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Conserved domains on  [gi|755522259|ref|XP_011240004|]
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mitochondrial disaggregase isoform X2 [Mus musculus]

Protein Classification

ankyrin repeat domain-containing protein( domain architecture ID 13793570)

ankyrin repeat (ANK) domain-containing protein mediates specific protein-protein interactions without necessarily recognizing specific primary sequences which allows for one ankyrin repeat domain to recognize and bind to a variety of intracellular substrates and may be involved in a wide array of functions

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 ...
 201-517 8.28e-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: 313.17  E-value: 8.28e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259 201 LEQRLKEHIIGQESAIATVGAAIRRKENGWYDEEHPL-VFLFLGSSGIGKTELAKQTAKYMHkDAKKGFIRLDMSEFQER 279
Cdd:COG0542  543 LEEELHERVIGQDEAVEAVADAIRRSRAGLKDPNRPIgSFLFLGPTGVGKTELAKALAEFLF-GDEDALIRIDMSEYMEK 621

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259 280 HEVAKFIGSPPGYIGHEEGGQLTKKLKQCPNAVVLFDEVDKAHPDVLTIMLQLFDEGRLTDGKGKTIDCKDAIFIMTSNV 359
Cdd:COG0542  622 HSVSRLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLLDEIEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTIIIMTSNI 701

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259 360 ASDEIAQHAlqlrqealemsrnriaenlGDVQMSDKItisknfkENVIRPILKAHFrRDEFLGRINEIVYFLPFCHSELI 439
Cdd:COG0542  702 GSELILDLA-------------------EDEPDYEEM-------KEAVMEELKKHF-RPEFLNRIDEIIVFHPLSKEELR 754

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755522259 440 QLVNKELNFWAKRAKQRhNITLLWDREVADVLVD-GYNVHYGARSIKHEVERRVVNQLAAAYEQDLLPGGCTLRITVED 517
Cdd:COG0542  755 KIVDLQLKRLRKRLAER-GITLELTDAAKDFLAEkGYDPEYGARPLKRAIQRELEDPLAEEILAGEIKEGDTITVDVDD 832
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-178 6.40e-24

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 101.95  E-value: 6.40e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259   1 MEAARANNVQEVRRLLSEGADVNARHKLGWTALMVASISHNESVVQVLLAAGADPNLgdefssvyktANEQGVHSL---- 76
Cdd:COG0666   92 HAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNA----------QDNDGNTPLhlaa 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259  77 EDGRQDCASWrmtnqwtsalefrrwlgvpvgvLVTREDDFNNRLNHrasfkGCTALHYAVLADDYSIVKELLDRGANPLQ 156
Cdd:COG0666  162 ANGNLEIVKL----------------------LLEAGADVNARDND-----GETPLHLAAENGHLEIVKLLLEAGADVNA 214

                        170       180
                 ....*....|....*....|....*
gi 755522259 157 RNEMGHTPLDYARE---GEVMKLLK 178
Cdd:COG0666  215 KDNDGKTALDLAAEngnLEIVKLLL 239
 
Name Accession Description Interval E-value
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 201-517 8.28e-97

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 313.17  E-value: 8.28e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259 201 LEQRLKEHIIGQESAIATVGAAIRRKENGWYDEEHPL-VFLFLGSSGIGKTELAKQTAKYMHkDAKKGFIRLDMSEFQER 279
Cdd:COG0542  543 LEEELHERVIGQDEAVEAVADAIRRSRAGLKDPNRPIgSFLFLGPTGVGKTELAKALAEFLF-GDEDALIRIDMSEYMEK 621

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259 280 HEVAKFIGSPPGYIGHEEGGQLTKKLKQCPNAVVLFDEVDKAHPDVLTIMLQLFDEGRLTDGKGKTIDCKDAIFIMTSNV 359
Cdd:COG0542  622 HSVSRLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLLDEIEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTIIIMTSNI 701

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259 360 ASDEIAQHAlqlrqealemsrnriaenlGDVQMSDKItisknfkENVIRPILKAHFrRDEFLGRINEIVYFLPFCHSELI 439
Cdd:COG0542  702 GSELILDLA-------------------EDEPDYEEM-------KEAVMEELKKHF-RPEFLNRIDEIIVFHPLSKEELR 754

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755522259 440 QLVNKELNFWAKRAKQRhNITLLWDREVADVLVD-GYNVHYGARSIKHEVERRVVNQLAAAYEQDLLPGGCTLRITVED 517
Cdd:COG0542  755 KIVDLQLKRLRKRLAER-GITLELTDAAKDFLAEkGYDPEYGARPLKRAIQRELEDPLAEEILAGEIKEGDTITVDVDD 832
chaperone_ClpB TIGR03346
ATP-dependent chaperone ClpB; Members of this protein family are the bacterial ATP-dependent ...
 170-517 1.87e-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: 269.52  E-value: 1.87e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259  170 EGEVMKLLKtsetkymekqrkreaeerrrfpLEQRLKEHIIGQESAIATVGAAIRRKENGWYDEEHPL-VFLFLGSSGIG 248
Cdd:TIGR03346 549 EGEREKLLH----------------------MEEELHERVVGQDEAVEAVSDAIRRSRAGLSDPNRPIgSFLFLGPTGVG 606

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259  249 KTELAKQTAKYMHkDAKKGFIRLDMSEFQERHEVAKFIGSPPGYIGHEEGGQLTKKLKQCPNAVVLFDEVDKAHPDVLTI 328
Cdd:TIGR03346 607 KTELAKALAEFLF-DSEDAMVRIDMSEYMEKHSVARLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLFDEVEKAHPDVFNV 685

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259  329 MLQLFDEGRLTDGKGKTIDCKDAIFIMTSNVASDEIAQhalQLRQEALEMSRNRIAEnlgdvqmsdkitisknfkenvir 408
Cdd:TIGR03346 686 LLQVLDDGRLTDGQGRTVDFRNTVIIMTSNLGSDFIQE---LAGGDDYEEMREAVME----------------------- 739

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259  409 pILKAHFrRDEFLGRINEIVYFLPFCHSELIQLVNKELNFWAKRAKQRHnITLLWDREVADVLVD-GYNVHYGARSIKHE 487
Cdd:TIGR03346 740 -VLRAHF-RPEFLNRIDEIVVFHPLGREQIARIVEIQLGRLRKRLAERK-ITLELSDAALDFLAEaGYDPVYGARPLKRA 816

                         330       340       350
                  ....*....|....*....|....*....|....
gi 755522259  488 VERRVVNQLAaayeQDLLPG----GCTLRITVED 517
Cdd:TIGR03346 817 IQREIENPLA----KKILAGevapGDTIRVDVEG 846
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
 201-363 1.20e-78

Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and eukaryotic Heat shock protein 104 (Hsp104) are ATP-dependent molecular chaperones and essential proteins of the heat-shock response. ClpB/Hsp104 ATPases, in concert with the DnaK/Hsp70 chaperone system, disaggregate and reactivate aggregated proteins. This RecA-like_ClpB_Hsp104_like subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410907 [Multi-domain]  Cd Length: 178  Bit Score: 245.55  E-value: 1.20e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259 201 LEQRLKEHIIGQESAIATVGAAIRRKENGWYDEEHPL-VFLFLGSSGIGKTELAKQTAKYMHKDaKKGFIRLDMSEFQER 279
Cdd:cd19499    5 LEERLHERVVGQDEAVKAVSDAIRRARAGLSDPNRPIgSFLFLGPTGVGKTELAKALAELLFGD-EDNLIRIDMSEYMEK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259 280 HEVAKFIGSPPGYIGHEEGGQLTKKLKQCPNAVVLFDEVDKAHPDVLTIMLQLFDEGRLTDGKGKTIDCKDAIFIMTSNV 359
Cdd:cd19499   84 HSVSRLIGAPPGYVGYTEGGQLTEAVRRKPYSVVLLDEIEKAHPDVQNLLLQVLDDGRLTDSHGRTVDFKNTIIIMTSNH 163


                 ....
gi 755522259 360 ASDE 363
Cdd:cd19499  164 FRPE 167
clpC CHL00095
Clp protease ATP binding subunit
 201-517 8.56e-78

Clp protease ATP binding subunit


Pssm-ID: 214361 [Multi-domain]  Cd Length: 821  Bit Score: 261.91  E-value: 8.56e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259 201 LEQRLKEHIIGQESAIATVGAAIRRKENGWYDEEHPLV-FLFLGSSGIGKTELAKQTAKYMHkDAKKGFIRLDMSEFQER 279
Cdd:CHL00095 503 MEETLHKRIIGQDEAVVAVSKAIRRARVGLKNPNRPIAsFLFSGPTGVGKTELTKALASYFF-GSEDAMIRLDMSEYMEK 581

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259 280 HEVAKFIGSPPGYIGHEEGGQLTKKLKQCPNAVVLFDEVDKAHPDVLTIMLQLFDEGRLTDGKGKTIDCKDAIFIMTSNV 359
Cdd:CHL00095 582 HTVSKLIGSPPGYVGYNEGGQLTEAVRKKPYTVVLFDEIEKAHPDIFNLLLQILDDGRLTDSKGRTIDFKNTLIIMTSNL 661

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259 360 ASdeiaqhalqlrqealemsrNRIAENLGDVQM--SDKITISKNFKE--NVIRPILKAHFrRDEFLGRINEIVYFLPFCH 435
Cdd:CHL00095 662 GS-------------------KVIETNSGGLGFelSENQLSEKQYKRlsNLVNEELKQFF-RPEFLNRLDEIIVFRQLTK 721

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259 436 SELIQLVNKELNFWAKRAKQRhNITLLWDREVADVLVD-GYNVHYGARSIKHEVERRVVNQLAAAYEQDLLPGGCTLRIT 514
Cdd:CHL00095 722 NDVWEIAEIMLKNLFKRLNEQ-GIQLEVTERIKTLLIEeGYNPLYGARPLRRAIMRLLEDPLAEEVLSFKIKPGDIIIVD 800


                 ...
gi 755522259 515 VED 517
Cdd:CHL00095 801 VND 803
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
 238-427 5.11e-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: 214.75  E-value: 5.11e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259  238 VFLFLGSSGIGKTELAKQTAKYMHKDAKKgFIRLDMSEFQERHEVAKFIGSPPGYIGHEEGGQLTKKLKQCPNAVVLFDE 317
Cdd:pfam07724   5 SFLFLGPTGVGKTELAKALAELLFGDERA-LIRIDMSEYMEEHSVSRLIGAPPGYVGYEEGGQLTEAVRRKPYSIVLIDE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259  318 VDKAHPDVLTIMLQLFDEGRLTDGKGKTIDCKDAIFIMTSNVASDEIAQHALqlrqealemsrnriaenlgdvqmsDKIT 397
Cdd:pfam07724  84 IEKAHPGVQNDLLQILEGGTLTDKQGRTVDFKNTLFIMTGNFGSEKISDASR------------------------LGDS 139

                         170       180       190
                  ....*....|....*....|....*....|
gi 755522259  398 ISKNFKENVIRPILKAHFRRdEFLGRINEI 427
Cdd:pfam07724 140 PDYELLKEEVMDLLKKGFIP-EFLGRLPII 168
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-178 6.40e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 101.95  E-value: 6.40e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259   1 MEAARANNVQEVRRLLSEGADVNARHKLGWTALMVASISHNESVVQVLLAAGADPNLgdefssvyktANEQGVHSL---- 76
Cdd:COG0666   92 HAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNA----------QDNDGNTPLhlaa 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259  77 EDGRQDCASWrmtnqwtsalefrrwlgvpvgvLVTREDDFNNRLNHrasfkGCTALHYAVLADDYSIVKELLDRGANPLQ 156
Cdd:COG0666  162 ANGNLEIVKL----------------------LLEAGADVNARDND-----GETPLHLAAENGHLEIVKLLLEAGADVNA 214

                        170       180
                 ....*....|....*....|....*
gi 755522259 157 RNEMGHTPLDYARE---GEVMKLLK 178
Cdd:COG0666  215 KDNDGKTALDLAAEngnLEIVKLLL 239
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 235-372 2.40e-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: 2.40e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259   235 HPLVFLFLGSSGIGKTELAKQTAKYMHKDaKKGFIRLDMSEFQERHEVAKFIGSPPGYIGHEEGGQ----LTKKLKQCPN 310
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPP-GGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELrlrlALALARKLKP 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755522259   311 AVVLFDEVDKAHPDVLTIMLQLFDEGRLtdgKGKTIDCKDAIFIMTSNVASDEIAqHALQLR 372
Cdd:smart00382  80 DVLILDEITSLLDAEQEALLLLLEELRL---LLLLKSEKNLTVILTTNDEKDLGP-ALLRRR 137
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1-158 2.33e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 57.43  E-value: 2.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259    1 MEAARANNVQEVRRLLSEGADVNARHKLGWTALMVASISHNESVVQVLLAagadpnlgdefssvyktaneqgvhsledgr 80
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE------------------------------ 51

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755522259   81 qdcaswrmtnqwtsalefrrwlgvpvgvlvtrEDDFNNRLNhrasfkGCTALHYAVLADDYSIVKELLDRGANPLQRN 158
Cdd:pfam12796  52 --------------------------------HADVNLKDN------GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 5-168 1.34e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 54.26  E-value: 1.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259   5 RANNVQEVRRLLSE-GADVNARHKLGWTALMV--ASISHNESVVQVLLAAGADPNLGDEFSSvyktaneqgvhsledgrq 81
Cdd:PHA03095  92 YNATTLDVIKLLIKaGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGM------------------ 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259  82 dcaswrmtnqwTSALEFRRWLGVPVGVL----------VTREDDFNNRLNHRA-SFKgctalhyavlaDDYSIVKELLDR 150
Cdd:PHA03095 154 -----------TPLAVLLKSRNANVELLrllidagadvYAVDDRFRSLLHHHLqSFK-----------PRARIVRELIRA 211

                        170
                 ....*....|....*...
gi 755522259 151 GANPLQRNEMGHTPLDYA 168
Cdd:PHA03095 212 GCDPAATDMLGNTPLHSM 229
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 2-165 1.09e-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: 51.55  E-value: 1.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259   2 EAARANNVQEVRRLL-SEGADVNARHKLGWTALMVASISHNESVVQVLLAagADPNLGDE--FSSVYK--TA-------- 68
Cdd:cd22192   23 LAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPELVNEpmTSDLYQgeTAlhiavvnq 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259  69 NEQGVHSLEDGRQDCASWRMTNQWtsaleFRRwlgVPVGVLVTREddfnnrlnHRASFKGCTALHyavladdySIVKELL 148
Cdd:cd22192  101 NLNLVRELIARGADVVSPRATGTF-----FRP---GPKNLIYYGE--------HPLSFAACVGNE--------EIVRLLI 156

                        170
                 ....*....|....*..
gi 755522259 149 DRGANPLQRNEMGHTPL 165
Cdd:cd22192  157 EHGADIRAQDSLGNTVL 173
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 127-154 2.43e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.42  E-value: 2.43e-05
                           10        20
                   ....*....|....*....|....*...
gi 755522259   127 KGCTALHYAVLADDYSIVKELLDRGANP 154
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 3-153 8.80e-04

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 42.38  E-value: 8.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259    3 AARANNVQEVRRLLSEGA--DVNARHKLGWTALMVASI-SHNESVVQVLLAAGADPNLGDefSSVYKTANEqgvhsLEDG 79
Cdd:TIGR00870  24 AAERGDLASVYRDLEEPKklNINCPDRLGRSALFVAAIeNENLELTELLLNLSCRGAVGD--TLLHAISLE-----YVDA 96

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755522259   80 RQDCASWRMTNQwtsalefrRWLGVPVGVLVTREDDFnnrlnhrasFKGCTALHYAVLADDYSIVKELLDRGAN 153
Cdd:TIGR00870  97 VEAILLHLLAAF--------RKSGPLELANDQYTSEF---------TPGITALHLAAHRQNYEIVKLLLERGAS 153
 
Name Accession Description Interval E-value
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 201-517 8.28e-97

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 313.17  E-value: 8.28e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259 201 LEQRLKEHIIGQESAIATVGAAIRRKENGWYDEEHPL-VFLFLGSSGIGKTELAKQTAKYMHkDAKKGFIRLDMSEFQER 279
Cdd:COG0542  543 LEEELHERVIGQDEAVEAVADAIRRSRAGLKDPNRPIgSFLFLGPTGVGKTELAKALAEFLF-GDEDALIRIDMSEYMEK 621

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259 280 HEVAKFIGSPPGYIGHEEGGQLTKKLKQCPNAVVLFDEVDKAHPDVLTIMLQLFDEGRLTDGKGKTIDCKDAIFIMTSNV 359
Cdd:COG0542  622 HSVSRLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLLDEIEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTIIIMTSNI 701

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259 360 ASDEIAQHAlqlrqealemsrnriaenlGDVQMSDKItisknfkENVIRPILKAHFrRDEFLGRINEIVYFLPFCHSELI 439
Cdd:COG0542  702 GSELILDLA-------------------EDEPDYEEM-------KEAVMEELKKHF-RPEFLNRIDEIIVFHPLSKEELR 754

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755522259 440 QLVNKELNFWAKRAKQRhNITLLWDREVADVLVD-GYNVHYGARSIKHEVERRVVNQLAAAYEQDLLPGGCTLRITVED 517
Cdd:COG0542  755 KIVDLQLKRLRKRLAER-GITLELTDAAKDFLAEkGYDPEYGARPLKRAIQRELEDPLAEEILAGEIKEGDTITVDVDD 832
chaperone_ClpB TIGR03346
ATP-dependent chaperone ClpB; Members of this protein family are the bacterial ATP-dependent ...
 170-517 1.87e-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: 269.52  E-value: 1.87e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259  170 EGEVMKLLKtsetkymekqrkreaeerrrfpLEQRLKEHIIGQESAIATVGAAIRRKENGWYDEEHPL-VFLFLGSSGIG 248
Cdd:TIGR03346 549 EGEREKLLH----------------------MEEELHERVVGQDEAVEAVSDAIRRSRAGLSDPNRPIgSFLFLGPTGVG 606

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259  249 KTELAKQTAKYMHkDAKKGFIRLDMSEFQERHEVAKFIGSPPGYIGHEEGGQLTKKLKQCPNAVVLFDEVDKAHPDVLTI 328
Cdd:TIGR03346 607 KTELAKALAEFLF-DSEDAMVRIDMSEYMEKHSVARLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLFDEVEKAHPDVFNV 685

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259  329 MLQLFDEGRLTDGKGKTIDCKDAIFIMTSNVASDEIAQhalQLRQEALEMSRNRIAEnlgdvqmsdkitisknfkenvir 408
Cdd:TIGR03346 686 LLQVLDDGRLTDGQGRTVDFRNTVIIMTSNLGSDFIQE---LAGGDDYEEMREAVME----------------------- 739

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259  409 pILKAHFrRDEFLGRINEIVYFLPFCHSELIQLVNKELNFWAKRAKQRHnITLLWDREVADVLVD-GYNVHYGARSIKHE 487
Cdd:TIGR03346 740 -VLRAHF-RPEFLNRIDEIVVFHPLGREQIARIVEIQLGRLRKRLAERK-ITLELSDAALDFLAEaGYDPVYGARPLKRA 816

                         330       340       350
                  ....*....|....*....|....*....|....
gi 755522259  488 VERRVVNQLAaayeQDLLPG----GCTLRITVED 517
Cdd:TIGR03346 817 IQREIENPLA----KKILAGevapGDTIRVDVEG 846
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
 201-363 1.20e-78

Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and eukaryotic Heat shock protein 104 (Hsp104) are ATP-dependent molecular chaperones and essential proteins of the heat-shock response. ClpB/Hsp104 ATPases, in concert with the DnaK/Hsp70 chaperone system, disaggregate and reactivate aggregated proteins. This RecA-like_ClpB_Hsp104_like subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410907 [Multi-domain]  Cd Length: 178  Bit Score: 245.55  E-value: 1.20e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259 201 LEQRLKEHIIGQESAIATVGAAIRRKENGWYDEEHPL-VFLFLGSSGIGKTELAKQTAKYMHKDaKKGFIRLDMSEFQER 279
Cdd:cd19499    5 LEERLHERVVGQDEAVKAVSDAIRRARAGLSDPNRPIgSFLFLGPTGVGKTELAKALAELLFGD-EDNLIRIDMSEYMEK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259 280 HEVAKFIGSPPGYIGHEEGGQLTKKLKQCPNAVVLFDEVDKAHPDVLTIMLQLFDEGRLTDGKGKTIDCKDAIFIMTSNV 359
Cdd:cd19499   84 HSVSRLIGAPPGYVGYTEGGQLTEAVRRKPYSVVLLDEIEKAHPDVQNLLLQVLDDGRLTDSHGRTVDFKNTIIIMTSNH 163


                 ....
gi 755522259 360 ASDE 363
Cdd:cd19499  164 FRPE 167
clpC CHL00095
Clp protease ATP binding subunit
 201-517 8.56e-78

Clp protease ATP binding subunit


Pssm-ID: 214361 [Multi-domain]  Cd Length: 821  Bit Score: 261.91  E-value: 8.56e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259 201 LEQRLKEHIIGQESAIATVGAAIRRKENGWYDEEHPLV-FLFLGSSGIGKTELAKQTAKYMHkDAKKGFIRLDMSEFQER 279
Cdd:CHL00095 503 MEETLHKRIIGQDEAVVAVSKAIRRARVGLKNPNRPIAsFLFSGPTGVGKTELTKALASYFF-GSEDAMIRLDMSEYMEK 581

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259 280 HEVAKFIGSPPGYIGHEEGGQLTKKLKQCPNAVVLFDEVDKAHPDVLTIMLQLFDEGRLTDGKGKTIDCKDAIFIMTSNV 359
Cdd:CHL00095 582 HTVSKLIGSPPGYVGYNEGGQLTEAVRKKPYTVVLFDEIEKAHPDIFNLLLQILDDGRLTDSKGRTIDFKNTLIIMTSNL 661

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259 360 ASdeiaqhalqlrqealemsrNRIAENLGDVQM--SDKITISKNFKE--NVIRPILKAHFrRDEFLGRINEIVYFLPFCH 435
Cdd:CHL00095 662 GS-------------------KVIETNSGGLGFelSENQLSEKQYKRlsNLVNEELKQFF-RPEFLNRLDEIIVFRQLTK 721

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259 436 SELIQLVNKELNFWAKRAKQRhNITLLWDREVADVLVD-GYNVHYGARSIKHEVERRVVNQLAAAYEQDLLPGGCTLRIT 514
Cdd:CHL00095 722 NDVWEIAEIMLKNLFKRLNEQ-GIQLEVTERIKTLLIEeGYNPLYGARPLRRAIMRLLEDPLAEEVLSFKIKPGDIIIVD 800


                 ...
gi 755522259 515 VED 517
Cdd:CHL00095 801 VND 803
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
 238-427 5.11e-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: 214.75  E-value: 5.11e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259  238 VFLFLGSSGIGKTELAKQTAKYMHKDAKKgFIRLDMSEFQERHEVAKFIGSPPGYIGHEEGGQLTKKLKQCPNAVVLFDE 317
Cdd:pfam07724   5 SFLFLGPTGVGKTELAKALAELLFGDERA-LIRIDMSEYMEEHSVSRLIGAPPGYVGYEEGGQLTEAVRRKPYSIVLIDE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259  318 VDKAHPDVLTIMLQLFDEGRLTDGKGKTIDCKDAIFIMTSNVASDEIAQHALqlrqealemsrnriaenlgdvqmsDKIT 397
Cdd:pfam07724  84 IEKAHPGVQNDLLQILEGGTLTDKQGRTVDFKNTLFIMTGNFGSEKISDASR------------------------LGDS 139

                         170       180       190
                  ....*....|....*....|....*....|
gi 755522259  398 ISKNFKENVIRPILKAHFRRdEFLGRINEI 427
Cdd:pfam07724 140 PDYELLKEEVMDLLKKGFIP-EFLGRLPII 168
ClpA TIGR02639
ATP-dependent Clp protease ATP-binding subunit clpA; [Protein fate, Degradation of proteins, ...
 201-497 2.10e-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: 226.83  E-value: 2.10e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259  201 LEQRLKEHIIGQESAIATVGAAIRRKENGWYDEEHPL-VFLFLGSSGIGKTELAKQTAKYMhkdakkG--FIRLDMSEFQ 277
Cdd:TIGR02639 447 LEKNLKAKIFGQDEAIDQLVSAIKRSRAGLGDPNKPVgSFLFVGPTGVGKTELAKQLAEEL------GvhLLRFDMSEYM 520

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259  278 ERHEVAKFIGSPPGYIGHEEGGQLTKKLKQCPNAVVLFDEVDKAHPDVLTIMLQLFDEGRLTDGKGKTIDCKDAIFIMTS 357
Cdd:TIGR02639 521 EKHTVSRLIGSPPGYVGFEQGGLLTDAVRKHPHCVLLLDEIEKAHPDIYNILLQVMDYATLTDNNGRKADFRNVILIMTS 600

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259  358 NVASDEIAQHALQLRQEALEMSRNRiaenlgdvqmsdkiTISKNFKenvirPilkahfrrdEFLGRINEIVYFLPFCHSE 437
Cdd:TIGR02639 601 NAGASEMSKPPIGFGGENRESKSLK--------------AIKKLFS-----P---------EFRNRLDAIIHFNDLSEEM 652

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755522259  438 LIQLVNKELNFWAKRAKQRhNITLLWDREVADVLVD-GYNVHYGARSIKHEVERRVVNQLA 497
Cdd:TIGR02639 653 AEKIVKKFLDELQDQLNEK-NIELELTDDAKKYLAEkGYDEEFGARPLARVIQEEIKKPLS 712
PRK10865 PRK10865
ATP-dependent chaperone ClpB;
201-518 2.11e-61

ATP-dependent chaperone ClpB;


Pssm-ID: 182791 [Multi-domain]  Cd Length: 857  Bit Score: 217.79  E-value: 2.11e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259 201 LEQRLKEHIIGQESAIATVGAAIRRKENGWYDEEHPL-VFLFLGSSGIGKTELAKQTAKYMHkDAKKGFIRLDMSEFQER 279
Cdd:PRK10865 562 MEQELHHRVIGQNEAVEAVSNAIRRSRAGLSDPNRPIgSFLFLGPTGVGKTELCKALANFMF-DSDDAMVRIDMSEFMEK 640

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259 280 HEVAKFIGSPPGYIGHEEGGQLTKKLKQCPNAVVLFDEVDKAHPDVLTIMLQLFDEGRLTDGKGKTIDCKDAIFIMTSNV 359
Cdd:PRK10865 641 HSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTVVIMTSNL 720

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259 360 ASDeiaqhalqlrqealemsrnRIAENLGDVQMSDkitisknFKENVIRpILKAHFrRDEFLGRINEIVYFLPFCHSELI 439
Cdd:PRK10865 721 GSD-------------------LIQERFGELDYAH-------MKELVLG-VVSHNF-RPEFINRIDEVVVFHPLGEQHIA 772

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259 440 QLVNKELNFWAKRAKQRHNITLLWDREVADVLVDGYNVHYGARSIKHEVERRVVNQLAaayeQDLLPG----GCTLRITV 515
Cdd:PRK10865 773 SIAQIQLQRLYKRLEERGYEIHISDEALKLLSENGYDPVYGARPLKRAIQQQIENPLA----QQILSGelvpGKVIRLEV 848


                 ...
gi 755522259 516 EDS 518
Cdd:PRK10865 849 NDD 851
VI_ClpV1 TIGR03345
type VI secretion ATPase, ClpV1 family; Members of this protein family are homologs of ClpB, ...
 201-497 3.64e-61

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: 3.64e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259  201 LEQRLKEHIIGQESAIATVGAAIRRKENGWYDEEHPL-VFLFLGSSGIGKTELAKQTAKYMHkDAKKGFIRLDMSEFQER 279
Cdd:TIGR03345 560 LPDRLAERVIGQDHALEAIAERIRTARAGLEDPRKPLgVFLLVGPSGVGKTETALALAELLY-GGEQNLITINMSEFQEA 638

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259  280 HEVAKFIGSPPGYIGHEEGGQLTKKLKQCPNAVVLFDEVDKAHPDVLTIMLQLFDEGRLTDGKGKTIDCKDAIFIMTSNV 359
Cdd:TIGR03345 639 HTVSRLKGSPPGYVGYGEGGVLTEAVRRKPYSVVLLDEVEKAHPDVLELFYQVFDKGVMEDGEGREIDFKNTVILLTSNA 718

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259  360 ASDEIAQHALQlrqealemsrnriaenlgDVQMSDKITISKnfkenVIRPILKAHFrRDEFLGRINeIVYFLPFCHSELI 439
Cdd:TIGR03345 719 GSDLIMALCAD------------------PETAPDPEALLE-----ALRPELLKVF-KPAFLGRMT-VIPYLPLDDDVLA 773

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 755522259  440 QLVNKELNFWAKRAKQRHNITLLWDREVADVLVDGYN-VHYGARSIKHEVERRVVNQLA 497
Cdd:TIGR03345 774 AIVRLKLDRIARRLKENHGAELVYSEALVEHIVARCTeVESGARNIDAILNQTLLPELS 832
clpA PRK11034
ATP-dependent Clp protease ATP-binding subunit; Provisional
 201-522 2.95e-40

ATP-dependent Clp protease ATP-binding subunit; Provisional


Pssm-ID: 236828 [Multi-domain]  Cd Length: 758  Bit Score: 156.15  E-value: 2.95e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259 201 LEQRLKEHIIGQESAIATVGAAIRRKENGWYDEEHPL-VFLFLGSSGIGKTELAKQTAKYMHKDakkgFIRLDMSEFQER 279
Cdd:PRK11034 452 LGDRLKMLVFGQDKAIEALTEAIKMSRAGLGHEHKPVgSFLFAGPTGVGKTEVTVQLSKALGIE----LLRFDMSEYMER 527

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259 280 HEVAKFIGSPPGYIGHEEGGQLTKKLKQCPNAVVLFDEVDKAHPDVLTIMLQLFDEGRLTDGKGKTIDCKDAIFIMTSNV 359
Cdd:PRK11034 528 HTVSRLIGAPPGYVGFDQGGLLTDAVIKHPHAVLLLDEIEKAHPDVFNLLLQVMDNGTLTDNNGRKADFRNVVLVMTTNA 607

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259 360 ASDEIAQHALQLRQEalEMSRNRIAEnlgdvqmsdkitISKNFKEnvirpilkahfrrdEFLGRINEIVYFLPFCHSELI 439
Cdd:PRK11034 608 GVRETERKSIGLIHQ--DNSTDAMEE------------IKKIFTP--------------EFRNRLDNIIWFDHLSTDVIH 659

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259 440 QLVNKelnFWAKRAKQ--RHNITLLWDREVADVLVD-GYNVHYGARSIKHEVERRVVNQLAAAYEQDLLPGGCTLRITVE 516
Cdd:PRK11034 660 QVVDK---FIVELQAQldQKGVSLEVSQEARDWLAEkGYDRAMGARPMARVIQDNLKKPLANELLFGSLVDGGQVTVALD 736


                 ....*.
gi 755522259 517 DSDKHL 522
Cdd:PRK11034 737 KEKNEL 742
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-178 6.40e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 101.95  E-value: 6.40e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259   1 MEAARANNVQEVRRLLSEGADVNARHKLGWTALMVASISHNESVVQVLLAAGADPNLgdefssvyktANEQGVHSL---- 76
Cdd:COG0666   92 HAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNA----------QDNDGNTPLhlaa 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259  77 EDGRQDCASWrmtnqwtsalefrrwlgvpvgvLVTREDDFNNRLNHrasfkGCTALHYAVLADDYSIVKELLDRGANPLQ 156
Cdd:COG0666  162 ANGNLEIVKL----------------------LLEAGADVNARDND-----GETPLHLAAENGHLEIVKLLLEAGADVNA 214

                        170       180
                 ....*....|....*....|....*
gi 755522259 157 RNEMGHTPLDYARE---GEVMKLLK 178
Cdd:COG0666  215 KDNDGKTALDLAAEngnLEIVKLLL 239
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-177 8.81e-15

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 74.99  E-value: 8.81e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259   1 MEAARANNVQEVRRLLSEGADVNARHKLGWTALMVASISHNESVVQVLLAAGADPNLGDefssvyktaneqgvhsledgr 80
Cdd:COG0666   59 LAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARD--------------------- 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259  81 qdcaswrmtNQWTSALEFRRWLGVP--VGVLVTREDDFNNRLNHrasfkGCTALHYAVLADDYSIVKELLDRGANPLQRN 158
Cdd:COG0666  118 ---------KDGETPLHLAAYNGNLeiVKLLLEAGADVNAQDND-----GNTPLHLAAANGNLEIVKLLLEAGADVNARD 183

                        170       180
                 ....*....|....*....|..
gi 755522259 159 EMGHTPLDYAREG---EVMKLL 177
Cdd:COG0666  184 NDGETPLHLAAENghlEIVKLL 205
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 210-364 1.47e-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: 71.02  E-value: 1.47e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259 210 IGQESAIATVGAAIRRKengwydeeHPLVFLFLGSSGIGKTELAKQTAKYMHKdAKKGFIRLDMSEFQERHEVAkfigsp 289
Cdd:cd00009    1 VGQEEAIEALREALELP--------PPKNLLLYGPPGTGKTTLARAIANELFR-PGAPFLYLNASDLLEGLVVA------ 65

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755522259 290 pGYIGHEEGGQLTKKLKQCPNAVVLFDEVDKAHPDVLTIMLQLFDEGRLTdgkgkTIDCKDAIFIMTSNVASDEI 364
Cdd:cd00009   66 -ELFGHFLVRLLFELAEKAKPGVLFIDEIDSLSRGAQNALLRVLETLNDL-----RIDRENVRVIGATNRPLLGD 134
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 235-372 2.40e-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: 2.40e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259   235 HPLVFLFLGSSGIGKTELAKQTAKYMHKDaKKGFIRLDMSEFQERHEVAKFIGSPPGYIGHEEGGQ----LTKKLKQCPN 310
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPP-GGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELrlrlALALARKLKP 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755522259   311 AVVLFDEVDKAHPDVLTIMLQLFDEGRLtdgKGKTIDCKDAIFIMTSNVASDEIAqHALQLR 372
Cdd:smart00382  80 DVLILDEITSLLDAEQEALLLLLEELRL---LLLLKSEKNLTVILTTNDEKDLGP-ALLRRR 137
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1-158 2.33e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 57.43  E-value: 2.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259    1 MEAARANNVQEVRRLLSEGADVNARHKLGWTALMVASISHNESVVQVLLAagadpnlgdefssvyktaneqgvhsledgr 80
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE------------------------------ 51

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755522259   81 qdcaswrmtnqwtsalefrrwlgvpvgvlvtrEDDFNNRLNhrasfkGCTALHYAVLADDYSIVKELLDRGANPLQRN 158
Cdd:pfam12796  52 --------------------------------HADVNLKDN------GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
ClpB_D2-small pfam10431
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ...
 435-513 3.30e-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: 56.65  E-value: 3.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259  435 HSELIQLVNKELNFWAKRAKQRhNITLLWDREVADVLVD-GYNVHYGARSIKHEVERRVVNQLAAAYEQDLLPGGCTLRI 513
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, ...
 437-519 1.21e-09

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: 55.14  E-value: 1.21e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259   437 ELIQLVNKELNFWAKRAKQRhNITLLWDREVADVLVD-GYNVHYGARSIKHEVERRVVNQLAAAYEQDLLPGGCTLRITV 515
Cdd:smart01086   5 DLVRIVDLPLNALQKRLAEK-GITLEFTDEALDWLAEkGYDPKYGARPLRRIIQRELEDPLAELILSGELKDGDTVVVDV 83


                   ....
gi 755522259   516 EDSD 519
Cdd:smart01086  84 DDGE 87
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
 203-320 1.80e-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: 1.80e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259 203 QRLKEHIIGQESAIATVGAAIRRK------ENGWYDEEHPLVFLFLGSSGIGKTELAKQTAKYmhkdAKKGFIRLDMSEF 276
Cdd:cd19498    7 SELDKYIIGQDEAKRAVAIALRNRwrrmqlPEELRDEVTPKNILMIGPTGVGKTEIARRLAKL----AGAPFIKVEATKF 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 755522259 277 QErhevakfigspPGYIGHEeggqLTKKLKQCPNAVVLFDEVDK 320
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 ...
 224-358 1.87e-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: 1.87e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259 224 RRKENGWYDEEHPLVFLFLGSSGIGKTELAKQTAKYMHKDakkgFIRLDMSEFQErhevaKFIGSppgyiGHEEGGQLTK 303
Cdd:cd19481   14 RGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLP----LIVVKLSSLLS-----KYVGE-----SEKNLRKIFE 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755522259 304 KLKQCPNAVVLFDEVDKAHPD------------VLTIMLQLFDEGRltdgkgktiDCKDAIFIMTSN 358
Cdd:cd19481   80 RARRLAPCILFIDEIDAIGRKrdssgesgelrrVLNQLLTELDGVN---------SRSKVLVIAATN 137
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-59 4.70e-08

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 54.96  E-value: 4.70e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 755522259   1 MEAARANNVQEVRRLLSEGADVNARHKLGWTALMVASISHNESVVQVLLAAGADPNLGD 59
Cdd:COG0666  191 HLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKD 249
PHA03095 PHA03095
ankyrin-like protein; Provisional
 5-168 1.34e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 54.26  E-value: 1.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259   5 RANNVQEVRRLLSE-GADVNARHKLGWTALMV--ASISHNESVVQVLLAAGADPNLGDEFSSvyktaneqgvhsledgrq 81
Cdd:PHA03095  92 YNATTLDVIKLLIKaGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGM------------------ 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259  82 dcaswrmtnqwTSALEFRRWLGVPVGVL----------VTREDDFNNRLNHRA-SFKgctalhyavlaDDYSIVKELLDR 150
Cdd:PHA03095 154 -----------TPLAVLLKSRNANVELLrllidagadvYAVDDRFRSLLHHHLqSFK-----------PRARIVRELIRA 211

                        170
                 ....*....|....*...
gi 755522259 151 GANPLQRNEMGHTPLDYA 168
Cdd:PHA03095 212 GCDPAATDMLGNTPLHSM 229
Ank_5 pfam13857
Ankyrin repeats (many copies);
114-168 3.57e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.34  E-value: 3.57e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 755522259  114 DDFNNRLNHRaSFKGCTALHYAVLADDYSIVKELLDRGANPLQRNEMGHTPLDYA 168
Cdd:pfam13857   3 EHGPIDLNRL-DGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 240-358 5.11e-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: 5.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259  240 LFLGSSGIGKTELAKQTAKYMHKDakkgFIRLDMSEFqerheVAKFIGSPPGYIghEEGGQLTKKLKQCpnaVVLFDEVD 319
Cdd:pfam00004   2 LLYGPPGTGKTTLAKAVAKELGAP----FIEISGSEL-----VSKYVGESEKRL--RELFEAAKKLAPC---VIFIDEID 67

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 755522259  320 KAHP-----------DVLTIMLQLFDegrltdgkGKTIDCKDAIFIMTSN 358
Cdd:pfam00004  68 ALAGsrgsggdsesrRVVNQLLTELD--------GFTSSNSKVIVIAATN 109
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 239-358 5.29e-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: 5.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259  239 FLFLGSSGIGKTELAKQTAKYMHKDakKGFIRL---DMSE---FQERH---EVAKFIGSPpgyigheeggqLTKKLKqcP 309
Cdd:pfam07728   2 VLLVGPPGTGKTELAERLAAALSNR--PVFYVQltrDTTEedlFGRRNidpGGASWVDGP-----------LVRAAR--E 66

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 755522259  310 NAVVLFDEVDKAHPDVLTIMLQLFDEGRLTDGKGKT-IDCKDAIF--IMTSN 358
Cdd:pfam07728  67 GEIAVLDEINRANPDVLNSLLSLLDERRLLLPDGGElVKAAPDGFrlIATMN 118
Ank_4 pfam13637
Ankyrin repeats (many copies);
3-49 1.03e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.73  E-value: 1.03e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 755522259    3 AARANNVQEVRRLLSEGADVNARHKLGWTALMVASISHNESVVQVLL 49
Cdd:pfam13637   8 AAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 2-165 1.09e-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: 51.55  E-value: 1.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259   2 EAARANNVQEVRRLL-SEGADVNARHKLGWTALMVASISHNESVVQVLLAagADPNLGDE--FSSVYK--TA-------- 68
Cdd:cd22192   23 LAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPELVNEpmTSDLYQgeTAlhiavvnq 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259  69 NEQGVHSLEDGRQDCASWRMTNQWtsaleFRRwlgVPVGVLVTREddfnnrlnHRASFKGCTALHyavladdySIVKELL 148
Cdd:cd22192  101 NLNLVRELIARGADVVSPRATGTF-----FRP---GPKNLIYYGE--------HPLSFAACVGNE--------EIVRLLI 156

                        170
                 ....*....|....*..
gi 755522259 149 DRGANPLQRNEMGHTPL 165
Cdd:cd22192  157 EHGADIRAQDSLGNTVL 173
PHA03095 PHA03095
ankyrin-like protein; Provisional
 9-166 1.47e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 50.79  E-value: 1.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259   9 VQEVRRLLSEGADVNARHKLGWTAL---MVASISHNESVVQVLLAAGADPNLGDEFSSvykTAneqgVHSLedgrqdcas 85
Cdd:PHA03095  27 VEEVRRLLAAGADVNFRGEYGKTPLhlyLHYSSEKVKDIVRLLLEAGADVNAPERCGF---TP----LHLY--------- 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259  86 wrMTNQWTsaLEFRRWLgVPVGVLVTREDDFNNrlnhrasfkgcTALH-Y-AVLADDYSIVKELLDRGANPLQRNEMGHT 163
Cdd:PHA03095  91 --LYNATT--LDVIKLL-IKAGADVNAKDKVGR-----------TPLHvYlSGFNINPKVIRLLLRKGADVNALDLYGMT 154


                 ...
gi 755522259 164 PLD 166
Cdd:PHA03095 155 PLA 157
PHA03095 PHA03095
ankyrin-like protein; Provisional
 12-57 2.42e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 50.02  E-value: 2.42e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 755522259  12 VRRLLSEGADVNARHKLGWTALMVASISHNESVVQVLLAAGADPNL 57
Cdd:PHA03095 240 VLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINA 285
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 12-177 2.55e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 50.45  E-value: 2.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259  12 VRRLLSEGADVNARHKLGWTAL-MVASISHNESVVQVLLAAGADPNLGDefsSVYKTANEQGvHSLEDGRQDCASWRMTN 90
Cdd:PHA02876 290 VPKLLERGADVNAKNIKGETPLyLMAKNGYDTENIRTLIMLGADVNAAD---RLYITPLHQA-STLDRNKDIVITLLELG 365

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259  91 QWTSALEFrrWLGVPVGVLVTREDD--FNNRLNHRA-----SFKGCTALHYAVLADD-YSIVKELLDRGANPLQRNEMGH 162
Cdd:PHA02876 366 ANVNARDY--CDKTPIHYAAVRNNVviINTLLDYGAdiealSQKIGTALHFALCGTNpYMSVKTLIDRGANVNSKNKDLS 443

                        170
                 ....*....|....*....
gi 755522259 163 TPLDYAREG----EVMKLL 177
Cdd:PHA02876 444 TPLHYACKKncklDVIEML 462
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 236-358 2.73e-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: 2.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259 236 PLVFLFLGSSGIGKTELAKQTAKYMHKDakkgFIRLDMSEFqerheVAKfigsppgYIGHEEGG--QLTKKLKQCPNAVV 313
Cdd:COG0464  191 PRGLLLYGPPGTGKTLLARALAGELGLP----LIEVDLSDL-----VSK-------YVGETEKNlrEVFDKARGLAPCVL 254

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 755522259 314 LFDEVDKAHPD-----------VLTIMLQLFDEGRltdgkgktidcKDAIFIMTSN 358
Cdd:COG0464  255 FIDEADALAGKrgevgdgvgrrVVNTLLTEMEELR-----------SDVVVIAATN 299
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 127-177 6.81e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 48.51  E-value: 6.81e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 755522259 127 KGCTALHYAVLADDYSIVKELLDRGANPLQRNEMGHTPLDYA---REGEVMKLL 177
Cdd:PHA03100 191 YGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAilnNNKEIFKLL 244
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 127-159 9.77e-06

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 42.66  E-value: 9.77e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 755522259  127 KGCTALHYAVL-ADDYSIVKELLDRGANPLQRNE 159
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 127-154 2.43e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.42  E-value: 2.43e-05
                           10        20
                   ....*....|....*....|....*...
gi 755522259   127 KGCTALHYAVLADDYSIVKELLDRGANP 154
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 15-165 6.88e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.82  E-value: 6.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259  15 LLSEGADVNARHKLGWTALMVASISHNESVVQVLLAAGADPNL--GDEFSSVYKTANEQGVHSLE---DGRQDC------ 83
Cdd:PHA02876 164 LLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIiaLDDLSVLECAVDSKNIDTIKaiiDNRSNInkndls 243

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259  84 --ASWRMTNQWTSALEFrrwlgvPVGVLVTREDDFNNrlnhrasfkgcTALHYAVLADDYS-IVKELLDRGANPLQRNEM 160
Cdd:PHA02876 244 llKAIRNEDLETSLLLY------DAGFSVNSIDDCKN-----------TPLHHASQAPSLSrLVPKLLERGADVNAKNIK 306


                 ....*
gi 755522259 161 GHTPL 165
Cdd:PHA02876 307 GETPL 311
Ank_2 pfam12796
Ankyrin repeats (3 copies);
109-177 8.40e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 41.64  E-value: 8.40e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755522259  109 LVTREDDFNNRLNhrasfKGCTALHYAVLADDYSIVKELLDRGAnpLQRNEMGHTPLDYA-REG--EVMKLL 177
Cdd:pfam12796  16 LLENGADANLQDK-----NGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAaRSGhlEIVKLL 80
Ank_2 pfam12796
Ankyrin repeats (3 copies);
132-177 1.63e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 40.87  E-value: 1.63e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 755522259  132 LHYAVLADDYSIVKELLDRGANPLQRNEMGHTPLDYA-REG--EVMKLL 177
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAaKNGhlEIVKLL 49
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 2-63 2.65e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 44.09  E-value: 2.65e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755522259   2 EAARANNVQEVRRLLSEGADVNARHKLGWTALMVASISHNESVVQVLLAAGAD---PNLGDEFSS 63
Cdd:PLN03192 628 TAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADvdkANTDDDFSP 692
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 7-61 2.67e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 43.50  E-value: 2.67e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 755522259   7 NNVQEVRRLLSEGADVNARHKLGWTALMVASISHNESVVQVLLAAGADPNLGDEF 61
Cdd:PHA03100 170 NAKNRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKY 224
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 12-59 2.98e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 43.73  E-value: 2.98e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 755522259  12 VRRLLSEGADVNARHKLGWTALMVASISHNESVVQVLLAAGADPNLGD 59
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLD 145
Zeta_toxin pfam06414
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is ...
 234-307 3.03e-04

Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is thought to be part of a postregulational killing system in bacteria. It relies on antitoxin/toxin systems that secure stable inheritance of low and medium copy number plasmids during cell division and kill cells that have lost the plasmid.


Pssm-ID: 428926  Cd Length: 192  Bit Score: 41.96  E-value: 3.03e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755522259  234 EHPLVFLFLGSSGIGKTELAKQTAKYMhkDAKKGFIRLDMSEFQERH-EVAKFIGSPP---GYIGHEEGGQLTKKLKQ 307
Cdd:pfam06414   9 ERPKAILLGGQPGAGKTELARALLDEL--GRQGNVVRIDPDDFRELHpHYRELQAADPktaSEYTQPDASRWVEKLLQ 84
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 29-60 5.48e-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: 37.65  E-value: 5.48e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 755522259   29 GWTALMVASISH-NESVVQVLLAAGADPNLGDE 60
Cdd:pfam00023   2 GNTPLHLAAGRRgNLEIVKLLLSKGADVNARDK 34
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 127-154 8.19e-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: 36.85  E-value: 8.19e-04
                          10        20
                  ....*....|....*....|....*...
gi 755522259  127 KGCTALHYAVLADDYSIVKELLDRGANP 154
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADI 28
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
 238-379 8.45e-04

lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an evolutionarily conserved ATP-dependent serine protease, present in bacteria and eukaryotic mitochondria and peroxisomes, which mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Lon protease is both an ATP-dependent peptidase and a protein-activated ATPase. This RecA-like Lon domain subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410908 [Multi-domain]  Cd Length: 182  Bit Score: 40.62  E-value: 8.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259 238 VFLFLGSSGIGKTELAKQTAKYMHKDakkgFIRL------DMSEFqeRHEVAKFIGSPPGYIgheeggqlTKKLKQCP-- 309
Cdd:cd19500   39 ILCLVGPPGVGKTSLGKSIARALGRK----FVRIslggvrDEAEI--RGHRRTYVGAMPGRI--------IQALKKAGtn 104

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755522259 310 NAVVLFDEVDK----AHPDVLTIMLQLFD---EGRLTDGK-GKTIDCKDAIFIMTSNVAsDEIAQhALQLRQEALEMS 379
Cdd:cd19500  105 NPVFLLDEIDKigssFRGDPASALLEVLDpeqNSTFSDHYlDVPFDLSKVLFIATANSL-DTIPG-PLLDRMEIIELS 180
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 3-153 8.80e-04

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 42.38  E-value: 8.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259    3 AARANNVQEVRRLLSEGA--DVNARHKLGWTALMVASI-SHNESVVQVLLAAGADPNLGDefSSVYKTANEqgvhsLEDG 79
Cdd:TIGR00870  24 AAERGDLASVYRDLEEPKklNINCPDRLGRSALFVAAIeNENLELTELLLNLSCRGAVGD--TLLHAISLE-----YVDA 96

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755522259   80 RQDCASWRMTNQwtsalefrRWLGVPVGVLVTREDDFnnrlnhrasFKGCTALHYAVLADDYSIVKELLDRGAN 153
Cdd:TIGR00870  97 VEAILLHLLAAF--------RKSGPLELANDQYTSEF---------TPGITALHLAAHRQNYEIVKLLLERGAS 153
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 1-54 1.59e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 41.19  E-value: 1.59e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 755522259   1 MEAARANNVQEVRRLLSEGADVNARHKLGWTALMVASISHNESVVQVLLAAGAD 54
Cdd:PHA03100 197 HYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 5-177 1.75e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 40.80  E-value: 1.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259   5 RANNVQEVRRLLSEGADVNARHKLGWTALMVASISHNESVVQVLLAAGADPNLGDEFSSVYKTANEQGVHSLEDGRQdca 84
Cdd:PHA03100  11 RIIKVKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLTDVKE--- 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259  85 swrmtnqwtsalefrrwlgvPVGVLVTREDDFNNRLNhrasfKGCTALHYAVLA--DDYSIVKELLDRGANPLQRNEMGH 162
Cdd:PHA03100  88 --------------------IVKLLLEYGANVNAPDN-----NGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGE 142

                        170       180
                 ....*....|....*....|
gi 755522259 163 TPLDYAREG-----EVMKLL 177
Cdd:PHA03100 143 NLLHLYLESnkidlKILKLL 162
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 239-319 3.22e-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: 3.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259 239 FLFLGSSGIGKTELAKQTAKYMhkDAKkgFIRLDMSEFqerheVAKFIGsppgyigheEGGQLTKKL----KQCPNAVVL 314
Cdd:COG1222  115 VLLYGPPGTGKTLLAKAVAGEL--GAP--FIRVRGSEL-----VSKYIG---------EGARNVREVfelaREKAPSIIF 176


                 ....*
gi 755522259 315 FDEVD 319
Cdd:COG1222  177 IDEID 181
Ank_4 pfam13637
Ankyrin repeats (many copies);
130-168 3.37e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 35.71  E-value: 3.37e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 755522259  130 TALHYAVLADDYSIVKELLDRGANPLQRNEMGHTPLDYA 168
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFA 41
Ank_5 pfam13857
Ankyrin repeats (many copies);
15-61 3.75e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.79  E-value: 3.75e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 755522259   15 LLSEG-ADVNARHKLGWTALMVASISHNESVVQVLLAAGADPNLGDEF 61
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEE 48
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 29-57 4.02e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.87  E-value: 4.02e-03
                           10        20
                   ....*....|....*....|....*....
gi 755522259    29 GWTALMVASISHNESVVQVLLAAGADPNL 57
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
ftsH CHL00176
cell division protein; Validated
 235-319 7.25e-03

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 39.26  E-value: 7.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522259 235 HPLVFLFLGSSGIGKTELAKQTAkymhKDAKKGFIRLDMSEFQERhevakFIGsppgyIGHEEGGQLTKKLKQCPNAVVL 314
Cdd:CHL00176 215 IPKGVLLVGPPGTGKTLLAKAIA----GEAEVPFFSISGSEFVEM-----FVG-----VGAARVRDLFKKAKENSPCIVF 280


                 ....*
gi 755522259 315 FDEVD 319
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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