVFL-LGPPGIAKSLIARRL-KFAFQHARAFEYL-MTRFSTP 79
Cdd:cd19499 5 LEERLHERvvgqDEAVKA-VSDAIRRAraglsdpnrpiGSFLfLGPTGVGKTELAKALaELLFGDEDNLIRIdMSEYMEK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012417618 80 EEV---FGPLSIQALKDEGryqrlikGYLPDA------EIVFLDEIWKAGPAILNTLLTAINERRFRngDSEEK-IPMR- 148
Cdd:cd19499 84 HSVsrlIGAPPGYVGYTEG-------GQLTEAvrrkpySVVLLDEIEKAHPDVQNLLLQVLDDGRLT--DSHGRtVDFKn 154
|
170
....*....|...
gi 1012417618 149 --LLVTASNELPE 159
Cdd:cd19499 155 tiIIMTSNHFRPE 167
|
|
| Mg_chelatase |
pfam01078 |
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ... |
27-59 |
7.45e-04 |
|
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that catalyzes the insertion of Mg2+ into protoporphyrin IX. This is the first unique step in the synthesis of (bacterio)chlorophyll. Due to this, it is thought that Mg-chelatase has an important role in channelling inter- mediates into the (bacterio)chlorophyll branch in response to conditions suitable for photosynthetic growth. ChlI and BchD have molecular weight between 38-42 kDa.
Pssm-ID: 426032 [Multi-domain] Cd Length: 207 Bit Score: 40.98 E-value: 7.45e-04
10 20 30
....*....|....*....|....*....|...
gi 1012417618 27 HAIRLCLLAALCGESVFLLGPPGIAKSLIARRL 59
Cdd:pfam01078 10 QAKRALEIAAAGGHNLLMIGPPGSGKTMLAKRL 42
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| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
42-178 |
8.89e-03 |
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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: 36.42 E-value: 8.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012417618 42 VFLLGPPGIAKSLIARRLkfafqhARAFEYLMTRFSTPEEVfgplsiqaLKDEGRYQRLIKGYLPDAE-----IVFLDEI 116
Cdd:pfam00004 1 LLLYGPPGTGKTTLAKAV------AKELGAPFIEISGSELV--------SKYVGESEKRLRELFEAAKklapcVIFIDEI 66
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90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1012417618 117 WKAGPA-----------ILNTLLTAINerrfrngDSEEKIPMRLLVTASNELPEADsglEALYDRMLIRLWLD 178
Cdd:pfam00004 67 DALAGSrgsggdsesrrVVNQLLTELD-------GFTSSNSKVIVIAATNRPDKLD---PALLGRFDRIIEFP 129
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