|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13531 |
PRK13531 |
regulatory ATPase RavA; Provisional |
1-498 |
0e+00 |
|
regulatory ATPase RavA; Provisional
Pssm-ID: 184118 [Multi-domain] Cd Length: 498 Bit Score: 993.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621035911 1 MAQTHLLAERISRLSAALEKGLFERSHAIRLCLLAALSGESVFLLGPPGIAKSLIARRLKFAFQQARAFEYLMTRFSTPE 80
Cdd:PRK13531 1 MAHPHLLAERISRLSSALEKGLYERSHAIRLCLLAALSGESVFLLGPPGIAKSLIARRLKFAFQNARAFEYLMTRFSTPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621035911 81 EVFGPLSIQALKDEGRYERLTAGYLPEAEIVFLDEIWKAGPAILNTLLTAINERHFRNGAHEEKIPMRLLVAASNELPEA 160
Cdd:PRK13531 81 EVFGPLSIQALKDEGRYQRLTSGYLPEAEIVFLDEIWKAGPAILNTLLTAINERRFRNGAHEEKIPMRLLVTASNELPEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621035911 161 DSSLEALYDRMLIRLWLDKVQDKGNFRSMLVSQQDENINPVPSALQVSDEEFTQWQQQIGNIKLPDAVFELIFQLRQQLD 240
Cdd:PRK13531 161 DSSLEALYDRMLIRLWLDKVQDKANFRSMLTSQQDENDNPVPASLQITDEEYQQWQKEIGKITLPDHVFELIFQLRQQLD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621035911 241 ALPNAPYVSDRRWKKAIRLLQASAFFSGRDSIAPIDLILLKDCLWHNVESMNLMSQQLETLMTCHAWQQQAMLTRLGAIV 320
Cdd:PRK13531 241 ALPNAPYVSDRRWKKAIRLLQASAFFSGRDAIAPIDLILLKDCLWHDAQSLNLLQQQLEQLMTEHAWQQQGMLTRLGAIV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621035911 321 QRRIQIQQQQSDKTALKVTRLGGMFSRKPHYELPAEIQGATLTLLLQQPLKLHDMEVIHITFEREALANWLEKGGEIRGK 400
Cdd:PRK13531 321 QRRLQLQQQQSDKTALTVIKQGGMFSRKPHYQLPVNLTASTLTLLLQKPLKLHDMEVNHITFERSALEQWLQKGGEIRGK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621035911 401 LNGIGFAQLLNMDVDTSQHLVVRDVSLQGSRLALPGSaSQENMPAEIRQQLEALDDEWHQQHNRFSEQQKCLFIPVEWLG 480
Cdd:PRK13531 401 LNGIGFAQKLNLEVDSAQHLVVRDVSLQGSTLALPGS-SAEGLPGEIKQQLEELESDWRQQHTLFSEQQPCLFIPSDWLA 479
|
490
....*....|....*...
gi 1621035911 481 RIEASLQDVGAQIKQAKQ 498
Cdd:PRK13531 480 RIEASLQQVGEQIRQAQQ 497
|
|
| bpMoxR |
pfam20030 |
MoxR domain in the MoxR-vWA-beta-propeller ternary systems; Core MoxR component domain of the ... |
9-182 |
3.23e-57 |
|
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: 188.99 E-value: 3.23e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621035911 9 ERISRLSAALEKGLFERSHAIRLCLLAALSGESVFLLGPPGIAKSLIARRLKFAFQqARAFEYLMTRFSTPEEVFGPLSI 88
Cdd:pfam20030 1 RRLREVLRPLKTGFVGKDEIIDLLGLALVARENLFLLGPPGTAKSALVRRLAARLG-GRYFEYLLTRFTEPNELFGPFDI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621035911 89 QALKdEGRYERLTAGYLPEAEIVFLDEIWKAGPAILNTLLTAINERHFRNGAHEEKIPMRLLVAASNELPEaDSSLEALY 168
Cdd:pfam20030 80 RKLR-EGELVTNTEGMLPEASLVFLDELFNANSAILNSLLMVLNERIFRRGKETRKLPALMFVGASNHLPE-DEALAALF 157
|
170
....*....|....
gi 1621035911 169 DRMLIRLWLDKVQD 182
Cdd:pfam20030 158 DRFLLRVKCDNVPP 171
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
13-288 |
7.62e-15 |
|
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: 74.82 E-value: 7.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621035911 13 RLSAALEKGLFERSHAIRLCLLAALSGESVFLLGPPGIAKSLIARRLkfafqqARAFEYLMTRF-----STPEEVFGpLS 87
Cdd:COG0714 5 RLRAEIGKVYVGQEELIELVLIALLAGGHLLLEGVPGVGKTTLAKAL------ARALGLPFIRIqftpdLLPSDILG-TY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621035911 88 IqALKDEGRyERLTAGYLPeAEIVFLDEIWKAGPAILNTLLTAINERHFRNGAHEEKIPMRLLV-AASN--------ELP 158
Cdd:COG0714 78 I-YDQQTGE-FEFRPGPLF-ANVLLADEINRAPPKTQSALLEAMEERQVTIPGGTYKLPEPFLViATQNpieqegtyPLP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621035911 159 eadsslEALYDRMLIRLWLDkVQDKGNFRSMLVSQQDENINPVPSALqvSDEEFTQWQQQIGNIKLPDAVFELIFQLRQQ 238
Cdd:COG0714 155 ------EAQLDRFLLKLYIG-YPDAEEEREILRRHTGRHLAEVEPVL--SPEELLALQELVRQVHVSEAVLDYIVDLVRA 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1621035911 239 LDALPNAPY-VSDRRWKKAIRLLQASAFFSGRDSIAPIDLI-LLKDCLWHNV 288
Cdd:COG0714 226 TREHPDLRKgPSPRASIALLRAARALALLDGRDYVTPDDVKaVAGPVLKHRL 277
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
23-175 |
1.36e-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: 53.69 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621035911 23 FERSHAIRLCLLAAL--SGESVFLLGPPGIAKSLIARRL--KFAFQQARAFEYLMTRFSTPEEVfgplsiqALKDEGRYE 98
Cdd:cd00009 1 VGQEEAIEALREALElpPPKNLLLYGPPGTGKTTLARAIanELFRPGAPFLYLNASDLLEGLVV-------AELFGHFLV 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1621035911 99 RLTAGYLPEAE--IVFLDEIWKAGPAILNTLLTAINERHFRNGAHEEkipmRLLVAASNElPEADSSLEALYDRMLIRL 175
Cdd:cd00009 74 RLLFELAEKAKpgVLFIDEIDSLSRGAQNALLRVLETLNDLRIDREN----VRVIGATNR-PLLGDLDRALYDRLDIRI 147
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13531 |
PRK13531 |
regulatory ATPase RavA; Provisional |
1-498 |
0e+00 |
|
regulatory ATPase RavA; Provisional
Pssm-ID: 184118 [Multi-domain] Cd Length: 498 Bit Score: 993.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621035911 1 MAQTHLLAERISRLSAALEKGLFERSHAIRLCLLAALSGESVFLLGPPGIAKSLIARRLKFAFQQARAFEYLMTRFSTPE 80
Cdd:PRK13531 1 MAHPHLLAERISRLSSALEKGLYERSHAIRLCLLAALSGESVFLLGPPGIAKSLIARRLKFAFQNARAFEYLMTRFSTPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621035911 81 EVFGPLSIQALKDEGRYERLTAGYLPEAEIVFLDEIWKAGPAILNTLLTAINERHFRNGAHEEKIPMRLLVAASNELPEA 160
Cdd:PRK13531 81 EVFGPLSIQALKDEGRYQRLTSGYLPEAEIVFLDEIWKAGPAILNTLLTAINERRFRNGAHEEKIPMRLLVTASNELPEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621035911 161 DSSLEALYDRMLIRLWLDKVQDKGNFRSMLVSQQDENINPVPSALQVSDEEFTQWQQQIGNIKLPDAVFELIFQLRQQLD 240
Cdd:PRK13531 161 DSSLEALYDRMLIRLWLDKVQDKANFRSMLTSQQDENDNPVPASLQITDEEYQQWQKEIGKITLPDHVFELIFQLRQQLD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621035911 241 ALPNAPYVSDRRWKKAIRLLQASAFFSGRDSIAPIDLILLKDCLWHNVESMNLMSQQLETLMTCHAWQQQAMLTRLGAIV 320
Cdd:PRK13531 241 ALPNAPYVSDRRWKKAIRLLQASAFFSGRDAIAPIDLILLKDCLWHDAQSLNLLQQQLEQLMTEHAWQQQGMLTRLGAIV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621035911 321 QRRIQIQQQQSDKTALKVTRLGGMFSRKPHYELPAEIQGATLTLLLQQPLKLHDMEVIHITFEREALANWLEKGGEIRGK 400
Cdd:PRK13531 321 QRRLQLQQQQSDKTALTVIKQGGMFSRKPHYQLPVNLTASTLTLLLQKPLKLHDMEVNHITFERSALEQWLQKGGEIRGK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621035911 401 LNGIGFAQLLNMDVDTSQHLVVRDVSLQGSRLALPGSaSQENMPAEIRQQLEALDDEWHQQHNRFSEQQKCLFIPVEWLG 480
Cdd:PRK13531 401 LNGIGFAQKLNLEVDSAQHLVVRDVSLQGSTLALPGS-SAEGLPGEIKQQLEELESDWRQQHTLFSEQQPCLFIPSDWLA 479
|
490
....*....|....*...
gi 1621035911 481 RIEASLQDVGAQIKQAKQ 498
Cdd:PRK13531 480 RIEASLQQVGEQIRQAQQ 497
|
|
| bpMoxR |
pfam20030 |
MoxR domain in the MoxR-vWA-beta-propeller ternary systems; Core MoxR component domain of the ... |
9-182 |
3.23e-57 |
|
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: 188.99 E-value: 3.23e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621035911 9 ERISRLSAALEKGLFERSHAIRLCLLAALSGESVFLLGPPGIAKSLIARRLKFAFQqARAFEYLMTRFSTPEEVFGPLSI 88
Cdd:pfam20030 1 RRLREVLRPLKTGFVGKDEIIDLLGLALVARENLFLLGPPGTAKSALVRRLAARLG-GRYFEYLLTRFTEPNELFGPFDI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621035911 89 QALKdEGRYERLTAGYLPEAEIVFLDEIWKAGPAILNTLLTAINERHFRNGAHEEKIPMRLLVAASNELPEaDSSLEALY 168
Cdd:pfam20030 80 RKLR-EGELVTNTEGMLPEASLVFLDELFNANSAILNSLLMVLNERIFRRGKETRKLPALMFVGASNHLPE-DEALAALF 157
|
170
....*....|....
gi 1621035911 169 DRMLIRLWLDKVQD 182
Cdd:pfam20030 158 DRFLLRVKCDNVPP 171
|
|
| LARA_dom |
pfam20265 |
ATPase, RavA, LARA domain; This is the LARA (LdcI Associating domain of RavA) domain of ... |
334-437 |
8.27e-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: 8.27e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621035911 334 TALKVTRLGGMFSRKPHYELPAEIQGATLTLLLQQPLKLHDMEVIHITFEREALANWLEKGGEIRGKLNGIGFAQLLNMD 413
Cdd:pfam20265 1 QALDVEKAKGLFGRKPQYSLPDNLTLEKLTLLLQSPLSLHDIEVRHVYVERDELEKWLNKGGEIYGKLNGIGFLQRLDFE 80
|
90 100
....*....|....*....|....
gi 1621035911 414 VDTSQHLVVRDVSLQGSRLALPGS 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 |
3.76e-31 |
|
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: 117.01 E-value: 3.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621035911 41 SVFLLGPPGIAKSLIARRLKFAFQQARAFEYLMTRFSTPEEVFGPLSIQALKDEGRYERLTAGYLpEAEIVFLDEIWKAG 120
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSNRPVFYVQLTRDTTEEDLFGRRNIDPGGASWVDGPLVRAAR-EGEIAVLDEINRAN 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1621035911 121 PAILNTLLTAINERHFR--NGAHEEKIPM--RLLVAASNELPEADSSL-EALYDRM 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 ... |
228-289 |
2.21e-20 |
|
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: 84.92 E-value: 2.21e-20
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1621035911 228 VFELIFQLRQQLDALPNAPYVSDRRWKKAIRLLQASAFFSGRDSIAPIDLILLKDCLWHNVE 289
Cdd:pfam17868 2 VIDLIYDIRNKLDEEEENIYVSDRRWKKIVKLLKASAYLNGRDEVNLSDLLLLKHCLWNKPE 63
|
|
| ATPase_RavA_C |
pfam12592 |
ATPase, RavA, C-terminal; This domain is found at the C-terminal of bacterial regulatory ... |
444-498 |
4.66e-20 |
|
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: 83.54 E-value: 4.66e-20
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1621035911 444 PAEIRQQLEALDDEWHQQHNRFSEQQKCLFIPVEWLGRIEASLQDVGAQIKQAKQ 498
Cdd:pfam12592 1 PEEWLEQLEALEQELRQQRRLFHQHQPHLFIEPEWLARIEASLQQVTEQLEQLQQ 55
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
13-288 |
7.62e-15 |
|
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: 74.82 E-value: 7.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621035911 13 RLSAALEKGLFERSHAIRLCLLAALSGESVFLLGPPGIAKSLIARRLkfafqqARAFEYLMTRF-----STPEEVFGpLS 87
Cdd:COG0714 5 RLRAEIGKVYVGQEELIELVLIALLAGGHLLLEGVPGVGKTTLAKAL------ARALGLPFIRIqftpdLLPSDILG-TY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621035911 88 IqALKDEGRyERLTAGYLPeAEIVFLDEIWKAGPAILNTLLTAINERHFRNGAHEEKIPMRLLV-AASN--------ELP 158
Cdd:COG0714 78 I-YDQQTGE-FEFRPGPLF-ANVLLADEINRAPPKTQSALLEAMEERQVTIPGGTYKLPEPFLViATQNpieqegtyPLP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621035911 159 eadsslEALYDRMLIRLWLDkVQDKGNFRSMLVSQQDENINPVPSALqvSDEEFTQWQQQIGNIKLPDAVFELIFQLRQQ 238
Cdd:COG0714 155 ------EAQLDRFLLKLYIG-YPDAEEEREILRRHTGRHLAEVEPVL--SPEELLALQELVRQVHVSEAVLDYIVDLVRA 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1621035911 239 LDALPNAPY-VSDRRWKKAIRLLQASAFFSGRDSIAPIDLI-LLKDCLWHNV 288
Cdd:COG0714 226 TREHPDLRKgPSPRASIALLRAARALALLDGRDYVTPDDVKaVAGPVLKHRL 277
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
23-175 |
1.36e-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: 53.69 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621035911 23 FERSHAIRLCLLAAL--SGESVFLLGPPGIAKSLIARRL--KFAFQQARAFEYLMTRFSTPEEVfgplsiqALKDEGRYE 98
Cdd:cd00009 1 VGQEEAIEALREALElpPPKNLLLYGPPGTGKTTLARAIanELFRPGAPFLYLNASDLLEGLVV-------AELFGHFLV 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1621035911 99 RLTAGYLPEAE--IVFLDEIWKAGPAILNTLLTAINERHFRNGAHEEkipmRLLVAASNElPEADSSLEALYDRMLIRL 175
Cdd:cd00009 74 RLLFELAEKAKpgVLFIDEIDSLSRGAQNALLRVLETLNDLRIDREN----VRVIGATNR-PLLGDLDRALYDRLDIRI 147
|
|
| PRK11361 |
PRK11361 |
acetoacetate metabolism transcriptional regulator AtoC; |
36-160 |
6.76e-05 |
|
acetoacetate metabolism transcriptional regulator AtoC;
Pssm-ID: 183099 [Multi-domain] Cd Length: 457 Bit Score: 45.22 E-value: 6.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621035911 36 ALSGESVFLLGPPGIAKSLIARRLKFAFQQARAFEYLMTRFSTPE-----EVFG----PLSIQALKDEGRYERLTAGYLp 106
Cdd:PRK11361 163 ALSQASVLISGESGTGKELIARAIHYNSRRAKGPFIKVNCAALPEsllesELFGhekgAFTGAQTLRQGLFERANEGTL- 241
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1621035911 107 eaeivFLDEIWKAGPAILNTLLTAINERHF-RNGAHEE-KIPMRlLVAASNELPEA 160
Cdd:PRK11361 242 -----LLDEIGEMPLVLQAKLLRILQEREFeRIGGHQTiKVDIR-IIAATNRDLQA 291
|
|
| Mg_chelatase |
pfam01078 |
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ... |
26-59 |
2.43e-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: 42.14 E-value: 2.43e-04
10 20 30
....*....|....*....|....*....|....
gi 1621035911 26 SHAIRLCLLAALSGESVFLLGPPGIAKSLIARRL 59
Cdd:pfam01078 9 EQAKRALEIAAAGGHNLLMIGPPGSGKTMLAKRL 42
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
18-160 |
6.07e-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: 40.62 E-value: 6.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621035911 18 LEKGLFER-----------SHAIRLCLlaalSGES-------VFL-LGPPGIAKSLIARRL-KFAFQQARAFEYL-MTRF 76
Cdd:cd19499 5 LEERLHERvvgqdeavkavSDAIRRAR----AGLSdpnrpigSFLfLGPTGVGKTELAKALaELLFGDEDNLIRIdMSEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621035911 77 STPEEV---FGPLSIQALKDEGryerltaGYLPEA------EIVFLDEIWKAGPAILNTLLTAINERHFRNGaHEEKIPM 147
Cdd:cd19499 81 MEKHSVsrlIGAPPGYVGYTEG-------GQLTEAvrrkpySVVLLDEIEKAHPDVQNLLLQVLDDGRLTDS-HGRTVDF 152
|
170
....*....|....*
gi 1621035911 148 R--LLVAASNELPEA 160
Cdd:cd19499 153 KntIIIMTSNHFRPE 167
|
|
| PRK10365 |
PRK10365 |
sigma-54-dependent response regulator transcription factor ZraR; |
1-171 |
1.33e-03 |
|
sigma-54-dependent response regulator transcription factor ZraR;
Pssm-ID: 182412 [Multi-domain] Cd Length: 441 Bit Score: 41.17 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621035911 1 MAQTHLLAERISRLSAAlEKGLFERSHAIRLCL----LAALSGESVFLLGPPGIAKSLIARRLKFAfqQARAFEYLMTRF 76
Cdd:PRK10365 121 LAHTHSIDAETPAVTAS-QFGMVGKSPAMQHLLseiaLVAPSEATVLIHGDSGTGKELVARAIHAS--SARSEKPLVTLN 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621035911 77 STP-------EEVFG----PLSIQALKDEGRYERLTAGYLpeaeivFLDEIWKAGPAILNTLLTAINERHF-RNGAHEE- 143
Cdd:PRK10365 198 CAAlneslleSELFGhekgAFTGADKRREGRFVEADGGTL------FLDEIGDISPMMQVRLLRAIQEREVqRVGSNQTi 271
|
170 180 190
....*....|....*....|....*....|.
gi 1621035911 144 KIPMRLLVAASNELPEADSS---LEALYDRM 171
Cdd:PRK10365 272 SVDVRLIAATHRDLAAEVNAgrfRQDLYYRL 302
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
42-178 |
4.31e-03 |
|
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: 37.57 E-value: 4.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621035911 42 VFLLGPPGIAKSLIARRLkfafqqARAFEYLMTRFSTPEEVfgplsiqaLKDEGRYERLTAGYLPEAE-----IVFLDEI 116
Cdd:pfam00004 1 LLLYGPPGTGKTTLAKAV------AKELGAPFIEISGSELV--------SKYVGESEKRLRELFEAAKklapcVIFIDEI 66
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1621035911 117 WKAGPA-----------ILNTLLTAINErhfrngaHEEKIPMRLLVAASNELPEADsslEALYDRMLIRLWLD 178
Cdd:pfam00004 67 DALAGSrgsggdsesrrVVNQLLTELDG-------FTSSNSKVIVIAATNRPDKLD---PALLGRFDRIIEFP 129
|
|
| AAA_2 |
pfam07724 |
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ... |
41-128 |
4.51e-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: 37.95 E-value: 4.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621035911 41 SVFLLGPPGIAKSLIARRL-KFAFQQARAFEYL-MTRFSTPEEVfgplsiqaLKDEG------RYERltAGYLPEA---- 108
Cdd:pfam07724 5 SFLFLGPTGVGKTELAKALaELLFGDERALIRIdMSEYMEEHSV--------SRLIGappgyvGYEE--GGQLTEAvrrk 74
|
90 100
....*....|....*....|..
gi 1621035911 109 --EIVFLDEIWKAGPAILNTLL 128
Cdd:pfam07724 75 pySIVLIDEIEKAHPGVQNDLL 96
|
|
| |
