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Conserved domains on  [gi|385719194|ref|NP_001245321|]
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mitochondrial disaggregase isoform 2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ClpA super family cl33938
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 309-625 1.68e-97

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


The actual alignment was detected with superfamily member COG0542:

Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 318.18  E-value: 1.68e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194 309 LEQRLKEHIIGQESAIATVGAAIRRKENGWYDEEHPL-VFLFLGSSGIGKTELAKQTAKYMHkDAKKGFIRLDMSEFQER 387
Cdd:COG0542  543 LEEELHERVIGQDEAVEAVADAIRRSRAGLKDPNRPIgSFLFLGPTGVGKTELAKALAEFLF-GDEDALIRIDMSEYMEK 621

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194 388 HEVAKFIGSPPGYVGHEEGGQLTKKLKQCPNAVVLFDEVDKAHPDVLTIMLQLFDEGRLTDGKGKTIDCKDAIFIMTSNV 467
Cdd:COG0542  622 HSVSRLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLLDEIEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTIIIMTSNI 701

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194 468 ASDEIAQHAlqlrqealemsrnriaenlGDVQISDKItisknfkENVIRPILKAHFrRDEFLGRINEIVYFLPFCHSELI 547
Cdd:COG0542  702 GSELILDLA-------------------EDEPDYEEM-------KEAVMEELKKHF-RPEFLNRIDEIIVFHPLSKEELR 754

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 385719194 548 QLVNKELNFWAKRAKQRhNITLLWDREVADVLVD-GYNVHYGARSIKHEVERRVVNQLAAAYEQDLLPGGCTLRITVED 625
Cdd:COG0542  755 KIVDLQLKRLRKRLAER-GITLELTDAAKDFLAEkGYDPEYGARPLKRAIQRELEDPLAEEILAGEIKEGDTITVDVDD 832
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
132-291 5.14e-27

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 111.58  E-value: 5.14e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194 132 SNKDAALLEAARANNMQEVSRLLSEGADVNAKHRLGWTALMVAAINRNNSVVQVLLAAGADPNLGDD--FSSVYKTAKEQ 209
Cdd:COG0666   85 DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNdgNTPLHLAAANG 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194 210 GIHSLEVLITREDDFNNRLNNrasfkGCTALHYAVLADDYRTVKELLDGGANPLQRNEMGHTPLDYARE---GEVMKLLR 286
Cdd:COG0666  165 NLEIVKLLLEAGADVNARDND-----GETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAEngnLEIVKLLL 239


                 ....*
gi 385719194 287 TSEAK 291
Cdd:COG0666  240 EAGAD 244
 
Name Accession Description Interval E-value
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 309-625 1.68e-97

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 318.18  E-value: 1.68e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194 309 LEQRLKEHIIGQESAIATVGAAIRRKENGWYDEEHPL-VFLFLGSSGIGKTELAKQTAKYMHkDAKKGFIRLDMSEFQER 387
Cdd:COG0542  543 LEEELHERVIGQDEAVEAVADAIRRSRAGLKDPNRPIgSFLFLGPTGVGKTELAKALAEFLF-GDEDALIRIDMSEYMEK 621

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194 388 HEVAKFIGSPPGYVGHEEGGQLTKKLKQCPNAVVLFDEVDKAHPDVLTIMLQLFDEGRLTDGKGKTIDCKDAIFIMTSNV 467
Cdd:COG0542  622 HSVSRLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLLDEIEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTIIIMTSNI 701

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194 468 ASDEIAQHAlqlrqealemsrnriaenlGDVQISDKItisknfkENVIRPILKAHFrRDEFLGRINEIVYFLPFCHSELI 547
Cdd:COG0542  702 GSELILDLA-------------------EDEPDYEEM-------KEAVMEELKKHF-RPEFLNRIDEIIVFHPLSKEELR 754

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 385719194 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 ...
 220-625 1.08e-80

ATP-dependent chaperone ClpB; Members of this protein family are the bacterial ATP-dependent chaperone ClpB. This protein belongs to the AAA family, ATPases associated with various cellular activities (pfam00004). This molecular chaperone does not act as a protease, but rather serves to disaggregate misfolded and aggregated proteins. [Protein fate, Protein folding and stabilization]


Pssm-ID: 274529 [Multi-domain]  Cd Length: 850  Bit Score: 273.37  E-value: 1.08e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194  220 REDDFNnrlnnRASfkgctALHYAVLADDYRTVKEL---LDGGANPLQRNEMGHT------------PLDYAREGEVMKL 284
Cdd:TIGR03346 486 REGDLA-----KAA-----ELQYGKLPELEKQLQAAeqkLGEEQNRLLREEVTAEeiaevvsrwtgiPVSKMLEGEREKL 555

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194  285 LRtseakyqekqrkreaeerrrfpLEQRLKEHIIGQESAIATVGAAIRRKENGWYDEEHPL-VFLFLGSSGIGKTELAKQ 363
Cdd:TIGR03346 556 LH----------------------MEEELHERVVGQDEAVEAVSDAIRRSRAGLSDPNRPIgSFLFLGPTGVGKTELAKA 613

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194  364 TAKYMHkDAKKGFIRLDMSEFQERHEVAKFIGSPPGYVGHEEGGQLTKKLKQCPNAVVLFDEVDKAHPDVLTIMLQLFDE 443
Cdd:TIGR03346 614 LAEFLF-DSEDAMVRIDMSEYMEKHSVARLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLFDEVEKAHPDVFNVLLQVLDD 692

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194  444 GRLTDGKGKTIDCKDAIFIMTSNVASDEIAQhalQLRQEALEMSRNRIAEnlgdvqisdkitisknfkenvirpILKAHF 523
Cdd:TIGR03346 693 GRLTDGQGRTVDFRNTVIIMTSNLGSDFIQE---LAGGDDYEEMREAVME------------------------VLRAHF 745

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194  524 rRDEFLGRINEIVYFLPFCHSELIQLVNKELNFWAKRAKQRHnITLLWDREVADVLVD-GYNVHYGARSIKHEVERRVVN 602
Cdd:TIGR03346 746 -RPEFLNRIDEIVVFHPLGREQIARIVEIQLGRLRKRLAERK-ITLELSDAALDFLAEaGYDPVYGARPLKRAIQREIEN 823

                         410       420
                  ....*....|....*....|....*..
gi 385719194  603 QLAaayeQDLLPG----GCTLRITVED 625
Cdd:TIGR03346 824 PLA----KKILAGevapGDTIRVDVEG 846
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
 309-471 2.45e-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: 247.48  E-value: 2.45e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194 309 LEQRLKEHIIGQESAIATVGAAIRRKENGWYDEEHPL-VFLFLGSSGIGKTELAKQTAKYMHKDaKKGFIRLDMSEFQER 387
Cdd:cd19499    5 LEERLHERVVGQDEAVKAVSDAIRRARAGLSDPNRPIgSFLFLGPTGVGKTELAKALAELLFGD-EDNLIRIDMSEYMEK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194 388 HEVAKFIGSPPGYVGHEEGGQLTKKLKQCPNAVVLFDEVDKAHPDVLTIMLQLFDEGRLTDGKGKTIDCKDAIFIMTSNV 467
Cdd:cd19499   84 HSVSRLIGAPPGYVGYTEGGQLTEAVRRKPYSVVLLDEIEKAHPDVQNLLLQVLDDGRLTDSHGRTVDFKNTIIIMTSNH 163


                 ....
gi 385719194 468 ASDE 471
Cdd:cd19499  164 FRPE 167
clpC CHL00095
Clp protease ATP binding subunit
 309-625 3.17e-78

Clp protease ATP binding subunit


Pssm-ID: 214361 [Multi-domain]  Cd Length: 821  Bit Score: 266.15  E-value: 3.17e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194 309 LEQRLKEHIIGQESAIATVGAAIRRKENGWYDEEHPLV-FLFLGSSGIGKTELAKQTAKYMHkDAKKGFIRLDMSEFQER 387
Cdd:CHL00095 503 MEETLHKRIIGQDEAVVAVSKAIRRARVGLKNPNRPIAsFLFSGPTGVGKTELTKALASYFF-GSEDAMIRLDMSEYMEK 581

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194 388 HEVAKFIGSPPGYVGHEEGGQLTKKLKQCPNAVVLFDEVDKAHPDVLTIMLQLFDEGRLTDGKGKTIDCKDAIFIMTSNV 467
Cdd:CHL00095 582 HTVSKLIGSPPGYVGYNEGGQLTEAVRKKPYTVVLFDEIEKAHPDIFNLLLQILDDGRLTDSKGRTIDFKNTLIIMTSNL 661

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194 468 ASdeiaqhalqlrqealemsrNRIAENLGDVQI--SDKITISKNFKE--NVIRPILKAHFrRDEFLGRINEIVYFLPFCH 543
Cdd:CHL00095 662 GS-------------------KVIETNSGGLGFelSENQLSEKQYKRlsNLVNEELKQFF-RPEFLNRLDEIIVFRQLTK 721

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194 544 SELIQLVNKELNFWAKRAKQRhNITLLWDREVADVLVD-GYNVHYGARSIKHEVERRVVNQLAAAYEQDLLPGGCTLRIT 622
Cdd:CHL00095 722 NDVWEIAEIMLKNLFKRLNEQ-GIQLEVTERIKTLLIEeGYNPLYGARPLRRAIMRLLEDPLAEEVLSFKIKPGDIIIVD 800


                 ...
gi 385719194 623 VED 625
Cdd:CHL00095 801 VND 803
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
 346-535 3.74e-67

AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.


Pssm-ID: 400187 [Multi-domain]  Cd Length: 168  Bit Score: 217.45  E-value: 3.74e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194  346 VFLFLGSSGIGKTELAKQTAKYMHKDAKKgFIRLDMSEFQERHEVAKFIGSPPGYVGHEEGGQLTKKLKQCPNAVVLFDE 425
Cdd:pfam07724   5 SFLFLGPTGVGKTELAKALAELLFGDERA-LIRIDMSEYMEEHSVSRLIGAPPGYVGYEEGGQLTEAVRRKPYSIVLIDE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194  426 VDKAHPDVLTIMLQLFDEGRLTDGKGKTIDCKDAIFIMTSNVASDEIAQHALqlrqealemsrnriaenlgdvqisDKIT 505
Cdd:pfam07724  84 IEKAHPGVQNDLLQILEGGTLTDKQGRTVDFKNTLFIMTGNFGSEKISDASR------------------------LGDS 139

                         170       180       190
                  ....*....|....*....|....*....|
gi 385719194  506 ISKNFKENVIRPILKAHFRRdEFLGRINEI 535
Cdd:pfam07724 140 PDYELLKEEVMDLLKKGFIP-EFLGRLPII 168
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
132-291 5.14e-27

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 111.58  E-value: 5.14e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194 132 SNKDAALLEAARANNMQEVSRLLSEGADVNAKHRLGWTALMVAAINRNNSVVQVLLAAGADPNLGDD--FSSVYKTAKEQ 209
Cdd:COG0666   85 DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNdgNTPLHLAAANG 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194 210 GIHSLEVLITREDDFNNRLNNrasfkGCTALHYAVLADDYRTVKELLDGGANPLQRNEMGHTPLDYARE---GEVMKLLR 286
Cdd:COG0666  165 NLEIVKLLLEAGADVNARDND-----GETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAEngnLEIVKLLL 239


                 ....*
gi 385719194 287 TSEAK 291
Cdd:COG0666  240 EAGAD 244
Ank_2 pfam12796
Ankyrin repeats (3 copies);
138-266 9.26e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 64.37  E-value: 9.26e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194  138 LLEAARANNMQEVSRLLSEGADVNAKHRLGWTALMVAAINRNNSVVQVLLAaGADPNLGDDfssvyktakeqgihslevl 217
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN------------------- 60

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 385719194  218 itreddfnnrlnnrasfkGCTALHYAVLADDYRTVKELLDGGANPLQRN 266
Cdd:pfam12796  61 ------------------GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 343-480 2.62e-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: 2.62e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194   343 HPLVFLFLGSSGIGKTELAKQTAKYMHKDaKKGFIRLDMSEFQERHEVAKFIGSPPGYVGHEEGGQ----LTKKLKQCPN 418
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPP-GGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELrlrlALALARKLKP 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 385719194   419 AVVLFDEVDKAHPDVLTIMLQLFDEGRLtdgKGKTIDCKDAIFIMTSNVASDEIAqHALQLR 480
Cdd:smart00382  80 DVLILDEITSLLDAEQEALLLLLEELRL---LLLLKSEKNLTVILTTNDEKDLGP-ALLRRR 137
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 145-285 4.89e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 61.99  E-value: 4.89e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194 145 NNMQEVSRLLSEGADVNAKHRLGWTALMVAAINRNNSV--VQVLLAAGADPNLGD-DFSSVYKTAKEQGIHSLEV---LI 218
Cdd:PHA03100  84 DVKEIVKLLLEYGANVNAPDNNGITPLLYAISKKSNSYsiVEYLLDNGANVNIKNsDGENLLHLYLESNKIDLKIlklLI 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194 219 TREDDFN--NRLN---------NRASFKGCTALHYAVLADDYRTVKELLDGGANPLQRNEMGHTPLDYA---REGEVMKL 284
Cdd:PHA03100 164 DKGVDINakNRVNyllsygvpiNIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAilnNNKEIFKL 243


                 .
gi 385719194 285 L 285
Cdd:PHA03100 244 L 244
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 138-260 1.17e-06

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 51.94  E-value: 1.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194 138 LLEAARANNMQEVSRLL-SEGADVNAKHRLGWTALMVAAINRNNSVVQVLLAagADPNLgddfssvyktakeqgihsLEV 216
Cdd:cd22192   21 LLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPEL------------------VNE 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 385719194 217 LITREddfnnrlnnraSFKGCTALHYAVLADDYRTVKELLDGGA 260
Cdd:cd22192   81 PMTSD-----------LYQGETALHIAVVNQNLNLVRELIARGA 113
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 132-261 3.15e-05

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: 47.38  E-value: 3.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194  132 SNKDAALLEAARANNMQEVSRLLSEGA--DVNAKHRLGWTALMVAAI-NRNNSVVQVLLAAGADPNLGDdfSSVYKTAKE 208
Cdd:TIGR00870  15 SDEEKAFLPAAERGDLASVYRDLEEPKklNINCPDRLGRSALFVAAIeNENLELTELLLNLSCRGAVGD--TLLHAISLE 92

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 385719194  209 -----QGIHSLEVLITREDDFNNRLNNRAS---FKGCTALHYAVLADDYRTVKELLDGGAN 261
Cdd:TIGR00870  93 yvdavEAILLHLLAAFRKSGPLELANDQYTsefTPGITALHLAAHRQNYEIVKLLLERGAS 153
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 235-262 4.60e-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: 4.60e-04
                           10        20
                   ....*....|....*....|....*...
gi 385719194   235 KGCTALHYAVLADDYRTVKELLDGGANP 262
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
 
Name Accession Description Interval E-value
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 309-625 1.68e-97

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 318.18  E-value: 1.68e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194 309 LEQRLKEHIIGQESAIATVGAAIRRKENGWYDEEHPL-VFLFLGSSGIGKTELAKQTAKYMHkDAKKGFIRLDMSEFQER 387
Cdd:COG0542  543 LEEELHERVIGQDEAVEAVADAIRRSRAGLKDPNRPIgSFLFLGPTGVGKTELAKALAEFLF-GDEDALIRIDMSEYMEK 621

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194 388 HEVAKFIGSPPGYVGHEEGGQLTKKLKQCPNAVVLFDEVDKAHPDVLTIMLQLFDEGRLTDGKGKTIDCKDAIFIMTSNV 467
Cdd:COG0542  622 HSVSRLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLLDEIEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTIIIMTSNI 701

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194 468 ASDEIAQHAlqlrqealemsrnriaenlGDVQISDKItisknfkENVIRPILKAHFrRDEFLGRINEIVYFLPFCHSELI 547
Cdd:COG0542  702 GSELILDLA-------------------EDEPDYEEM-------KEAVMEELKKHF-RPEFLNRIDEIIVFHPLSKEELR 754

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 385719194 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 ...
 220-625 1.08e-80

ATP-dependent chaperone ClpB; Members of this protein family are the bacterial ATP-dependent chaperone ClpB. This protein belongs to the AAA family, ATPases associated with various cellular activities (pfam00004). This molecular chaperone does not act as a protease, but rather serves to disaggregate misfolded and aggregated proteins. [Protein fate, Protein folding and stabilization]


Pssm-ID: 274529 [Multi-domain]  Cd Length: 850  Bit Score: 273.37  E-value: 1.08e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194  220 REDDFNnrlnnRASfkgctALHYAVLADDYRTVKEL---LDGGANPLQRNEMGHT------------PLDYAREGEVMKL 284
Cdd:TIGR03346 486 REGDLA-----KAA-----ELQYGKLPELEKQLQAAeqkLGEEQNRLLREEVTAEeiaevvsrwtgiPVSKMLEGEREKL 555

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194  285 LRtseakyqekqrkreaeerrrfpLEQRLKEHIIGQESAIATVGAAIRRKENGWYDEEHPL-VFLFLGSSGIGKTELAKQ 363
Cdd:TIGR03346 556 LH----------------------MEEELHERVVGQDEAVEAVSDAIRRSRAGLSDPNRPIgSFLFLGPTGVGKTELAKA 613

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194  364 TAKYMHkDAKKGFIRLDMSEFQERHEVAKFIGSPPGYVGHEEGGQLTKKLKQCPNAVVLFDEVDKAHPDVLTIMLQLFDE 443
Cdd:TIGR03346 614 LAEFLF-DSEDAMVRIDMSEYMEKHSVARLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLFDEVEKAHPDVFNVLLQVLDD 692

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194  444 GRLTDGKGKTIDCKDAIFIMTSNVASDEIAQhalQLRQEALEMSRNRIAEnlgdvqisdkitisknfkenvirpILKAHF 523
Cdd:TIGR03346 693 GRLTDGQGRTVDFRNTVIIMTSNLGSDFIQE---LAGGDDYEEMREAVME------------------------VLRAHF 745

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194  524 rRDEFLGRINEIVYFLPFCHSELIQLVNKELNFWAKRAKQRHnITLLWDREVADVLVD-GYNVHYGARSIKHEVERRVVN 602
Cdd:TIGR03346 746 -RPEFLNRIDEIVVFHPLGREQIARIVEIQLGRLRKRLAERK-ITLELSDAALDFLAEaGYDPVYGARPLKRAIQREIEN 823

                         410       420
                  ....*....|....*....|....*..
gi 385719194  603 QLAaayeQDLLPG----GCTLRITVED 625
Cdd:TIGR03346 824 PLA----KKILAGevapGDTIRVDVEG 846
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
 309-471 2.45e-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: 247.48  E-value: 2.45e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194 309 LEQRLKEHIIGQESAIATVGAAIRRKENGWYDEEHPL-VFLFLGSSGIGKTELAKQTAKYMHKDaKKGFIRLDMSEFQER 387
Cdd:cd19499    5 LEERLHERVVGQDEAVKAVSDAIRRARAGLSDPNRPIgSFLFLGPTGVGKTELAKALAELLFGD-EDNLIRIDMSEYMEK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194 388 HEVAKFIGSPPGYVGHEEGGQLTKKLKQCPNAVVLFDEVDKAHPDVLTIMLQLFDEGRLTDGKGKTIDCKDAIFIMTSNV 467
Cdd:cd19499   84 HSVSRLIGAPPGYVGYTEGGQLTEAVRRKPYSVVLLDEIEKAHPDVQNLLLQVLDDGRLTDSHGRTVDFKNTIIIMTSNH 163


                 ....
gi 385719194 468 ASDE 471
Cdd:cd19499  164 FRPE 167
clpC CHL00095
Clp protease ATP binding subunit
 309-625 3.17e-78

Clp protease ATP binding subunit


Pssm-ID: 214361 [Multi-domain]  Cd Length: 821  Bit Score: 266.15  E-value: 3.17e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194 309 LEQRLKEHIIGQESAIATVGAAIRRKENGWYDEEHPLV-FLFLGSSGIGKTELAKQTAKYMHkDAKKGFIRLDMSEFQER 387
Cdd:CHL00095 503 MEETLHKRIIGQDEAVVAVSKAIRRARVGLKNPNRPIAsFLFSGPTGVGKTELTKALASYFF-GSEDAMIRLDMSEYMEK 581

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194 388 HEVAKFIGSPPGYVGHEEGGQLTKKLKQCPNAVVLFDEVDKAHPDVLTIMLQLFDEGRLTDGKGKTIDCKDAIFIMTSNV 467
Cdd:CHL00095 582 HTVSKLIGSPPGYVGYNEGGQLTEAVRKKPYTVVLFDEIEKAHPDIFNLLLQILDDGRLTDSKGRTIDFKNTLIIMTSNL 661

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194 468 ASdeiaqhalqlrqealemsrNRIAENLGDVQI--SDKITISKNFKE--NVIRPILKAHFrRDEFLGRINEIVYFLPFCH 543
Cdd:CHL00095 662 GS-------------------KVIETNSGGLGFelSENQLSEKQYKRlsNLVNEELKQFF-RPEFLNRLDEIIVFRQLTK 721

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194 544 SELIQLVNKELNFWAKRAKQRhNITLLWDREVADVLVD-GYNVHYGARSIKHEVERRVVNQLAAAYEQDLLPGGCTLRIT 622
Cdd:CHL00095 722 NDVWEIAEIMLKNLFKRLNEQ-GIQLEVTERIKTLLIEeGYNPLYGARPLRRAIMRLLEDPLAEEVLSFKIKPGDIIIVD 800


                 ...
gi 385719194 623 VED 625
Cdd:CHL00095 801 VND 803
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
 346-535 3.74e-67

AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.


Pssm-ID: 400187 [Multi-domain]  Cd Length: 168  Bit Score: 217.45  E-value: 3.74e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194  346 VFLFLGSSGIGKTELAKQTAKYMHKDAKKgFIRLDMSEFQERHEVAKFIGSPPGYVGHEEGGQLTKKLKQCPNAVVLFDE 425
Cdd:pfam07724   5 SFLFLGPTGVGKTELAKALAELLFGDERA-LIRIDMSEYMEEHSVSRLIGAPPGYVGYEEGGQLTEAVRRKPYSIVLIDE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194  426 VDKAHPDVLTIMLQLFDEGRLTDGKGKTIDCKDAIFIMTSNVASDEIAQHALqlrqealemsrnriaenlgdvqisDKIT 505
Cdd:pfam07724  84 IEKAHPGVQNDLLQILEGGTLTDKQGRTVDFKNTLFIMTGNFGSEKISDASR------------------------LGDS 139

                         170       180       190
                  ....*....|....*....|....*....|
gi 385719194  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 2.58e-65

ATP-dependent Clp protease ATP-binding subunit clpA; [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 274241 [Multi-domain]  Cd Length: 730  Bit Score: 229.14  E-value: 2.58e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194  309 LEQRLKEHIIGQESAIATVGAAIRRKENGWYDEEHPL-VFLFLGSSGIGKTELAKQTAKYMhkdakkG--FIRLDMSEFQ 385
Cdd:TIGR02639 447 LEKNLKAKIFGQDEAIDQLVSAIKRSRAGLGDPNKPVgSFLFVGPTGVGKTELAKQLAEEL------GvhLLRFDMSEYM 520

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194  386 ERHEVAKFIGSPPGYVGHEEGGQLTKKLKQCPNAVVLFDEVDKAHPDVLTIMLQLFDEGRLTDGKGKTIDCKDAIFIMTS 465
Cdd:TIGR02639 521 EKHTVSRLIGSPPGYVGFEQGGLLTDAVRKHPHCVLLLDEIEKAHPDIYNILLQVMDYATLTDNNGRKADFRNVILIMTS 600

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194  466 NVASDEIAQHALQLRQEALEMSRNRiaenlgdvqisdkiTISKNFKenvirPilkahfrrdEFLGRINEIVYFLPFCHSE 545
Cdd:TIGR02639 601 NAGASEMSKPPIGFGGENRESKSLK--------------AIKKLFS-----P---------EFRNRLDAIIHFNDLSEEM 652

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 385719194  546 LIQLVNKELNFWAKRAKQRhNITLLWDREVADVLVD-GYNVHYGARSIKHEVERRVVNQLA 605
Cdd:TIGR02639 653 AEKIVKKFLDELQDQLNEK-NIELELTDDAKKYLAEkGYDEEFGARPLARVIQEEIKKPLS 712
PRK10865 PRK10865
ATP-dependent chaperone ClpB;
272-626 4.50e-61

ATP-dependent chaperone ClpB;


Pssm-ID: 182791 [Multi-domain]  Cd Length: 857  Bit Score: 219.33  E-value: 4.50e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194 272 PLDYAREGEVMKLLRtseakyqekqrkreaeerrrfpLEQRLKEHIIGQESAIATVGAAIRRKENGWYDEEHPL-VFLFL 350
Cdd:PRK10865 547 PVSRMLESEREKLLR----------------------MEQELHHRVIGQNEAVEAVSNAIRRSRAGLSDPNRPIgSFLFL 604

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194 351 GSSGIGKTELAKQTAKYMHkDAKKGFIRLDMSEFQERHEVAKFIGSPPGYVGHEEGGQLTKKLKQCPNAVVLFDEVDKAH 430
Cdd:PRK10865 605 GPTGVGKTELCKALANFMF-DSDDAMVRIDMSEFMEKHSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAH 683

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194 431 PDVLTIMLQLFDEGRLTDGKGKTIDCKDAIFIMTSNVASDeiaqhalqlrqealemsrnRIAENLGDVQISDkitisknF 510
Cdd:PRK10865 684 PDVFNILLQVLDDGRLTDGQGRTVDFRNTVVIMTSNLGSD-------------------LIQERFGELDYAH-------M 737

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194 511 KENVIRpILKAHFrRDEFLGRINEIVYFLPFCHSELIQLVNKELNFWAKRAKQRHNITLLWDREVADVLVDGYNVHYGAR 590
Cdd:PRK10865 738 KELVLG-VVSHNF-RPEFINRIDEVVVFHPLGEQHIASIAQIQLQRLYKRLEERGYEIHISDEALKLLSENGYDPVYGAR 815

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 385719194 591 SIKHEVERRVVNQLAaayeQDLLPG----GCTLRITVEDS 626
Cdd:PRK10865 816 PLKRAIQQQIENPLA----QQILSGelvpGKVIRLEVNDD 851
VI_ClpV1 TIGR03345
type VI secretion ATPase, ClpV1 family; Members of this protein family are homologs of ClpB, ...
 309-605 3.07e-60

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: 216.73  E-value: 3.07e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194  309 LEQRLKEHIIGQESAIATVGAAIRRKENGWYDEEHPL-VFLFLGSSGIGKTELAKQTAKYMHkDAKKGFIRLDMSEFQER 387
Cdd:TIGR03345 560 LPDRLAERVIGQDHALEAIAERIRTARAGLEDPRKPLgVFLLVGPSGVGKTETALALAELLY-GGEQNLITINMSEFQEA 638

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194  388 HEVAKFIGSPPGYVGHEEGGQLTKKLKQCPNAVVLFDEVDKAHPDVLTIMLQLFDEGRLTDGKGKTIDCKDAIFIMTSNV 467
Cdd:TIGR03345 639 HTVSRLKGSPPGYVGYGEGGVLTEAVRRKPYSVVLLDEVEKAHPDVLELFYQVFDKGVMEDGEGREIDFKNTVILLTSNA 718

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194  468 ASDEIAQHALqlrQEALEMSRNRIAENLgdvqisdkitisknfkenviRPILKAHFrRDEFLGRINeIVYFLPFCHSELI 547
Cdd:TIGR03345 719 GSDLIMALCA---DPETAPDPEALLEAL--------------------RPELLKVF-KPAFLGRMT-VIPYLPLDDDVLA 773

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 385719194  548 QLVNKELNFWAKRAKQRHNITLLWDREVADVLVDGYN-VHYGARSIKHEVERRVVNQLA 605
Cdd:TIGR03345 774 AIVRLKLDRIARRLKENHGAELVYSEALVEHIVARCTeVESGARNIDAILNQTLLPELS 832
clpA PRK11034
ATP-dependent Clp protease ATP-binding subunit; Provisional
 309-630 6.59e-41

ATP-dependent Clp protease ATP-binding subunit; Provisional


Pssm-ID: 236828 [Multi-domain]  Cd Length: 758  Bit Score: 159.62  E-value: 6.59e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194 309 LEQRLKEHIIGQESAIATVGAAIRRKENGWYDEEHPL-VFLFLGSSGIGKTELAKQTAKYMHKDakkgFIRLDMSEFQER 387
Cdd:PRK11034 452 LGDRLKMLVFGQDKAIEALTEAIKMSRAGLGHEHKPVgSFLFAGPTGVGKTEVTVQLSKALGIE----LLRFDMSEYMER 527

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194 388 HEVAKFIGSPPGYVGHEEGGQLTKKLKQCPNAVVLFDEVDKAHPDVLTIMLQLFDEGRLTDGKGKTIDCKDAIFIMTSNV 467
Cdd:PRK11034 528 HTVSRLIGAPPGYVGFDQGGLLTDAVIKHPHAVLLLDEIEKAHPDVFNLLLQVMDNGTLTDNNGRKADFRNVVLVMTTNA 607

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194 468 ASDEIAQHALQLRQEalEMSRNRIAEnlgdvqisdkitISKNFKEnvirpilkahfrrdEFLGRINEIVYFLPFCHSELI 547
Cdd:PRK11034 608 GVRETERKSIGLIHQ--DNSTDAMEE------------IKKIFTP--------------EFRNRLDNIIWFDHLSTDVIH 659

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194 548 QLVNKelnFWAKRAKQ--RHNITLLWDREVADVLVD-GYNVHYGARSIKHEVERRVVNQLAAAYEQDLLPGGCTLRITVE 624
Cdd:PRK11034 660 QVVDK---FIVELQAQldQKGVSLEVSQEARDWLAEkGYDRAMGARPMARVIQDNLKKPLANELLFGSLVDGGQVTVALD 736


                 ....*.
gi 385719194 625 DSDKQL 630
Cdd:PRK11034 737 KEKNEL 742
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
132-291 5.14e-27

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 111.58  E-value: 5.14e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194 132 SNKDAALLEAARANNMQEVSRLLSEGADVNAKHRLGWTALMVAAINRNNSVVQVLLAAGADPNLGDD--FSSVYKTAKEQ 209
Cdd:COG0666   85 DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNdgNTPLHLAAANG 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194 210 GIHSLEVLITREDDFNNRLNNrasfkGCTALHYAVLADDYRTVKELLDGGANPLQRNEMGHTPLDYARE---GEVMKLLR 286
Cdd:COG0666  165 NLEIVKLLLEAGADVNARDND-----GETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAEngnLEIVKLLL 239


                 ....*
gi 385719194 287 TSEAK 291
Cdd:COG0666  240 EAGAD 244
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
132-286 1.04e-19

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 90.01  E-value: 1.04e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194 132 SNKDAALLEAARANNMQEVSRLLSEGADVNAKHRLGWTALMVAAINRNNSVVQVLLAAGADPNLGDD--FSSVYKTAKEQ 209
Cdd:COG0666  118 KDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNdgETPLHLAAENG 197

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 385719194 210 GIHSLEVLITREDDFNNRLNNrasfkGCTALHYAVLADDYRTVKELLDGGANPLQRNEMGHTPLDYAREGEVMKLLR 286
Cdd:COG0666  198 HLEIVKLLLEAGADVNAKDND-----GKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVK 269
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
129-285 1.61e-19

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 89.63  E-value: 1.61e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194 129 KSPSNKDAALLEAARANNMQEVSRLLSEGADVNAKHRLGWTALMVAAINRNNSVVQVLLAAGADPNLGD--DFSSVYKTA 206
Cdd:COG0666   49 LADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDkdGETPLHLAA 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194 207 KEQGIHSLEVLITREDDFNNRLNNrasfkGCTALHYAVLADDYRTVKELLDGGANPLQRNEMGHTPLDYAREG---EVMK 283
Cdd:COG0666  129 YNGNLEIVKLLLEAGADVNAQDND-----GNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENghlEIVK 203


                 ..
gi 385719194 284 LL 285
Cdd:COG0666  204 LL 205
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 318-472 1.70e-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: 71.41  E-value: 1.70e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194 318 IGQESAIATVGAAIRRKengwydeeHPLVFLFLGSSGIGKTELAKQTAKYMHKdAKKGFIRLDMSEFQERHEVAkfigsp 397
Cdd:cd00009    1 VGQEEAIEALREALELP--------PPKNLLLYGPPGTGKTTLARAIANELFR-PGAPFLYLNASDLLEGLVVA------ 65

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 385719194 398 pGYVGHEEGGQLTKKLKQCPNAVVLFDEVDKAHPDVLTIMLQLFDEGRLTdgkgkTIDCKDAIFIMTSNVASDEI 472
Cdd:cd00009   66 -ELFGHFLVRLLFELAEKAKPGVLFIDEIDSLSRGAQNALLRVLETLNDL-----RIDRENVRVIGATNRPLLGD 134
Ank_2 pfam12796
Ankyrin repeats (3 copies);
138-266 9.26e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 64.37  E-value: 9.26e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194  138 LLEAARANNMQEVSRLLSEGADVNAKHRLGWTALMVAAINRNNSVVQVLLAaGADPNLGDDfssvyktakeqgihslevl 217
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN------------------- 60

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 385719194  218 itreddfnnrlnnrasfkGCTALHYAVLADDYRTVKELLDGGANPLQRN 266
Cdd:pfam12796  61 ------------------GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 343-480 2.62e-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: 2.62e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194   343 HPLVFLFLGSSGIGKTELAKQTAKYMHKDaKKGFIRLDMSEFQERHEVAKFIGSPPGYVGHEEGGQ----LTKKLKQCPN 418
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPP-GGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELrlrlALALARKLKP 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 385719194   419 AVVLFDEVDKAHPDVLTIMLQLFDEGRLtdgKGKTIDCKDAIFIMTSNVASDEIAqHALQLR 480
Cdd:smart00382  80 DVLILDEITSLLDAEQEALLLLLEELRL---LLLLKSEKNLTVILTTNDEKDLGP-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 2.29e-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: 57.03  E-value: 2.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194  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, ...
 545-630 4.53e-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: 4.53e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194   545 ELIQLVNKELNFWAKRAKQRhNITLLWDREVADVLVD-GYNVHYGARSIKHEVERRVVNQLAAAYEQDLLPGGCTLRITV 623
Cdd:smart01086   5 DLVRIVDLPLNALQKRLAEK-GITLEFTDEALDWLAEkGYDPKYGARPLRRIIQRELEDPLAELILSGELKDGDTVVVDV 83


                   ....*..
gi 385719194   624 EDSDKQL 630
Cdd:smart01086  84 DDGELVF 90
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 145-285 4.89e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 61.99  E-value: 4.89e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194 145 NNMQEVSRLLSEGADVNAKHRLGWTALMVAAINRNNSV--VQVLLAAGADPNLGD-DFSSVYKTAKEQGIHSLEV---LI 218
Cdd:PHA03100  84 DVKEIVKLLLEYGANVNAPDNNGITPLLYAISKKSNSYsiVEYLLDNGANVNIKNsDGENLLHLYLESNKIDLKIlklLI 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194 219 TREDDFN--NRLN---------NRASFKGCTALHYAVLADDYRTVKELLDGGANPLQRNEMGHTPLDYA---REGEVMKL 284
Cdd:PHA03100 164 DKGVDINakNRVNyllsygvpiNIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAilnNNKEIFKL 243


                 .
gi 385719194 285 L 285
Cdd:PHA03100 244 L 244
Ank_2 pfam12796
Ankyrin repeats (3 copies);
111-197 9.12e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 55.89  E-value: 9.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194  111 AGLGMCALAAALVVHCYSKSPSNKDA--ALLEAARANNMQEVSRLLSEgADVNAKHRlGWTALMVAAINRNNSVVQVLLA 188
Cdd:pfam12796   5 AKNGNLELVKLLLENGADANLQDKNGrtALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLLE 82


                  ....*....
gi 385719194  189 AGADPNLGD 197
Cdd:pfam12796  83 KGADINVKD 91
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
 311-428 6.55e-09

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: 55.85  E-value: 6.55e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194 311 QRLKEHIIGQESAIATVGAAIRRK------ENGWYDEEHPLVFLFLGSSGIGKTELAKQTAKYmhkdAKKGFIRLDMSEF 384
Cdd:cd19498    7 SELDKYIIGQDEAKRAVAIALRNRwrrmqlPEELRDEVTPKNILMIGPTGVGKTEIARRLAKL----AGAPFIKVEATKF 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 385719194 385 QErhevakfigspPGYVGHEeggqLTKKLKQCPNAVVLFDEVDK 428
Cdd:cd19498   83 TE-----------VGYVGRD----VESIIRDLVEGIVFIDEIDK 111
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
137-232 9.40e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 57.27  E-value: 9.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194 137 ALLEAARANNMQEVSRLLSEGADVNAKHRLGWTALMVAAINRNNSVVQVLLAAGADPNLGDDFSSVYKTAKEQGIHSLEV 216
Cdd:COG0666  189 PLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIV 268

                         90
                 ....*....|....*.
gi 385719194 217 LITREDDFNNRLNNRA 232
Cdd:COG0666  269 KLLLLALLLLAAALLD 284
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 139-285 1.72e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 57.77  E-value: 1.72e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194 139 LEAARANNMQEVSRLLSEGADVNAKHRLGWTALMVAA-INRNNSVVQVLLAAGADPNLGD--DFSSVYKTAKEQGIhsle 215
Cdd:PHA02876 313 LMAKNGYDTENIRTLIMLGADVNAADRLYITPLHQAStLDRNKDIVITLLELGANVNARDycDKTPIHYAAVRNNV---- 388

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 385719194 216 VLITREDDFNNRLNNRASFKGcTALHYAVLADD-YRTVKELLDGGANPLQRNEMGHTPLDYAREG----EVMKLL 285
Cdd:PHA02876 389 VIINTLLDYGADIEALSQKIG-TALHFALCGTNpYMSVKTLIDRGANVNSKNKDLSTPLHYACKKncklDVIEML 462
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 332-466 2.48e-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: 53.83  E-value: 2.48e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194 332 RRKENGWYDEEHPLVFLFLGSSGIGKTELAKQTAKYMHKDakkgFIRLDMSEFQERHevakfigsppGYVGHEEGGQLTK 411
Cdd:cd19481   14 RGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLP----LIVVKLSSLLSKY----------VGESEKNLRKIFE 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 385719194 412 KLKQCPNAVVLFDEVDKAHPD------------VLTIMLQLFDEGRltdgkgktiDCKDAIFIMTSN 466
Cdd:cd19481   80 RARRLAPCILFIDEIDAIGRKrdssgesgelrrVLNQLLTELDGVN---------SRSKVLVIAATN 137
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 146-276 6.10e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 55.35  E-value: 6.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194 146 NMQEVSRLLSEGADVNAKHRLGWTALMVAAINRNNSVVQVLLAAGADPNLGDDFSS--VYKTAKEQGIHSLEVLITREDD 223
Cdd:PHA02874 103 EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCypIHIAIKHNFFDIIKLLLEKGAY 182

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 385719194 224 FNNRLNNrasfkGCTALHYAVLADDYRTVKELLDGGANPLQRNEMGHTPLDYA 276
Cdd:PHA02874 183 ANVKDNN-----GESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNA 230
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
153-285 2.41e-07

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 53.03  E-value: 2.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194 153 LLSEGADVNAKHRLGWTALMVAAINRNNSVVQVLLAAGADPNLGDDFSSVYKTAKEQGIHSLEVLITREDDFNNrlnNRA 232
Cdd:COG0666    7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI---NAK 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 385719194 233 SFKGCTALHYAVLADDYRTVKELLDGGANPLQRNEMGHTPLDYAREG---EVMKLL 285
Cdd:COG0666   84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNgnlEIVKLL 139
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 347-466 7.59e-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: 7.59e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194  347 FLFLGSSGIGKTELAKQTAKYMHKDakKGFIRL---DMSE---FQERH---EVAKFIGSPpgyvgheeggqLTKKLKqcP 417
Cdd:pfam07728   2 VLLVGPPGTGKTELAERLAAALSNR--PVFYVQltrDTTEedlFGRRNidpGGASWVDGP-----------LVRAAR--E 66

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 385719194  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 1.08e-06

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: 48.36  E-value: 1.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194  348 LFLGSSGIGKTELAKQTAKYMHKDakkgFIRLDMSEFqerheVAKFIGSPPGYVghEEGGQLTKKLKQCpnaVVLFDEVD 427
Cdd:pfam00004   2 LLYGPPGTGKTTLAKAVAKELGAP----FIEISGSEL-----VSKYVGESEKRL--RELFEAAKKLAPC---VIFIDEID 67

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 385719194  428 KAHP-----------DVLTIMLQLFDegrltdgkGKTIDCKDAIFIMTSN 466
Cdd:pfam00004  68 ALAGsrgsggdsesrRVVNQLLTELD--------GFTSSNSKVIVIAATN 109
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 138-260 1.17e-06

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 51.94  E-value: 1.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194 138 LLEAARANNMQEVSRLL-SEGADVNAKHRLGWTALMVAAINRNNSVVQVLLAagADPNLgddfssvyktakeqgihsLEV 216
Cdd:cd22192   21 LLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPEL------------------VNE 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 385719194 217 LITREddfnnrlnnraSFKGCTALHYAVLADDYRTVKELLDGGA 260
Cdd:cd22192   81 PMTSD-----------LYQGETALHIAVVNQNLNLVRELIARGA 113
Ank_4 pfam13637
Ankyrin repeats (many copies);
137-187 2.80e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.96  E-value: 2.80e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 385719194  137 ALLEAARANNMQEVSRLLSEGADVNAKHRLGWTALMVAAINRNNSVVQVLL 187
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 344-466 3.65e-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: 3.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194 344 PLVFLFLGSSGIGKTELAKQTAKYMHKDakkgFIRLDMSEFqerheVAKfigsppgYVGHEEGG--QLTKKLKQCPNAVV 421
Cdd:COG0464  191 PRGLLLYGPPGTGKTLLARALAGELGLP----LIEVDLSDL-----VSK-------YVGETEKNlrEVFDKARGLAPCVL 254

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 385719194 422 LFDEVDKAHPD-----------VLTIMLQLFDEGRltdgkgktidcKDAIFIMTSN 466
Cdd:COG0464  255 FIDEADALAGKrgevgdgvgrrVVNTLLTEMEELR-----------SDVVVIAATN 299
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 138-262 5.06e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 49.22  E-value: 5.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194 138 LLEAARANNMQEVSRLLSEGADVN-AKHRLGWTALMVAAINRNNSVVQVLLAAGADPNLG--DDFSSVYKTAKEQGIHSL 214
Cdd:PHA02875  72 LHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPntDKFSPLHLAVMMGDIKGI 151

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 385719194 215 EVLItredDFNNRLNNRASFkGCTALHYAVLADDYRTVKELLDGGANP 262
Cdd:PHA02875 152 ELLI----DHKACLDIEDCC-GCTPLIIAMAKGDIAICKMLLDSGANI 194
Ank_5 pfam13857
Ankyrin repeats (many copies);
223-276 5.15e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.26  E-value: 5.15e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 385719194  223 DFNNRLNNRASFKGCTALHYAVLADDYRTVKELLDGGANPLQRNEMGHTPLDYA 276
Cdd:pfam13857   3 EHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA03095 PHA03095
ankyrin-like protein; Provisional
 150-195 5.26e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 49.64  E-value: 5.26e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 385719194 150 VSRLLSEGADVNAKHRLGWTALMVAAINRNNSVVQVLLAAGADPNL 195
Cdd:PHA03095 240 VLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINA 285
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 125-236 8.94e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 49.10  E-value: 8.94e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194 125 HCYSKS-PSNKDAALLEAARANNMQEVSRLLSEGADVNAKHRLGWTALMVAAINRNNSVVQVLLAAGAD---PNLGDDFS 200
Cdd:PLN03192 612 HFASISdPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADvdkANTDDDFS 691

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 385719194 201 SVYKT---AKEQGIHSLEVLITREDDFNNRLNNRASFKG 236
Cdd:PLN03192 692 PTELRellQKRELGHSITIVDSVPADEPDLGRDGGSRPG 730
PHA03095 PHA03095
ankyrin-like protein; Provisional
 150-274 2.14e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 47.33  E-value: 2.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194 150 VSRLLSEGADVNAKHRLGWTALMVAAINRNN-SVVQVLLAAGADPNLGDDFssvyktakeqgihslevlitreddfnnrl 228
Cdd:PHA03095  66 VRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKAGADVNAKDKV----------------------------- 116

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 385719194 229 nnrasfkGCTALH-Y-AVLADDYRTVKELLDGGANPLQRNEMGHTPLD 274
Cdd:PHA03095 117 -------GRTPLHvYlSGFNINPKVIRLLLRKGADVNALDLYGMTPLA 157
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 133-276 2.76e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 47.18  E-value: 2.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194 133 NKDAALLEAARANNMQEVSR-LLSEGADVNAKHRLGWTALMVAAINRNNSVVQVLLAAGADPNLGDDFSSV---YKTAKE 208
Cdd:PHA02878 166 HKGNTALHYATENKDQRLTElLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTplhISVGYC 245

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 385719194 209 QGIHSLEVLITREDDfnnrLNNRASFKGCTALHYAVlaDDYRTVKELLDGGANPLQRNEMGHTPLDYA 276
Cdd:PHA02878 246 KDYDILKLLLEHGVD----VNAKSYILGLTALHSSI--KSERKLKLLLEYGADINSLNSYKLTPLSSA 307
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 132-261 3.15e-05

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: 47.38  E-value: 3.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194  132 SNKDAALLEAARANNMQEVSRLLSEGA--DVNAKHRLGWTALMVAAI-NRNNSVVQVLLAAGADPNLGDdfSSVYKTAKE 208
Cdd:TIGR00870  15 SDEEKAFLPAAERGDLASVYRDLEEPKklNINCPDRLGRSALFVAAIeNENLELTELLLNLSCRGAVGD--TLLHAISLE 92

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 385719194  209 -----QGIHSLEVLITREDDFNNRLNNRAS---FKGCTALHYAVLADDYRTVKELLDGGAN 261
Cdd:TIGR00870  93 yvdavEAILLHLLAAFRKSGPLELANDQYTsefTPGITALHLAAHRQNYEIVKLLLERGAS 153
PHA03095 PHA03095
ankyrin-like protein; Provisional
 153-276 3.72e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.56  E-value: 3.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194 153 LLSEGADVNAKHRLGWTALMVAAINRNNSV--VQVLLAAGADPnlgddfssvyktakeqgihslevlITREDDFNNRLNN 230
Cdd:PHA03095 138 LLRKGADVNALDLYGMTPLAVLLKSRNANVelLRLLIDAGADV------------------------YAVDDRFRSLLHH 193

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 385719194 231 RA-SFKgctalhyavlaDDYRTVKELLDGGANPLQRNEMGHTPLDYA 276
Cdd:PHA03095 194 HLqSFK-----------PRARIVRELIRAGCDPAATDMLGNTPLHSM 229
Ank_5 pfam13857
Ankyrin repeats (many copies);
153-199 4.13e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.56  E-value: 4.13e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 385719194  153 LLSEG-ADVNAKHRLGWTALMVAAINRNNSVVQVLLAAGADPNLGDDF 199
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEE 48
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 153-273 5.23e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.60  E-value: 5.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194 153 LLSEGADVNAKHRLGWTALMVAAINRNNSVVQVLLAAGADPNL--GDDFSSVYKTAKEQGIHSLEVLITREDDFN----- 225
Cdd:PHA02876 164 LLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIiaLDDLSVLECAVDSKNIDTIKAIIDNRSNINkndls 243

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 385719194 226 --NRLNNR---------------ASFKGC--TALHYAVLADDY-RTVKELLDGGANPLQRNEMGHTPL 273
Cdd:PHA02876 244 llKAIRNEdletslllydagfsvNSIDDCknTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPL 311
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 138-278 5.27e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 46.11  E-value: 5.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194 138 LLEAARANNMQEVSRLLSEGADVNAKHRLGWTALMVAAINRNNSVVQVLLAAGAD------PNLGDDF------------ 199
Cdd:PHA02874  39 LIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDtsilpiPCIEKDMiktildcgidvn 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194 200 -------SSVYKTAKEQGIHSLEVLITREDDFNNRLNNrasfkGCTALHYAVLADDYRTVKELLDGGANPLQRNEMGHTP 272
Cdd:PHA02874 119 ikdaelkTFLHYAIKKGDLESIKMLFEYGADVNIEDDN-----GCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESP 193


                 ....*.
gi 385719194 273 LDYARE 278
Cdd:PHA02874 194 LHNAAE 199
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 167-198 5.47e-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: 40.74  E-value: 5.47e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 385719194  167 GWTALMVAAINRNN-SVVQVLLAAGADPNLGDD 198
Cdd:pfam00023   2 GNTPLHLAAGRRGNlEIVKLLLSKGADVNARDK 34
Zeta_toxin pfam06414
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is ...
 342-415 9.61e-05

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: 43.89  E-value: 9.61e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 385719194  342 EHPLVFLFLGSSGIGKTELAKQTAKYMhkDAKKGFIRLDMSEFQERH-EVAKFIGSPP---GYVGHEEGGQLTKKLKQ 415
Cdd:pfam06414   9 ERPKAILLGGQPGAGKTELARALLDEL--GRQGNVVRIDPDDFRELHpHYRELQAADPktaSEYTQPDASRWVEKLLQ 84
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 133-276 1.23e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 44.98  E-value: 1.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194 133 NKDAALLEAARANNMQEVSRLLSEGADVNAKHRLGWTALMVAAINRNNSVVQVLLAAGADPNLGD-DFSSVYKTAKEQG- 210
Cdd:PHA02875   1 MDQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYpDIESELHDAVEEGd 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 385719194 211 IHSLEVLItredDFNNRLNNRASFKGCTALHYAVLADDYRTVKELLDGGANPLQRNEMGHTPLDYA 276
Cdd:PHA02875  81 VKAVEELL----DLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLA 142
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 235-267 1.83e-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: 39.19  E-value: 1.83e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 385719194  235 KGCTALHYAVL-ADDYRTVKELLDGGANPLQRNE 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 4.60e-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: 4.60e-04
                           10        20
                   ....*....|....*....|....*...
gi 385719194   235 KGCTALHYAVLADDYRTVKELLDGGANP 262
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
Ank_2 pfam12796
Ankyrin repeats (3 copies);
240-285 5.38e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 39.33  E-value: 5.38e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 385719194  240 LHYAVLADDYRTVKELLDGGANPLQRNEMGHTPLDYA-REG--EVMKLL 285
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAaKNGhlEIVKLL 49
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 167-195 5.60e-04

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.57  E-value: 5.60e-04
                           10        20
                   ....*....|....*....|....*....
gi 385719194   167 GWTALMVAAINRNNSVVQVLLAAGADPNL 195
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 167-194 7.99e-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: 37.24  E-value: 7.99e-04
                          10        20
                  ....*....|....*....|....*...
gi 385719194  167 GWTALMVAAINRNNSVVQVLLAAGADPN 194
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADIN 29
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 153-236 1.70e-03

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.42  E-value: 1.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194 153 LLSEGADVNAKHRLGWTALMVAAINRNNSVVQVLLAAGADPNLGD-DFSSVYKTAKEQGIHSLEVLITREDDFNNRLNNR 231
Cdd:PTZ00322 101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDkDGKTPLELAEENGFREVVQLLSRHSQCHFELGAN 180


                 ....*...
gi 385719194 232 A---SFKG 236
Cdd:PTZ00322 181 AkpdSFTG 188
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
 346-487 1.96e-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: 39.85  E-value: 1.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194 346 VFLFLGSSGIGKTELAKQTAKYMHKDakkgFIRL------DMSEFqeRHEVAKFIGSPPGyvgheeggQLTKKLKQCP-- 417
Cdd:cd19500   39 ILCLVGPPGVGKTSLGKSIARALGRK----FVRIslggvrDEAEI--RGHRRTYVGAMPG--------RIIQALKKAGtn 104

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 385719194 418 NAVVLFDEVDK----AHPDVLTIMLQLFD---EGRLTDGK-GKTIDCKDAIFIMTSNVAsDEIAQhALQLRQEALEMS 487
Cdd:cd19500  105 NPVFLLDEIDKigssFRGDPASALLEVLDpeqNSTFSDHYlDVPFDLSKVLFIATANSL-DTIPG-PLLDRMEIIELS 180
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 347-427 3.98e-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: 3.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194 347 FLFLGSSGIGKTELAKQTAKYMhkDAKkgFIRLDMSEFqerheVAKFIGsppgyvgheEGGQLTKKL----KQCPNAVVL 422
Cdd:COG1222  115 VLLYGPPGTGKTLLAKAVAGEL--GAP--FIRVRGSEL-----VSKYIG---------EGARNVREVfelaREKAPSIIF 176


                 ....*
gi 385719194 423 FDEVD 427
Cdd:COG1222  177 IDEID 181
Ank_4 pfam13637
Ankyrin repeats (many copies);
238-276 5.73e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 35.33  E-value: 5.73e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 385719194  238 TALHYAVLADDYRTVKELLDGGANPLQRNEMGHTPLDYA 276
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFA 41
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 137-192 6.63e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 39.26  E-value: 6.63e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 385719194 137 ALLEAARANNMQEVSRLLSEGADVNAKHRLGWTALMVAAINRNNSVVQVLLAAGAD 192
Cdd:PHA03100 195 PLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
ftsH CHL00176
cell division protein; Validated
 343-427 8.86e-03

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 39.26  E-value: 8.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385719194 343 HPLVFLFLGSSGIGKTELAKQTAkymhKDAKKGFIRLDMSEFQERhevakFIGsppgyVGHEEGGQLTKKLKQCPNAVVL 422
Cdd:CHL00176 215 IPKGVLLVGPPGTGKTLLAKAIA----GEAEVPFFSISGSEFVEM-----FVG-----VGAARVRDLFKKAKENSPCIVF 280


                 ....*
gi 385719194 423 FDEVD 427
Cdd:CHL00176 281 IDEID 285
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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