|
Name |
Accession |
Description |
Interval |
E-value |
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
309-625 |
9.55e-97 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 316.25 E-value: 9.55e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 309 LEQRLKEHIIGQESAIATVGAAIRRKENGWYDEEHPL-VFLFLGSSGIGKTELAKQTAKYMHkDAKKGFIRLDMSEFQER 387
Cdd:COG0542 543 LEEELHERVIGQDEAVEAVADAIRRSRAGLKDPNRPIgSFLFLGPTGVGKTELAKALAEFLF-GDEDALIRIDMSEYMEK 621
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 388 HEVAKFIGSPPGYIGHEEGGQLTKKLKQCPNAVVLFDEVDKAHPDVLTIMLQLFDEGRLTDGKGKTIDCKDAIFIMTSNV 467
Cdd:COG0542 622 HSVSRLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLLDEIEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTIIIMTSNI 701
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 468 ASDEIAQHAlqlrqealemsrnriaenlGDVQISDKItisknfkENVIRPILKAHFrRDEFLGRINEIVYFLPFCHSELI 547
Cdd:COG0542 702 GSELILDLA-------------------EDEPDYEEM-------KEAVMEELKKHF-RPEFLNRIDEIIVFHPLSKEELR 754
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1937369566 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 |
1.14e-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: 270.67 E-value: 1.14e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 278 EGEVMKLLKtsetkymekqrkreaeerrrfpLEQRLKEHIIGQESAIATVGAAIRRKENGWYDEEHPL-VFLFLGSSGIG 356
Cdd:TIGR03346 549 EGEREKLLH----------------------MEEELHERVVGQDEAVEAVSDAIRRSRAGLSDPNRPIgSFLFLGPTGVG 606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 357 KTELAKQTAKYMHkDAKKGFIRLDMSEFQERHEVAKFIGSPPGYIGHEEGGQLTKKLKQCPNAVVLFDEVDKAHPDVLTI 436
Cdd:TIGR03346 607 KTELAKALAEFLF-DSEDAMVRIDMSEYMEKHSVARLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLFDEVEKAHPDVFNV 685
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 437 MLQLFDEGRLTDGKGKTIDCKDAIFIMTSNVASDEIAQhalQLRQEALEMSRNRIAEnlgdvqisdkitisknfkenvir 516
Cdd:TIGR03346 686 LLQVLDDGRLTDGQGRTVDFRNTVIIMTSNLGSDFIQE---LAGGDDYEEMREAVME----------------------- 739
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 517 pILKAHFrRDEFLGRINEIVYFLPFCHSELIQLVNKELNFWAKRAKQRHnITLLWDREVADVLVD-GYNVHYGARSIKHE 595
Cdd:TIGR03346 740 -VLRAHF-RPEFLNRIDEIVVFHPLGREQIARIVEIQLGRLRKRLAERK-ITLELSDAALDFLAEaGYDPVYGARPLKRA 816
|
330 340 350
....*....|....*....|....*....|....
gi 1937369566 596 VERRVVNQLAaayeQDLLPG----GCTLRITVED 625
Cdd:TIGR03346 817 IQREIENPLA----KKILAGevapGDTIRVDVEG 846
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
309-471 |
7.14e-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: 246.32 E-value: 7.14e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 309 LEQRLKEHIIGQESAIATVGAAIRRKENGWYDEEHPL-VFLFLGSSGIGKTELAKQTAKYMHKDaKKGFIRLDMSEFQER 387
Cdd:cd19499 5 LEERLHERVVGQDEAVKAVSDAIRRARAGLSDPNRPIgSFLFLGPTGVGKTELAKALAELLFGD-EDNLIRIDMSEYMEK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 388 HEVAKFIGSPPGYIGHEEGGQLTKKLKQCPNAVVLFDEVDKAHPDVLTIMLQLFDEGRLTDGKGKTIDCKDAIFIMTSNV 467
Cdd:cd19499 84 HSVSRLIGAPPGYVGYTEGGQLTEAVRRKPYSVVLLDEIEKAHPDVQNLLLQVLDDGRLTDSHGRTVDFKNTIIIMTSNH 163
|
....
gi 1937369566 468 ASDE 471
Cdd:cd19499 164 FRPE 167
|
|
| clpC |
CHL00095 |
Clp protease ATP binding subunit |
281-625 |
1.11e-77 |
|
Clp protease ATP binding subunit
Pssm-ID: 214361 [Multi-domain] Cd Length: 821 Bit Score: 264.61 E-value: 1.11e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 281 VMKLLKTSETKYMEkqrkreaeerrrfpLEQRLKEHIIGQESAIATVGAAIRRKENGWYDEEHPLV-FLFLGSSGIGKTE 359
Cdd:CHL00095 489 VNKLTKSESEKLLH--------------MEETLHKRIIGQDEAVVAVSKAIRRARVGLKNPNRPIAsFLFSGPTGVGKTE 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 360 LAKQTAKYMHkDAKKGFIRLDMSEFQERHEVAKFIGSPPGYIGHEEGGQLTKKLKQCPNAVVLFDEVDKAHPDVLTIMLQ 439
Cdd:CHL00095 555 LTKALASYFF-GSEDAMIRLDMSEYMEKHTVSKLIGSPPGYVGYNEGGQLTEAVRKKPYTVVLFDEIEKAHPDIFNLLLQ 633
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 440 LFDEGRLTDGKGKTIDCKDAIFIMTSNVASdeiaqhalqlrqealemsrNRIAENLGDVQI--SDKITISKNFKE--NVI 515
Cdd:CHL00095 634 ILDDGRLTDSKGRTIDFKNTLIIMTSNLGS-------------------KVIETNSGGLGFelSENQLSEKQYKRlsNLV 694
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 516 RPILKAHFrRDEFLGRINEIVYFLPFCHSELIQLVNKELNFWAKRAKQRhNITLLWDREVADVLVD-GYNVHYGARSIKH 594
Cdd:CHL00095 695 NEELKQFF-RPEFLNRLDEIIVFRQLTKNDVWEIAEIMLKNLFKRLNEQ-GIQLEVTERIKTLLIEeGYNPLYGARPLRR 772
|
330 340 350
....*....|....*....|....*....|.
gi 1937369566 595 EVERRVVNQLAAAYEQDLLPGGCTLRITVED 625
Cdd:CHL00095 773 AIMRLLEDPLAEEVLSFKIKPGDIIIVDVND 803
|
|
| AAA_2 |
pfam07724 |
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ... |
346-535 |
1.52e-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: 215.91 E-value: 1.52e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 346 VFLFLGSSGIGKTELAKQTAKYMHKDAKKgFIRLDMSEFQERHEVAKFIGSPPGYIGHEEGGQLTKKLKQCPNAVVLFDE 425
Cdd:pfam07724 5 SFLFLGPTGVGKTELAKALAELLFGDERA-LIRIDMSEYMEEHSVSRLIGAPPGYVGYEEGGQLTEAVRRKPYSIVLIDE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 426 VDKAHPDVLTIMLQLFDEGRLTDGKGKTIDCKDAIFIMTSNVASDEIAQHALqlrqealemsrnriaenlgdvqisDKIT 505
Cdd:pfam07724 84 IEKAHPGVQNDLLQILEGGTLTDKQGRTVDFKNTLFIMTGNFGSEKISDASR------------------------LGDS 139
|
170 180 190
....*....|....*....|....*....|
gi 1937369566 506 ISKNFKENVIRPILKAHFRRdEFLGRINEI 535
Cdd:pfam07724 140 PDYELLKEEVMDLLKKGFIP-EFLGRLPII 168
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
128-286 |
1.15e-27 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 113.51 E-value: 1.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 128 NKNPSNKDAALMEAARANNVQEVRRLLSEGADVNARHKLGWTALMVAAISHNESVVQVLLAAGADPNLGDD--FSSVYKT 205
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNdgNTPLHLA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 206 ANEQGVHSLEVLVTREDDFNNRLNHrasfkGCTALHYAVLADDYSIVKELLGGGANPLQRNEMGHTPLDYARE---GEVM 282
Cdd:COG0666 161 AANGNLEIVKLLLEAGADVNARDND-----GETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAEngnLEIV 235
|
....
gi 1937369566 283 KLLK 286
Cdd:COG0666 236 KLLL 239
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
138-266 |
2.81e-15 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 71.69 E-value: 2.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 138 LMEAARANNVQEVRRLLSEGADVNARHKLGWTALMVAAISHNESVVQVLLaAGADPNLGDDfssvyktaneqgvhslevl 217
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKDN------------------- 60
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1937369566 218 vtreddfnnrlnhrasfkGCTALHYAVLADDYSIVKELLGGGANPLQRN 266
Cdd:pfam12796 61 ------------------GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
343-480 |
2.65e-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: 62.01 E-value: 2.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 343 HPLVFLFLGSSGIGKTELAKQTAKYMHKDaKKGFIRLDMSEFQERHEVAKFIGSPPGYIGHEEGGQ----LTKKLKQCPN 418
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPP-GGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELrlrlALALARKLKP 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937369566 419 AVVLFDEVDKAHPDVLTIMLQLFDEGRLTDGKGKtidCKDAIFIMTSNVASDEIAqHALQLR 480
Cdd:smart00382 80 DVLILDEITSLLDAEQEALLLLLEELRLLLLLKS---EKNLTVILTTNDEKDLGP-ALLRRR 137
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
126-260 |
4.29e-09 |
|
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: 59.64 E-value: 4.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 126 CYNKNPSnkDAALMEAARANNVQEVRRLL-SEGADVNARHKLGWTALMVAAISHNESVVQVLLAagADPNLgddfssvyk 204
Cdd:cd22192 11 LQQKRIS--ESPLLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPEL--------- 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1937369566 205 tANEQGVHSLevlvtreddfnnrlnhrasFKGCTALHYAVLADDYSIVKELLGGGA 260
Cdd:cd22192 78 -VNEPMTSDL-------------------YQGETALHIAVVNQNLNLVRELIARGA 113
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
127-285 |
1.12e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 57.75 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 127 YNKNPSNKDAALMeaARANNVQEVRRLLSE-GADVNARHKLGWTALMVAAISHNESV--VQVLLAAGADPNL----GDDF 199
Cdd:PHA03100 67 NNSTPLHYLSNIK--YNLTDVKEIVKLLLEyGANVNAPDNNGITPLLYAISKKSNSYsiVEYLLDNGANVNIknsdGENL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 200 SSVYKTANEQGVHSLEVLVTREDDFN--NRLNHRASF---------KGCTALHYAVLADDYSIVKELLGGGANPLQRNEM 268
Cdd:PHA03100 145 LHLYLESNKIDLKILKLLIDKGVDINakNRVNYLLSYgvpinikdvYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKY 224
|
170 180
....*....|....*....|
gi 1937369566 269 GHTPLDYA---REGEVMKLL 285
Cdd:PHA03100 225 GDTPLHIAilnNNKEIFKLL 244
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
235-262 |
4.55e-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: 37.95 E-value: 4.55e-04
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
132-261 |
1.92e-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: 41.61 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 132 SNKDAALMEAARANNVQEVRRLLSEGA--DVNARHKLGWTALMVAAI-SHNESVVQVLLAAGADPNLGDdfSSVYKTANE 208
Cdd:TIGR00870 15 SDEEKAFLPAAERGDLASVYRDLEEPKklNINCPDRLGRSALFVAAIeNENLELTELLLNLSCRGAVGD--TLLHAISLE 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1937369566 209 --QGVHSLEVL---VTREDDFNNRLNHRAS---FKGCTALHYAVLADDYSIVKELLGGGAN 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 |
9.55e-97 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 316.25 E-value: 9.55e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 309 LEQRLKEHIIGQESAIATVGAAIRRKENGWYDEEHPL-VFLFLGSSGIGKTELAKQTAKYMHkDAKKGFIRLDMSEFQER 387
Cdd:COG0542 543 LEEELHERVIGQDEAVEAVADAIRRSRAGLKDPNRPIgSFLFLGPTGVGKTELAKALAEFLF-GDEDALIRIDMSEYMEK 621
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 388 HEVAKFIGSPPGYIGHEEGGQLTKKLKQCPNAVVLFDEVDKAHPDVLTIMLQLFDEGRLTDGKGKTIDCKDAIFIMTSNV 467
Cdd:COG0542 622 HSVSRLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLLDEIEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTIIIMTSNI 701
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 468 ASDEIAQHAlqlrqealemsrnriaenlGDVQISDKItisknfkENVIRPILKAHFrRDEFLGRINEIVYFLPFCHSELI 547
Cdd:COG0542 702 GSELILDLA-------------------EDEPDYEEM-------KEAVMEELKKHF-RPEFLNRIDEIIVFHPLSKEELR 754
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1937369566 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 |
1.14e-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: 270.67 E-value: 1.14e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 278 EGEVMKLLKtsetkymekqrkreaeerrrfpLEQRLKEHIIGQESAIATVGAAIRRKENGWYDEEHPL-VFLFLGSSGIG 356
Cdd:TIGR03346 549 EGEREKLLH----------------------MEEELHERVVGQDEAVEAVSDAIRRSRAGLSDPNRPIgSFLFLGPTGVG 606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 357 KTELAKQTAKYMHkDAKKGFIRLDMSEFQERHEVAKFIGSPPGYIGHEEGGQLTKKLKQCPNAVVLFDEVDKAHPDVLTI 436
Cdd:TIGR03346 607 KTELAKALAEFLF-DSEDAMVRIDMSEYMEKHSVARLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLFDEVEKAHPDVFNV 685
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 437 MLQLFDEGRLTDGKGKTIDCKDAIFIMTSNVASDEIAQhalQLRQEALEMSRNRIAEnlgdvqisdkitisknfkenvir 516
Cdd:TIGR03346 686 LLQVLDDGRLTDGQGRTVDFRNTVIIMTSNLGSDFIQE---LAGGDDYEEMREAVME----------------------- 739
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 517 pILKAHFrRDEFLGRINEIVYFLPFCHSELIQLVNKELNFWAKRAKQRHnITLLWDREVADVLVD-GYNVHYGARSIKHE 595
Cdd:TIGR03346 740 -VLRAHF-RPEFLNRIDEIVVFHPLGREQIARIVEIQLGRLRKRLAERK-ITLELSDAALDFLAEaGYDPVYGARPLKRA 816
|
330 340 350
....*....|....*....|....*....|....
gi 1937369566 596 VERRVVNQLAaayeQDLLPG----GCTLRITVED 625
Cdd:TIGR03346 817 IQREIENPLA----KKILAGevapGDTIRVDVEG 846
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
309-471 |
7.14e-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: 246.32 E-value: 7.14e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 309 LEQRLKEHIIGQESAIATVGAAIRRKENGWYDEEHPL-VFLFLGSSGIGKTELAKQTAKYMHKDaKKGFIRLDMSEFQER 387
Cdd:cd19499 5 LEERLHERVVGQDEAVKAVSDAIRRARAGLSDPNRPIgSFLFLGPTGVGKTELAKALAELLFGD-EDNLIRIDMSEYMEK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 388 HEVAKFIGSPPGYIGHEEGGQLTKKLKQCPNAVVLFDEVDKAHPDVLTIMLQLFDEGRLTDGKGKTIDCKDAIFIMTSNV 467
Cdd:cd19499 84 HSVSRLIGAPPGYVGYTEGGQLTEAVRRKPYSVVLLDEIEKAHPDVQNLLLQVLDDGRLTDSHGRTVDFKNTIIIMTSNH 163
|
....
gi 1937369566 468 ASDE 471
Cdd:cd19499 164 FRPE 167
|
|
| clpC |
CHL00095 |
Clp protease ATP binding subunit |
281-625 |
1.11e-77 |
|
Clp protease ATP binding subunit
Pssm-ID: 214361 [Multi-domain] Cd Length: 821 Bit Score: 264.61 E-value: 1.11e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 281 VMKLLKTSETKYMEkqrkreaeerrrfpLEQRLKEHIIGQESAIATVGAAIRRKENGWYDEEHPLV-FLFLGSSGIGKTE 359
Cdd:CHL00095 489 VNKLTKSESEKLLH--------------MEETLHKRIIGQDEAVVAVSKAIRRARVGLKNPNRPIAsFLFSGPTGVGKTE 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 360 LAKQTAKYMHkDAKKGFIRLDMSEFQERHEVAKFIGSPPGYIGHEEGGQLTKKLKQCPNAVVLFDEVDKAHPDVLTIMLQ 439
Cdd:CHL00095 555 LTKALASYFF-GSEDAMIRLDMSEYMEKHTVSKLIGSPPGYVGYNEGGQLTEAVRKKPYTVVLFDEIEKAHPDIFNLLLQ 633
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 440 LFDEGRLTDGKGKTIDCKDAIFIMTSNVASdeiaqhalqlrqealemsrNRIAENLGDVQI--SDKITISKNFKE--NVI 515
Cdd:CHL00095 634 ILDDGRLTDSKGRTIDFKNTLIIMTSNLGS-------------------KVIETNSGGLGFelSENQLSEKQYKRlsNLV 694
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 516 RPILKAHFrRDEFLGRINEIVYFLPFCHSELIQLVNKELNFWAKRAKQRhNITLLWDREVADVLVD-GYNVHYGARSIKH 594
Cdd:CHL00095 695 NEELKQFF-RPEFLNRLDEIIVFRQLTKNDVWEIAEIMLKNLFKRLNEQ-GIQLEVTERIKTLLIEeGYNPLYGARPLRR 772
|
330 340 350
....*....|....*....|....*....|.
gi 1937369566 595 EVERRVVNQLAAAYEQDLLPGGCTLRITVED 625
Cdd:CHL00095 773 AIMRLLEDPLAEEVLSFKIKPGDIIIVDVND 803
|
|
| AAA_2 |
pfam07724 |
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ... |
346-535 |
1.52e-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: 215.91 E-value: 1.52e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 346 VFLFLGSSGIGKTELAKQTAKYMHKDAKKgFIRLDMSEFQERHEVAKFIGSPPGYIGHEEGGQLTKKLKQCPNAVVLFDE 425
Cdd:pfam07724 5 SFLFLGPTGVGKTELAKALAELLFGDERA-LIRIDMSEYMEEHSVSRLIGAPPGYVGYEEGGQLTEAVRRKPYSIVLIDE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 426 VDKAHPDVLTIMLQLFDEGRLTDGKGKTIDCKDAIFIMTSNVASDEIAQHALqlrqealemsrnriaenlgdvqisDKIT 505
Cdd:pfam07724 84 IEKAHPGVQNDLLQILEGGTLTDKQGRTVDFKNTLFIMTGNFGSEKISDASR------------------------LGDS 139
|
170 180 190
....*....|....*....|....*....|
gi 1937369566 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: 228.37 E-value: 4.26e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 309 LEQRLKEHIIGQESAIATVGAAIRRKENGWYDEEHPL-VFLFLGSSGIGKTELAKQTAKYMhkdakkG--FIRLDMSEFQ 385
Cdd:TIGR02639 447 LEKNLKAKIFGQDEAIDQLVSAIKRSRAGLGDPNKPVgSFLFVGPTGVGKTELAKQLAEEL------GvhLLRFDMSEYM 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 386 ERHEVAKFIGSPPGYIGHEEGGQLTKKLKQCPNAVVLFDEVDKAHPDVLTIMLQLFDEGRLTDGKGKTIDCKDAIFIMTS 465
Cdd:TIGR02639 521 EKHTVSRLIGSPPGYVGFEQGGLLTDAVRKHPHCVLLLDEIEKAHPDIYNILLQVMDYATLTDNNGRKADFRNVILIMTS 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 466 NVASDEIAQHALQLRQEALEMSRNRiaenlgdvqisdkiTISKNFKenvirPilkahfrrdEFLGRINEIVYFLPFCHSE 545
Cdd:TIGR02639 601 NAGASEMSKPPIGFGGENRESKSLK--------------AIKKLFS-----P---------EFRNRLDAIIHFNDLSEEM 652
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1937369566 546 LIQLVNKELNFWAKRAKQRhNITLLWDREVADVLVD-GYNVHYGARSIKHEVERRVVNQLA 605
Cdd:TIGR02639 653 AEKIVKKFLDELQDQLNEK-NIELELTDDAKKYLAEkGYDEEFGARPLARVIQEEIKKPLS 712
|
|
| PRK10865 |
PRK10865 |
ATP-dependent chaperone ClpB; |
309-626 |
1.56e-60 |
|
ATP-dependent chaperone ClpB;
Pssm-ID: 182791 [Multi-domain] Cd Length: 857 Bit Score: 217.79 E-value: 1.56e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 309 LEQRLKEHIIGQESAIATVGAAIRRKENGWYDEEHPL-VFLFLGSSGIGKTELAKQTAKYMHkDAKKGFIRLDMSEFQER 387
Cdd:PRK10865 562 MEQELHHRVIGQNEAVEAVSNAIRRSRAGLSDPNRPIgSFLFLGPTGVGKTELCKALANFMF-DSDDAMVRIDMSEFMEK 640
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 388 HEVAKFIGSPPGYIGHEEGGQLTKKLKQCPNAVVLFDEVDKAHPDVLTIMLQLFDEGRLTDGKGKTIDCKDAIFIMTSNV 467
Cdd:PRK10865 641 HSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTVVIMTSNL 720
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 468 ASDeiaqhalqlrqealemsrnRIAENLGDVQISDkitisknFKENVIRpILKAHFrRDEFLGRINEIVYFLPFCHSELI 547
Cdd:PRK10865 721 GSD-------------------LIQERFGELDYAH-------MKELVLG-VVSHNF-RPEFINRIDEVVVFHPLGEQHIA 772
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 548 QLVNKELNFWAKRAKQRHNITLLWDREVADVLVDGYNVHYGARSIKHEVERRVVNQLAaayeQDLLPG----GCTLRITV 623
Cdd:PRK10865 773 SIAQIQLQRLYKRLEERGYEIHISDEALKLLSENGYDPVYGARPLKRAIQQQIENPLA----QQILSGelvpGKVIRLEV 848
|
...
gi 1937369566 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 |
1.51e-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: 214.81 E-value: 1.51e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 309 LEQRLKEHIIGQESAIATVGAAIRRKENGWYDEEHPL-VFLFLGSSGIGKTELAKQTAKYMHkDAKKGFIRLDMSEFQER 387
Cdd:TIGR03345 560 LPDRLAERVIGQDHALEAIAERIRTARAGLEDPRKPLgVFLLVGPSGVGKTETALALAELLY-GGEQNLITINMSEFQEA 638
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 388 HEVAKFIGSPPGYIGHEEGGQLTKKLKQCPNAVVLFDEVDKAHPDVLTIMLQLFDEGRLTDGKGKTIDCKDAIFIMTSNV 467
Cdd:TIGR03345 639 HTVSRLKGSPPGYVGYGEGGVLTEAVRRKPYSVVLLDEVEKAHPDVLELFYQVFDKGVMEDGEGREIDFKNTVILLTSNA 718
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 468 ASDEIAQHALqlrQEALEMSRNRIAENLgdvqisdkitisknfkenviRPILKAHFrRDEFLGRINeIVYFLPFCHSELI 547
Cdd:TIGR03345 719 GSDLIMALCA---DPETAPDPEALLEAL--------------------RPELLKVF-KPAFLGRMT-VIPYLPLDDDVLA 773
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1937369566 548 QLVNKELNFWAKRAKQRHNITLLWDREVADVLVDGYN-VHYGARSIKHEVERRVVNQLA 605
Cdd:TIGR03345 774 AIVRLKLDRIARRLKENHGAELVYSEALVEHIVARCTeVESGARNIDAILNQTLLPELS 832
|
|
| clpA |
PRK11034 |
ATP-dependent Clp protease ATP-binding subunit; Provisional |
309-630 |
1.54e-40 |
|
ATP-dependent Clp protease ATP-binding subunit; Provisional
Pssm-ID: 236828 [Multi-domain] Cd Length: 758 Bit Score: 158.46 E-value: 1.54e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 309 LEQRLKEHIIGQESAIATVGAAIRRKENGWYDEEHPL-VFLFLGSSGIGKTELAKQTAKYMHKDakkgFIRLDMSEFQER 387
Cdd:PRK11034 452 LGDRLKMLVFGQDKAIEALTEAIKMSRAGLGHEHKPVgSFLFAGPTGVGKTEVTVQLSKALGIE----LLRFDMSEYMER 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 388 HEVAKFIGSPPGYIGHEEGGQLTKKLKQCPNAVVLFDEVDKAHPDVLTIMLQLFDEGRLTDGKGKTIDCKDAIFIMTSNV 467
Cdd:PRK11034 528 HTVSRLIGAPPGYVGFDQGGLLTDAVIKHPHAVLLLDEIEKAHPDVFNLLLQVMDNGTLTDNNGRKADFRNVVLVMTTNA 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 468 ASDEIAQHALQLRQEalEMSRNRIAEnlgdvqisdkitISKNFKEnvirpilkahfrrdEFLGRINEIVYFLPFCHSELI 547
Cdd:PRK11034 608 GVRETERKSIGLIHQ--DNSTDAMEE------------IKKIFTP--------------EFRNRLDNIIWFDHLSTDVIH 659
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 548 QLVNKelnFWAKRAKQ--RHNITLLWDREVADVLVD-GYNVHYGARSIKHEVERRVVNQLAAAYEQDLLPGGCTLRITVE 624
Cdd:PRK11034 660 QVVDK---FIVELQAQldQKGVSLEVSQEARDWLAEkGYDRAMGARPMARVIQDNLKKPLANELLFGSLVDGGQVTVALD 736
|
....*.
gi 1937369566 625 DSDKQL 630
Cdd:PRK11034 737 KEKNEL 742
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
128-286 |
1.15e-27 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 113.51 E-value: 1.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 128 NKNPSNKDAALMEAARANNVQEVRRLLSEGADVNARHKLGWTALMVAAISHNESVVQVLLAAGADPNLGDD--FSSVYKT 205
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNdgNTPLHLA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 206 ANEQGVHSLEVLVTREDDFNNRLNHrasfkGCTALHYAVLADDYSIVKELLGGGANPLQRNEMGHTPLDYARE---GEVM 282
Cdd:COG0666 161 AANGNLEIVKLLLEAGADVNARDND-----GETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAEngnLEIV 235
|
....
gi 1937369566 283 KLLK 286
Cdd:COG0666 236 KLLL 239
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
132-286 |
3.63e-21 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 94.25 E-value: 3.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 132 SNKDAALMEAARANNVQEVRRLLSEGADVNARHKLGWTALMVAAISHNESVVQVLLAAGADPNLGDDFssvYKT----AN 207
Cdd:COG0666 118 KDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDND---GETplhlAA 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 208 EQG-VHSLEVLVTREDDFNNRLNhrasfKGCTALHYAVLADDYSIVKELLGGGANPLQRNEMGHTPLDYAREGEVMKLLK 286
Cdd:COG0666 195 ENGhLEIVKLLLEAGADVNAKDN-----DGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVK 269
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
109-285 |
8.10e-20 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 90.40 E-value: 8.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 109 NKAGLGMWALAMALVVQCYNKNPSNKDAALMEAARANNVQEVRRLLSEGADVNARHKLGWTALMVAAISHNESVVQVLLA 188
Cdd:COG0666 29 ALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 189 AGADPNLGD--DFSSVYKTANEQGVHSLEVLVTREDDFNNRLNHrasfkGCTALHYAVLADDYSIVKELLGGGANPLQRN 266
Cdd:COG0666 109 AGADVNARDkdGETPLHLAAYNGNLEIVKLLLEAGADVNAQDND-----GNTPLHLAAANGNLEIVKLLLEAGADVNARD 183
|
170 180
....*....|....*....|..
gi 1937369566 267 EMGHTPLDYAREG---EVMKLL 285
Cdd:COG0666 184 NDGETPLHLAAENghlEIVKLL 205
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
138-266 |
2.81e-15 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 71.69 E-value: 2.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 138 LMEAARANNVQEVRRLLSEGADVNARHKLGWTALMVAAISHNESVVQVLLaAGADPNLGDDfssvyktaneqgvhslevl 217
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKDN------------------- 60
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1937369566 218 vtreddfnnrlnhrasfkGCTALHYAVLADDYSIVKELLGGGANPLQRN 266
Cdd:pfam12796 61 ------------------GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
318-472 |
1.08e-14 |
|
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: 71.79 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 318 IGQESAIATVGAAIRRKengwydeeHPLVFLFLGSSGIGKTELAKQTAKYMHKdAKKGFIRLDMSEFQERHEVAkfigsp 397
Cdd:cd00009 1 VGQEEAIEALREALELP--------PPKNLLLYGPPGTGKTTLARAIANELFR-PGAPFLYLNASDLLEGLVVA------ 65
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1937369566 398 pGYIGHEEGGQLTKKLKQCPNAVVLFDEVDKAHPDVLTIMLQLFDEGRLTdgkgkTIDCKDAIFIMTSNVASDEI 472
Cdd:cd00009 66 -ELFGHFLVRLLFELAEKAKPGVLFIDEIDSLSRGAQNALLRVLETLNDL-----RIDRENVRVIGATNRPLLGD 134
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
111-197 |
1.80e-12 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 63.60 E-value: 1.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 111 AGLGMWALAMALVVQCYNKNPSNKDA--ALMEAARANNVQEVRRLLSEgADVNARHKlGWTALMVAAISHNESVVQVLLA 188
Cdd:pfam12796 5 AKNGNLELVKLLLENGADANLQDKNGrtALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLLE 82
|
....*....
gi 1937369566 189 AGADPNLGD 197
Cdd:pfam12796 83 KGADINVKD 91
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
343-480 |
2.65e-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: 62.01 E-value: 2.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 343 HPLVFLFLGSSGIGKTELAKQTAKYMHKDaKKGFIRLDMSEFQERHEVAKFIGSPPGYIGHEEGGQ----LTKKLKQCPN 418
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPP-GGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELrlrlALALARKLKP 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937369566 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 |
2.06e-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: 2.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 543 HSELIQLVNKELNFWAKRAKQRhNITLLWDREVADVLVD-GYNVHYGARSIKHEVERRVVNQLAAAYEQDLLPGGCTLRI 621
Cdd:pfam10431 3 KEELRKIVDLQLKELQKRLAER-GITLELTDAAKDWLAEkGYDPEYGARPLRRAIQREIEDPLAEEILSGELKEGDTVRV 81
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
137-232 |
2.77e-10 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 61.89 E-value: 2.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 137 ALMEAARANNVQEVRRLLSEGADVNARHKLGWTALMVAAISHNESVVQVLLAAGADPNLGDDFSSVYKTANEQGVHSLEV 216
Cdd:COG0666 189 PLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIV 268
|
90
....*....|....*.
gi 1937369566 217 LVTREDDFNNRLNHRA 232
Cdd:COG0666 269 KLLLLALLLLAAALLD 284
|
|
| ClpB_D2-small |
smart01086 |
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ... |
545-630 |
4.36e-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: 56.68 E-value: 4.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 545 ELIQLVNKELNFWAKRAKQRhNITLLWDREVADVLVD-GYNVHYGARSIKHEVERRVVNQLAAAYEQDLLPGGCTLRITV 623
Cdd:smart01086 5 DLVRIVDLPLNALQKRLAEK-GITLEFTDEALDWLAEkGYDPKYGARPLRRIIQRELEDPLAELILSGELKDGDTVVVDV 83
|
....*..
gi 1937369566 624 EDSDKQL 630
Cdd:smart01086 84 DDGELVF 90
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
126-260 |
4.29e-09 |
|
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: 59.64 E-value: 4.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 126 CYNKNPSnkDAALMEAARANNVQEVRRLL-SEGADVNARHKLGWTALMVAAISHNESVVQVLLAagADPNLgddfssvyk 204
Cdd:cd22192 11 LQQKRIS--ESPLLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPEL--------- 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1937369566 205 tANEQGVHSLevlvtreddfnnrlnhrasFKGCTALHYAVLADDYSIVKELLGGGA 260
Cdd:cd22192 78 -VNEPMTSDL-------------------YQGETALHIAVVNQNLNLVRELIARGA 113
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
127-285 |
1.12e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 57.75 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 127 YNKNPSNKDAALMeaARANNVQEVRRLLSE-GADVNARHKLGWTALMVAAISHNESV--VQVLLAAGADPNL----GDDF 199
Cdd:PHA03100 67 NNSTPLHYLSNIK--YNLTDVKEIVKLLLEyGANVNAPDNNGITPLLYAISKKSNSYsiVEYLLDNGANVNIknsdGENL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 200 SSVYKTANEQGVHSLEVLVTREDDFN--NRLNHRASF---------KGCTALHYAVLADDYSIVKELLGGGANPLQRNEM 268
Cdd:PHA03100 145 LHLYLESNKIDLKILKLLIDKGVDINakNRVNYLLSYgvpinikdvYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKY 224
|
170 180
....*....|....*....|
gi 1937369566 269 GHTPLDYA---REGEVMKLL 285
Cdd:PHA03100 225 GDTPLHIAilnNNKEIFKLL 244
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
128-262 |
2.47e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 56.54 E-value: 2.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 128 NKNPSNKDAALMEAARANNVQEVRRLLSEGADVN-ARHKLGWTALMVAAISHNESVVQVLLAAGADPNLG--DDFSSVYK 204
Cdd:PHA02875 62 DVKYPDIESELHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPntDKFSPLHL 141
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1937369566 205 TANEQGVHSLEVLvtreddfnnrLNHRASFK-----GCTALHYAVLADDYSIVKELLGGGANP 262
Cdd:PHA02875 142 AVMMGDIKGIELL----------IDHKACLDiedccGCTPLIIAMAKGDIAICKMLLDSGANI 194
|
|
| RecA-like_HslU |
cd19498 |
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ... |
311-428 |
2.54e-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: 2.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 311 QRLKEHIIGQESAIATVGAAIRRK------ENGWYDEEHPLVFLFLGSSGIGKTELAKQTAKYmhkdAKKGFIRLDMSEF 384
Cdd:cd19498 7 SELDKYIIGQDEAKRAVAIALRNRwrrmqlPEELRDEVTPKNILMIGPTGVGKTEIARRLAKL----AGAPFIKVEATKF 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1937369566 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 |
3.12e-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: 3.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 332 RRKENGWYDEEHPLVFLFLGSSGIGKTELAKQTAKYMHKDakkgFIRLDMSEFQErhevaKFIGSppgyiGHEEGGQLTK 411
Cdd:cd19481 14 RGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLP----LIVVKLSSLLS-----KYVGE-----SEKNLRKIFE 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1937369566 412 KLKQCPNAVVLFDEVDKAHPD------------VLTIMLQLFDEGRltdgkgktiDCKDAIFIMTSN 466
Cdd:cd19481 80 RARRLAPCILFIDEIDAIGRKrdssgesgelrrVLNQLLTELDGVN---------SRSKVLVIAATN 137
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
137-187 |
5.77e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 49.58 E-value: 5.77e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1937369566 137 ALMEAARANNVQEVRRLLSEGADVNARHKLGWTALMVAAISHNESVVQVLL 187
Cdd:pfam13637 4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
150-276 |
6.98e-08 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 55.42 E-value: 6.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 150 VRRLLSEGADVNARHKLGWTALMVAAISHNESV--VQVLLAAGADPnlgddfssvyktaneqgvhslevlVTREDDFNNR 227
Cdd:PHA03095 135 IRLLLRKGADVNALDLYGMTPLAVLLKSRNANVelLRLLIDAGADV------------------------YAVDDRFRSL 190
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1937369566 228 LNHRA-SFKgctalhyavlaDDYSIVKELLGGGANPLQRNEMGHTPLDYA 276
Cdd:PHA03095 191 LHHHLqSFK-----------PRARIVRELIRAGCDPAATDMLGNTPLHSM 229
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
147-274 |
2.26e-07 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 53.88 E-value: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 147 VQEVRRLLSEGADVNARHKLGWTAL---MVAAISHNESVVQVLLAAGADPNLGD--DFSSVY---KTANEQGVhsLEVLV 218
Cdd:PHA03095 27 VEEVRRLLAAGADVNFRGEYGKTPLhlyLHYSSEKVKDIVRLLLEAGADVNAPErcGFTPLHlylYNATTLDV--IKLLI 104
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1937369566 219 TREDDFNNRlnhraSFKGCTALH-Y-AVLADDYSIVKELLGGGANPLQRNEMGHTPLD 274
Cdd:PHA03095 105 KAGADVNAK-----DKVGRTPLHvYlSGFNINPKVIRLLLRKGADVNALDLYGMTPLA 157
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
347-466 |
7.10e-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: 7.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 347 FLFLGSSGIGKTELAKQTAKYMHKDakKGFIRL---DMSE---FQERH---EVAKFIGSPpgyigheeggqLTKKLKqcP 417
Cdd:pfam07728 2 VLLVGPPGTGKTELAERLAAALSNR--PVFYVQltrDTTEedlFGRRNidpGGASWVDGP-----------LVRAAR--E 66
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1937369566 418 NAVVLFDEVDKAHPDVLTIMLQLFDEGRLTDGKGKT-IDCKDAIF--IMTSN 466
Cdd:pfam07728 67 GEIAVLDEINRANPDVLNSLLSLLDERRLLLPDGGElVKAAPDGFrlIATMN 118
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
348-466 |
7.83e-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: 7.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 348 LFLGSSGIGKTELAKQTAKYMHKDakkgFIRLDMSEFqerheVAKFIGSPPGYIghEEGGQLTKKLKQCpnaVVLFDEVD 427
Cdd:pfam00004 2 LLYGPPGTGKTTLAKAVAKELGAP----FIEISGSEL-----VSKYVGESEKRL--RELFEAAKKLAPC---VIFIDEID 67
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1937369566 428 KAHP-----------DVLTIMLQLFDegrltdgkGKTIDCKDAIFIMTSN 466
Cdd:pfam00004 68 ALAGsrgsggdsesrRVVNQLLTELD--------GFTSSNSKVIVIAATN 109
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
129-285 |
8.44e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 52.37 E-value: 8.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 129 KNPSNKDAALMEAARANNVQEVRRLLSEGADVNARHKLGWTALMVAA-ISHNESVVQVLLAAGADPNLGD--DFSSVYKT 205
Cdd:PHA02876 303 KNIKGETPLYLMAKNGYDTENIRTLIMLGADVNAADRLYITPLHQAStLDRNKDIVITLLELGANVNARDycDKTPIHYA 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 206 ANEQGVhsleVLVTREDDFNNRLNHRASFKGcTALHYAVLADD-YSIVKELLGGGANPLQRNEMGHTPLDYAREG----E 280
Cdd:PHA02876 383 AVRNNV----VIINTLLDYGADIEALSQKIG-TALHFALCGTNpYMSVKTLIDRGANVNSKNKDLSTPLHYACKKncklD 457
|
....*
gi 1937369566 281 VMKLL 285
Cdd:PHA02876 458 VIEML 462
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
150-195 |
1.65e-06 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 51.18 E-value: 1.65e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1937369566 150 VRRLLSEGADVNARHKLGWTALMVAAISHNESVVQVLLAAGADPNL 195
Cdd:PHA03095 240 VLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINA 285
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
222-276 |
2.70e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 45.03 E-value: 2.70e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1937369566 222 DDFNNRLNHRaSFKGCTALHYAVLADDYSIVKELLGGGANPLQRNEMGHTPLDYA 276
Cdd:pfam13857 3 EHGPIDLNRL-DGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
344-466 |
3.06e-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: 3.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 344 PLVFLFLGSSGIGKTELAKQTAKYMHKDakkgFIRLDMSEFqerheVAKfigsppgYIGHEEGG--QLTKKLKQCPNAVV 421
Cdd:COG0464 191 PRGLLLYGPPGTGKTLLARALAGELGLP----LIEVDLSDL-----VSK-------YVGETEKNlrEVFDKARGLAPCVL 254
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1937369566 422 LFDEVDKAHPD-----------VLTIMLQLFDEGRltdgkgktidcKDAIFIMTSN 466
Cdd:COG0464 255 FIDEADALAGKrgevgdgvgrrVVNTLLTEMEELR-----------SDVVVIAATN 299
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
130-267 |
1.13e-05 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 48.71 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 130 NPSNKDAALMEAARANNVQEVRRLLSEGADVNARHKLGWTALMVAAISHNESVVQVLLAAGAD---PNLGDDFSSVYKta 206
Cdd:PLN03192 618 DPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADvdkANTDDDFSPTEL-- 695
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1937369566 207 neqgvhsLEVLVTREddfnnrLNHRASF-KGCTALHYAVLADDYSIVKELLGGGAN-------------PLQRNE 267
Cdd:PLN03192 696 -------RELLQKRE------LGHSITIvDSVPADEPDLGRDGGSRPGRLQGTSSDnqcrprvsiykghPLLRNE 757
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
145-261 |
5.73e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 46.20 E-value: 5.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 145 NNVQEVRRLLSEGADVNARHKLGWTALMVAAISHNESVVQVLLAAGADPNLGDDFssvyktaneqgvhslevlvtreddf 224
Cdd:PHA03100 170 NAKNRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKY------------------------- 224
|
90 100 110
....*....|....*....|....*....|....*..
gi 1937369566 225 nnrlnhrasfkGCTALHYAVLADDYSIVKELLGGGAN 261
Cdd:PHA03100 225 -----------GDTPLHIAILNNNKEIFKLLLNNGPS 250
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
137-192 |
6.81e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 45.81 E-value: 6.81e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1937369566 137 ALMEAARANNVQEVRRLLSEGADVNARHKLGWTALMVAAISHNESVVQVLLAAGAD 192
Cdd:PHA03100 195 PLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
146-276 |
8.86e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 45.34 E-value: 8.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 146 NVQEVRRLLSEGADVNARHKLGWTALMVAAISHNESVVQVLLAAGADPNLGDDFSS--VYKTANEQGVHSLEVLVTREDD 223
Cdd:PHA02874 103 EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCypIHIAIKHNFFDIIKLLLEKGAY 182
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1937369566 224 FNNRLNHrasfkGCTALHYAVLADDYSIVKELLGGGANPLQRNEMGHTPLDYA 276
Cdd:PHA02874 183 ANVKDNN-----GESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNA 230
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
167-198 |
9.86e-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: 9.86e-05
10 20 30
....*....|....*....|....*....|...
gi 1937369566 167 GWTALMVAAISH-NESVVQVLLAAGADPNLGDD 198
Cdd:pfam00023 2 GNTPLHLAAGRRgNLEIVKLLLSKGADVNARDK 34
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
235-267 |
1.34e-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: 1.34e-04
10 20 30
....*....|....*....|....*....|....
gi 1937369566 235 KGCTALHYAVL-ADDYSIVKELLGGGANPLQRNE 267
Cdd:pfam00023 1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
138-276 |
1.52e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 44.57 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 138 LMEAARANNVQEVRRLLSEGADVNARHKLGWTALMVAAISHNESVVQVLLAAGADPNLGDDF--SSVYKTANEQGVHSLE 215
Cdd:PHA02874 128 LHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNgeSPLHNAAEYGDYACIK 207
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1937369566 216 VLVTREDDFNNRLNhrasfKGCTALHYAVLADDYSIvkELLGGGANPLQRNEMGHTPLDYA 276
Cdd:PHA02874 208 LLIDHGNHIMNKCK-----NGFTPLHNAIIHNRSAI--ELLINNASINDQDIDGSTPLHHA 261
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
240-285 |
2.17e-04 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 40.48 E-value: 2.17e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1937369566 240 LHYAVLADDYSIVKELLGGGANPLQRNEMGHTPLDYA-REG--EVMKLL 285
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAaKNGhlEIVKLL 49
|
|
| Zeta_toxin |
pfam06414 |
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is ... |
342-415 |
3.34e-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: 3.34e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1937369566 342 EHPLVFLFLGSSGIGKTELAKQTAKYMhkDAKKGFIRLDMSEFQERH-EVAKFIGSPP---GYIGHEEGGQLTKKLKQ 415
Cdd:pfam06414 9 ERPKAILLGGQPGAGKTELARALLDEL--GRQGNVVRIDPDDFRELHpHYRELQAADPktaSEYTQPDASRWVEKLLQ 84
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
126-295 |
3.67e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 43.41 E-value: 3.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 126 CYNKNPSNKDAALMEAARANNVQEVRRLLSEGADVNARHKLGWTALMVAAISHNESVVQVLLAAGAD------PNLGDDf 199
Cdd:PHA02874 27 CINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDtsilpiPCIEKD- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 200 ssVYKTANEQGVHS----------LEVLVTRED--DFNNRLNHRASF-----KGCTALHYAVLADDYSIVKELLGGGANP 262
Cdd:PHA02874 106 --MIKTILDCGIDVnikdaelktfLHYAIKKGDleSIKMLFEYGADVnieddNGCYPIHIAIKHNFFDIIKLLLEKGAYA 183
|
170 180 190
....*....|....*....|....*....|....*.
gi 1937369566 263 LQRNEMGHTPLDYARE-GE--VMKLLKTSETKYMEK 295
Cdd:PHA02874 184 NVKDNNGESPLHNAAEyGDyaCIKLLIDHGNHIMNK 219
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
235-262 |
4.55e-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: 37.95 E-value: 4.55e-04
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
138-236 |
5.49e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 43.35 E-value: 5.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 138 LMEAARANNVQEVRRLLSEGADVNARHKLGWTALMVAAISHNESVVQVLLAAGADPNLGD-DFSSVYKTANEQGVHSLEV 216
Cdd:PTZ00322 86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDkDGKTPLELAEENGFREVVQ 165
|
90 100
....*....|....*....|...
gi 1937369566 217 LVTREDDFNNRLNHRA---SFKG 236
Cdd:PTZ00322 166 LLSRHSQCHFELGANAkpdSFTG 188
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
118-285 |
7.44e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 42.56 E-value: 7.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 118 LAMALVVQCYNKNPSNKDAALMEAARANNVQE--VRRLLSEGADVNA--RHKLGwTALMVAAISHNESVVQVLLAAGADP 193
Cdd:PHA02878 116 IFKIILTNRYKNIQTIDLVYIDKKSKDDIIEAeiTKLLLSYGADINMkdRHKGN-TALHYATENKDQRLTELLLSYGANV 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 194 NLGDdfssvyKTANeqgvhslevlvtreddfnnrlnhrasfkgcTALHYAVLADDYSIVKELLGGGANPLQRNEMGHTPL 273
Cdd:PHA02878 195 NIPD------KTNN------------------------------SPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPL 238
|
170
....*....|....*.
gi 1937369566 274 DYA----REGEVMKLL 285
Cdd:PHA02878 239 HISvgycKDYDILKLL 254
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
167-195 |
8.13e-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: 37.18 E-value: 8.13e-04
10 20
....*....|....*....|....*....
gi 1937369566 167 GWTALMVAAISHNESVVQVLLAAGADPNL 195
Cdd:smart00248 2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
133-276 |
8.47e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 42.29 E-value: 8.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 133 NKDAALMEAARANNVQEVRRLLSEGADVNARHKLGWTALMVAAISHNESVVQVLLAAGADPNLGD-DFSSVYKTANEQG- 210
Cdd:PHA02875 1 MDQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYpDIESELHDAVEEGd 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1937369566 211 VHSLEVLVtredDFNNRLNHRASFKGCTALHYAVLADDYSIVKELLGGGANPLQRNEMGHTPLDYA 276
Cdd:PHA02875 81 VKAVEELL----DLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLA 142
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
141-273 |
1.23e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 41.97 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 141 AARANNVQEVRRLLSEGADVNARHKLGWTALMVAAISHNESVVQVLLAAGADPNlGDDFSSVYKTANEQGVHSLEVL--- 217
Cdd:PHA02876 185 AAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNIN-KNDLSLLKAIRNEDLETSLLLYdag 263
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1937369566 218 --VTREDDFNNrlnhrasfkgcTALHYAVLADDYS-IVKELLGGGANPLQRNEMGHTPL 273
Cdd:PHA02876 264 fsVNSIDDCKN-----------TPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPL 311
|
|
| RecA-like_Lon |
cd19500 |
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ... |
346-487 |
1.32e-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: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 346 VFLFLGSSGIGKTELAKQTAKYMHKDakkgFIRL------DMSEFqeRHEVAKFIGSPPGYIgheeggqlTKKLKQCP-- 417
Cdd:cd19500 39 ILCLVGPPGVGKTSLGKSIARALGRK----FVRIslggvrDEAEI--RGHRRTYVGAMPGRI--------IQALKKAGtn 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1937369566 418 NAVVLFDEVDK----AHPDVLTIMLQLFD---EGRLTDGK-GKTIDCKDAIFIMTSNVAsDEIAQhALQLRQEALEMS 487
Cdd:cd19500 105 NPVFLLDEIDKigssFRGDPASALLEVLDpeqNSTFSDHYlDVPFDLSKVLFIATANSL-DTIPG-PLLDRMEIIELS 180
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
132-261 |
1.92e-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: 41.61 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 132 SNKDAALMEAARANNVQEVRRLLSEGA--DVNARHKLGWTALMVAAI-SHNESVVQVLLAAGADPNLGDdfSSVYKTANE 208
Cdd:TIGR00870 15 SDEEKAFLPAAERGDLASVYRDLEEPKklNINCPDRLGRSALFVAAIeNENLELTELLLNLSCRGAVGD--TLLHAISLE 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1937369566 209 --QGVHSLEVL---VTREDDFNNRLNHRAS---FKGCTALHYAVLADDYSIVKELLGGGAN 261
Cdd:TIGR00870 93 yvDAVEAILLHllaAFRKSGPLELANDQYTsefTPGITALHLAAHRQNYEIVKLLLERGAS 153
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
153-199 |
2.38e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 36.56 E-value: 2.38e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1937369566 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 |
2.92e-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: 2.92e-03
10 20
....*....|....*....|....*...
gi 1937369566 167 GWTALMVAAISHNESVVQVLLAAGADPN 194
Cdd:pfam13606 2 GNTPLHLAARNGRLEIVKLLLENGADIN 29
|
|
| RPT1 |
COG1222 |
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ... |
347-427 |
3.71e-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: 3.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 347 FLFLGSSGIGKTELAKQTAKYMhkDAKkgFIRLDMSEFqerheVAKFIGsppgyigheEGGQLTKKL----KQCPNAVVL 422
Cdd:COG1222 115 VLLYGPPGTGKTLLAKAVAGEL--GAP--FIRVRGSEL-----VSKYIG---------EGARNVREVfelaREKAPSIIF 176
|
....*
gi 1937369566 423 FDEVD 427
Cdd:COG1222 177 IDEID 181
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
235-262 |
6.36e-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: 34.54 E-value: 6.36e-03
10 20
....*....|....*....|....*...
gi 1937369566 235 KGCTALHYAVLADDYSIVKELLGGGANP 262
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADI 28
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
137-174 |
8.33e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 35.01 E-value: 8.33e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1937369566 137 ALMEAARANNVQEVRRLLSEGADVNARHKLGWTALMVA 174
Cdd:pfam13857 19 PLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| ftsH |
CHL00176 |
cell division protein; Validated |
343-427 |
8.93e-03 |
|
cell division protein; Validated
Pssm-ID: 214386 [Multi-domain] Cd Length: 638 Bit Score: 39.26 E-value: 8.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369566 343 HPLVFLFLGSSGIGKTELAKQTAkymhKDAKKGFIRLDMSEFQERhevakFIGsppgyIGHEEGGQLTKKLKQCPNAVVL 422
Cdd:CHL00176 215 IPKGVLLVGPPGTGKTLLAKAIA----GEAEVPFFSISGSEFVEM-----FVG-----VGAARVRDLFKKAKENSPCIVF 280
|
....*
gi 1937369566 423 FDEVD 427
Cdd:CHL00176 281 IDEID 285
|
|
| |
