|
Name |
Accession |
Description |
Interval |
E-value |
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
309-625 |
5.12e-96 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 314.33 E-value: 5.12e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 309 LEQRLKEHIIGQESAIATVGAAIRRKENGWYDEEHPL-VFLFLGSSGIGKTELAKQTAKYMHkDAKKGFIRLDMSEFQER 387
Cdd:COG0542 543 LEEELHERVIGQDEAVEAVADAIRRSRAGLKDPNRPIgSFLFLGPTGVGKTELAKALAEFLF-GDEDALIRIDMSEYMEK 621
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 388 HEVAKFIGSPPGYIGHEEGGQLTKKLKQCPNAVVLFDEVDKAHPDVLTIMLQLFDEGRLTDGKGKTIDCKDAIFIMTSNV 467
Cdd:COG0542 622 HSVSRLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLLDEIEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTIIIMTSNI 701
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 468 ASDEIAQHAlqlrqealemsrnriaenlGDVQMSDKItisknfkENVIRPILKAHFrRDEFLGRINEIVYFLPFCHSELI 547
Cdd:COG0542 702 GSELILDLA-------------------EDEPDYEEM-------KEAVMEELKKHF-RPEFLNRIDEIIVFHPLSKEELR 754
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1395168490 548 QLVNKELNFWAKRAKQRhNITLLWDREVADVLVD-GYNVHYGARSIKHEVERRVVNQLAAAYEQDLLPGGCTLRITVED 625
Cdd:COG0542 755 KIVDLQLKRLRKRLAER-GITLELTDAAKDFLAEkGYDPEYGARPLKRAIQRELEDPLAEEILAGEIKEGDTITVDVDD 832
|
|
| chaperone_ClpB |
TIGR03346 |
ATP-dependent chaperone ClpB; Members of this protein family are the bacterial ATP-dependent ... |
278-625 |
1.84e-79 |
|
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: 270.29 E-value: 1.84e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 278 EGEVMKLLKtsetkymekqrkreaeerrrfpLEQRLKEHIIGQESAIATVGAAIRRKENGWYDEEHPL-VFLFLGSSGIG 356
Cdd:TIGR03346 549 EGEREKLLH----------------------MEEELHERVVGQDEAVEAVSDAIRRSRAGLSDPNRPIgSFLFLGPTGVG 606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 357 KTELAKQTAKYMHkDAKKGFIRLDMSEFQERHEVAKFIGSPPGYIGHEEGGQLTKKLKQCPNAVVLFDEVDKAHPDVLTI 436
Cdd:TIGR03346 607 KTELAKALAEFLF-DSEDAMVRIDMSEYMEKHSVARLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLFDEVEKAHPDVFNV 685
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 437 MLQLFDEGRLTDGKGKTIDCKDAIFIMTSNVASDEIAQhalQLRQEALEMSRNRIAEnlgdvqmsdkitisknfkenvir 516
Cdd:TIGR03346 686 LLQVLDDGRLTDGQGRTVDFRNTVIIMTSNLGSDFIQE---LAGGDDYEEMREAVME----------------------- 739
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 517 pILKAHFrRDEFLGRINEIVYFLPFCHSELIQLVNKELNFWAKRAKQRHnITLLWDREVADVLVD-GYNVHYGARSIKHE 595
Cdd:TIGR03346 740 -VLRAHF-RPEFLNRIDEIVVFHPLGREQIARIVEIQLGRLRKRLAERK-ITLELSDAALDFLAEaGYDPVYGARPLKRA 816
|
330 340 350
....*....|....*....|....*....|....
gi 1395168490 596 VERRVVNQLAaayeQDLLPG----GCTLRITVED 625
Cdd:TIGR03346 817 IQREIENPLA----KKILAGevapGDTIRVDVEG 846
|
|
| clpC |
CHL00095 |
Clp protease ATP binding subunit |
281-625 |
6.17e-78 |
|
Clp protease ATP binding subunit
Pssm-ID: 214361 [Multi-domain] Cd Length: 821 Bit Score: 265.38 E-value: 6.17e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 281 VMKLLKTSETKYMEkqrkreaeerrrfpLEQRLKEHIIGQESAIATVGAAIRRKENGWYDEEHPLV-FLFLGSSGIGKTE 359
Cdd:CHL00095 489 VNKLTKSESEKLLH--------------MEETLHKRIIGQDEAVVAVSKAIRRARVGLKNPNRPIAsFLFSGPTGVGKTE 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 360 LAKQTAKYMHkDAKKGFIRLDMSEFQERHEVAKFIGSPPGYIGHEEGGQLTKKLKQCPNAVVLFDEVDKAHPDVLTIMLQ 439
Cdd:CHL00095 555 LTKALASYFF-GSEDAMIRLDMSEYMEKHTVSKLIGSPPGYVGYNEGGQLTEAVRKKPYTVVLFDEIEKAHPDIFNLLLQ 633
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 440 LFDEGRLTDGKGKTIDCKDAIFIMTSNVASdeiaqhalqlrqealemsrNRIAENLGDVQM--SDKITISKNFKE--NVI 515
Cdd:CHL00095 634 ILDDGRLTDSKGRTIDFKNTLIIMTSNLGS-------------------KVIETNSGGLGFelSENQLSEKQYKRlsNLV 694
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 516 RPILKAHFrRDEFLGRINEIVYFLPFCHSELIQLVNKELNFWAKRAKQRhNITLLWDREVADVLVD-GYNVHYGARSIKH 594
Cdd:CHL00095 695 NEELKQFF-RPEFLNRLDEIIVFRQLTKNDVWEIAEIMLKNLFKRLNEQ-GIQLEVTERIKTLLIEeGYNPLYGARPLRR 772
|
330 340 350
....*....|....*....|....*....|.
gi 1395168490 595 EVERRVVNQLAAAYEQDLLPGGCTLRITVED 625
Cdd:CHL00095 773 AIMRLLEDPLAEEVLSFKIKPGDIIIVDVND 803
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
309-471 |
7.45e-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: 245.94 E-value: 7.45e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 309 LEQRLKEHIIGQESAIATVGAAIRRKENGWYDEEHPL-VFLFLGSSGIGKTELAKQTAKYMHKDaKKGFIRLDMSEFQER 387
Cdd:cd19499 5 LEERLHERVVGQDEAVKAVSDAIRRARAGLSDPNRPIgSFLFLGPTGVGKTELAKALAELLFGD-EDNLIRIDMSEYMEK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 388 HEVAKFIGSPPGYIGHEEGGQLTKKLKQCPNAVVLFDEVDKAHPDVLTIMLQLFDEGRLTDGKGKTIDCKDAIFIMTSNV 467
Cdd:cd19499 84 HSVSRLIGAPPGYVGYTEGGQLTEAVRRKPYSVVLLDEIEKAHPDVQNLLLQVLDDGRLTDSHGRTVDFKNTIIIMTSNH 163
|
....
gi 1395168490 468 ASDE 471
Cdd:cd19499 164 FRPE 167
|
|
| AAA_2 |
pfam07724 |
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ... |
346-535 |
1.30e-66 |
|
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: 216.29 E-value: 1.30e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 346 VFLFLGSSGIGKTELAKQTAKYMHKDAKKgFIRLDMSEFQERHEVAKFIGSPPGYIGHEEGGQLTKKLKQCPNAVVLFDE 425
Cdd:pfam07724 5 SFLFLGPTGVGKTELAKALAELLFGDERA-LIRIDMSEYMEEHSVSRLIGAPPGYVGYEEGGQLTEAVRRKPYSIVLIDE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 426 VDKAHPDVLTIMLQLFDEGRLTDGKGKTIDCKDAIFIMTSNVASDEIAQHALqlrqealemsrnriaenlgdvqmsDKIT 505
Cdd:pfam07724 84 IEKAHPGVQNDLLQILEGGTLTDKQGRTVDFKNTLFIMTGNFGSEKISDASR------------------------LGDS 139
|
170 180 190
....*....|....*....|....*....|
gi 1395168490 506 ISKNFKENVIRPILKAHFRRdEFLGRINEI 535
Cdd:pfam07724 140 PDYELLKEEVMDLLKKGFIP-EFLGRLPII 168
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
130-286 |
1.13e-28 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 116.21 E-value: 1.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 130 NPSNKDAALMEAARANNVQEVRRLLSEGADVNARHKLGWTALMVASISHNESVVQVLLAAGADPNLGDEF-SSVYKTANE 208
Cdd:COG0666 83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDgNTPLHLAAA 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 209 QG-VHSLEVLVTREDDFNNRLNHrasfkGCTALHYAVLADDYSIVKELLDRGANPLQRNEMGHTPLDYARE---GEVMKL 284
Cdd:COG0666 163 NGnLEIVKLLLEAGADVNARDND-----GETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAEngnLEIVKL 237
|
..
gi 1395168490 285 LK 286
Cdd:COG0666 238 LL 239
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
138-266 |
7.86e-16 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 73.23 E-value: 7.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 138 LMEAARANNVQEVRRLLSEGADVNARHKLGWTALMVASISHNESVVQVLLAagadpnlgdefssvyktaneqgvhslevl 217
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE----------------------------- 51
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1395168490 218 vtrEDDFNNRLNhrasfkGCTALHYAVLADDYSIVKELLDRGANPLQRN 266
Cdd:pfam12796 52 ---HADVNLKDN------GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
343-480 |
1.91e-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: 62.39 E-value: 1.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 343 HPLVFLFLGSSGIGKTELAKQTAKYMHKDaKKGFIRLDMSEFQERHEVAKFIGSPPGYIGHEEGGQ----LTKKLKQCPN 418
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPP-GGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELrlrlALALARKLKP 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1395168490 419 AVVLFDEVDKAHPDVLTIMLQLFDEGRLTDGKGKtidCKDAIFIMTSNVASDEIAqHALQLR 480
Cdd:smart00382 80 DVLILDEITSLLDAEQEALLLLLEELRLLLLLKS---EKNLTVILTTNDEKDLGP-ALLRRR 137
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
144-285 |
1.02e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 61.22 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 144 ANNVQEVRRLLSE-GADVNARHKLGWTALMVASISHNESV--VQVLLAAGADPNL----GDEFSSVYKTANEQGVHSLEV 216
Cdd:PHA03100 82 LTDVKEIVKLLLEyGANVNAPDNNGITPLLYAISKKSNSYsiVEYLLDNGANVNIknsdGENLLHLYLESNKIDLKILKL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 217 LVTREDDFN--NRLNHRASF---------KGCTALHYAVLADDYSIVKELLDRGANPLQRNEMGHTPLDYA---REGEVM 282
Cdd:PHA03100 162 LIDKGVDINakNRVNYLLSYgvpinikdvYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAilnNNKEIF 241
|
...
gi 1395168490 283 KLL 285
Cdd:PHA03100 242 KLL 244
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
126-273 |
4.73e-08 |
|
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: 56.17 E-value: 4.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 126 CYSKNPSnkDAALMEAARANNVQEVRRLL-SEGADVNARHKLGWTALMVASISHNESVVQVLLAAgaDPNLGDE--FSSV 202
Cdd:cd22192 11 LQQKRIS--ESPLLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEA--APELVNEpmTSDL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 203 YK--------TANeQGVHSLEVLVTREDDFNN--------RLN---------HRASFKGCTALHyavladdySIVKELLD 257
Cdd:cd22192 87 YQgetalhiaVVN-QNLNLVRELIARGADVVSpratgtffRPGpknliyygeHPLSFAACVGNE--------EIVRLLIE 157
|
170
....*....|....*.
gi 1395168490 258 RGANPLQRNEMGHTPL 273
Cdd:cd22192 158 HGADIRAQDSLGNTVL 173
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
235-262 |
1.27e-05 |
|
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: 42.19 E-value: 1.27e-05
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
132-261 |
2.13e-04 |
|
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: 44.69 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 132 SNKDAALMEAARANNVQEVRRLLSEGA--DVNARHKLGWTALMVASI-SHNESVVQVLLAAGADPNLGDefSSVYKTANE 208
Cdd:TIGR00870 15 SDEEKAFLPAAERGDLASVYRDLEEPKklNINCPDRLGRSALFVAAIeNENLELTELLLNLSCRGAVGD--TLLHAISLE 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1395168490 209 --QGVHSLEVL---VTREDDFNNRLNHRAS---FKGCTALHYAVLADDYSIVKELLDRGAN 261
Cdd:TIGR00870 93 yvDAVEAILLHllaAFRKSGPLELANDQYTsefTPGITALHLAAHRQNYEIVKLLLERGAS 153
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
309-625 |
5.12e-96 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 314.33 E-value: 5.12e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 309 LEQRLKEHIIGQESAIATVGAAIRRKENGWYDEEHPL-VFLFLGSSGIGKTELAKQTAKYMHkDAKKGFIRLDMSEFQER 387
Cdd:COG0542 543 LEEELHERVIGQDEAVEAVADAIRRSRAGLKDPNRPIgSFLFLGPTGVGKTELAKALAEFLF-GDEDALIRIDMSEYMEK 621
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 388 HEVAKFIGSPPGYIGHEEGGQLTKKLKQCPNAVVLFDEVDKAHPDVLTIMLQLFDEGRLTDGKGKTIDCKDAIFIMTSNV 467
Cdd:COG0542 622 HSVSRLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLLDEIEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTIIIMTSNI 701
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 468 ASDEIAQHAlqlrqealemsrnriaenlGDVQMSDKItisknfkENVIRPILKAHFrRDEFLGRINEIVYFLPFCHSELI 547
Cdd:COG0542 702 GSELILDLA-------------------EDEPDYEEM-------KEAVMEELKKHF-RPEFLNRIDEIIVFHPLSKEELR 754
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1395168490 548 QLVNKELNFWAKRAKQRhNITLLWDREVADVLVD-GYNVHYGARSIKHEVERRVVNQLAAAYEQDLLPGGCTLRITVED 625
Cdd:COG0542 755 KIVDLQLKRLRKRLAER-GITLELTDAAKDFLAEkGYDPEYGARPLKRAIQRELEDPLAEEILAGEIKEGDTITVDVDD 832
|
|
| chaperone_ClpB |
TIGR03346 |
ATP-dependent chaperone ClpB; Members of this protein family are the bacterial ATP-dependent ... |
278-625 |
1.84e-79 |
|
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: 270.29 E-value: 1.84e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 278 EGEVMKLLKtsetkymekqrkreaeerrrfpLEQRLKEHIIGQESAIATVGAAIRRKENGWYDEEHPL-VFLFLGSSGIG 356
Cdd:TIGR03346 549 EGEREKLLH----------------------MEEELHERVVGQDEAVEAVSDAIRRSRAGLSDPNRPIgSFLFLGPTGVG 606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 357 KTELAKQTAKYMHkDAKKGFIRLDMSEFQERHEVAKFIGSPPGYIGHEEGGQLTKKLKQCPNAVVLFDEVDKAHPDVLTI 436
Cdd:TIGR03346 607 KTELAKALAEFLF-DSEDAMVRIDMSEYMEKHSVARLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLFDEVEKAHPDVFNV 685
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 437 MLQLFDEGRLTDGKGKTIDCKDAIFIMTSNVASDEIAQhalQLRQEALEMSRNRIAEnlgdvqmsdkitisknfkenvir 516
Cdd:TIGR03346 686 LLQVLDDGRLTDGQGRTVDFRNTVIIMTSNLGSDFIQE---LAGGDDYEEMREAVME----------------------- 739
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 517 pILKAHFrRDEFLGRINEIVYFLPFCHSELIQLVNKELNFWAKRAKQRHnITLLWDREVADVLVD-GYNVHYGARSIKHE 595
Cdd:TIGR03346 740 -VLRAHF-RPEFLNRIDEIVVFHPLGREQIARIVEIQLGRLRKRLAERK-ITLELSDAALDFLAEaGYDPVYGARPLKRA 816
|
330 340 350
....*....|....*....|....*....|....
gi 1395168490 596 VERRVVNQLAaayeQDLLPG----GCTLRITVED 625
Cdd:TIGR03346 817 IQREIENPLA----KKILAGevapGDTIRVDVEG 846
|
|
| clpC |
CHL00095 |
Clp protease ATP binding subunit |
281-625 |
6.17e-78 |
|
Clp protease ATP binding subunit
Pssm-ID: 214361 [Multi-domain] Cd Length: 821 Bit Score: 265.38 E-value: 6.17e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 281 VMKLLKTSETKYMEkqrkreaeerrrfpLEQRLKEHIIGQESAIATVGAAIRRKENGWYDEEHPLV-FLFLGSSGIGKTE 359
Cdd:CHL00095 489 VNKLTKSESEKLLH--------------MEETLHKRIIGQDEAVVAVSKAIRRARVGLKNPNRPIAsFLFSGPTGVGKTE 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 360 LAKQTAKYMHkDAKKGFIRLDMSEFQERHEVAKFIGSPPGYIGHEEGGQLTKKLKQCPNAVVLFDEVDKAHPDVLTIMLQ 439
Cdd:CHL00095 555 LTKALASYFF-GSEDAMIRLDMSEYMEKHTVSKLIGSPPGYVGYNEGGQLTEAVRKKPYTVVLFDEIEKAHPDIFNLLLQ 633
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 440 LFDEGRLTDGKGKTIDCKDAIFIMTSNVASdeiaqhalqlrqealemsrNRIAENLGDVQM--SDKITISKNFKE--NVI 515
Cdd:CHL00095 634 ILDDGRLTDSKGRTIDFKNTLIIMTSNLGS-------------------KVIETNSGGLGFelSENQLSEKQYKRlsNLV 694
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 516 RPILKAHFrRDEFLGRINEIVYFLPFCHSELIQLVNKELNFWAKRAKQRhNITLLWDREVADVLVD-GYNVHYGARSIKH 594
Cdd:CHL00095 695 NEELKQFF-RPEFLNRLDEIIVFRQLTKNDVWEIAEIMLKNLFKRLNEQ-GIQLEVTERIKTLLIEeGYNPLYGARPLRR 772
|
330 340 350
....*....|....*....|....*....|.
gi 1395168490 595 EVERRVVNQLAAAYEQDLLPGGCTLRITVED 625
Cdd:CHL00095 773 AIMRLLEDPLAEEVLSFKIKPGDIIIVDVND 803
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
309-471 |
7.45e-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: 245.94 E-value: 7.45e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 309 LEQRLKEHIIGQESAIATVGAAIRRKENGWYDEEHPL-VFLFLGSSGIGKTELAKQTAKYMHKDaKKGFIRLDMSEFQER 387
Cdd:cd19499 5 LEERLHERVVGQDEAVKAVSDAIRRARAGLSDPNRPIgSFLFLGPTGVGKTELAKALAELLFGD-EDNLIRIDMSEYMEK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 388 HEVAKFIGSPPGYIGHEEGGQLTKKLKQCPNAVVLFDEVDKAHPDVLTIMLQLFDEGRLTDGKGKTIDCKDAIFIMTSNV 467
Cdd:cd19499 84 HSVSRLIGAPPGYVGYTEGGQLTEAVRRKPYSVVLLDEIEKAHPDVQNLLLQVLDDGRLTDSHGRTVDFKNTIIIMTSNH 163
|
....
gi 1395168490 468 ASDE 471
Cdd:cd19499 164 FRPE 167
|
|
| AAA_2 |
pfam07724 |
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ... |
346-535 |
1.30e-66 |
|
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: 216.29 E-value: 1.30e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 346 VFLFLGSSGIGKTELAKQTAKYMHKDAKKgFIRLDMSEFQERHEVAKFIGSPPGYIGHEEGGQLTKKLKQCPNAVVLFDE 425
Cdd:pfam07724 5 SFLFLGPTGVGKTELAKALAELLFGDERA-LIRIDMSEYMEEHSVSRLIGAPPGYVGYEEGGQLTEAVRRKPYSIVLIDE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 426 VDKAHPDVLTIMLQLFDEGRLTDGKGKTIDCKDAIFIMTSNVASDEIAQHALqlrqealemsrnriaenlgdvqmsDKIT 505
Cdd:pfam07724 84 IEKAHPGVQNDLLQILEGGTLTDKQGRTVDFKNTLFIMTGNFGSEKISDASR------------------------LGDS 139
|
170 180 190
....*....|....*....|....*....|
gi 1395168490 506 ISKNFKENVIRPILKAHFRRdEFLGRINEI 535
Cdd:pfam07724 140 PDYELLKEEVMDLLKKGFIP-EFLGRLPII 168
|
|
| ClpA |
TIGR02639 |
ATP-dependent Clp protease ATP-binding subunit clpA; [Protein fate, Degradation of proteins, ... |
309-605 |
4.26e-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: 228.76 E-value: 4.26e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 309 LEQRLKEHIIGQESAIATVGAAIRRKENGWYDEEHPL-VFLFLGSSGIGKTELAKQTAKYMhkdakkG--FIRLDMSEFQ 385
Cdd:TIGR02639 447 LEKNLKAKIFGQDEAIDQLVSAIKRSRAGLGDPNKPVgSFLFVGPTGVGKTELAKQLAEEL------GvhLLRFDMSEYM 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 386 ERHEVAKFIGSPPGYIGHEEGGQLTKKLKQCPNAVVLFDEVDKAHPDVLTIMLQLFDEGRLTDGKGKTIDCKDAIFIMTS 465
Cdd:TIGR02639 521 EKHTVSRLIGSPPGYVGFEQGGLLTDAVRKHPHCVLLLDEIEKAHPDIYNILLQVMDYATLTDNNGRKADFRNVILIMTS 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 466 NVASDEIAQHALQLRQEALEMSRNRiaenlgdvqmsdkiTISKNFKenvirPilkahfrrdEFLGRINEIVYFLPFCHSE 545
Cdd:TIGR02639 601 NAGASEMSKPPIGFGGENRESKSLK--------------AIKKLFS-----P---------EFRNRLDAIIHFNDLSEEM 652
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1395168490 546 LIQLVNKELNFWAKRAKQRhNITLLWDREVADVLVD-GYNVHYGARSIKHEVERRVVNQLA 605
Cdd:TIGR02639 653 AEKIVKKFLDELQDQLNEK-NIELELTDDAKKYLAEkGYDEEFGARPLARVIQEEIKKPLS 712
|
|
| PRK10865 |
PRK10865 |
ATP-dependent chaperone ClpB; |
309-626 |
2.05e-60 |
|
ATP-dependent chaperone ClpB;
Pssm-ID: 182791 [Multi-domain] Cd Length: 857 Bit Score: 217.41 E-value: 2.05e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 309 LEQRLKEHIIGQESAIATVGAAIRRKENGWYDEEHPL-VFLFLGSSGIGKTELAKQTAKYMHkDAKKGFIRLDMSEFQER 387
Cdd:PRK10865 562 MEQELHHRVIGQNEAVEAVSNAIRRSRAGLSDPNRPIgSFLFLGPTGVGKTELCKALANFMF-DSDDAMVRIDMSEFMEK 640
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 388 HEVAKFIGSPPGYIGHEEGGQLTKKLKQCPNAVVLFDEVDKAHPDVLTIMLQLFDEGRLTDGKGKTIDCKDAIFIMTSNV 467
Cdd:PRK10865 641 HSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTVVIMTSNL 720
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 468 ASDeiaqhalqlrqealemsrnRIAENLGDVQMSDkitisknFKENVIRpILKAHFrRDEFLGRINEIVYFLPFCHSELI 547
Cdd:PRK10865 721 GSD-------------------LIQERFGELDYAH-------MKELVLG-VVSHNF-RPEFINRIDEVVVFHPLGEQHIA 772
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 548 QLVNKELNFWAKRAKQRHNITLLWDREVADVLVDGYNVHYGARSIKHEVERRVVNQLAaayeQDLLPG----GCTLRITV 623
Cdd:PRK10865 773 SIAQIQLQRLYKRLEERGYEIHISDEALKLLSENGYDPVYGARPLKRAIQQQIENPLA----QQILSGelvpGKVIRLEV 848
|
...
gi 1395168490 624 EDS 626
Cdd:PRK10865 849 NDD 851
|
|
| VI_ClpV1 |
TIGR03345 |
type VI secretion ATPase, ClpV1 family; Members of this protein family are homologs of ClpB, ... |
309-605 |
1.06e-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: 215.19 E-value: 1.06e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 309 LEQRLKEHIIGQESAIATVGAAIRRKENGWYDEEHPL-VFLFLGSSGIGKTELAKQTAKYMHkDAKKGFIRLDMSEFQER 387
Cdd:TIGR03345 560 LPDRLAERVIGQDHALEAIAERIRTARAGLEDPRKPLgVFLLVGPSGVGKTETALALAELLY-GGEQNLITINMSEFQEA 638
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 388 HEVAKFIGSPPGYIGHEEGGQLTKKLKQCPNAVVLFDEVDKAHPDVLTIMLQLFDEGRLTDGKGKTIDCKDAIFIMTSNV 467
Cdd:TIGR03345 639 HTVSRLKGSPPGYVGYGEGGVLTEAVRRKPYSVVLLDEVEKAHPDVLELFYQVFDKGVMEDGEGREIDFKNTVILLTSNA 718
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 468 ASDEIAQHALQlrqealemsrnriaenlgDVQMSDKITISKnfkenVIRPILKAHFrRDEFLGRINeIVYFLPFCHSELI 547
Cdd:TIGR03345 719 GSDLIMALCAD------------------PETAPDPEALLE-----ALRPELLKVF-KPAFLGRMT-VIPYLPLDDDVLA 773
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1395168490 548 QLVNKELNFWAKRAKQRHNITLLWDREVADVLVDGYN-VHYGARSIKHEVERRVVNQLA 605
Cdd:TIGR03345 774 AIVRLKLDRIARRLKENHGAELVYSEALVEHIVARCTeVESGARNIDAILNQTLLPELS 832
|
|
| clpA |
PRK11034 |
ATP-dependent Clp protease ATP-binding subunit; Provisional |
309-630 |
7.00e-40 |
|
ATP-dependent Clp protease ATP-binding subunit; Provisional
Pssm-ID: 236828 [Multi-domain] Cd Length: 758 Bit Score: 156.54 E-value: 7.00e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 309 LEQRLKEHIIGQESAIATVGAAIRRKENGWYDEEHPL-VFLFLGSSGIGKTELAKQTAKYMHKDakkgFIRLDMSEFQER 387
Cdd:PRK11034 452 LGDRLKMLVFGQDKAIEALTEAIKMSRAGLGHEHKPVgSFLFAGPTGVGKTEVTVQLSKALGIE----LLRFDMSEYMER 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 388 HEVAKFIGSPPGYIGHEEGGQLTKKLKQCPNAVVLFDEVDKAHPDVLTIMLQLFDEGRLTDGKGKTIDCKDAIFIMTSNV 467
Cdd:PRK11034 528 HTVSRLIGAPPGYVGFDQGGLLTDAVIKHPHAVLLLDEIEKAHPDVFNLLLQVMDNGTLTDNNGRKADFRNVVLVMTTNA 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 468 ASDEIAQHALQLRQEalEMSRNRIAEnlgdvqmsdkitISKNFKEnvirpilkahfrrdEFLGRINEIVYFLPFCHSELI 547
Cdd:PRK11034 608 GVRETERKSIGLIHQ--DNSTDAMEE------------IKKIFTP--------------EFRNRLDNIIWFDHLSTDVIH 659
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 548 QLVNKelnFWAKRAKQ--RHNITLLWDREVADVLVD-GYNVHYGARSIKHEVERRVVNQLAAAYEQDLLPGGCTLRITVE 624
Cdd:PRK11034 660 QVVDK---FIVELQAQldQKGVSLEVSQEARDWLAEkGYDRAMGARPMARVIQDNLKKPLANELLFGSLVDGGQVTVALD 736
|
....*.
gi 1395168490 625 DSDKHL 630
Cdd:PRK11034 737 KEKNEL 742
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
130-286 |
1.13e-28 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 116.21 E-value: 1.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 130 NPSNKDAALMEAARANNVQEVRRLLSEGADVNARHKLGWTALMVASISHNESVVQVLLAAGADPNLGDEF-SSVYKTANE 208
Cdd:COG0666 83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDgNTPLHLAAA 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 209 QG-VHSLEVLVTREDDFNNRLNHrasfkGCTALHYAVLADDYSIVKELLDRGANPLQRNEMGHTPLDYARE---GEVMKL 284
Cdd:COG0666 163 NGnLEIVKLLLEAGADVNARDND-----GETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAEngnLEIVKL 237
|
..
gi 1395168490 285 LK 286
Cdd:COG0666 238 LL 239
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
132-286 |
1.29e-21 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 95.79 E-value: 1.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 132 SNKDAALMEAARANNVQEVRRLLSEGADVNARHKLGWTALMVASISHNESVVQVLLAAGADPNLGDEFssvYKT----AN 207
Cdd:COG0666 118 KDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDND---GETplhlAA 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 208 EQG-VHSLEVLVTREDDFNNRLNhrasfKGCTALHYAVLADDYSIVKELLDRGANPLQRNEMGHTPLDYAREGEVMKLLK 286
Cdd:COG0666 195 ENGhLEIVKLLLEAGADVNAKDN-----DGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVK 269
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
109-285 |
9.33e-21 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 93.09 E-value: 9.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 109 NKTGLGMWALAMALVVQCYSKNPSNKDAALMEAARANNVQEVRRLLSEGADVNARHKLGWTALMVASISHNESVVQVLLA 188
Cdd:COG0666 29 ALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 189 AGADPNLGDEF--SSVYKTANEQGVHSLEVLVTREDDFNNRLNHrasfkGCTALHYAVLADDYSIVKELLDRGANPLQRN 266
Cdd:COG0666 109 AGADVNARDKDgeTPLHLAAYNGNLEIVKLLLEAGADVNAQDND-----GNTPLHLAAANGNLEIVKLLLEAGADVNARD 183
|
170 180
....*....|....*....|..
gi 1395168490 267 EMGHTPLDYAREG---EVMKLL 285
Cdd:COG0666 184 NDGETPLHLAAENghlEIVKLL 205
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
138-266 |
7.86e-16 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 73.23 E-value: 7.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 138 LMEAARANNVQEVRRLLSEGADVNARHKLGWTALMVASISHNESVVQVLLAagadpnlgdefssvyktaneqgvhslevl 217
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE----------------------------- 51
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1395168490 218 vtrEDDFNNRLNhrasfkGCTALHYAVLADDYSIVKELLDRGANPLQRN 266
Cdd:pfam12796 52 ---HADVNLKDN------GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
318-472 |
8.82e-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: 8.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 318 IGQESAIATVGAAIRRKengwydeeHPLVFLFLGSSGIGKTELAKQTAKYMHKdAKKGFIRLDMSEFQERHEVAkfigsp 397
Cdd:cd00009 1 VGQEEAIEALREALELP--------PPKNLLLYGPPGTGKTTLARAIANELFR-PGAPFLYLNASDLLEGLVVA------ 65
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1395168490 398 pGYIGHEEGGQLTKKLKQCPNAVVLFDEVDKAHPDVLTIMLQLFDEGRLTdgkgkTIDCKDAIFIMTSNVASDEI 472
Cdd:cd00009 66 -ELFGHFLVRLLFELAEKAKPGVLFIDEIDSLSRGAQNALLRVLETLNDL-----RIDRENVRVIGATNRPLLGD 134
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
114-197 |
1.03e-11 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 61.29 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 114 GMWALAMALVVQCYSKNPSNKDA--ALMEAARANNVQEVRRLLSEgADVNARHKlGWTALMVASISHNESVVQVLLAAGA 191
Cdd:pfam12796 8 GNLELVKLLLENGADANLQDKNGrtALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGA 85
|
....*.
gi 1395168490 192 DPNLGD 197
Cdd:pfam12796 86 DINVKD 91
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
343-480 |
1.91e-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: 62.39 E-value: 1.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 343 HPLVFLFLGSSGIGKTELAKQTAKYMHKDaKKGFIRLDMSEFQERHEVAKFIGSPPGYIGHEEGGQ----LTKKLKQCPN 418
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPP-GGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELrlrlALALARKLKP 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1395168490 419 AVVLFDEVDKAHPDVLTIMLQLFDEGRLTDGKGKtidCKDAIFIMTSNVASDEIAqHALQLR 480
Cdd:smart00382 80 DVLILDEITSLLDAEQEALLLLLEELRLLLLLKS---EKNLTVILTTNDEKDLGP-ALLRRR 137
|
|
| ClpB_D2-small |
pfam10431 |
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ... |
543-621 |
2.02e-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: 2.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 543 HSELIQLVNKELNFWAKRAKQRhNITLLWDREVADVLVD-GYNVHYGARSIKHEVERRVVNQLAAAYEQDLLPGGCTLRI 621
Cdd:pfam10431 3 KEELRKIVDLQLKELQKRLAER-GITLELTDAAKDWLAEkGYDPEYGARPLRRAIQREIEDPLAEEILSGELKEGDTVRV 81
|
|
| ClpB_D2-small |
smart01086 |
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ... |
545-627 |
5.96e-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: 56.30 E-value: 5.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 545 ELIQLVNKELNFWAKRAKQRhNITLLWDREVADVLVD-GYNVHYGARSIKHEVERRVVNQLAAAYEQDLLPGGCTLRITV 623
Cdd:smart01086 5 DLVRIVDLPLNALQKRLAEK-GITLEFTDEALDWLAEkGYDPKYGARPLRRIIQRELEDPLAELILSGELKDGDTVVVDV 83
|
....
gi 1395168490 624 EDSD 627
Cdd:smart01086 84 DDGE 87
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
137-232 |
8.77e-10 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 60.35 E-value: 8.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 137 ALMEAARANNVQEVRRLLSEGADVNARHKLGWTALMVASISHNESVVQVLLAAGADPNLGDEFSSVYKTANEQGVHSLEV 216
Cdd:COG0666 189 PLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIV 268
|
90
....*....|....*.
gi 1395168490 217 LVTREDDFNNRLNHRA 232
Cdd:COG0666 269 KLLLLALLLLAAALLD 284
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
144-285 |
1.02e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 61.22 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 144 ANNVQEVRRLLSE-GADVNARHKLGWTALMVASISHNESV--VQVLLAAGADPNL----GDEFSSVYKTANEQGVHSLEV 216
Cdd:PHA03100 82 LTDVKEIVKLLLEyGANVNAPDNNGITPLLYAISKKSNSYsiVEYLLDNGANVNIknsdGENLLHLYLESNKIDLKILKL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 217 LVTREDDFN--NRLNHRASF---------KGCTALHYAVLADDYSIVKELLDRGANPLQRNEMGHTPLDYA---REGEVM 282
Cdd:PHA03100 162 LIDKGVDINakNRVNYLLSYgvpinikdvYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAilnNNKEIF 241
|
...
gi 1395168490 283 KLL 285
Cdd:PHA03100 242 KLL 244
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
138-262 |
2.11e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 60.00 E-value: 2.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 138 LMEAARANNVQEVRRLLSEGADVN-ARHKLGWTALMVASISHNESVVQVLLAAGADPNLG--DEFSSVYKTANEQGVHSL 214
Cdd:PHA02875 72 LHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPntDKFSPLHLAVMMGDIKGI 151
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1395168490 215 EVLvtreddfnnrLNHRASFK-----GCTALHYAVLADDYSIVKELLDRGANP 262
Cdd:PHA02875 152 ELL----------IDHKACLDiedccGCTPLIIAMAKGDIAICKMLLDSGANI 194
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
128-285 |
2.78e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 60.46 E-value: 2.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 128 SKNPSNKDAALMEAARANNVQEVRRLLSEGADVNARHKLGWTALMVAS-ISHNESVVQVLLAAGADPNLGD--EFSSVYK 204
Cdd:PHA02876 302 AKNIKGETPLYLMAKNGYDTENIRTLIMLGADVNAADRLYITPLHQAStLDRNKDIVITLLELGANVNARDycDKTPIHY 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 205 TANEQGVHSLEVLVtredDFNNRLNHRASFKGcTALHYAVLADD-YSIVKELLDRGANPLQRNEMGHTPLDYAREG---- 279
Cdd:PHA02876 382 AAVRNNVVIINTLL----DYGADIEALSQKIG-TALHFALCGTNpYMSVKTLIDRGANVNSKNKDLSTPLHYACKKnckl 456
|
....*.
gi 1395168490 280 EVMKLL 285
Cdd:PHA02876 457 DVIEML 462
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
147-274 |
5.51e-09 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 58.88 E-value: 5.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 147 VQEVRRLLSEGADVNARHKLGWTAL---MVASISHNESVVQVLLAAGADPNLGDE-----FSSVYKTANEQGVhsLEVLV 218
Cdd:PHA03095 27 VEEVRRLLAAGADVNFRGEYGKTPLhlyLHYSSEKVKDIVRLLLEAGADVNAPERcgftpLHLYLYNATTLDV--IKLLI 104
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1395168490 219 TREDDFNNRlnhraSFKGCTALH-Y-AVLADDYSIVKELLDRGANPLQRNEMGHTPLD 274
Cdd:PHA03095 105 KAGADVNAK-----DKVGRTPLHvYlSGFNINPKVIRLLLRKGADVNALDLYGMTPLA 157
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
150-276 |
2.09e-08 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 56.96 E-value: 2.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 150 VRRLLSEGADVNARHKLGWTALMVASISHNESV--VQVLLAAGADPnlgdefssvyktaneqgvhslevlVTREDDFNNR 227
Cdd:PHA03095 135 IRLLLRKGADVNALDLYGMTPLAVLLKSRNANVelLRLLIDAGADV------------------------YAVDDRFRSL 190
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1395168490 228 LNHRA-SFKgctalhyavlaDDYSIVKELLDRGANPLQRNEMGHTPLDYA 276
Cdd:PHA03095 191 LHHHLqSFK-----------PRARIVRELIRAGCDPAATDMLGNTPLHSM 229
|
|
| RecA-like_HslU |
cd19498 |
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ... |
311-428 |
2.96e-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: 53.92 E-value: 2.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 311 QRLKEHIIGQESAIATVGAAIRRK------ENGWYDEEHPLVFLFLGSSGIGKTELAKQTAKYmhkdAKKGFIRLDMSEF 384
Cdd:cd19498 7 SELDKYIIGQDEAKRAVAIALRNRwrrmqlPEELRDEVTPKNILMIGPTGVGKTEIARRLAKL----AGAPFIKVEATKF 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1395168490 385 QErhevakfigspPGYIGHEeggqLTKKLKQCPNAVVLFDEVDK 428
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 ... |
332-466 |
3.10e-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: 3.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 332 RRKENGWYDEEHPLVFLFLGSSGIGKTELAKQTAKYMHKDakkgFIRLDMSEFQErhevaKFIGSppgyiGHEEGGQLTK 411
Cdd:cd19481 14 RGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLP----LIVVKLSSLLS-----KYVGE-----SEKNLRKIFE 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1395168490 412 KLKQCPNAVVLFDEVDKAHPD------------VLTIMLQLFDEGRltdgkgktiDCKDAIFIMTSN 466
Cdd:cd19481 80 RARRLAPCILFIDEIDAIGRKrdssgesgelrrVLNQLLTELDGVN---------SRSKVLVIAATN 137
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
126-273 |
4.73e-08 |
|
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: 56.17 E-value: 4.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 126 CYSKNPSnkDAALMEAARANNVQEVRRLL-SEGADVNARHKLGWTALMVASISHNESVVQVLLAAgaDPNLGDE--FSSV 202
Cdd:cd22192 11 LQQKRIS--ESPLLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEA--APELVNEpmTSDL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 203 YK--------TANeQGVHSLEVLVTREDDFNN--------RLN---------HRASFKGCTALHyavladdySIVKELLD 257
Cdd:cd22192 87 YQgetalhiaVVN-QNLNLVRELIARGADVVSpratgtffRPGpknliyygeHPLSFAACVGNE--------EIVRLLIE 157
|
170
....*....|....*.
gi 1395168490 258 RGANPLQRNEMGHTPL 273
Cdd:cd22192 158 HGADIRAQDSLGNTVL 173
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
150-285 |
7.83e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 55.27 E-value: 7.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 150 VRRLLSEGADVNA--RHKLGwTALMVASISHNESVVQVLLAAGADPNLGD--EFSSVYKT---ANEQGVHSLEvlvtred 222
Cdd:PHA02878 150 TKLLLSYGADINMkdRHKGN-TALHYATENKDQRLTELLLSYGANVNIPDktNNSPLHHAvkhYNKPIVHILL------- 221
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1395168490 223 DFNNRLNHRASFkGCTALHYAV-LADDYSIVKELLDRGAN-PLQRNEMGHTPLDYA-REGEVMKLL 285
Cdd:PHA02878 222 ENGASTDARDKC-GNTPLHISVgYCKDYDILKLLLEHGVDvNAKSYILGLTALHSSiKSERKLKLL 286
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
137-187 |
1.51e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 48.42 E-value: 1.51e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1395168490 137 ALMEAARANNVQEVRRLLSEGADVNARHKLGWTALMVASISHNESVVQVLL 187
Cdd:pfam13637 4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
222-276 |
2.77e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 47.73 E-value: 2.77e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1395168490 222 DDFNNRLNHRaSFKGCTALHYAVLADDYSIVKELLDRGANPLQRNEMGHTPLDYA 276
Cdd:pfam13857 3 EHGPIDLNRL-DGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
348-466 |
6.79e-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: 6.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 348 LFLGSSGIGKTELAKQTAKYMHKDakkgFIRLDMSEFqerheVAKFIGSPPGYIghEEGGQLTKKLKQCpnaVVLFDEVD 427
Cdd:pfam00004 2 LLYGPPGTGKTTLAKAVAKELGAP----FIEISGSEL-----VSKYVGESEKRL--RELFEAAKKLAPC---VIFIDEID 67
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1395168490 428 KAHP-----------DVLTIMLQLFDegrltdgkGKTIDCKDAIFIMTSN 466
Cdd:pfam00004 68 ALAGsrgsggdsesrRVVNQLLTELD--------GFTSSNSKVIVIAATN 109
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
347-466 |
7.83e-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: 7.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 347 FLFLGSSGIGKTELAKQTAKYMHKDakKGFIRL---DMSE---FQERH---EVAKFIGSPpgyigheeggqLTKKLKqcP 417
Cdd:pfam07728 2 VLLVGPPGTGKTELAERLAAALSNR--PVFYVQltrDTTEedlFGRRNidpGGASWVDGP-----------LVRAAR--E 66
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1395168490 418 NAVVLFDEVDKAHPDVLTIMLQLFDEGRLTDGKGKT-IDCKDAIF--IMTSN 466
Cdd:pfam07728 67 GEIAVLDEINRANPDVLNSLLSLLDERRLLLPDGGElVKAAPDGFrlIATMN 118
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
150-195 |
2.37e-06 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 50.41 E-value: 2.37e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1395168490 150 VRRLLSEGADVNARHKLGWTALMVASISHNESVVQVLLAAGADPNL 195
Cdd:PHA03095 240 VLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINA 285
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
344-466 |
3.50e-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: 49.91 E-value: 3.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 344 PLVFLFLGSSGIGKTELAKQTAKYMHKDakkgFIRLDMSEFqerheVAKfigsppgYIGHEEGG--QLTKKLKQCPNAVV 421
Cdd:COG0464 191 PRGLLLYGPPGTGKTLLARALAGELGLP----LIEVDLSDL-----VSK-------YVGETEKNlrEVFDKARGLAPCVL 254
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1395168490 422 LFDEVDKAHPD-----------VLTIMLQLFDEGRltdgkgktidcKDAIFIMTSN 466
Cdd:COG0464 255 FIDEADALAGKrgevgdgvgrrVVNTLLTEMEELR-----------SDVVVIAATN 299
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
235-267 |
7.11e-06 |
|
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: 43.05 E-value: 7.11e-06
10 20 30
....*....|....*....|....*....|....
gi 1395168490 235 KGCTALHYAVL-ADDYSIVKELLDRGANPLQRNE 267
Cdd:pfam00023 1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
235-262 |
1.27e-05 |
|
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: 42.19 E-value: 1.27e-05
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
130-201 |
6.08e-05 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 46.40 E-value: 6.08e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1395168490 130 NPSNKDAALMEAARANNVQEVRRLLSEGADVNARHKLGWTALMVASISHNESVVQVLLAAGAD---PNLGDEFSS 201
Cdd:PLN03192 618 DPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADvdkANTDDDFSP 692
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
146-276 |
6.44e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 45.72 E-value: 6.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 146 NVQEVRRLLSEGADVNARHKLGWTALMVASISHNESVVQVLLAAGADPNLGDEFSS--VYKTANEQGVHSLEVLVTREDD 223
Cdd:PHA02874 103 EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCypIHIAIKHNFFDIIKLLLEKGAY 182
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1395168490 224 FNNRLNHrasfkGCTALHYAVLADDYSIVKELLDRGANPLQRNEMGHTPLDYA 276
Cdd:PHA02874 183 ANVKDNN-----GESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNA 230
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
240-285 |
9.19e-05 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 41.64 E-value: 9.19e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1395168490 240 LHYAVLADDYSIVKELLDRGANPLQRNEMGHTPLDYA-REG--EVMKLL 285
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAaKNGhlEIVKLL 49
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
141-273 |
1.27e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 45.44 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 141 AARANNVQEVRRLLSEGADVNARHKLGWTALMVASISHNESVVQVLLAAGADPNLGDeFSSVYKTANEQGVHSLEVL--- 217
Cdd:PHA02876 185 AAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKND-LSLLKAIRNEDLETSLLLYdag 263
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1395168490 218 --VTREDDFNNrlnhrasfkgcTALHYAVLADDYS-IVKELLDRGANPLQRNEMGHTPL 273
Cdd:PHA02876 264 fsVNSIDDCKN-----------TPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPL 311
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
138-276 |
1.32e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 44.95 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 138 LMEAARANNVQEVRRLLSEGADVNARHKLGWTALMVASISHNESVVQVLLAAGADPNLGDEF--SSVYKTANEQGVHSLE 215
Cdd:PHA02874 128 LHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNgeSPLHNAAEYGDYACIK 207
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1395168490 216 VLVTREDDFNNRLNhrasfKGCTALHYAVLADDYSIvkELLDRGANPLQRNEMGHTPLDYA 276
Cdd:PHA02874 208 LLIDHGNHIMNKCK-----NGFTPLHNAIIHNRSAI--ELLINNASINDQDIDGSTPLHHA 261
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
138-295 |
1.51e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 44.57 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 138 LMEAARANNVQEVRRLLSEGADVNARHKLGWTALMVASISHNESVVQVLLAAGAD------PNLGDEfssVYKTANEQGV 211
Cdd:PHA02874 39 LIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDtsilpiPCIEKD---MIKTILDCGI 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 212 HS----------LEVLVTRED--DFNNRLNHRASF-----KGCTALHYAVLADDYSIVKELLDRGANPLQRNEMGHTPLD 274
Cdd:PHA02874 116 DVnikdaelktfLHYAIKKGDleSIKMLFEYGADVnieddNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLH 195
|
170 180
....*....|....*....|....
gi 1395168490 275 YARE-GE--VMKLLKTSETKYMEK 295
Cdd:PHA02874 196 NAAEyGDyaCIKLLIDHGNHIMNK 219
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
133-276 |
1.97e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 44.21 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 133 NKDAALMEAARANNVQEVRRLLSEGADVNARHKLGWTALMVASISHNESVVQVLLAAGADPNLG--DEFSSVYKTANEQG 210
Cdd:PHA02875 1 MDQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKypDIESELHDAVEEGD 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1395168490 211 VHSLEVLVtredDFNNRLNHRASFKGCTALHYAVLADDYSIVKELLDRGANPLQRNEMGHTPLDYA 276
Cdd:PHA02875 81 VKAVEELL----DLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLA 142
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
132-261 |
2.13e-04 |
|
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: 44.69 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 132 SNKDAALMEAARANNVQEVRRLLSEGA--DVNARHKLGWTALMVASI-SHNESVVQVLLAAGADPNLGDefSSVYKTANE 208
Cdd:TIGR00870 15 SDEEKAFLPAAERGDLASVYRDLEEPKklNINCPDRLGRSALFVAAIeNENLELTELLLNLSCRGAVGD--TLLHAISLE 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1395168490 209 --QGVHSLEVL---VTREDDFNNRLNHRAS---FKGCTALHYAVLADDYSIVKELLDRGAN 261
Cdd:TIGR00870 93 yvDAVEAILLHllaAFRKSGPLELANDQYTsefTPGITALHLAAHRQNYEIVKLLLERGAS 153
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
137-192 |
2.62e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 43.89 E-value: 2.62e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1395168490 137 ALMEAARANNVQEVRRLLSEGADVNARHKLGWTALMVASISHNESVVQVLLAAGAD 192
Cdd:PHA03100 195 PLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
138-197 |
3.77e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 43.73 E-value: 3.77e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 138 LMEAARANNVQEVRRLLSEGADVNARHKLGWTALMVASISHNESVVQVLLAAGADPNLGD 197
Cdd:PTZ00322 86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLD 145
|
|
| Zeta_toxin |
pfam06414 |
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is ... |
342-415 |
3.85e-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: 41.96 E-value: 3.85e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1395168490 342 EHPLVFLFLGSSGIGKTELAKQTAKYMhkDAKKGFIRLDMSEFQERH-EVAKFIGSPP---GYIGHEEGGQLTKKLKQ 415
Cdd:pfam06414 9 ERPKAILLGGQPGAGKTELARALLDEL--GRQGNVVRIDPDDFRELHpHYRELQAADPktaSEYTQPDASRWVEKLLQ 84
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
167-198 |
4.11e-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: 38.04 E-value: 4.11e-04
10 20 30
....*....|....*....|....*....|...
gi 1395168490 167 GWTALMVASISH-NESVVQVLLAAGADPNLGDE 198
Cdd:pfam00023 2 GNTPLHLAAGRRgNLEIVKLLLSKGADVNARDK 34
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
235-262 |
5.51e-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.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 37.62 E-value: 5.51e-04
10 20
....*....|....*....|....*...
gi 1395168490 235 KGCTALHYAVLADDYSIVKELLDRGANP 262
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADI 28
|
|
| RecA-like_Lon |
cd19500 |
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ... |
346-487 |
1.24e-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: 40.23 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 346 VFLFLGSSGIGKTELAKQTAKYMHKDakkgFIRL------DMSEFqeRHEVAKFIGSPPGYIgheeggqlTKKLKQCP-- 417
Cdd:cd19500 39 ILCLVGPPGVGKTSLGKSIARALGRK----FVRIslggvrDEAEI--RGHRRTYVGAMPGRI--------IQALKKAGtn 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1395168490 418 NAVVLFDEVDK----AHPDVLTIMLQLFD---EGRLTDGK-GKTIDCKDAIFIMTSNVAsDEIAQhALQLRQEALEMS 487
Cdd:cd19500 105 NPVFLLDEIDKigssFRGDPASALLEVLDpeqNSTFSDHYlDVPFDLSKVLFIATANSL-DTIPG-PLLDRMEIIELS 180
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
167-195 |
2.38e-03 |
|
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: 36.03 E-value: 2.38e-03
10 20
....*....|....*....|....*....
gi 1395168490 167 GWTALMVASISHNESVVQVLLAAGADPNL 195
Cdd:smart00248 2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
238-276 |
2.56e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 36.48 E-value: 2.56e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1395168490 238 TALHYAVLADDYSIVKELLDRGANPLQRNEMGHTPLDYA 276
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFA 41
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
153-199 |
3.14e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 36.17 E-value: 3.14e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1395168490 153 LLSEG-ADVNARHKLGWTALMVASISHNESVVQVLLAAGADPNLGDEF 199
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEE 48
|
|
| RPT1 |
COG1222 |
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ... |
347-427 |
4.06e-03 |
|
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440835 [Multi-domain] Cd Length: 326 Bit Score: 39.99 E-value: 4.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 347 FLFLGSSGIGKTELAKQTAKYMhkDAKkgFIRLDMSEFqerheVAKFIGsppgyigheEGGQLTKKL----KQCPNAVVL 422
Cdd:COG1222 115 VLLYGPPGTGKTLLAKAVAGEL--GAP--FIRVRGSEL-----VSKYIG---------EGARNVREVfelaREKAPSIIF 176
|
....*
gi 1395168490 423 FDEVD 427
Cdd:COG1222 177 IDEID 181
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
137-174 |
6.85e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 35.40 E-value: 6.85e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1395168490 137 ALMEAARANNVQEVRRLLSEGADVNARHKLGWTALMVA 174
Cdd:pfam13857 19 PLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| ftsH |
CHL00176 |
cell division protein; Validated |
343-427 |
8.14e-03 |
|
cell division protein; Validated
Pssm-ID: 214386 [Multi-domain] Cd Length: 638 Bit Score: 39.26 E-value: 8.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168490 343 HPLVFLFLGSSGIGKTELAKQTAkymhKDAKKGFIRLDMSEFQERhevakFIGsppgyIGHEEGGQLTKKLKQCPNAVVL 422
Cdd:CHL00176 215 IPKGVLLVGPPGTGKTLLAKAIA----GEAEVPFFSISGSEFVEM-----FVG-----VGAARVRDLFKKAKENSPCIVF 280
|
....*
gi 1395168490 423 FDEVD 427
Cdd:CHL00176 281 IDEID 285
|
|
| |
