|
Name |
Accession |
Description |
Interval |
E-value |
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
339-655 |
8.00e-97 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 317.41 E-value: 8.00e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 339 LEQRLKEHIIGQESAIATVGAAIRRKENGWYDEEHPL-VFLFLGSSGIGKTELAKQTAKYMHkDAKKGFIRLDMSEFQER 417
Cdd:COG0542 543 LEEELHERVIGQDEAVEAVADAIRRSRAGLKDPNRPIgSFLFLGPTGVGKTELAKALAEFLF-GDEDALIRIDMSEYMEK 621
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 418 HEVAKFIGSPPGYIGHEEGGQLTKKLKQCPNAVVLFDEVDKAHPDVLTIMLQLFDEGRLTDGKGKTIDCKDAIFIMTSNV 497
Cdd:COG0542 622 HSVSRLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLLDEIEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTIIIMTSNI 701
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 498 ASDEIAQHAlqlrqealemsrnriaenlGDVQISDKItisknfkENVIRPILKAHFrRDEFLGRINEIVYFLPFCHSELI 577
Cdd:COG0542 702 GSELILDLA-------------------EDEPDYEEM-------KEAVMEELKKHF-RPEFLNRIDEIIVFHPLSKEELR 754
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 672038081 578 QLVNKELNFWAKRAKQRhNITLLWDREVADVLVD-GYNVHYGARSIKHEVERRVVNQLAAAYEQDLLPGGCTLRITVED 655
Cdd:COG0542 755 KIVDLQLKRLRKRLAER-GITLELTDAAKDFLAEkGYDPEYGARPLKRAIQRELEDPLAEEILAGEIKEGDTITVDVDD 832
|
|
| chaperone_ClpB |
TIGR03346 |
ATP-dependent chaperone ClpB; Members of this protein family are the bacterial ATP-dependent ... |
308-655 |
9.43e-80 |
|
ATP-dependent chaperone ClpB; Members of this protein family are the bacterial ATP-dependent chaperone ClpB. This protein belongs to the AAA family, ATPases associated with various cellular activities (pfam00004). This molecular chaperone does not act as a protease, but rather serves to disaggregate misfolded and aggregated proteins. [Protein fate, Protein folding and stabilization]
Pssm-ID: 274529 [Multi-domain] Cd Length: 850 Bit Score: 271.83 E-value: 9.43e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 308 EGEVMKLLKtsetkymekqrkreaeerrrfpLEQRLKEHIIGQESAIATVGAAIRRKENGWYDEEHPL-VFLFLGSSGIG 386
Cdd:TIGR03346 549 EGEREKLLH----------------------MEEELHERVVGQDEAVEAVSDAIRRSRAGLSDPNRPIgSFLFLGPTGVG 606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 387 KTELAKQTAKYMHkDAKKGFIRLDMSEFQERHEVAKFIGSPPGYIGHEEGGQLTKKLKQCPNAVVLFDEVDKAHPDVLTI 466
Cdd:TIGR03346 607 KTELAKALAEFLF-DSEDAMVRIDMSEYMEKHSVARLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLFDEVEKAHPDVFNV 685
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 467 MLQLFDEGRLTDGKGKTIDCKDAIFIMTSNVASDEIAQhalQLRQEALEMSRNRIAEnlgdvqisdkitisknfkenvir 546
Cdd:TIGR03346 686 LLQVLDDGRLTDGQGRTVDFRNTVIIMTSNLGSDFIQE---LAGGDDYEEMREAVME----------------------- 739
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 547 pILKAHFrRDEFLGRINEIVYFLPFCHSELIQLVNKELNFWAKRAKQRHnITLLWDREVADVLVD-GYNVHYGARSIKHE 625
Cdd:TIGR03346 740 -VLRAHF-RPEFLNRIDEIVVFHPLGREQIARIVEIQLGRLRKRLAERK-ITLELSDAALDFLAEaGYDPVYGARPLKRA 816
|
330 340 350
....*....|....*....|....*....|....
gi 672038081 626 VERRVVNQLAaayeQDLLPG----GCTLRITVED 655
Cdd:TIGR03346 817 IQREIENPLA----KKILAGevapGDTIRVDVEG 846
|
|
| clpC |
CHL00095 |
Clp protease ATP binding subunit |
311-655 |
4.87e-78 |
|
Clp protease ATP binding subunit
Pssm-ID: 214361 [Multi-domain] Cd Length: 821 Bit Score: 266.54 E-value: 4.87e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 311 VMKLLKTSETKYMEkqrkreaeerrrfpLEQRLKEHIIGQESAIATVGAAIRRKENGWYDEEHPLV-FLFLGSSGIGKTE 389
Cdd:CHL00095 489 VNKLTKSESEKLLH--------------MEETLHKRIIGQDEAVVAVSKAIRRARVGLKNPNRPIAsFLFSGPTGVGKTE 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 390 LAKQTAKYMHkDAKKGFIRLDMSEFQERHEVAKFIGSPPGYIGHEEGGQLTKKLKQCPNAVVLFDEVDKAHPDVLTIMLQ 469
Cdd:CHL00095 555 LTKALASYFF-GSEDAMIRLDMSEYMEKHTVSKLIGSPPGYVGYNEGGQLTEAVRKKPYTVVLFDEIEKAHPDIFNLLLQ 633
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 470 LFDEGRLTDGKGKTIDCKDAIFIMTSNVASdeiaqhalqlrqealemsrNRIAENLGDVQI--SDKITISKNFKE--NVI 545
Cdd:CHL00095 634 ILDDGRLTDSKGRTIDFKNTLIIMTSNLGS-------------------KVIETNSGGLGFelSENQLSEKQYKRlsNLV 694
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 546 RPILKAHFrRDEFLGRINEIVYFLPFCHSELIQLVNKELNFWAKRAKQRhNITLLWDREVADVLVD-GYNVHYGARSIKH 624
Cdd:CHL00095 695 NEELKQFF-RPEFLNRLDEIIVFRQLTKNDVWEIAEIMLKNLFKRLNEQ-GIQLEVTERIKTLLIEeGYNPLYGARPLRR 772
|
330 340 350
....*....|....*....|....*....|.
gi 672038081 625 EVERRVVNQLAAAYEQDLLPGGCTLRITVED 655
Cdd:CHL00095 773 AIMRLLEDPLAEEVLSFKIKPGDIIIVDVND 803
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
339-501 |
8.24e-78 |
|
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: 246.71 E-value: 8.24e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 339 LEQRLKEHIIGQESAIATVGAAIRRKENGWYDEEHPL-VFLFLGSSGIGKTELAKQTAKYMHKDaKKGFIRLDMSEFQER 417
Cdd:cd19499 5 LEERLHERVVGQDEAVKAVSDAIRRARAGLSDPNRPIgSFLFLGPTGVGKTELAKALAELLFGD-EDNLIRIDMSEYMEK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 418 HEVAKFIGSPPGYIGHEEGGQLTKKLKQCPNAVVLFDEVDKAHPDVLTIMLQLFDEGRLTDGKGKTIDCKDAIFIMTSNV 497
Cdd:cd19499 84 HSVSRLIGAPPGYVGYTEGGQLTEAVRRKPYSVVLLDEIEKAHPDVQNLLLQVLDDGRLTDSHGRTVDFKNTIIIMTSNH 163
|
....
gi 672038081 498 ASDE 501
Cdd:cd19499 164 FRPE 167
|
|
| AAA_2 |
pfam07724 |
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ... |
376-565 |
9.12e-67 |
|
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: 217.06 E-value: 9.12e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 376 VFLFLGSSGIGKTELAKQTAKYMHKDAKKgFIRLDMSEFQERHEVAKFIGSPPGYIGHEEGGQLTKKLKQCPNAVVLFDE 455
Cdd:pfam07724 5 SFLFLGPTGVGKTELAKALAELLFGDERA-LIRIDMSEYMEEHSVSRLIGAPPGYVGYEEGGQLTEAVRRKPYSIVLIDE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 456 VDKAHPDVLTIMLQLFDEGRLTDGKGKTIDCKDAIFIMTSNVASDEIAQHALqlrqealemsrnriaenlgdvqisDKIT 535
Cdd:pfam07724 84 IEKAHPGVQNDLLQILEGGTLTDKQGRTVDFKNTLFIMTGNFGSEKISDASR------------------------LGDS 139
|
170 180 190
....*....|....*....|....*....|
gi 672038081 536 ISKNFKENVIRPILKAHFRRdEFLGRINEI 565
Cdd:pfam07724 140 PDYELLKEEVMDLLKKGFIP-EFLGRLPII 168
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
128-316 |
2.82e-25 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 106.58 E-value: 2.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 128 NKNPSNKDAALMEAARANNVQEVRRLLSEGADVNARHKLGWTALMVAAISHNESVVQVLLAAGADPNLGDDfssvyktan 207
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDN--------- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 208 eQGVHSL----EDGRQDCASWritnqwtsalefrrwlgvpvgvLVTREDDFNNRLNHrasfkGCTALHYAVLADDYSIVK 283
Cdd:COG0666 152 -DGNTPLhlaaANGNLEIVKL----------------------LLEAGADVNARDND-----GETPLHLAAENGHLEIVK 203
|
170 180 190
....*....|....*....|....*....|....*.
gi 672038081 284 ELLGGGANPLQRNEMGHTPLDYARE---GEVMKLLK 316
Cdd:COG0666 204 LLLEAGADVNAKDNDGKTALDLAAEngnLEIVKLLL 239
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
111-197 |
1.17e-12 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 63.98 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 111 AGLGMWALAMALVVQCYNKNPSNKDA--ALMEAARANNVQEVRRLLSEgADVNARHKlGWTALMVAAISHNESVVQVLLA 188
Cdd:pfam12796 5 AKNGNLELVKLLLENGADANLQDKNGrtALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLLE 82
|
....*....
gi 672038081 189 AGADPNLGD 197
Cdd:pfam12796 83 KGADINVKD 91
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
373-510 |
1.67e-11 |
|
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: 62.78 E-value: 1.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 373 HPLVFLFLGSSGIGKTELAKQTAKYMHKDaKKGFIRLDMSEFQERHEVAKFIGSPPGYIGHEEGGQ----LTKKLKQCPN 448
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPP-GGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELrlrlALALARKLKP 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 672038081 449 AVVLFDEVDKAHPDVLTIMLQLFDEGRLTDGKGKtidCKDAIFIMTSNVASDEIAqHALQLR 510
Cdd:smart00382 80 DVLILDEITSLLDAEQEALLLLLEELRLLLLLKS---EKNLTVILTTNDEKDLGP-ALLRRR 137
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
128-306 |
2.64e-07 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 53.88 E-value: 2.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 128 NKNPSNKDAALMEAARANNVQEVRRLLSE-GADVNARHKLGWTALMV--AAISHNESVVQVLLAAGADPNLGDdfssvyk 204
Cdd:PHA03095 77 NAPERCGFTPLHLYLYNATTLDVIKLLIKaGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALD------- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 205 taneqgvhslEDGRqdcaswritnqwTSALEFRRWLGVPVGVL----------VTREDDFNNRLNHRA-SFKgctalhya 273
Cdd:PHA03095 150 ----------LYGM------------TPLAVLLKSRNANVELLrllidagadvYAVDDRFRSLLHHHLqSFK-------- 199
|
170 180 190
....*....|....*....|....*....|...
gi 672038081 274 vlaDDYSIVKELLGGGANPLQRNEMGHTPLDYA 306
Cdd:PHA03095 200 ---PRARIVRELIRAGCDPAATDMLGNTPLHSM 229
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
126-290 |
1.22e-06 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 51.94 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 126 CYNKNPSnkDAALMEAARANNVQEVRRLL-SEGADVNARHKLGWTALMVAAISHNESVVQVLLAagADPNLgddfssvyk 204
Cdd:cd22192 11 LQQKRIS--ESPLLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPEL--------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 205 taneqgvhsledgrqdcaswrITNQWTSALefrrwlgvpvgvlvtreddfnnrlnhrasFKGCTALHYAVLADDYSIVKE 284
Cdd:cd22192 78 ---------------------VNEPMTSDL-----------------------------YQGETALHIAVVNQNLNLVRE 107
|
....*.
gi 672038081 285 LLGGGA 290
Cdd:cd22192 108 LIARGA 113
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
265-292 |
3.72e-04 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 38.34 E-value: 3.72e-04
10 20
....*....|....*....|....*...
gi 672038081 265 KGCTALHYAVLADDYSIVKELLGGGANP 292
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
132-291 |
4.93e-03 |
|
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 40.06 E-value: 4.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 132 SNKDAALMEAARANNVQEVRRLLSEGA--DVNARHKLGWTALMVAAI-SHNESVVQVLLAAGADPNLGDdfSSVYKTANE 208
Cdd:TIGR00870 15 SDEEKAFLPAAERGDLASVYRDLEEPKklNINCPDRLGRSALFVAAIeNENLELTELLLNLSCRGAVGD--TLLHAISLE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 209 qgvhsLEDGRQDCASWritnqwtsaLEFRRWLGVPVGVLVTRE-DDFnnrlnhrasFKGCTALHYAVLADDYSIVKELLG 287
Cdd:TIGR00870 93 -----YVDAVEAILLH---------LLAAFRKSGPLELANDQYtSEF---------TPGITALHLAAHRQNYEIVKLLLE 149
|
....
gi 672038081 288 GGAN 291
Cdd:TIGR00870 150 RGAS 153
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
339-655 |
8.00e-97 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 317.41 E-value: 8.00e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 339 LEQRLKEHIIGQESAIATVGAAIRRKENGWYDEEHPL-VFLFLGSSGIGKTELAKQTAKYMHkDAKKGFIRLDMSEFQER 417
Cdd:COG0542 543 LEEELHERVIGQDEAVEAVADAIRRSRAGLKDPNRPIgSFLFLGPTGVGKTELAKALAEFLF-GDEDALIRIDMSEYMEK 621
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 418 HEVAKFIGSPPGYIGHEEGGQLTKKLKQCPNAVVLFDEVDKAHPDVLTIMLQLFDEGRLTDGKGKTIDCKDAIFIMTSNV 497
Cdd:COG0542 622 HSVSRLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLLDEIEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTIIIMTSNI 701
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 498 ASDEIAQHAlqlrqealemsrnriaenlGDVQISDKItisknfkENVIRPILKAHFrRDEFLGRINEIVYFLPFCHSELI 577
Cdd:COG0542 702 GSELILDLA-------------------EDEPDYEEM-------KEAVMEELKKHF-RPEFLNRIDEIIVFHPLSKEELR 754
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 672038081 578 QLVNKELNFWAKRAKQRhNITLLWDREVADVLVD-GYNVHYGARSIKHEVERRVVNQLAAAYEQDLLPGGCTLRITVED 655
Cdd:COG0542 755 KIVDLQLKRLRKRLAER-GITLELTDAAKDFLAEkGYDPEYGARPLKRAIQRELEDPLAEEILAGEIKEGDTITVDVDD 832
|
|
| chaperone_ClpB |
TIGR03346 |
ATP-dependent chaperone ClpB; Members of this protein family are the bacterial ATP-dependent ... |
308-655 |
9.43e-80 |
|
ATP-dependent chaperone ClpB; Members of this protein family are the bacterial ATP-dependent chaperone ClpB. This protein belongs to the AAA family, ATPases associated with various cellular activities (pfam00004). This molecular chaperone does not act as a protease, but rather serves to disaggregate misfolded and aggregated proteins. [Protein fate, Protein folding and stabilization]
Pssm-ID: 274529 [Multi-domain] Cd Length: 850 Bit Score: 271.83 E-value: 9.43e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 308 EGEVMKLLKtsetkymekqrkreaeerrrfpLEQRLKEHIIGQESAIATVGAAIRRKENGWYDEEHPL-VFLFLGSSGIG 386
Cdd:TIGR03346 549 EGEREKLLH----------------------MEEELHERVVGQDEAVEAVSDAIRRSRAGLSDPNRPIgSFLFLGPTGVG 606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 387 KTELAKQTAKYMHkDAKKGFIRLDMSEFQERHEVAKFIGSPPGYIGHEEGGQLTKKLKQCPNAVVLFDEVDKAHPDVLTI 466
Cdd:TIGR03346 607 KTELAKALAEFLF-DSEDAMVRIDMSEYMEKHSVARLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLFDEVEKAHPDVFNV 685
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 467 MLQLFDEGRLTDGKGKTIDCKDAIFIMTSNVASDEIAQhalQLRQEALEMSRNRIAEnlgdvqisdkitisknfkenvir 546
Cdd:TIGR03346 686 LLQVLDDGRLTDGQGRTVDFRNTVIIMTSNLGSDFIQE---LAGGDDYEEMREAVME----------------------- 739
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 547 pILKAHFrRDEFLGRINEIVYFLPFCHSELIQLVNKELNFWAKRAKQRHnITLLWDREVADVLVD-GYNVHYGARSIKHE 625
Cdd:TIGR03346 740 -VLRAHF-RPEFLNRIDEIVVFHPLGREQIARIVEIQLGRLRKRLAERK-ITLELSDAALDFLAEaGYDPVYGARPLKRA 816
|
330 340 350
....*....|....*....|....*....|....
gi 672038081 626 VERRVVNQLAaayeQDLLPG----GCTLRITVED 655
Cdd:TIGR03346 817 IQREIENPLA----KKILAGevapGDTIRVDVEG 846
|
|
| clpC |
CHL00095 |
Clp protease ATP binding subunit |
311-655 |
4.87e-78 |
|
Clp protease ATP binding subunit
Pssm-ID: 214361 [Multi-domain] Cd Length: 821 Bit Score: 266.54 E-value: 4.87e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 311 VMKLLKTSETKYMEkqrkreaeerrrfpLEQRLKEHIIGQESAIATVGAAIRRKENGWYDEEHPLV-FLFLGSSGIGKTE 389
Cdd:CHL00095 489 VNKLTKSESEKLLH--------------MEETLHKRIIGQDEAVVAVSKAIRRARVGLKNPNRPIAsFLFSGPTGVGKTE 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 390 LAKQTAKYMHkDAKKGFIRLDMSEFQERHEVAKFIGSPPGYIGHEEGGQLTKKLKQCPNAVVLFDEVDKAHPDVLTIMLQ 469
Cdd:CHL00095 555 LTKALASYFF-GSEDAMIRLDMSEYMEKHTVSKLIGSPPGYVGYNEGGQLTEAVRKKPYTVVLFDEIEKAHPDIFNLLLQ 633
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 470 LFDEGRLTDGKGKTIDCKDAIFIMTSNVASdeiaqhalqlrqealemsrNRIAENLGDVQI--SDKITISKNFKE--NVI 545
Cdd:CHL00095 634 ILDDGRLTDSKGRTIDFKNTLIIMTSNLGS-------------------KVIETNSGGLGFelSENQLSEKQYKRlsNLV 694
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 546 RPILKAHFrRDEFLGRINEIVYFLPFCHSELIQLVNKELNFWAKRAKQRhNITLLWDREVADVLVD-GYNVHYGARSIKH 624
Cdd:CHL00095 695 NEELKQFF-RPEFLNRLDEIIVFRQLTKNDVWEIAEIMLKNLFKRLNEQ-GIQLEVTERIKTLLIEeGYNPLYGARPLRR 772
|
330 340 350
....*....|....*....|....*....|.
gi 672038081 625 EVERRVVNQLAAAYEQDLLPGGCTLRITVED 655
Cdd:CHL00095 773 AIMRLLEDPLAEEVLSFKIKPGDIIIVDVND 803
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
339-501 |
8.24e-78 |
|
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: 246.71 E-value: 8.24e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 339 LEQRLKEHIIGQESAIATVGAAIRRKENGWYDEEHPL-VFLFLGSSGIGKTELAKQTAKYMHKDaKKGFIRLDMSEFQER 417
Cdd:cd19499 5 LEERLHERVVGQDEAVKAVSDAIRRARAGLSDPNRPIgSFLFLGPTGVGKTELAKALAELLFGD-EDNLIRIDMSEYMEK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 418 HEVAKFIGSPPGYIGHEEGGQLTKKLKQCPNAVVLFDEVDKAHPDVLTIMLQLFDEGRLTDGKGKTIDCKDAIFIMTSNV 497
Cdd:cd19499 84 HSVSRLIGAPPGYVGYTEGGQLTEAVRRKPYSVVLLDEIEKAHPDVQNLLLQVLDDGRLTDSHGRTVDFKNTIIIMTSNH 163
|
....
gi 672038081 498 ASDE 501
Cdd:cd19499 164 FRPE 167
|
|
| AAA_2 |
pfam07724 |
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ... |
376-565 |
9.12e-67 |
|
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: 217.06 E-value: 9.12e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 376 VFLFLGSSGIGKTELAKQTAKYMHKDAKKgFIRLDMSEFQERHEVAKFIGSPPGYIGHEEGGQLTKKLKQCPNAVVLFDE 455
Cdd:pfam07724 5 SFLFLGPTGVGKTELAKALAELLFGDERA-LIRIDMSEYMEEHSVSRLIGAPPGYVGYEEGGQLTEAVRRKPYSIVLIDE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 456 VDKAHPDVLTIMLQLFDEGRLTDGKGKTIDCKDAIFIMTSNVASDEIAQHALqlrqealemsrnriaenlgdvqisDKIT 535
Cdd:pfam07724 84 IEKAHPGVQNDLLQILEGGTLTDKQGRTVDFKNTLFIMTGNFGSEKISDASR------------------------LGDS 139
|
170 180 190
....*....|....*....|....*....|
gi 672038081 536 ISKNFKENVIRPILKAHFRRdEFLGRINEI 565
Cdd:pfam07724 140 PDYELLKEEVMDLLKKGFIP-EFLGRLPII 168
|
|
| ClpA |
TIGR02639 |
ATP-dependent Clp protease ATP-binding subunit clpA; [Protein fate, Degradation of proteins, ... |
339-635 |
2.21e-65 |
|
ATP-dependent Clp protease ATP-binding subunit clpA; [Protein fate, Degradation of proteins, peptides, and glycopeptides]
Pssm-ID: 274241 [Multi-domain] Cd Length: 730 Bit Score: 229.91 E-value: 2.21e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 339 LEQRLKEHIIGQESAIATVGAAIRRKENGWYDEEHPL-VFLFLGSSGIGKTELAKQTAKYMhkdakkG--FIRLDMSEFQ 415
Cdd:TIGR02639 447 LEKNLKAKIFGQDEAIDQLVSAIKRSRAGLGDPNKPVgSFLFVGPTGVGKTELAKQLAEEL------GvhLLRFDMSEYM 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 416 ERHEVAKFIGSPPGYIGHEEGGQLTKKLKQCPNAVVLFDEVDKAHPDVLTIMLQLFDEGRLTDGKGKTIDCKDAIFIMTS 495
Cdd:TIGR02639 521 EKHTVSRLIGSPPGYVGFEQGGLLTDAVRKHPHCVLLLDEIEKAHPDIYNILLQVMDYATLTDNNGRKADFRNVILIMTS 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 496 NVASDEIAQHALQLRQEALEMSRNRiaenlgdvqisdkiTISKNFKenvirPilkahfrrdEFLGRINEIVYFLPFCHSE 575
Cdd:TIGR02639 601 NAGASEMSKPPIGFGGENRESKSLK--------------AIKKLFS-----P---------EFRNRLDAIIHFNDLSEEM 652
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 672038081 576 LIQLVNKELNFWAKRAKQRhNITLLWDREVADVLVD-GYNVHYGARSIKHEVERRVVNQLA 635
Cdd:TIGR02639 653 AEKIVKKFLDELQDQLNEK-NIELELTDDAKKYLAEkGYDEEFGARPLARVIQEEIKKPLS 712
|
|
| PRK10865 |
PRK10865 |
ATP-dependent chaperone ClpB; |
339-656 |
1.19e-60 |
|
ATP-dependent chaperone ClpB;
Pssm-ID: 182791 [Multi-domain] Cd Length: 857 Bit Score: 218.95 E-value: 1.19e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 339 LEQRLKEHIIGQESAIATVGAAIRRKENGWYDEEHPL-VFLFLGSSGIGKTELAKQTAKYMHkDAKKGFIRLDMSEFQER 417
Cdd:PRK10865 562 MEQELHHRVIGQNEAVEAVSNAIRRSRAGLSDPNRPIgSFLFLGPTGVGKTELCKALANFMF-DSDDAMVRIDMSEFMEK 640
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 418 HEVAKFIGSPPGYIGHEEGGQLTKKLKQCPNAVVLFDEVDKAHPDVLTIMLQLFDEGRLTDGKGKTIDCKDAIFIMTSNV 497
Cdd:PRK10865 641 HSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTVVIMTSNL 720
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 498 ASDeiaqhalqlrqealemsrnRIAENLGDVQISDkitisknFKENVIRpILKAHFrRDEFLGRINEIVYFLPFCHSELI 577
Cdd:PRK10865 721 GSD-------------------LIQERFGELDYAH-------MKELVLG-VVSHNF-RPEFINRIDEVVVFHPLGEQHIA 772
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 578 QLVNKELNFWAKRAKQRHNITLLWDREVADVLVDGYNVHYGARSIKHEVERRVVNQLAaayeQDLLPG----GCTLRITV 653
Cdd:PRK10865 773 SIAQIQLQRLYKRLEERGYEIHISDEALKLLSENGYDPVYGARPLKRAIQQQIENPLA----QQILSGelvpGKVIRLEV 848
|
...
gi 672038081 654 EDS 656
Cdd:PRK10865 849 NDD 851
|
|
| VI_ClpV1 |
TIGR03345 |
type VI secretion ATPase, ClpV1 family; Members of this protein family are homologs of ClpB, ... |
339-635 |
1.46e-59 |
|
type VI secretion ATPase, ClpV1 family; Members of this protein family are homologs of ClpB, an ATPase associated with chaperone-related functions. These ClpB homologs, designated ClpV1, are a key component of the bacterial pathogenicity-associated type VI secretion system. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274528 [Multi-domain] Cd Length: 852 Bit Score: 215.58 E-value: 1.46e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 339 LEQRLKEHIIGQESAIATVGAAIRRKENGWYDEEHPL-VFLFLGSSGIGKTELAKQTAKYMHkDAKKGFIRLDMSEFQER 417
Cdd:TIGR03345 560 LPDRLAERVIGQDHALEAIAERIRTARAGLEDPRKPLgVFLLVGPSGVGKTETALALAELLY-GGEQNLITINMSEFQEA 638
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 418 HEVAKFIGSPPGYIGHEEGGQLTKKLKQCPNAVVLFDEVDKAHPDVLTIMLQLFDEGRLTDGKGKTIDCKDAIFIMTSNV 497
Cdd:TIGR03345 639 HTVSRLKGSPPGYVGYGEGGVLTEAVRRKPYSVVLLDEVEKAHPDVLELFYQVFDKGVMEDGEGREIDFKNTVILLTSNA 718
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 498 ASDEIAQHALqlrQEALEMSRNRIAENLgdvqisdkitisknfkenviRPILKAHFrRDEFLGRINeIVYFLPFCHSELI 577
Cdd:TIGR03345 719 GSDLIMALCA---DPETAPDPEALLEAL--------------------RPELLKVF-KPAFLGRMT-VIPYLPLDDDVLA 773
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 672038081 578 QLVNKELNFWAKRAKQRHNITLLWDREVADVLVDGYN-VHYGARSIKHEVERRVVNQLA 635
Cdd:TIGR03345 774 AIVRLKLDRIARRLKENHGAELVYSEALVEHIVARCTeVESGARNIDAILNQTLLPELS 832
|
|
| clpA |
PRK11034 |
ATP-dependent Clp protease ATP-binding subunit; Provisional |
339-660 |
1.38e-40 |
|
ATP-dependent Clp protease ATP-binding subunit; Provisional
Pssm-ID: 236828 [Multi-domain] Cd Length: 758 Bit Score: 159.23 E-value: 1.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 339 LEQRLKEHIIGQESAIATVGAAIRRKENGWYDEEHPL-VFLFLGSSGIGKTELAKQTAKYMHKDakkgFIRLDMSEFQER 417
Cdd:PRK11034 452 LGDRLKMLVFGQDKAIEALTEAIKMSRAGLGHEHKPVgSFLFAGPTGVGKTEVTVQLSKALGIE----LLRFDMSEYMER 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 418 HEVAKFIGSPPGYIGHEEGGQLTKKLKQCPNAVVLFDEVDKAHPDVLTIMLQLFDEGRLTDGKGKTIDCKDAIFIMTSNV 497
Cdd:PRK11034 528 HTVSRLIGAPPGYVGFDQGGLLTDAVIKHPHAVLLLDEIEKAHPDVFNLLLQVMDNGTLTDNNGRKADFRNVVLVMTTNA 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 498 ASDEIAQHALQLRQEalEMSRNRIAEnlgdvqisdkitISKNFKEnvirpilkahfrrdEFLGRINEIVYFLPFCHSELI 577
Cdd:PRK11034 608 GVRETERKSIGLIHQ--DNSTDAMEE------------IKKIFTP--------------EFRNRLDNIIWFDHLSTDVIH 659
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 578 QLVNKelnFWAKRAKQ--RHNITLLWDREVADVLVD-GYNVHYGARSIKHEVERRVVNQLAAAYEQDLLPGGCTLRITVE 654
Cdd:PRK11034 660 QVVDK---FIVELQAQldQKGVSLEVSQEARDWLAEkGYDRAMGARPMARVIQDNLKKPLANELLFGSLVDGGQVTVALD 736
|
....*.
gi 672038081 655 DSDKQL 660
Cdd:PRK11034 737 KEKNEL 742
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
128-316 |
2.82e-25 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 106.58 E-value: 2.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 128 NKNPSNKDAALMEAARANNVQEVRRLLSEGADVNARHKLGWTALMVAAISHNESVVQVLLAAGADPNLGDDfssvyktan 207
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDN--------- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 208 eQGVHSL----EDGRQDCASWritnqwtsalefrrwlgvpvgvLVTREDDFNNRLNHrasfkGCTALHYAVLADDYSIVK 283
Cdd:COG0666 152 -DGNTPLhlaaANGNLEIVKL----------------------LLEAGADVNARDND-----GETPLHLAAENGHLEIVK 203
|
170 180 190
....*....|....*....|....*....|....*.
gi 672038081 284 ELLGGGANPLQRNEMGHTPLDYARE---GEVMKLLK 316
Cdd:COG0666 204 LLLEAGADVNAKDNDGKTALDLAAEngnLEIVKLLL 239
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
109-315 |
2.41e-16 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 80.00 E-value: 2.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 109 NKAGLGMWALAMALVVQCYNKNPSNKDAALMEAARANNVQEVRRLLSEGADVNARHKLGWTALMVAAISHNESVVQVLLA 188
Cdd:COG0666 29 ALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 189 AGADPNlgddfssvykTANEQGVHSLedgrqdcaSWRITNQWTSALEFrrwlgvpvgvLVTREDDFNNRLNHrasfkGCT 268
Cdd:COG0666 109 AGADVN----------ARDKDGETPL--------HLAAYNGNLEIVKL----------LLEAGADVNAQDND-----GNT 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 672038081 269 ALHYAVLADDYSIVKELLGGGANPLQRNEMGHTPLDYAREG---EVMKLL 315
Cdd:COG0666 156 PLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENghlEIVKLL 205
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
348-502 |
7.63e-15 |
|
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: 72.18 E-value: 7.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 348 IGQESAIATVGAAIRRKengwydeeHPLVFLFLGSSGIGKTELAKQTAKYMHKdAKKGFIRLDMSEFQERHEVAkfigsp 427
Cdd:cd00009 1 VGQEEAIEALREALELP--------PPKNLLLYGPPGTGKTTLARAIANELFR-PGAPFLYLNASDLLEGLVVA------ 65
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 672038081 428 pGYIGHEEGGQLTKKLKQCPNAVVLFDEVDKAHPDVLTIMLQLFDEGRLTdgkgkTIDCKDAIFIMTSNVASDEI 502
Cdd:cd00009 66 -ELFGHFLVRLLFELAEKAKPGVLFIDEIDSLSRGAQNALLRVLETLNDL-----RIDRENVRVIGATNRPLLGD 134
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
111-197 |
1.17e-12 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 63.98 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 111 AGLGMWALAMALVVQCYNKNPSNKDA--ALMEAARANNVQEVRRLLSEgADVNARHKlGWTALMVAAISHNESVVQVLLA 188
Cdd:pfam12796 5 AKNGNLELVKLLLENGADANLQDKNGrtALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLLE 82
|
....*....
gi 672038081 189 AGADPNLGD 197
Cdd:pfam12796 83 KGADINVKD 91
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
373-510 |
1.67e-11 |
|
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: 62.78 E-value: 1.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 373 HPLVFLFLGSSGIGKTELAKQTAKYMHKDaKKGFIRLDMSEFQERHEVAKFIGSPPGYIGHEEGGQ----LTKKLKQCPN 448
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPP-GGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELrlrlALALARKLKP 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 672038081 449 AVVLFDEVDKAHPDVLTIMLQLFDEGRLTDGKGKtidCKDAIFIMTSNVASDEIAqHALQLR 510
Cdd:smart00382 80 DVLILDEITSLLDAEQEALLLLLEELRLLLLLKS---EKNLTVILTTNDEKDLGP-ALLRRR 137
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
138-296 |
1.89e-11 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 60.51 E-value: 1.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 138 LMEAARANNVQEVRRLLSEGADVNARHKLGWTALMVAAISHNESVVQVLLaAGADPNLGDDfssvyktaneqgvhsledg 217
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKDN------------------- 60
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 672038081 218 rqdcaswritnqwtsalefrrwlgvpvgvlvtreddfnnrlnhrasfkGCTALHYAVLADDYSIVKELLGGGANPLQRN 296
Cdd:pfam12796 61 ------------------------------------------------GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
|
|
| ClpB_D2-small |
pfam10431 |
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ... |
573-651 |
1.74e-10 |
|
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, referred to as the D2-small domain, and is a mixed alpha-beta structure. Compared with the D1-small domain (included in AAA, pfam00004) it lacks the long coiled-coil insertion, and instead of helix C4 contains a beta-strand (e3) that is part of a three stranded beta-pleated sheet. In Thermophilus the whole protein forms a hexamer with the D1-small and D2-small domains located on the outside of the hexamer, with the long coiled-coil being exposed on the surface. The D2-small domain is essential for oligomerization, forming a tight interface with the D2-large domain of a neighbouring subunit and thereby providing enough binding energy to stabilize the functional assembly. The domain is associated with two Clp_N, pfam02861, at the N-terminus as well as AAA, pfam00004 and AAA_2, pfam07724.
Pssm-ID: 463090 [Multi-domain] Cd Length: 81 Bit Score: 57.42 E-value: 1.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 573 HSELIQLVNKELNFWAKRAKQRhNITLLWDREVADVLVD-GYNVHYGARSIKHEVERRVVNQLAAAYEQDLLPGGCTLRI 651
Cdd:pfam10431 3 KEELRKIVDLQLKELQKRLAER-GITLELTDAAKDWLAEkGYDPEYGARPLRRAIQREIEDPLAEEILSGELKEGDTVRV 81
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
137-198 |
3.31e-10 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 61.89 E-value: 3.31e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 672038081 137 ALMEAARANNVQEVRRLLSEGADVNARHKLGWTALMVAAISHNESVVQVLLAAGADPNLGDD 198
Cdd:COG0666 189 PLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250
|
|
| ClpB_D2-small |
smart01086 |
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ... |
575-660 |
3.50e-10 |
|
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, referred to as the D2-small domain, and is a mixed alpha-beta structure. Compared with the D1-small domain (included in AAA) it lacks the long coiled-coil insertion, and instead of helix C4 contains a beta-strand (e3) that is part of a three stranded beta-pleated sheet. In Thermophilus the whole protein forms a hexamer with the D1-small and D2-small domains located on the outside of the hexamer, with the long coiled-coil being exposed on the surface. The D2-small domain is essential for oligomerisation, forming a tight interface with the D2-large domain of a neighbouring subunit and thereby providing enough binding energy to stabilise the functional assembly. The domain is associated with two Clp_N at the N-terminus as well as AAA and AAA_2.
Pssm-ID: 198154 [Multi-domain] Cd Length: 90 Bit Score: 57.07 E-value: 3.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 575 ELIQLVNKELNFWAKRAKQRhNITLLWDREVADVLVD-GYNVHYGARSIKHEVERRVVNQLAAAYEQDLLPGGCTLRITV 653
Cdd:smart01086 5 DLVRIVDLPLNALQKRLAEK-GITLEFTDEALDWLAEkGYDPKYGARPLRRIIQRELEDPLAELILSGELKDGDTVVVDV 83
|
....*..
gi 672038081 654 EDSDKQL 660
Cdd:smart01086 84 DDGELVF 90
|
|
| RecA-like_HslU |
cd19498 |
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ... |
341-458 |
2.26e-08 |
|
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease HslVU. In HslVU, HslU ATPase serves to unfold and translocate protein substrate, and the HslV protease degrades the unfolded proteins. This RecA-like_HslU 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: 410906 [Multi-domain] Cd Length: 183 Bit Score: 54.31 E-value: 2.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 341 QRLKEHIIGQESAIATVGAAIRRK------ENGWYDEEHPLVFLFLGSSGIGKTELAKQTAKYmhkdAKKGFIRLDMSEF 414
Cdd:cd19498 7 SELDKYIIGQDEAKRAVAIALRNRwrrmqlPEELRDEVTPKNILMIGPTGVGKTEIARRLAKL----AGAPFIKVEATKF 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 672038081 415 QErhevakfigspPGYIGHEeggqLTKKLKQCPNAVVLFDEVDK 458
Cdd:cd19498 83 TE-----------VGYVGRD----VESIIRDLVEGIVFIDEIDK 111
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
362-496 |
2.74e-08 |
|
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: 53.44 E-value: 2.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 362 RRKENGWYDEEHPLVFLFLGSSGIGKTELAKQTAKYMHKDakkgFIRLDMSEFQErhevaKFIGSppgyiGHEEGGQLTK 441
Cdd:cd19481 14 RGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLP----LIVVKLSSLLS-----KYVGE-----SEKNLRKIFE 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 672038081 442 KLKQCPNAVVLFDEVDKAHPD------------VLTIMLQLFDEGRltdgkgktiDCKDAIFIMTSN 496
Cdd:cd19481 80 RARRLAPCILFIDEIDAIGRKrdssgesgelrrVLNQLLTELDGVN---------SRSKVLVIAATN 137
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
137-187 |
5.74e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 49.58 E-value: 5.74e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 672038081 137 ALMEAARANNVQEVRRLLSEGADVNARHKLGWTALMVAAISHNESVVQVLL 187
Cdd:pfam13637 4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
128-306 |
2.64e-07 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 53.88 E-value: 2.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 128 NKNPSNKDAALMEAARANNVQEVRRLLSE-GADVNARHKLGWTALMV--AAISHNESVVQVLLAAGADPNLGDdfssvyk 204
Cdd:PHA03095 77 NAPERCGFTPLHLYLYNATTLDVIKLLIKaGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALD------- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 205 taneqgvhslEDGRqdcaswritnqwTSALEFRRWLGVPVGVL----------VTREDDFNNRLNHRA-SFKgctalhya 273
Cdd:PHA03095 150 ----------LYGM------------TPLAVLLKSRNANVELLrllidagadvYAVDDRFRSLLHHHLqSFK-------- 199
|
170 180 190
....*....|....*....|....*....|...
gi 672038081 274 vlaDDYSIVKELLGGGANPLQRNEMGHTPLDYA 306
Cdd:PHA03095 200 ---PRARIVRELIRAGCDPAATDMLGNTPLHSM 229
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
378-496 |
6.91e-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: 6.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 378 LFLGSSGIGKTELAKQTAKYMHKDakkgFIRLDMSEFqerheVAKFIGSPPGYIghEEGGQLTKKLKQCpnaVVLFDEVD 457
Cdd:pfam00004 2 LLYGPPGTGKTTLAKAVAKELGAP----FIEISGSEL-----VSKYVGESEKRL--RELFEAAKKLAPC---VIFIDEID 67
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 672038081 458 KAHP-----------DVLTIMLQLFDegrltdgkGKTIDCKDAIFIMTSN 496
Cdd:pfam00004 68 ALAGsrgsggdsesrRVVNQLLTELD--------GFTSSNSKVIVIAATN 109
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
377-496 |
7.31e-07 |
|
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: 48.83 E-value: 7.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 377 FLFLGSSGIGKTELAKQTAKYMHKDakKGFIRL---DMSE---FQERH---EVAKFIGSPpgyigheeggqLTKKLKqcP 447
Cdd:pfam07728 2 VLLVGPPGTGKTELAERLAAALSNR--PVFYVQltrDTTEedlFGRRNidpGGASWVDGP-----------LVRAAR--E 66
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 672038081 448 NAVVLFDEVDKAHPDVLTIMLQLFDEGRLTDGKGKT-IDCKDAIF--IMTSN 496
Cdd:pfam07728 67 GEIAVLDEINRANPDVLNSLLSLLDERRLLLPDGGElVKAAPDGFrlIATMN 118
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
126-290 |
1.22e-06 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 51.94 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 126 CYNKNPSnkDAALMEAARANNVQEVRRLL-SEGADVNARHKLGWTALMVAAISHNESVVQVLLAagADPNLgddfssvyk 204
Cdd:cd22192 11 LQQKRIS--ESPLLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPEL--------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 205 taneqgvhsledgrqdcaswrITNQWTSALefrrwlgvpvgvlvtreddfnnrlnhrasFKGCTALHYAVLADDYSIVKE 284
Cdd:cd22192 78 ---------------------VNEPMTSDL-----------------------------YQGETALHIAVVNQNLNLVRE 107
|
....*.
gi 672038081 285 LLGGGA 290
Cdd:cd22192 108 LIARGA 113
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
150-195 |
1.43e-06 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 51.18 E-value: 1.43e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 672038081 150 VRRLLSEGADVNARHKLGWTALMVAAISHNESVVQVLLAAGADPNL 195
Cdd:PHA03095 240 VLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINA 285
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
252-306 |
2.25e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 45.03 E-value: 2.25e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 672038081 252 DDFNNRLNHRaSFKGCTALHYAVLADDYSIVKELLGGGANPLQRNEMGHTPLDYA 306
Cdd:pfam13857 3 EHGPIDLNRL-DGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
374-496 |
3.03e-06 |
|
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 440232 [Multi-domain] Cd Length: 397 Bit Score: 50.29 E-value: 3.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 374 PLVFLFLGSSGIGKTELAKQTAKYMHKDakkgFIRLDMSEFqerheVAKfigsppgYIGHEEGG--QLTKKLKQCPNAVV 451
Cdd:COG0464 191 PRGLLLYGPPGTGKTLLARALAGELGLP----LIEVDLSDL-----VSK-------YVGETEKNlrEVFDKARGLAPCVL 254
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 672038081 452 LFDEVDKAHPD-----------VLTIMLQLFDEGRltdgkgktidcKDAIFIMTSN 496
Cdd:COG0464 255 FIDEADALAGKrgevgdgvgrrVVNTLLTEMEELR-----------SDVVVIAATN 299
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
130-201 |
2.96e-05 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 47.56 E-value: 2.96e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 672038081 130 NPSNKDAALMEAARANNVQEVRRLLSEGADVNARHKLGWTALMVAAISHNESVVQVLLAAGAD---PNLGDDFSS 201
Cdd:PLN03192 618 DPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADvdkANTDDDFSP 692
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
127-315 |
5.37e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 46.20 E-value: 5.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 127 YNKNPSNKDAALMeaARANNVQEVRRLLSE-GADVNARHKLGWTALMVAAISHNESV--VQVLLAAGADPNLgddfSSVY 203
Cdd:PHA03100 67 NNSTPLHYLSNIK--YNLTDVKEIVKLLLEyGANVNAPDNNGITPLLYAISKKSNSYsiVEYLLDNGANVNI----KNSD 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 204 ktaNEQGVH-SLEDGRQDcaswritnqwTSALEFRRWLGVPVGV------LVTREDDFNNRLNhrasfKGCTALHYAVLA 276
Cdd:PHA03100 141 ---GENLLHlYLESNKID----------LKILKLLIDKGVDINAknrvnyLLSYGVPINIKDV-----YGFTPLHYAVYN 202
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 672038081 277 DDYSIVKELLGGGANPLQRNEMGHTPLDYA---REGEVMKLL 315
Cdd:PHA03100 203 NNPEFVKYLLDLGANPNLVNKYGDTPLHIAilnNNKEIFKLL 244
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
147-304 |
6.57e-05 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 46.17 E-value: 6.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 147 VQEVRRLLSEGADVNARHKLGWTAL---MVAAISHNESVVQVLLAAGADPNLGDdfsSVYKTAneqgVHSLedgrqdcas 223
Cdd:PHA03095 27 VEEVRRLLAAGADVNFRGEYGKTPLhlyLHYSSEKVKDIVRLLLEAGADVNAPE---RCGFTP----LHLY--------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 224 wrITNQWTsaLEFRRWLgVPVGVLVTREDDFNNrlnhrasfkgcTALH-Y-AVLADDYSIVKELLGGGANPLQRNEMGHT 301
Cdd:PHA03095 91 --LYNATT--LDVIKLL-IKAGADVNAKDKVGR-----------TPLHvYlSGFNINPKVIRLLLRKGADVNALDLYGMT 154
|
...
gi 672038081 302 PLD 304
Cdd:PHA03095 155 PLA 157
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
137-192 |
7.21e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 45.81 E-value: 7.21e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 672038081 137 ALMEAARANNVQEVRRLLSEGADVNARHKLGWTALMVAAISHNESVVQVLLAAGAD 192
Cdd:PHA03100 195 PLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
167-198 |
8.63e-05 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 39.97 E-value: 8.63e-05
10 20 30
....*....|....*....|....*....|...
gi 672038081 167 GWTALMVAAISH-NESVVQVLLAAGADPNLGDD 198
Cdd:pfam00023 2 GNTPLHLAAGRRgNLEIVKLLLSKGADVNARDK 34
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
265-297 |
1.17e-04 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 39.58 E-value: 1.17e-04
10 20 30
....*....|....*....|....*....|....
gi 672038081 265 KGCTALHYAVL-ADDYSIVKELLGGGANPLQRNE 297
Cdd:pfam00023 1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
270-315 |
1.68e-04 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 40.87 E-value: 1.68e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 672038081 270 LHYAVLADDYSIVKELLGGGANPLQRNEMGHTPLDYA-REG--EVMKLL 315
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAaKNGhlEIVKLL 49
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
153-303 |
3.23e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 43.90 E-value: 3.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 153 LLSEGADVNARHKLGWTALMVAAISHNESVVQVLLAAGADPNL--GDDFSSVYKTANEQGVHSLE---DGRQDC------ 221
Cdd:PHA02876 164 LLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIiaLDDLSVLECAVDSKNIDTIKaiiDNRSNInkndls 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 222 --ASWRITNQWTSALEFrrwlgvPVGVLVTREDDFNNrlnhrasfkgcTALHYAVLADDYS-IVKELLGGGANPLQRNEM 298
Cdd:PHA02876 244 llKAIRNEDLETSLLLY------DAGFSVNSIDDCKN-----------TPLHHASQAPSLSrLVPKLLERGADVNAKNIK 306
|
....*
gi 672038081 299 GHTPL 303
Cdd:PHA02876 307 GETPL 311
|
|
| Zeta_toxin |
pfam06414 |
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is ... |
372-445 |
3.33e-04 |
|
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is thought to be part of a postregulational killing system in bacteria. It relies on antitoxin/toxin systems that secure stable inheritance of low and medium copy number plasmids during cell division and kill cells that have lost the plasmid.
Pssm-ID: 428926 Cd Length: 192 Bit Score: 42.35 E-value: 3.33e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 672038081 372 EHPLVFLFLGSSGIGKTELAKQTAKYMhkDAKKGFIRLDMSEFQERH-EVAKFIGSPP---GYIGHEEGGQLTKKLKQ 445
Cdd:pfam06414 9 ERPKAILLGGQPGAGKTELARALLDEL--GRQGNVVRIDPDDFRELHpHYRELQAADPktaSEYTQPDASRWVEKLLQ 84
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
265-292 |
3.72e-04 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 38.34 E-value: 3.72e-04
10 20
....*....|....*....|....*...
gi 672038081 265 KGCTALHYAVLADDYSIVKELLGGGANP 292
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
247-315 |
4.16e-04 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 39.71 E-value: 4.16e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 672038081 247 LVTREDDFNNRLNhrasfKGCTALHYAVLADDYSIVKELLGGGAnpLQRNEMGHTPLDYA-REG--EVMKLL 315
Cdd:pfam12796 16 LLENGADANLQDK-----NGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAaRSGhlEIVKLL 80
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
138-210 |
6.55e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 42.96 E-value: 6.55e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 672038081 138 LMEAARANNVQEVRRLLSEGADVNARHKLGWTALMVAAISHNESVVQVLLAAGADPNLGD-DFSSVYKTANEQG 210
Cdd:PTZ00322 86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDkDGKTPLELAEENG 159
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
167-195 |
6.64e-04 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 37.57 E-value: 6.64e-04
10 20
....*....|....*....|....*....
gi 672038081 167 GWTALMVAAISHNESVVQVLLAAGADPNL 195
Cdd:smart00248 2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| RecA-like_Lon |
cd19500 |
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ... |
376-517 |
1.04e-03 |
|
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an evolutionarily conserved ATP-dependent serine protease, present in bacteria and eukaryotic mitochondria and peroxisomes, which mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Lon protease is both an ATP-dependent peptidase and a protein-activated ATPase. This RecA-like Lon domain 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: 410908 [Multi-domain] Cd Length: 182 Bit Score: 40.62 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 376 VFLFLGSSGIGKTELAKQTAKYMHKDakkgFIRL------DMSEFqeRHEVAKFIGSPPGYIgheeggqlTKKLKQCP-- 447
Cdd:cd19500 39 ILCLVGPPGVGKTSLGKSIARALGRK----FVRIslggvrDEAEI--RGHRRTYVGAMPGRI--------IQALKKAGtn 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 672038081 448 NAVVLFDEVDK----AHPDVLTIMLQLFD---EGRLTDGK-GKTIDCKDAIFIMTSNVAsDEIAQhALQLRQEALEMS 517
Cdd:cd19500 105 NPVFLLDEIDKigssFRGDPASALLEVLDpeqNSTFSDHYlDVPFDLSKVLFIATANSL-DTIPG-PLLDRMEIIELS 180
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
118-315 |
1.08e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 42.17 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 118 LAMALVVQCYNKNPSNKDAALMEAARANNVQE--VRRLLSEGADVNA--RHKLGwTALMVAAISHNESVVQVLLAAGADP 193
Cdd:PHA02878 116 IFKIILTNRYKNIQTIDLVYIDKKSKDDIIEAeiTKLLLSYGADINMkdRHKGN-TALHYATENKDQRLTELLLSYGANV 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 194 NLGD--DFSSVYKT---ANEQGVHSL-EDGrqdcaswritnqwtsalefrrwlgvpvgvlvtreddfnNRLNHRASFkGC 267
Cdd:PHA02878 195 NIPDktNNSPLHHAvkhYNKPIVHILlENG--------------------------------------ASTDARDKC-GN 235
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 672038081 268 TALHYAV-LADDYSIVKELLGGGAN-PLQRNEMGHTPLDYA-REGEVMKLL 315
Cdd:PHA02878 236 TPLHISVgYCKDYDILKLLLEHGVDvNAKSYILGLTALHSSiKSERKLKLL 286
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
153-199 |
2.09e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 36.94 E-value: 2.09e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 672038081 153 LLSEG-ADVNARHKLGWTALMVAAISHNESVVQVLLAAGADPNLGDDF 199
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEE 48
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
167-194 |
2.61e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 35.70 E-value: 2.61e-03
10 20
....*....|....*....|....*...
gi 672038081 167 GWTALMVAAISHNESVVQVLLAAGADPN 194
Cdd:pfam13606 2 GNTPLHLAARNGRLEIVKLLLENGADIN 29
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
138-306 |
3.35e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 40.33 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 138 LMEAARANNVQEVRRLLSEGADVNARHKLGWTALMVAAISHNESVVQVLLAAGADPNLGDDFSsvyktanEQGVH-SLED 216
Cdd:PHA02874 128 LHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNG-------ESPLHnAAEY 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 217 GRQDCASWRITNqwTSALEFRRWLGV-PV--GVLVTR---EDDFNNRLNHRASFKGCTALHYAVLAD-DYSIVKELLGGG 289
Cdd:PHA02874 201 GDYACIKLLIDH--GNHIMNKCKNGFtPLhnAIIHNRsaiELLINNASINDQDIDGSTPLHHAINPPcDIDIIDILLYHK 278
|
170
....*....|....*..
gi 672038081 290 ANPLQRNEMGHTPLDYA 306
Cdd:PHA02874 279 ADISIKDNKGENPIDTA 295
|
|
| RPT1 |
COG1222 |
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ... |
377-457 |
3.41e-03 |
|
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440835 [Multi-domain] Cd Length: 326 Bit Score: 40.37 E-value: 3.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 377 FLFLGSSGIGKTELAKQTAKYMhkDAKkgFIRLDMSEFqerheVAKFIGsppgyigheEGGQLTKKL----KQCPNAVVL 452
Cdd:COG1222 115 VLLYGPPGTGKTLLAKAVAGEL--GAP--FIRVRGSEL-----VSKYIG---------EGARNVREVfelaREKAPSIIF 176
|
....*
gi 672038081 453 FDEVD 457
Cdd:COG1222 177 IDEID 181
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
132-291 |
4.93e-03 |
|
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 40.06 E-value: 4.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 132 SNKDAALMEAARANNVQEVRRLLSEGA--DVNARHKLGWTALMVAAI-SHNESVVQVLLAAGADPNLGDdfSSVYKTANE 208
Cdd:TIGR00870 15 SDEEKAFLPAAERGDLASVYRDLEEPKklNINCPDRLGRSALFVAAIeNENLELTELLLNLSCRGAVGD--TLLHAISLE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 209 qgvhsLEDGRQDCASWritnqwtsaLEFRRWLGVPVGVLVTRE-DDFnnrlnhrasFKGCTALHYAVLADDYSIVKELLG 287
Cdd:TIGR00870 93 -----YVDAVEAILLH---------LLAAFRKSGPLELANDQYtSEF---------TPGITALHLAAHRQNYEIVKLLLE 149
|
....
gi 672038081 288 GGAN 291
Cdd:TIGR00870 150 RGAS 153
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
265-292 |
5.78e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 34.93 E-value: 5.78e-03
10 20
....*....|....*....|....*...
gi 672038081 265 KGCTALHYAVLADDYSIVKELLGGGANP 292
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADI 28
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
143-315 |
6.59e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 39.65 E-value: 6.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 143 RANNVQEVRRLLSEGADVNARHKLgWTALMVAAISH-NESVVQVLLAAGADPNLGDDFSSVYKTANEQGVHSLEDGRqdc 221
Cdd:PHA03100 11 RIIKVKNIKYIIMEDDLNDYSYKK-PVLPLYLAKEArNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLTDVK--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 222 aswRItnqwtsalefrrwlgvpVGVLVTREDDFNNRLNhrasfKGCTALHYAVLA--DDYSIVKELLGGGANPLQRNEMG 299
Cdd:PHA03100 87 ---EI-----------------VKLLLEYGANVNAPDN-----NGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDG 141
|
170 180
....*....|....*....|.
gi 672038081 300 HTPLDYAREG-----EVMKLL 315
Cdd:PHA03100 142 ENLLHLYLESnkidlKILKLL 162
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
137-174 |
7.44e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 35.40 E-value: 7.44e-03
10 20 30
....*....|....*....|....*....|....*...
gi 672038081 137 ALMEAARANNVQEVRRLLSEGADVNARHKLGWTALMVA 174
Cdd:pfam13857 19 PLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| ftsH |
CHL00176 |
cell division protein; Validated |
373-457 |
8.02e-03 |
|
cell division protein; Validated
Pssm-ID: 214386 [Multi-domain] Cd Length: 638 Bit Score: 39.65 E-value: 8.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672038081 373 HPLVFLFLGSSGIGKTELAKQTAkymhKDAKKGFIRLDMSEFQERhevakFIGsppgyIGHEEGGQLTKKLKQCPNAVVL 452
Cdd:CHL00176 215 IPKGVLLVGPPGTGKTLLAKAIA----GEAEVPFFSISGSEFVEM-----FVG-----VGAARVRDLFKKAKENSPCIVF 280
|
....*
gi 672038081 453 FDEVD 457
Cdd:CHL00176 281 IDEID 285
|
|
| |
