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Conserved domains on  [gi|1622849896|ref|XP_001093218|]
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protein TANC1 isoform X1 [Macaca mulatta]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1079-1285 3.80e-52

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 185.93  E-value: 3.80e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1079 GETALTAAAGRGKLEVCELLLGRGAAVSRTNRRGVPPLFCAARQGHWQIVRLLLERGCDVNLSDKQGRTPLMVAACEGHL 1158
Cdd:COG0666     54 GALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNL 133

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1159 STVEFLLSKGAALSSLDKEGLSALSWACLKGHRAVVQYLVEEGAAIDQMDKNGRTPLDLAAFYGDAETVLYLVEKGAVIE 1238
Cdd:COG0666    134 EIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVN 213

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1622849896 1239 HVDHSGMRPLDRAIGCRNTSVVVALLRKGAKLGNAAWAMATSKPDIL 1285
Cdd:COG0666    214 AKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAA 260
PHA02876 super family cl31517
ankyrin repeat protein; Provisional
 854-1270 8.61e-12

ankyrin repeat protein; Provisional


The actual alignment was detected with superfamily member PHA02876:

Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 70.48  E-value: 8.61e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896  854 LNRQQTMELGHHILKAhifkglskktGISSSHLQALWIGYSTEGLSAALASLRNlytPNVKVSRLLILGGANVNYRtEVL 933
Cdd:PHA02876   112 LNKHKLDEACIHILKE----------AISGNDIHYDKINESIEYMKLIKERIQQ---DELLIAEMLLEGGADVNAK-DIY 177

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896  934 NNAPILCVQSHlGHEEVVTLLLEFGACLDGTSENGMTALCYAAAAGHMKLVCLLTKKGARVDHLDKKGQCALVHSALRGH 1013
Cdd:PHA02876   178 CITPIHYAAER-GNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKNDLSLLKAIRNEDLETS 256

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1014 ------GDILQYLLTCEWSPgppqpgalrknhalqqALTAAASMGHSSVVQCLLgmekEHEVEVNGTDtLWGETALTAAA 1087
Cdd:PHA02876   257 lllydaGFSVNSIDDCKNTP----------------LHHASQAPSLSRLVPKLL----ERGADVNAKN-IKGETPLYLMA 315

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1088 GRG-KLEVCELLLGRGAAVSRTNRRGVPPLFCAARQGHWQ-IVRLLLERGCDVNLSDKQGRTPLMVAACEGHLSTVEFLL 1165
Cdd:PHA02876   316 KNGyDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKdIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLL 395

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1166 SKGAALSSLDKEGLSALSWA-CLKGHRAVVQYLVEEGAAIDQMDKNGRTPLDLAAFYG-DAETVLYLVEKGAVIEHVDHS 1243
Cdd:PHA02876   396 DYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQ 475

                          410       420
                   ....*....|....*....|....*..
gi 1622849896 1244 GMRPLDRAIGCRntSVVVALLRKGAKL 1270
Cdd:PHA02876   476 NQYPLLIALEYH--GIVNILLHYGAEL 500
Spy super family cl27809
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 1273-1410 4.35e-11

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


The actual alignment was detected with superfamily member COG3914:

Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 68.10  E-value: 4.35e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1273 AAWAMATSKPDILIILLQKLMEE-----------GNVMYKKGKMKEAAQRYQYALRKFPREgfgedmrpfnelrVSLYLN 1341
Cdd:COG3914     85 ALLLQALGRYEEALALYRRALALnpdnaealfnlGNLLLALGRLEEALAALRRALALNPDF-------------AEAYLN 151

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622849896 1342 LSRCRRKTNDFGMAEEFASKALEMKPKSYEAFYARARAKRNSRQFVAALADLQEAVKLCPTNQEIKRLL 1410
Cdd:COG3914    152 LGEALRRLGRLEEAIAALRRALELDPDNAEALNNLGNALQDLGRLEEAIAAYRRALELDPDNADAHSNL 220
NACHT super family cl26020
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
521-822 3.94e-08

Predicted NTPase, NACHT family domain [Signal transduction mechanisms];


The actual alignment was detected with superfamily member COG5635:

Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 58.66  E-value: 3.94e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896  521 FVHSIAALLCRSHQLAAYR-DLLIKEPQLQSMLSLRSCVQDPVAAFKRGVLEPLTNLRNEQKIpeeeyIILIDGLNEAEF 599
Cdd:COG5635    196 LLRYLALELAERYLDAEDPiPILIELRDLAEEASLEDLLAEALEKRGGEPEDALERLLRNGRL-----LLLLDGLDEVPD 270

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896  600 hkPDYGDTLSSFITKIISKFPAwLKLIVTVRANFQEIISALPFVKLSLDDFpDNKDIHSDLHAYVQHRVHSSQDILSNIS 679
Cdd:COG5635    271 --EADRDEVLNQLRRFLERYPK-ARVIITSRPEGYDSSELEGFEVLELAPL-SDEQIEEFLKKWFEATERKAERLLEALE 346

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896  680 LNGKadatligkvsshlvLRSL-GSYLYLKLTLDLFQRGHlviksasykVVPVSLSELYLLQCNMkFMTQSAFERALPIL 758
Cdd:COG5635    347 ENPE--------------LRELaRNPLLLTLLALLLRERG---------ELPDTRAELYEQFVEL-LLERWDEQRGLTIY 402

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896  759 N-------------VALASLH----PMTDEQIFQAINAgHIQGEQGWEDFQQRMDALSCFLIKRRDKTRMFCHPSFREWL 821
Cdd:COG5635    403 RelsreelrellseLALAMQEngrtEFAREELEEILRE-YLGRRKDAEALLDELLLRTGLLVERGEGRYSFAHRSFQEYL 481


                   .
gi 1622849896  822 V 822
Cdd:COG5635    482 A 482
PHA03307 super family cl33723
transcriptional regulator ICP4; Provisional
 25-319 1.69e-03

transcriptional regulator ICP4; Provisional


The actual alignment was detected with superfamily member PHA03307:

Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 43.62  E-value: 1.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896   25 GPETSPVLPLDHGADSPVSSLPAAEDTYRVSLAKGVSMSLPSSPLLPRQSHLVQSRANKKSPGPVRKPKYVESPRVPG-D 103
Cdd:PHA03307   131 APDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRrS 210

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896  104 AVIMPFREVSKPTEPDEHEAKADNEPSCSPAAQELLTRLGFLLGEGIPSATHITieDKNETMCTALSQGISPCSTLTSST 183
Cdd:PHA03307   211 SPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPIT--LPTRIWEASGWNGPSSRPGPASSS 288

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896  184 ASPSTDSPCStlnscvSKTAANKSPCETISSPSSTLESKDSGIIATITSSSENDDRSGSSLEWNKDGSLRLGVQKGVL-- 261
Cdd:PHA03307   289 SSPRERSPSP------SPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPAdp 362

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622849896  262 -HDRRADNCSPVAEEETTGSAESTLPKAESSAGDGPVPySQGSSSLIMPRPNSVAATSS 319
Cdd:PHA03307   363 sSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARR-RDATGRFPAGRPRPSPLDAG 420
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1079-1285 3.80e-52

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 185.93  E-value: 3.80e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1079 GETALTAAAGRGKLEVCELLLGRGAAVSRTNRRGVPPLFCAARQGHWQIVRLLLERGCDVNLSDKQGRTPLMVAACEGHL 1158
Cdd:COG0666     54 GALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNL 133

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1159 STVEFLLSKGAALSSLDKEGLSALSWACLKGHRAVVQYLVEEGAAIDQMDKNGRTPLDLAAFYGDAETVLYLVEKGAVIE 1238
Cdd:COG0666    134 EIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVN 213

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1622849896 1239 HVDHSGMRPLDRAIGCRNTSVVVALLRKGAKLGNAAWAMATSKPDIL 1285
Cdd:COG0666    214 AKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAA 260
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1116-1208 2.92e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.87  E-value: 2.92e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1116 LFCAARQGHWQIVRLLLERGCDVNLSDKQGRTPLMVAACEGHLSTVEFLLSKGAAlsSLDKEGLSALSWACLKGHRAVVQ 1195
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 1622849896 1196 YLVEEGAAIDQMD 1208
Cdd:pfam12796   79 LLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 1092-1268 1.26e-21

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 99.74  E-value: 1.26e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1092 LEVCELLLGRGAAVSRTNRRGVPPLFCAA--RQGHWQIVRLLLERGCDVNLSDKQGRTPLMVAA--CEGHLSTVEFLLSK 1167
Cdd:PHA03100    86 KEIVKLLLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLesNKIDLKILKLLIDK 165

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1168 GAALSSLDKeglsalswaclkghravVQYLVEEGAAIDQMDKNGRTPLDLAAFYGDAETVLYLVEKGAVIEHVDHSGMRP 1247
Cdd:PHA03100   166 GVDINAKNR-----------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTP 228

                          170       180
                   ....*....|....*....|.
gi 1622849896 1248 LDRAIGCRNTSVVVALLRKGA 1268
Cdd:PHA03100   229 LHIAILNNNKEIFKLLLNNGP 249
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 854-1270 8.61e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 70.48  E-value: 8.61e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896  854 LNRQQTMELGHHILKAhifkglskktGISSSHLQALWIGYSTEGLSAALASLRNlytPNVKVSRLLILGGANVNYRtEVL 933
Cdd:PHA02876   112 LNKHKLDEACIHILKE----------AISGNDIHYDKINESIEYMKLIKERIQQ---DELLIAEMLLEGGADVNAK-DIY 177

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896  934 NNAPILCVQSHlGHEEVVTLLLEFGACLDGTSENGMTALCYAAAAGHMKLVCLLTKKGARVDHLDKKGQCALVHSALRGH 1013
Cdd:PHA02876   178 CITPIHYAAER-GNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKNDLSLLKAIRNEDLETS 256

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1014 ------GDILQYLLTCEWSPgppqpgalrknhalqqALTAAASMGHSSVVQCLLgmekEHEVEVNGTDtLWGETALTAAA 1087
Cdd:PHA02876   257 lllydaGFSVNSIDDCKNTP----------------LHHASQAPSLSRLVPKLL----ERGADVNAKN-IKGETPLYLMA 315

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1088 GRG-KLEVCELLLGRGAAVSRTNRRGVPPLFCAARQGHWQ-IVRLLLERGCDVNLSDKQGRTPLMVAACEGHLSTVEFLL 1165
Cdd:PHA02876   316 KNGyDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKdIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLL 395

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1166 SKGAALSSLDKEGLSALSWA-CLKGHRAVVQYLVEEGAAIDQMDKNGRTPLDLAAFYG-DAETVLYLVEKGAVIEHVDHS 1243
Cdd:PHA02876   396 DYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQ 475

                          410       420
                   ....*....|....*....|....*..
gi 1622849896 1244 GMRPLDRAIGCRntSVVVALLRKGAKL 1270
Cdd:PHA02876   476 NQYPLLIALEYH--GIVNILLHYGAEL 500
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 1273-1410 4.35e-11

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 68.10  E-value: 4.35e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1273 AAWAMATSKPDILIILLQKLMEE-----------GNVMYKKGKMKEAAQRYQYALRKFPREgfgedmrpfnelrVSLYLN 1341
Cdd:COG3914     85 ALLLQALGRYEEALALYRRALALnpdnaealfnlGNLLLALGRLEEALAALRRALALNPDF-------------AEAYLN 151

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622849896 1342 LSRCRRKTNDFGMAEEFASKALEMKPKSYEAFYARARAKRNSRQFVAALADLQEAVKLCPTNQEIKRLL 1410
Cdd:COG3914    152 LGEALRRLGRLEEAIAALRRALELDPDNAEALNNLGNALQDLGRLEEAIAAYRRALELDPDNADAHSNL 220
Ank_2 pfam12796
Ankyrin repeats (3 copies);
946-1021 1.55e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 59.36  E-value: 1.55e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622849896  946 GHEEVVTLLLEFGACLDGTSENGMTALCYAAAAGHMKLV-CLLTKKGARVDHldkKGQCALVHSALRGHGDILQYLL 1021
Cdd:pfam12796    8 GNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVkLLLEHADVNLKD---NGRTALHYAARSGHLEIVKLLL 81
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
521-822 3.94e-08

Predicted NTPase, NACHT family domain [Signal transduction mechanisms];


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 58.66  E-value: 3.94e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896  521 FVHSIAALLCRSHQLAAYR-DLLIKEPQLQSMLSLRSCVQDPVAAFKRGVLEPLTNLRNEQKIpeeeyIILIDGLNEAEF 599
Cdd:COG5635    196 LLRYLALELAERYLDAEDPiPILIELRDLAEEASLEDLLAEALEKRGGEPEDALERLLRNGRL-----LLLLDGLDEVPD 270

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896  600 hkPDYGDTLSSFITKIISKFPAwLKLIVTVRANFQEIISALPFVKLSLDDFpDNKDIHSDLHAYVQHRVHSSQDILSNIS 679
Cdd:COG5635    271 --EADRDEVLNQLRRFLERYPK-ARVIITSRPEGYDSSELEGFEVLELAPL-SDEQIEEFLKKWFEATERKAERLLEALE 346

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896  680 LNGKadatligkvsshlvLRSL-GSYLYLKLTLDLFQRGHlviksasykVVPVSLSELYLLQCNMkFMTQSAFERALPIL 758
Cdd:COG5635    347 ENPE--------------LRELaRNPLLLTLLALLLRERG---------ELPDTRAELYEQFVEL-LLERWDEQRGLTIY 402

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896  759 N-------------VALASLH----PMTDEQIFQAINAgHIQGEQGWEDFQQRMDALSCFLIKRRDKTRMFCHPSFREWL 821
Cdd:COG5635    403 RelsreelrellseLALAMQEngrtEFAREELEEILRE-YLGRRKDAEALLDELLLRTGLLVERGEGRYSFAHRSFQEYL 481


                   .
gi 1622849896  822 V 822
Cdd:COG5635    482 A 482
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 1079-1198 9.62e-08

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 56.94  E-value: 9.62e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1079 GETALTAAAGRGKLEVCELLLGRGAAVS---------RTNRR-----GVPPLFCAARQGHWQIVRLLLERGCDVNLSDKQ 1144
Cdd:cd22192     89 GETALHIAVVNQNLNLVRELIARGADVVspratgtffRPGPKnliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSL 168

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622849896 1145 GRTPLMV--------AACEghlsTVEFLLS--KGAALSSLD----KEGLSALSWACLKGHRAVVQYLV 1198
Cdd:cd22192    169 GNTVLHIlvlqpnktFACQ----MYDLILSydKEDDLQPLDlvpnNQGLTPFKLAAKEGNIVMFQHLV 232
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 1144-1169 3.56e-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: 39.49  E-value: 3.56e-04
                            10        20
                    ....*....|....*....|....*.
gi 1622849896  1144 QGRTPLMVAACEGHLSTVEFLLSKGA 1169
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 25-319 1.69e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 43.62  E-value: 1.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896   25 GPETSPVLPLDHGADSPVSSLPAAEDTYRVSLAKGVSMSLPSSPLLPRQSHLVQSRANKKSPGPVRKPKYVESPRVPG-D 103
Cdd:PHA03307   131 APDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRrS 210

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896  104 AVIMPFREVSKPTEPDEHEAKADNEPSCSPAAQELLTRLGFLLGEGIPSATHITieDKNETMCTALSQGISPCSTLTSST 183
Cdd:PHA03307   211 SPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPIT--LPTRIWEASGWNGPSSRPGPASSS 288

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896  184 ASPSTDSPCStlnscvSKTAANKSPCETISSPSSTLESKDSGIIATITSSSENDDRSGSSLEWNKDGSLRLGVQKGVL-- 261
Cdd:PHA03307   289 SSPRERSPSP------SPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPAdp 362

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622849896  262 -HDRRADNCSPVAEEETTGSAESTLPKAESSAGDGPVPySQGSSSLIMPRPNSVAATSS 319
Cdd:PHA03307   363 sSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARR-RDATGRFPAGRPRPSPLDAG 420
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 1300-1412 1.81e-03

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 43.15  E-value: 1.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1300 YKKGKMKEAAQRYQYALRKFPREgfgedmrpfnelrVSLYLNLSRCRRKTNDFGMAEEFASKALEMKPKSYEAFYARARA 1379
Cdd:TIGR02917  510 IQEGNPDDAIQRFEKVLTIDPKN-------------LRAILALAGLYLRTGNEEEAVAWLEKAAELNPQEIEPALALAQY 576

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1622849896 1380 KRNSRQFVAALADLQEAVKLCPTNQEIKRLLAR 1412
Cdd:TIGR02917  577 YLGKGQLKKALAILNEAADAAPDSPEAWLMLGR 609
TPR_14 pfam13428
Tetratricopeptide repeat;
1371-1413 3.16e-03

Tetratricopeptide repeat;


Pssm-ID: 463874 [Multi-domain]  Cd Length: 44  Bit Score: 37.02  E-value: 3.16e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1622849896 1371 EAFYARARAKRNSRQFVAALADLQEAVKLCPTNQEIKRLLARV 1413
Cdd:pfam13428    2 EALLALARALLALGDPDEALALLERALALDPDDPEAWLALAQL 44
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 1079-1162 8.13e-03

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 41.22  E-value: 8.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1079 GETALTAAAGRGKLEVCELLLGRGAAVS-RTN-------------RRGVPPLFCAARQGHWQIVRLLLERGCDVNLSDKQ 1144
Cdd:TIGR00870  128 GITALHLAAHRQNYEIVKLLLERGASVPaRACgdffvksqgvdsfYHGESPLNAAACLGSPSIVALLSEDPADILTADSL 207

                           90
                   ....*....|....*...
gi 1622849896 1145 GRTPLmvaacegHLSTVE 1162
Cdd:TIGR00870  208 GNTLL-------HLLVME 218
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1079-1285 3.80e-52

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 185.93  E-value: 3.80e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1079 GETALTAAAGRGKLEVCELLLGRGAAVSRTNRRGVPPLFCAARQGHWQIVRLLLERGCDVNLSDKQGRTPLMVAACEGHL 1158
Cdd:COG0666     54 GALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNL 133

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1159 STVEFLLSKGAALSSLDKEGLSALSWACLKGHRAVVQYLVEEGAAIDQMDKNGRTPLDLAAFYGDAETVLYLVEKGAVIE 1238
Cdd:COG0666    134 EIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVN 213

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1622849896 1239 HVDHSGMRPLDRAIGCRNTSVVVALLRKGAKLGNAAWAMATSKPDIL 1285
Cdd:COG0666    214 AKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAA 260
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1072-1274 1.63e-50

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 181.31  E-value: 1.63e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1072 NGTDTLWGETALTAAAGRGKLEVCELLLGRGAAVSRTNRRGVPPLFCAARQGHWQIVRLLLERGCDVNLSDKQGRTPLMV 1151
Cdd:COG0666     80 INAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHL 159

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1152 AACEGHLSTVEFLLSKGAALSSLDKEGLSALSWACLKGHRAVVQYLVEEGAAIDQMDKNGRTPLDLAAFYGDAETVLYLV 1231
Cdd:COG0666    160 AAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1622849896 1232 EKGAVIEHVDHSGMRPLDRAIGCRNTSVVVALLRKGAKLGNAA 1274
Cdd:COG0666    240 EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
933-1248 1.11e-45

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 167.05  E-value: 1.11e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896  933 LNNAPILCVQSHLGHEEVVTLLLEFGACLDGTSENGMTALCYAAAAGHMKLVCLLTKKGARVDHLDKKGQCALVHSALRG 1012
Cdd:COG0666     19 LLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNG 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1013 HGDILQYLLtcewspgppqpgalrknhalqqaltaaasmghssvvqcllgmekEHEVEVNGTDTlWGETALTAAAGRGKL 1092
Cdd:COG0666     99 DLEIVKLLL--------------------------------------------EAGADVNARDK-DGETPLHLAAYNGNL 133

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1093 EVCELLLGRGAAVSRTNRRGVPPLFCAARQGHWQIVRLLLERGCDVNLSDKQGRTPLMVAACEGHLSTVEFLLSKGAALS 1172
Cdd:COG0666    134 EIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVN 213

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622849896 1173 SLDKEGLSALSWACLKGHRAVVQYLVEEGAAIDQMDKNGRTPLDLAAFYGDAETVLYLVEKGAVIEHVDHSGMRPL 1248
Cdd:COG0666    214 AKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
900-1215 5.30e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 156.65  E-value: 5.30e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896  900 AALASLRNLYTPNVKVSRLLILGGANVNYRTEVLNNAPILCVQSHLGHEEVVTLLLEFGACLDGTSENGMTALCYAAAAG 979
Cdd:COG0666     19 LLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNG 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896  980 HMKLVCLLTKKGARVDHLDKKGQCALVHSALRGHGDILQYLLtcewspgppqpgalrknhalqqaltaaasmghssvvqc 1059
Cdd:COG0666     99 DLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLL-------------------------------------- 140

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1060 llgmekEHEVEVNGTDTlWGETALTAAAGRGKLEVCELLLGRGAAVSRTNRRGVPPLFCAARQGHWQIVRLLLERGCDVN 1139
Cdd:COG0666    141 ------EAGADVNAQDN-DGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVN 213

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622849896 1140 LSDKQGRTPLMVAACEGHLSTVEFLLSKGAALSSLDKEGLSALSWACLKGHRAVVQYLVEEGAAIDQMDKNGRTPL 1215
Cdd:COG0666    214 AKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1060-1318 8.13e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 153.19  E-value: 8.13e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1060 LLGMEKEHEVEVNGTDTLWGETALTAAAGRGKLEVCELLLGRGAAVSRTNRRGVPPLFCAARQGHWQIVRLLLERGCDVN 1139
Cdd:COG0666      2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1140 LSDKQGRTPLMVAACEGHLSTVEFLLSKGAALSSLDKEGLSALSWACLKGHRAVVQYLVEEGAAIDQMDKNGRTPLDLAA 1219
Cdd:COG0666     82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1220 FYGDAETVLYLVEKGAVIEHVDHSGMRPLDRAIGCRNTSVVVALLRKGA------KLGNAA--WAMATSKPDILIILLQK 1291
Cdd:COG0666    162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGAdvnakdNDGKTAldLAAENGNLEIVKLLLEA 241

                          250       260
                   ....*....|....*....|....*..
gi 1622849896 1292 LMEEGNVMYKKGKMKEAAQRYQYALRK 1318
Cdd:COG0666    242 GADLNAKDKDGLTALLLAAAAGAALIV 268
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1092-1291 1.61e-27

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 114.67  E-value: 1.61e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1092 LEVCELLLGRGAAVSRTNRRGVPPLFCAARQGHWQIVRLLLERGCDVNLSDKQGRTPLMVAACEGHLSTVEFLLSKGAAL 1171
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1172 SSLDKEGLSALSWACLKGHRAVVQYLVEEGAAIDQMDKNGRTPLDLAAFYGDAETVLYLVEKGAVIEHVDHSGMRPLDRA 1251
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1622849896 1252 IGCRNTSVVVALLRKGA------KLGNAA--WAMATSKPDILIILLQK 1291
Cdd:COG0666    161 AANGNLEIVKLLLEAGAdvnardNDGETPlhLAAENGHLEIVKLLLEA 208
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1116-1208 2.92e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.87  E-value: 2.92e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1116 LFCAARQGHWQIVRLLLERGCDVNLSDKQGRTPLMVAACEGHLSTVEFLLSKGAAlsSLDKEGLSALSWACLKGHRAVVQ 1195
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 1622849896 1196 YLVEEGAAIDQMD 1208
Cdd:pfam12796   79 LLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 1092-1268 1.26e-21

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 99.74  E-value: 1.26e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1092 LEVCELLLGRGAAVSRTNRRGVPPLFCAA--RQGHWQIVRLLLERGCDVNLSDKQGRTPLMVAA--CEGHLSTVEFLLSK 1167
Cdd:PHA03100    86 KEIVKLLLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLesNKIDLKILKLLIDK 165

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1168 GAALSSLDKeglsalswaclkghravVQYLVEEGAAIDQMDKNGRTPLDLAAFYGDAETVLYLVEKGAVIEHVDHSGMRP 1247
Cdd:PHA03100   166 GVDINAKNR-----------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTP 228

                          170       180
                   ....*....|....*....|.
gi 1622849896 1248 LDRAIGCRNTSVVVALLRKGA 1268
Cdd:PHA03100   229 LHIAILNNNKEIFKLLLNNGP 249
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1149-1241 2.50e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 90.18  E-value: 2.50e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1149 LMVAACEGHLSTVEFLLSKGAALSSLDKEGLSALSWACLKGHRAVVQYLVEEGAAidQMDKNGRTPLDLAAFYGDAETVL 1228
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 1622849896 1229 YLVEKGAVIEHVD 1241
Cdd:pfam12796   79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1083-1169 1.01e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.55  E-value: 1.01e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1083 LTAAAGRGKLEVCELLLGRGAAVSRTNRRGVPPLFCAARQGHWQIVRLLLERgCDVNLSDkQGRTPLMVAACEGHLSTVE 1162
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78


                   ....*..
gi 1622849896 1163 FLLSKGA 1169
Cdd:pfam12796   79 LLLEKGA 85
PHA03095 PHA03095
ankyrin-like protein; Provisional
 906-1266 1.33e-19

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 94.32  E-value: 1.33e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896  906 RNLYTPNVKVS--RLLILGGANVNYRTEvLNNAPiLCVQSHLGHE---EVVTLLLEFGACLDGTSENGMTAL-CYAAAAG 979
Cdd:PHA03095    18 YLLNASNVTVEevRRLLAAGADVNFRGE-YGKTP-LHLYLHYSSEkvkDIVRLLLEAGADVNAPERCGFTPLhLYLYNAT 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896  980 HMKLVCLLTKKGARVDHLDKKGQCALvHSALRG---HGDILQYLLtcewspgppqpgalrknhalqqaltaaasmghssv 1056
Cdd:PHA03095    96 TLDVIKLLIKAGADVNAKDKVGRTPL-HVYLSGfniNPKVIRLLL----------------------------------- 139

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1057 vqcllgmekEHEVEVNGTDtLWGETALTA--AAGRGKLEVCELLLGRGAAVSRTNRRGVPPL-----FCAARQGhwqIVR 1129
Cdd:PHA03095   140 ---------RKGADVNALD-LYGMTPLAVllKSRNANVELLRLLIDAGADVYAVDDRFRSLLhhhlqSFKPRAR---IVR 206

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1130 LLLERGCDVNLSDKQGRTPLMVAACEGhlstvefllskgaalssldkeglsalswAClkgHRAVVQYLVEEGAAIDQMDK 1209
Cdd:PHA03095   207 ELIRAGCDPAATDMLGNTPLHSMATGS----------------------------SC---KRSLVLPLLIAGISINARNR 255

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622849896 1210 NGRTPLDLAAFYGDAETVLYLVEKGAVIEHVDHSGMRPLDRAIGCRNTSVVVALLRK 1266
Cdd:PHA03095   256 YGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAK 312
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 958-1274 3.05e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 86.56  E-value: 3.05e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896  958 GACLDGTSENGMTALCYAAAAGHMKLVCLLTKKGARVDHLDKKGQCALVHSALRGHGDILQYLLTCEWSPGP-PQPGAlr 1036
Cdd:PHA02874    25 GNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSIlPIPCI-- 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1037 knhalqqaltaaasmgHSSVVQCLLgmekEHEVEVNGTDTLwGETALTAAAGRGKLEVCELLLGRGAAVSRTNRRGVPPL 1116
Cdd:PHA02874   103 ----------------EKDMIKTIL----DCGIDVNIKDAE-LKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPI 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1117 FCAARQGHWQIVRLLLERGCDVNLSDKQGRTPLMVAACEGHLSTVEFLLSKGAALSSLDKEGLSALSWACLKgHRAVVQY 1196
Cdd:PHA02874   162 HIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIH-NRSAIEL 240

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622849896 1197 LVEEgAAIDQMDKNGRTPLDLAAFYG-DAETVLYLVEKGAVIEHVDHSGMRPLDRAIGCRNTSVVVALLRKGAKLGNAA 1274
Cdd:PHA02874   241 LINN-ASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTAFKYINKDPVIKDIIANAVLIKEA 318
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1052-1142 7.79e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 71.69  E-value: 7.79e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1052 GHSSVVQCLLgmekEHEVEVNGTDTlWGETALTAAAGRGKLEVCELLLGRGAAVSRTNrrGVPPLFCAARQGHWQIVRLL 1131
Cdd:pfam12796    8 GNLELVKLLL----ENGADANLQDK-NGRTALHLAAKNGHLEIVKLLLEHADVNLKDN--GRTALHYAARSGHLEIVKLL 80

                           90
                   ....*....|.
gi 1622849896 1132 LERGCDVNLSD 1142
Cdd:pfam12796   81 LEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1182-1270 1.51e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.92  E-value: 1.51e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1182 LSWACLKGHRAVVQYLVEEGAAIDQMDKNGRTPLDLAAFYGDAETVLYLVEKGAVieHVDHSGMRPLDRAIGCRNTSVVV 1261
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78


                   ....*....
gi 1622849896 1262 ALLRKGAKL 1270
Cdd:pfam12796   79 LLLEKGADI 87
PHA03095 PHA03095
ankyrin-like protein; Provisional
 1092-1268 2.86e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 77.76  E-value: 2.86e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1092 LEVCELLLGRGAAVSRTNRRGVPPLFCAARQGH-WQIVRLLLERGCDVNLSDKQGRTPLMVAAC--EGHLSTVEFLLSKG 1168
Cdd:PHA03095    63 KDIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAGADVNAKDKVGRTPLHVYLSgfNINPKVIRLLLRKG 142

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1169 AALSSLDKEGLSALSwACLKGHRA---VVQYLVEEGA-----------AIDQM------------------------DKN 1210
Cdd:PHA03095   143 ADVNALDLYGMTPLA-VLLKSRNAnveLLRLLIDAGAdvyavddrfrsLLHHHlqsfkprarivreliragcdpaatDML 221

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1211 GRTPLDLAAFYGDAET--VLYLVEKGAVIEHVDHSGMRPLDRAIGCRNTSVVVALLRKGA 1268
Cdd:PHA03095   222 GNTPLHSMATGSSCKRslVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGA 281
PHA03095 PHA03095
ankyrin-like protein; Provisional
 1127-1270 4.00e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 76.99  E-value: 4.00e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1127 IVRLLLERGCDVNLSDKQGRTPL---MVAACEGHLSTVEFLLSKGAALSSLDKEGLSAL-SWACLKGHRAVVQYLVEEGA 1202
Cdd:PHA03095    29 EVRRLLAAGADVNFRGEYGKTPLhlyLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLhLYLYNATTLDVIKLLIKAGA 108

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622849896 1203 AIDQMDKNGRTPLD--LAAFYGDAETVLYLVEKGAVIEHVDHSGMRPLDRAIGCRNTSV--VVALLRKGAKL 1270
Cdd:PHA03095   109 DVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVelLRLLIDAGADV 180
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 948-1210 5.45e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 73.16  E-value: 5.45e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896  948 EEVVTLLLEFGACLDGTSENGMTALCYAAAAGH-----MKLVCLLTKKGARVDHLDKKGqcalVHsalrghgdILQYLLT 1022
Cdd:PHA03100    48 IDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVNAPDNNG----IT--------PLLYAIS 115

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1023 CEwspgppqpgalrknhalqqaltaaasMGHSSVVQCLLgmekEHEVEVNgTDTLWGETALTAAA--GRGKLEVCELLLG 1100
Cdd:PHA03100   116 KK--------------------------SNSYSIVEYLL----DNGANVN-IKNSDGENLLHLYLesNKIDLKILKLLID 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1101 RGAAVSRTNRrgvpplfcaarqghwqiVRLLLERGCDVNLSDKQGRTPLMVAACEGHLSTVEFLLSKGAALSSLDKEGLS 1180
Cdd:PHA03100   165 KGVDINAKNR-----------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDT 227

                          250       260       270
                   ....*....|....*....|....*....|
gi 1622849896 1181 ALSWACLKGHRAVVQYLVEEGAAIDQMDKN 1210
Cdd:PHA03100   228 PLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 1126-1275 4.08e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 70.68  E-value: 4.08e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1126 QIVRLLLERGCDVNLSDK-QGRTPLMVAACEGHLSTVEFLLSKGAALSSLDKEGLSALSWACLKGHRAVVQYLVEEGAAI 1204
Cdd:PHA02878   148 EITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAST 227

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622849896 1205 DQMDKNGRTPLDLAAFY-GDAETVLYLVEKGAVIEHVDH-SGMRPLDRAIgcRNTSVVVALLRKGAKLGNAAW 1275
Cdd:PHA02878   228 DARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYiLGLTALHSSI--KSERKLKLLLEYGADINSLNS 298
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 854-1270 8.61e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 70.48  E-value: 8.61e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896  854 LNRQQTMELGHHILKAhifkglskktGISSSHLQALWIGYSTEGLSAALASLRNlytPNVKVSRLLILGGANVNYRtEVL 933
Cdd:PHA02876   112 LNKHKLDEACIHILKE----------AISGNDIHYDKINESIEYMKLIKERIQQ---DELLIAEMLLEGGADVNAK-DIY 177

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896  934 NNAPILCVQSHlGHEEVVTLLLEFGACLDGTSENGMTALCYAAAAGHMKLVCLLTKKGARVDHLDKKGQCALVHSALRGH 1013
Cdd:PHA02876   178 CITPIHYAAER-GNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKNDLSLLKAIRNEDLETS 256

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1014 ------GDILQYLLTCEWSPgppqpgalrknhalqqALTAAASMGHSSVVQCLLgmekEHEVEVNGTDtLWGETALTAAA 1087
Cdd:PHA02876   257 lllydaGFSVNSIDDCKNTP----------------LHHASQAPSLSRLVPKLL----ERGADVNAKN-IKGETPLYLMA 315

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1088 GRG-KLEVCELLLGRGAAVSRTNRRGVPPLFCAARQGHWQ-IVRLLLERGCDVNLSDKQGRTPLMVAACEGHLSTVEFLL 1165
Cdd:PHA02876   316 KNGyDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKdIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLL 395

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1166 SKGAALSSLDKEGLSALSWA-CLKGHRAVVQYLVEEGAAIDQMDKNGRTPLDLAAFYG-DAETVLYLVEKGAVIEHVDHS 1243
Cdd:PHA02876   396 DYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQ 475

                          410       420
                   ....*....|....*....|....*..
gi 1622849896 1244 GMRPLDRAIGCRntSVVVALLRKGAKL 1270
Cdd:PHA02876   476 NQYPLLIALEYH--GIVNILLHYGAEL 500
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 1273-1410 4.35e-11

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 68.10  E-value: 4.35e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1273 AAWAMATSKPDILIILLQKLMEE-----------GNVMYKKGKMKEAAQRYQYALRKFPREgfgedmrpfnelrVSLYLN 1341
Cdd:COG3914     85 ALLLQALGRYEEALALYRRALALnpdnaealfnlGNLLLALGRLEEALAALRRALALNPDF-------------AEAYLN 151

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622849896 1342 LSRCRRKTNDFGMAEEFASKALEMKPKSYEAFYARARAKRNSRQFVAALADLQEAVKLCPTNQEIKRLL 1410
Cdd:COG3914    152 LGEALRRLGRLEEAIAALRRALELDPDNAEALNNLGNALQDLGRLEEAIAAYRRALELDPDNADAHSNL 220
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
1296-1413 7.44e-11

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 64.64  E-value: 7.44e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1296 GNVMYKKGKMKEAAQRYQYALRKFPREgfgedmrpfnelrVSLYLNLSRCRRKTNDFGMAEEFASKALEMKPKSYEAFYA 1375
Cdd:COG0457     15 GLAYRRLGRYEEAIEDYEKALELDPDD-------------AEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNN 81

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1622849896 1376 RARAKRNSRQFVAALADLQEAVKLCPTNQEIKRLLARV 1413
Cdd:COG0457     82 LGLALQALGRYEEALEDYDKALELDPDDAEALYNLGLA 119
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
1296-1416 1.23e-10

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 63.87  E-value: 1.23e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1296 GNVMYKKGKMKEAAQRYQYALRKFPRegfgedmrpfnelRVSLYLNLSRCRRKTNDFGMAEEFASKALEMKPKSYEAFYA 1375
Cdd:COG0457     49 GLAYLRLGRYEEALADYEQALELDPD-------------DAEALNNLGLALQALGRYEEALEDYDKALELDPDDAEALYN 115

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1622849896 1376 RARAKRNSRQFVAALADLQEAVKLCPTNQEIKRLLARVEEE 1416
Cdd:COG0457    116 LGLALLELGRYDEAIEAYERALELDPDDADALYNLGIALEK 156
Ank_2 pfam12796
Ankyrin repeats (3 copies);
946-1021 1.55e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 59.36  E-value: 1.55e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622849896  946 GHEEVVTLLLEFGACLDGTSENGMTALCYAAAAGHMKLV-CLLTKKGARVDHldkKGQCALVHSALRGHGDILQYLL 1021
Cdd:pfam12796    8 GNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVkLLLEHADVNLKD---NGRTALHYAARSGHLEIVKLLL 81
Ank_2 pfam12796
Ankyrin repeats (3 copies);
972-1109 2.25e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 58.97  E-value: 2.25e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896  972 LCYAAAAGHMKLVCLLTKKGARVDHLDKKGQCALVHSALRGHGDILQYLLTcewspgppqpgalrknhalqqaltaaasm 1051
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE----------------------------- 51

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622849896 1052 ghssvvqcllgmekehevEVNGTDTLWGETALTAAAGRGKLEVCELLLGRGAAVSRTN 1109
Cdd:pfam12796   52 ------------------HADVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 1289-1416 7.13e-10

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 59.05  E-value: 7.13e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1289 LQKLMEEGNVMYKKGKMKEAAQRYQYALRKFPREgfgedmrpfnelrVSLYLNLSRCRRKTNDFGMAEEFASKALEMKPK 1368
Cdd:COG4783      4 AEALYALAQALLLAGDYDEAEALLEKALELDPDN-------------PEAFALLGEILLQLGDLDEAIVLLHEALELDPD 70

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1622849896 1369 SYEAFYARARAKRNSRQFVAALADLQEAVKLCPTNQEIKRLLARVEEE 1416
Cdd:COG4783     71 EPEARLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRA 118
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
1298-1405 8.69e-10

Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 57.49  E-value: 8.69e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1298 VMYKKGKMKEAAQRYQYALRKFPREGfgedmrpfnelrvSLYLNLSRCRRKTNDFGMAEEFaSKALEMKPKSYEAFYARA 1377
Cdd:COG3063      1 LYLKLGDLEEAEEYYEKALELDPDNA-------------DALNNLGLLLLEQGRYDEAIAL-EKALKLDPNNAEALLNLA 66

                           90       100
                   ....*....|....*....|....*...
gi 1622849896 1378 RAKRNSRQFVAALADLQEAVKLCPTNQE 1405
Cdd:COG3063     67 ELLLELGDYDEALAYLERALELDPSALR 94
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 1083-1249 1.64e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 62.96  E-value: 1.64e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1083 LTAAAGRGKLEVCELLLGRGAAVSRTNRRGVPPLFCAARQGHWQIVRLLLERGCDVNLSDKQGRTPLMVAACEGHlSTVE 1162
Cdd:PLN03192   529 LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKH-HKIF 607

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1163 FLLSKGAALSSLDKEGlSALSWACLKGHRAVVQYLVEEGAAIDQMDKNGRTPLDLAAFYGDAETVLYLVEKGAVIEHVD- 1241
Cdd:PLN03192   608 RILYHFASISDPHAAG-DLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANt 686


                   ....*...
gi 1622849896 1242 HSGMRPLD 1249
Cdd:PLN03192   687 DDDFSPTE 694
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 1296-1415 2.02e-09

Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 57.32  E-value: 2.02e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1296 GNVMYKKGKMKEAAQRYQYALRKFPREgfgedmrpfnelrVSLYLNLSRCRRKTNDFGMAEEFASKALEMKPKSYEAFYA 1375
Cdd:COG4235     24 GRAYLRLGRYDEALAAYEKALRLDPDN-------------ADALLDLAEALLAAGDTEEAEELLERALALDPDNPEALYL 90

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1622849896 1376 RARAKRNSRQFVAALADLQEAVKLCPTNQEIKRLLARVEE 1415
Cdd:COG4235     91 LGLAAFQQGDYAEAIAAWQKLLALLPADAPARLLEASIAE 130
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 1080-1211 2.33e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 61.55  E-value: 2.33e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1080 ETALTAAAGRGKLEVCELLLGRGAAVSRT-NRRGVPPLFCAARQGHWQIVRLLLERGCDVNLSDKQGRTPLMVAACEGHL 1158
Cdd:PHA02875    69 ESELHDAVEEGDVKAVEELLDLGKFADDVfYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDI 148

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1622849896 1159 STVEFLLSKGAALSSLDKEGLSALSWACLKGHRAVVQYLVEEGAAIDQMDKNG 1211
Cdd:PHA02875   149 KGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNG 201
Ank_4 pfam13637
Ankyrin repeats (many copies);
1112-1165 2.66e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.59  E-value: 2.66e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1622849896 1112 GVPPLFCAARQGHWQIVRLLLERGCDVNLSDKQGRTPLMVAACEGHLSTVEFLL 1165
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 1285-1413 3.21e-09

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 61.93  E-value: 3.21e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1285 LIILLQKLMEEGNVMYKKGKMKEAAQRYQYALRKFPREgfgedmrpfnelrVSLYLNLSRCRRKTNDFGMAEEFASKALE 1364
Cdd:COG3914     74 LLLLAALLELAALLLQALGRYEEALALYRRALALNPDN-------------AEALFNLGNLLLALGRLEEALAALRRALA 140

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1622849896 1365 MKPKSYEAFYARARAKRNSRQFVAALADLQEAVKLCPTNQEIKRLLARV 1413
Cdd:COG3914    141 LNPDFAEAYLNLGEALRRLGRLEEAIAALRRALELDPDNAEALNNLGNA 189
PHA03095 PHA03095
ankyrin-like protein; Provisional
 892-1158 3.55e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 61.19  E-value: 3.55e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896  892 GYSTEGLSAALASLRNLYTpnVKVSRLLILGGANVNYRTEVLNNApilcVQSHLG----HEEVVTLLLEFGACLDGTSEN 967
Cdd:PHA03095    78 APERCGFTPLHLYLYNATT--LDVIKLLIKAGADVNAKDKVGRTP----LHVYLSgfniNPKVIRLLLRKGADVNALDLY 151

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896  968 GMTAL-CYAAAAG-HMKLVCLLTKKGARVDHLDKKGQCALVHsalrghgdILQYlltcewspgppqpgaLRKNhalqqal 1045
Cdd:PHA03095   152 GMTPLaVLLKSRNaNVELLRLLIDAGADVYAVDDRFRSLLHH--------HLQS---------------FKPR------- 201

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1046 taaasmghSSVVQCLLgmekEHEVEVNGTDTLwGETALTAAA--GRGKLEVCELLLGRGAAVSRTNRRGVPPLFCAARQG 1123
Cdd:PHA03095   202 --------ARIVRELI----RAGCDPAATDML-GNTPLHSMAtgSSCKRSLVLPLLIAGISINARNRYGQTPLHYAAVFN 268

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1622849896 1124 HWQIVRLLLERGCDVNLSDKQGRTPL--MVAACEGHL 1158
Cdd:PHA03095   269 NPRACRRLIALGADINAVSSDGNTPLslMVRNNNGRA 305
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 1307-1416 4.00e-09

Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 56.55  E-value: 4.00e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1307 EAAQRYQYALRKFPREGFGedmrpfnelrvslYLNLSRCRRKTNDFGMAEEFASKALEMKPKSYEAFYARARAKRNSRQF 1386
Cdd:COG4235      1 EAIARLRQALAANPNDAEG-------------WLLLGRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDT 67

                           90       100       110
                   ....*....|....*....|....*....|
gi 1622849896 1387 VAALADLQEAVKLCPTNQEIKRLLARVEEE 1416
Cdd:COG4235     68 EEAEELLERALALDPDNPEALYLLGLAAFQ 97
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 1128-1211 6.34e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 61.07  E-value: 6.34e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1128 VRLLLERGCDVNLSDKQGRTPLMVAACEGHLSTVEFLLSKGAALSSLDKEGLSALSWACLKGHRAVVQYLVEEGAAIDQM 1207
Cdd:PTZ00322    98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFEL 177


                   ....
gi 1622849896 1208 DKNG 1211
Cdd:PTZ00322   178 GANA 181
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 1305-1413 7.09e-09

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 56.51  E-value: 7.09e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1305 MKEAAQRYQYALRKFPREGFGEDMRPFNELRVSLYLNLSRCRRKTNDFGMAEEFASKALEMKPKSYEAFYARARAKRNSR 1384
Cdd:COG5010     23 LVEKYEAALAGANNTKEDELAAAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQALQLDPNNPELYYNLALLYSRSG 102

                           90       100
                   ....*....|....*....|....*....
gi 1622849896 1385 QFVAALADLQEAVKLCPTNQEIKRLLARV 1413
Cdd:COG5010    103 DKDEAKEYYEKALALSPDNPNAYSNLAAL 131
Ank_4 pfam13637
Ankyrin repeats (many copies);
1178-1231 9.60e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.05  E-value: 9.60e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1622849896 1178 GLSALSWACLKGHRAVVQYLVEEGAAIDQMDKNGRTPLDLAAFYGDAETVLYLV 1231
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
917-998 1.14e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 53.97  E-value: 1.14e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896  917 RLLILGGANVNYRTEVLNNAPILCVQShlGHEEVVTLLLEFgACLDGTsENGMTALCYAAAAGHMKLVCLLTKKGARVDH 996
Cdd:pfam12796   14 KLLLENGADANLQDKNGRTALHLAAKN--GHLEIVKLLLEH-ADVNLK-DNGRTALHYAARSGHLEIVKLLLEKGADINV 89


                   ..
gi 1622849896  997 LD 998
Cdd:pfam12796   90 KD 91
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
1260-1405 1.25e-08

Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 57.23  E-value: 1.25e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1260 VVALLRKGAKLGNAAWAMATSKPDiliiLLQKLMEEGNVMYKKGKMKEAAQRYQYALRKFPRegfgedmrpfnelRVSLY 1339
Cdd:COG4785     48 LAAAALAAAALAAERIDRALALPD----LAQLYYERGVAYDSLGDYDLAIADFDQALELDPD-------------LAEAY 110

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622849896 1340 LNLSRCRRKTNDFGMAEEFASKALEMKPKSYEAFYARARAKRNSRQFVAALADLQEAVKLCPTNQE 1405
Cdd:COG4785    111 NNRGLAYLLLGDYDAALEDFDRALELDPDYAYAYLNRGIALYYLGRYELAIADLEKALELDPNDPE 176
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 1262-1401 1.53e-08

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 55.74  E-value: 1.53e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1262 ALLRKGAKLGNAAWAMATSKPDILIILLQKLMEEGNVMYKKGKMKEAAQRYQYALRKFPREGfgedmrpfnelrvSLYLN 1341
Cdd:COG5010     27 YEAALAGANNTKEDELAAAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQALQLDPNNP-------------ELYYN 93

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1342 LSRCRRKTNDFGMAEEFASKALEMKPKSYEAFYARARAKRNSRQFVAALADLQEAVKLCP 1401
Cdd:COG5010     94 LALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQRALGTSP 153
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 1066-1218 2.12e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 58.74  E-value: 2.12e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1066 EHEVEVNGTDTLWGETALTAAAGRGKLEVCELLLGRGAAVSRTNRRGVPPLFCAARQGHWQIVRLLLERGCDVNLSDKQG 1145
Cdd:PHA02878   155 SYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCG 234

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622849896 1146 RTPLMVAAceGHL---STVEFLLSKGA---ALSSLdkEGLSALSWAcLKGHRaVVQYLVEEGAAIDQMDKNGRTPLDLA 1218
Cdd:PHA02878   235 NTPLHISV--GYCkdyDILKLLLEHGVdvnAKSYI--LGLTALHSS-IKSER-KLKLLLEYGADINSLNSYKLTPLSSA 307
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 1286-1416 2.17e-08

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 57.43  E-value: 2.17e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1286 IILLQKLMEE-----------GNVMYKKGKMKEAAQRYQYALrkfpregfgeDMRPFNElrvSLYLNLSRCRRKTNDFGM 1354
Cdd:COG2956     62 IRIHQKLLERdpdraeallelAQDYLKAGLLDRAEELLEKLL----------ELDPDDA---EALRLLAEIYEQEGDWEK 128

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622849896 1355 AEEFASKALEMKPKSYEAFYARARAKRNSRQFVAALADLQEAVKLCPTNQEIKRLLARVEEE 1416
Cdd:COG2956    129 AIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAELYLE 190
Ank_4 pfam13637
Ankyrin repeats (many copies);
1081-1132 2.51e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.89  E-value: 2.51e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1622849896 1081 TALTAAAGRGKLEVCELLLGRGAAVSRTNRRGVPPLFCAARQGHWQIVRLLL 1132
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
968-1021 3.02e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.51  E-value: 3.02e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1622849896  968 GMTALCYAAAAGHMKLVCLLTKKGARVDHLDKKGQCALVHSALRGHGDILQYLL 1021
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
521-822 3.94e-08

Predicted NTPase, NACHT family domain [Signal transduction mechanisms];


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 58.66  E-value: 3.94e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896  521 FVHSIAALLCRSHQLAAYR-DLLIKEPQLQSMLSLRSCVQDPVAAFKRGVLEPLTNLRNEQKIpeeeyIILIDGLNEAEF 599
Cdd:COG5635    196 LLRYLALELAERYLDAEDPiPILIELRDLAEEASLEDLLAEALEKRGGEPEDALERLLRNGRL-----LLLLDGLDEVPD 270

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896  600 hkPDYGDTLSSFITKIISKFPAwLKLIVTVRANFQEIISALPFVKLSLDDFpDNKDIHSDLHAYVQHRVHSSQDILSNIS 679
Cdd:COG5635    271 --EADRDEVLNQLRRFLERYPK-ARVIITSRPEGYDSSELEGFEVLELAPL-SDEQIEEFLKKWFEATERKAERLLEALE 346

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896  680 LNGKadatligkvsshlvLRSL-GSYLYLKLTLDLFQRGHlviksasykVVPVSLSELYLLQCNMkFMTQSAFERALPIL 758
Cdd:COG5635    347 ENPE--------------LRELaRNPLLLTLLALLLRERG---------ELPDTRAELYEQFVEL-LLERWDEQRGLTIY 402

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896  759 N-------------VALASLH----PMTDEQIFQAINAgHIQGEQGWEDFQQRMDALSCFLIKRRDKTRMFCHPSFREWL 821
Cdd:COG5635    403 RelsreelrellseLALAMQEngrtEFAREELEEILRE-YLGRRKDAEALLDELLLRTGLLVERGEGRYSFAHRSFQEYL 481


                   .
gi 1622849896  822 V 822
Cdd:COG5635    482 A 482
Ank_4 pfam13637
Ankyrin repeats (many copies);
937-987 4.21e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.12  E-value: 4.21e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1622849896  937 PILCVQSHLGHEEVVTLLLEFGACLDGTSENGMTALCYAAAAGHMKLVCLL 987
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
Ank_4 pfam13637
Ankyrin repeats (many copies);
1145-1198 4.30e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.12  E-value: 4.30e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1622849896 1145 GRTPLMVAACEGHLSTVEFLLSKGAALSSLDKEGLSALSWACLKGHRAVVQYLV 1198
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 1079-1198 9.62e-08

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 56.94  E-value: 9.62e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1079 GETALTAAAGRGKLEVCELLLGRGAAVS---------RTNRR-----GVPPLFCAARQGHWQIVRLLLERGCDVNLSDKQ 1144
Cdd:cd22192     89 GETALHIAVVNQNLNLVRELIARGADVVspratgtffRPGPKnliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSL 168

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622849896 1145 GRTPLMV--------AACEghlsTVEFLLS--KGAALSSLD----KEGLSALSWACLKGHRAVVQYLV 1198
Cdd:cd22192    169 GNTVLHIlvlqpnktFACQ----MYDLILSydKEDDLQPLDlvpnNQGLTPFKLAAKEGNIVMFQHLV 232
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 1090-1272 1.00e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 56.51  E-value: 1.00e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1090 GKLEVCE-LLLGRGAAVSRTNRRGVPPLFCAARQGHWQIVRLLLERGCDVNLSDKQGRTPLMVAACEGHLSTVEFLLSKG 1168
Cdd:PHA02874    12 GDIEAIEkIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNG 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1169 AALSSL-----------------------DKEGLSALSWACLKGHRAVVQYLVEEGAAIDQMDKNGRTPLDLAAFYGDAE 1225
Cdd:PHA02874    92 VDTSILpipciekdmiktildcgidvnikDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFD 171

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1622849896 1226 TVLYLVEKGAVIEHVDHSGMRPLDRAIGCRNTSVVVALLRKGAKLGN 1272
Cdd:PHA02874   172 IIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMN 218
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 1296-1416 1.77e-07

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 54.74  E-value: 1.77e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1296 GNVMYKKGKMKEAAQRYQYALRKfpregfgedmrpfNELRVSLYLNLSRCRRKTNDFGMAEEFASKALEMKPKSYEAFYA 1375
Cdd:COG2956     49 GNLYRRRGEYDRAIRIHQKLLER-------------DPDRAEALLELAQDYLKAGLLDRAEELLEKLLELDPDDAEALRL 115

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1622849896 1376 RARAKRNSRQFVAALADLQEAVKLCPTNQEIKRLLARVEEE 1416
Cdd:COG2956    116 LAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLE 156
Ank_5 pfam13857
Ankyrin repeats (many copies);
1097-1152 3.37e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.88  E-value: 3.37e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622849896 1097 LLLGRGAAVSRTNRRGVPPLFCAARQGHWQIVRLLLERGCDVNLSDKQGRTPLMVA 1152
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
1339-1413 3.66e-07

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 53.47  E-value: 3.66e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622849896 1339 YLNLSRCRRKTNDFGMAEEFASKALEMKPKSYEAFYARARAKRNSRQFVAALADLQEAVKLCPTNQEIKRLLARV 1413
Cdd:COG0457     11 YNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNLGLA 85
PHA02946 PHA02946
ankyin-like protein; Provisional
 1096-1299 4.73e-07

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 54.29  E-value: 4.73e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1096 ELLLGRGAAVSRTNRRGVPPLFCAARQGHWQIVRLLLERGCDVNLSDKQGRTPL--MVAACEGHLSTVEFLLSKGAAL-S 1172
Cdd:PHA02946    56 EELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLyyLSGTDDEVIERINLLVQYGAKInN 135

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1173 SLDKEGLSALsWACLKGHRAVVQYLVEEGAAIDQMDKNGRTPL--DLAAFYGDAETVLYLVEKGAVIEHVDHSGMRPLDr 1250
Cdd:PHA02946   136 SVDEEGCGPL-LACTDPSERVFKKIMSIGFEARIVDKFGKNHIhrHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLH- 213

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1251 aIGC----RNTSVVVALL-----RKGAKLGNAAWAM--ATSKPDILIillQKLMEEGNVM 1299
Cdd:PHA02946   214 -IVCsktvKNVDIINLLLpstdvNKQNKFGDSPLTLliKTLSPAHLI---NKLLSTSNVI 269
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 1092-1178 4.88e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.90  E-value: 4.88e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1092 LEVCEL-----------LLGRGAAVSRTNRRGVPPLFCAARQGHWQIVRLLLERGCDVNLSDKQGRTPLMVAACEGHLST 1160
Cdd:PTZ00322    84 VELCQLaasgdavgariLLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREV 163

                           90
                   ....*....|....*...
gi 1622849896 1161 VEFLLSKGAALSSLDKEG 1178
Cdd:PTZ00322   164 VQLLSRHSQCHFELGANA 181
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 1335-1413 5.68e-07

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 50.58  E-value: 5.68e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622849896 1335 RVSLYLNLSRCRRKTNDFGMAEEFASKALEMKPKSYEAFYARARAKRNSRQFVAALADLQEAVKLCPTNQEIKRLLARV 1413
Cdd:COG4783      3 CAEALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLA 81
Ank_4 pfam13637
Ankyrin repeats (many copies);
1211-1264 8.29e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.65  E-value: 8.29e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1622849896 1211 GRTPLDLAAFYGDAETVLYLVEKGAVIEHVDHSGMRPLDRAIGCRNTSVVVALL 1264
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 1116-1268 9.25e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 54.10  E-value: 9.25e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1116 LFCAARQGHWQIVRLLLERGCDVNLSDKQGRTPLMVAACEGHLSTVEFLLSKGAALSSLDKEGLSALSWACLKGHRAVVQ 1195
Cdd:PLN03192   529 LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFR 608

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622849896 1196 YLVEEGAAIDQmdKNGRTPLDLAAFYGDAETVLYLVEKGAVIEHVDHSGMRPLDRAIGCRNTSVVVALLRKGA 1268
Cdd:PLN03192   609 ILYHFASISDP--HAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGA 679
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 1079-1268 9.95e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 53.46  E-value: 9.95e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1079 GETALTAAAGRGKLEVCELLLGRGAaVSRTNRRGV-PPLFCAARQGHWQIVRLLLERGCDVN-LSDKQGRTPLMVAACEG 1156
Cdd:PHA02875    35 GISPIKLAMKFRDSEAIKLLMKHGA-IPDVKYPDIeSELHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILK 113

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1157 HLSTVEFLLSKGA--ALSSLDKegLSALSWACLKGHRAVVQYLVEEGAAIDQMDKNGRTPLDLAAFYGDAETVLYLVEKG 1234
Cdd:PHA02875   114 KLDIMKLLIARGAdpDIPNTDK--FSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSG 191

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1622849896 1235 AVIEHVDHSG-MRPLDRAIGCRNTSVVVALLRKGA 1268
Cdd:PHA02875   192 ANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGA 226
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 910-1140 1.04e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 53.46  E-value: 1.04e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896  910 TPNVKVSRLLILGGANVNYrtEVLNNAPILCVQSHLGHEEVVTLLLEFGACLDGTSENGMTALCYAAAAGHMKLVCLLTK 989
Cdd:PHA02875    12 FGELDIARRLLDIGINPNF--EIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLD 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896  990 KGARVDH-LDKKGQCALVHSALRGHGDILQYLLTCEWSPGPPQPGALRKNHALQQaltaaasMGHSSVVQCLLgmekEHE 1068
Cdd:PHA02875    90 LGKFADDvFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVM-------MGDIKGIELLI----DHK 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622849896 1069 VEVNGTDTlWGETALTAAAGRGKLEVCELLLGRGAAVSRTNRRGVPPLFCAARQGHW-QIVRLLLERGCDVNL 1140
Cdd:PHA02875   159 ACLDIEDC-CGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKiDIVRLFIKRGADCNI 230
Ank_5 pfam13857
Ankyrin repeats (many copies);
1164-1218 1.48e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.96  E-value: 1.48e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622849896 1164 LLSKG-AALSSLDKEGLSALSWACLKGHRAVVQYLVEEGAAIDQMDKNGRTPLDLA 1218
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 1149-1230 1.55e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 53.36  E-value: 1.55e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1149 LMVAACE----GHLSTVEFLLSKGAALSSLDKEGLSALSWACLKGHRAVVQYLVEEGAAIDQMDKNGRTPLDLAAFYGDA 1224
Cdd:PTZ00322    82 LTVELCQlaasGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFR 161


                   ....*.
gi 1622849896 1225 ETVLYL 1230
Cdd:PTZ00322   162 EVVQLL 167
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 949-1152 2.47e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 52.19  E-value: 2.47e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896  949 EVVTLLLEFGACLDGTSEN-GMTALCYAAAAGHMKLVCLLTKKGARVDHLDKKGQCALVHSALRGHGDILQYLLtcewsp 1027
Cdd:PHA02878   148 EITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILL------ 221

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1028 gppQPGAlrknhalqqaltaaaSMGHSSvvqcllgmekehevevngtdtLWGETALTAAAGRGK-LEVCELLLGRGAAVS 1106
Cdd:PHA02878   222 ---ENGA---------------STDARD---------------------KCGNTPLHISVGYCKdYDILKLLLEHGVDVN 262

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1622849896 1107 -RTNRRGVPPLFCAARQGhwQIVRLLLERGCDVNLSDKQGRTPLMVA 1152
Cdd:PHA02878   263 aKSYILGLTALHSSIKSE--RKLKLLLEYGADINSLNSYKLTPLSSA 307
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 1296-1381 2.71e-06

Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane constriction [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 441335 [Multi-domain]  Cd Length: 113  Bit Score: 48.06  E-value: 2.71e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1296 GNVMYKKGKMKEAAQRYQYALRKFPREGFGEDMrpfnelrvslYLNLSRCRRKTNDFGMAEEFASKALEMKPKSYEAFYA 1375
Cdd:COG1729     37 GEAYYALGDYDEAAEAFEKLLKRYPDSPKAPDA----------LLKLGLSYLELGDYDKARATLEELIKKYPDSEAAKEA 106


                   ....*.
gi 1622849896 1376 RARAKR 1381
Cdd:COG1729    107 RARLAR 112
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 1300-1415 3.16e-06

Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane constriction [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 441335 [Multi-domain]  Cd Length: 113  Bit Score: 47.68  E-value: 3.16e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1300 YKKGKMKEAAQRYQYALRKFPRegfgedmrpfNELRVSLYLNLSRCRRKTNDFGMAEEFASKALEMKPKSY---EAFYAR 1376
Cdd:COG1729      4 LKAGDYDEAIAAFKAFLKRYPN----------SPLAPDALYWLGEAYYALGDYDEAAEAFEKLLKRYPDSPkapDALLKL 73

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1622849896 1377 ARAKRNSRQFVAALADLQEAVKLCPTNQEIKRLLARVEE 1415
Cdd:COG1729     74 GLSYLELGDYDKARATLEELIKKYPDSEAAKEARARLAR 112
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 1050-1177 3.32e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 52.18  E-value: 3.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1050 SMGHSSVVQCLLgmekEHEVEVNGTDtLWGETALTAAAGRGKLEVCELLLgRGAAVSRTNRRGvpPLFC-AARQGHWQIV 1128
Cdd:PLN03192   567 SKGYEDCVLVLL----KHACNVHIRD-ANGNTALWNAISAKHHKIFRILY-HFASISDPHAAG--DLLCtAAKRNDLTAM 638

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1622849896 1129 RLLLERGCDVNLSDKQGRTPLMVAACEGHLSTVEFLLSKGAAL--SSLDKE 1177
Cdd:PLN03192   639 KELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVdkANTDDD 689
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
1345-1416 5.06e-06

Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 46.70  E-value: 5.06e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622849896 1345 CRRKTNDFGMAEEFASKALEMKPKSYEAFYARARAKRNSRQFVAALAdLQEAVKLCPTNQEIKRLLARVEEE 1416
Cdd:COG3063      1 LYLKLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIA-LEKALKLDPNNAEALLNLAELLLE 71
Ank_5 pfam13857
Ankyrin repeats (many copies);
1131-1182 1.03e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.64  E-value: 1.03e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1622849896 1131 LLERG-CDVNLSDKQGRTPLMVAACEGHLSTVEFLLSKGAALSSLDKEGLSAL 1182
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
PHA02798 PHA02798
ankyrin-like protein; Provisional
 1127-1243 1.80e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 49.45  E-value: 1.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1127 IVRLLLERGCDVNLSDKQGRTPLMVAACEGHLSTVEFLL---SKGAALSSLDKEGLSALSWACLKGHRA---VVQYLVEE 1200
Cdd:PHA02798    91 IVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLfmiENGADTTLLDKDGFTMLQVYLQSNHHIdieIIKLLLEK 170

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1622849896 1201 GAAIDQM-DKNGRTPLDLAAFYG----DAETVLYLVEKGAVIEHVDHS 1243
Cdd:PHA02798   171 GVDINTHnNKEKYDTLHCYFKYNidriDADILKLFVDNGFIINKENKS 218
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 1292-1418 2.02e-05

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 48.57  E-value: 2.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1292 LMEEGNVMYKKGKMKEAAQRYQYALRKFPREgfgedmrpfnelrVSLYLNLSRCRRKTNDFGMAEEFASKALEMKPKSYE 1371
Cdd:COG2956    147 YCELAELYLEQGDYDEAIEALEKALKLDPDC-------------ARALLLLAELYLEQGDYEEAIAALERALEQDPDYLP 213

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1622849896 1372 AFYARARAKRNSRQFVAALADLQEAVKLCPTNqEIKRLLARVEEECK 1418
Cdd:COG2956    214 ALPRLAELYEKLGDPEEALELLRKALELDPSD-DLLLALADLLERKE 259
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 1092-1220 2.26e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 47.51  E-value: 2.26e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1092 LEVCELLLGRGAAVS-RTNRRGVPPLfcaarqGHW---------QIVRLLLERGCDVNLSDKQGRTPLMV--AACEGHLS 1159
Cdd:PHA02859    66 VEILKFLIENGADVNfKTRDNNLSAL------HHYlsfnknvepEILKILIDSGSSITEEDEDGKNLLHMymCNFNVRIN 139

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622849896 1160 TVEFLLSKGAALSSLDKEGLSAL-SWACLKGHRAVVQYLVEEGAAIDQMDKNGRTPLDLAAF 1220
Cdd:PHA02859   140 VIKLLIDSGVSFLNKDFDNNNILySYILFHSDKKIFDFLTSLGIDINETNKSGYNCYDLIKF 201
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 1103-1233 2.37e-05

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 49.37  E-value: 2.37e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1103 AAVSRTNRRGVPPLFCAARQGHWQIVRLLLERGCDVNLSDKQ--------------GRTPLMVAACEGHLSTVEFLLSKG 1168
Cdd:cd22194    132 AEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGvffnpkykhegfyfGETPLALAACTNQPEIVQLLMEKE 211

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622849896 1169 AA-LSSLDKEG---LSALSWAC--LKGHRAVVQYLVE------EGAAIDQM-DKNGRTPLDLAAFYGDAETVLYLVEK 1233
Cdd:cd22194    212 STdITSQDSRGntvLHALVTVAedSKTQNDFVKRMYDmillksENKNLETIrNNEGLTPLQLAAKMGKAEILKYILSR 289
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 1079-1233 6.17e-05

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: 48.09  E-value: 6.17e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1079 GETALTAAAGRGKLEVCELLLgrGAAVSRTNR-------RGVPPLFCAARQGHWQIVRLLLERGCDVN----------LS 1141
Cdd:cd22192     51 GETALHVAALYDNLEAAVVLM--EAAPELVNEpmtsdlyQGETALHIAVVNQNLNLVRELIARGADVVspratgtffrPG 128

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1142 DKQ----GRTPLMVAACEGHLSTVEFLLSKGAALSSLDKEGLSALSWACLKGHRAVVQYLVE---------EGAAIDQM- 1207
Cdd:cd22192    129 PKNliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTFACQMYDlilsydkedDLQPLDLVp 208

                          170       180
                   ....*....|....*....|....*.
gi 1622849896 1208 DKNGRTPLDLAAFYGDAETVLYLVEK 1233
Cdd:cd22192    209 NNQGLTPFKLAAKEGNIVMFQHLVQK 234
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 1144-1176 2.15e-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: 39.97  E-value: 2.15e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1622849896 1144 QGRTPLMVAACE-GHLSTVEFLLSKGAALSSLDK 1176
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 1115-1143 2.47e-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: 39.97  E-value: 2.47e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1622849896 1115 PLFCAA-RQGHWQIVRLLLERGCDVNLSDK 1143
Cdd:pfam00023    5 PLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 905-1149 2.59e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 46.01  E-value: 2.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896  905 LRNLYTPNVKVSRLLI--LGGANVNYRTEVLNNAPILCVQShLGHEEVVTLLLEFGACLDGTSENGMTALCYAAAAGHMK 982
Cdd:PLN03192   494 LKNFLQHHKELHDLNVgdLLGDNGGEHDDPNMASNLLTVAS-TGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYED 572

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896  983 LVCLLTKKGARVDHLDKKGQCALVHSALRGHGDILQYLLTCEWSPGPPQPGALrknhalqqaltaaasmghssvvqcllg 1062
Cdd:PLN03192   573 CVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAGDL--------------------------- 625

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1063 mekehevevngtdtlwgetaLTAAAGRGKLEVCELLLGRGAAVSRTNRRGVPPLFCAARQGHWQIVRLLLERGCDV---N 1139
Cdd:PLN03192   626 --------------------LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVdkaN 685

                          250
                   ....*....|
gi 1622849896 1140 LSDKQGRTPL 1149
Cdd:PLN03192   686 TDDDFSPTEL 695
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 1144-1169 3.56e-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: 39.49  E-value: 3.56e-04
                            10        20
                    ....*....|....*....|....*.
gi 1622849896  1144 QGRTPLMVAACEGHLSTVEFLLSKGA 1169
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
PHA02798 PHA02798
ankyrin-like protein; Provisional
 1091-1268 4.85e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 44.83  E-value: 4.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1091 KLEVCELLLGRGAAVSRTNRRGVPPLFCAARQGH---WQIVRLLLERGCDVNLSDKQGRTPLMVAACEGH---LSTVEFL 1164
Cdd:PHA02798    88 MLDIVKILIENGADINKKNSDGETPLYCLLSNGYinnLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLL 167

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1165 LSKGAALSSL-DKEGLSAL------SWACLKGHraVVQYLVEEGAAIDQMDKNGRTPL--DLAAFYGDA----ETVLYLV 1231
Cdd:PHA02798   168 LEKGVDINTHnNKEKYDTLhcyfkyNIDRIDAD--ILKLFVDNGFIINKENKSHKKKFmeYLNSLLYDNkrfkKNILDFI 245

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1622849896 1232 EKGAVIEHVDHSGMRPLDRAIGCRNTSVVVALLRKGA 1268
Cdd:PHA02798   246 FSYIDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGG 282
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 1111-1139 6.56e-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: 38.78  E-value: 6.56e-04
                           10        20
                   ....*....|....*....|....*....
gi 1622849896 1111 RGVPPLFCAARQGHWQIVRLLLERGCDVN 1139
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 1079-1250 7.27e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 44.49  E-value: 7.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1079 GETALTAAA---GRGKLEVCELLLGRGAAVSRTNRRGVPPLFCAARQGH-----------WQIVRLLLERGCDVNLS--- 1141
Cdd:cd21882     26 GKTCLHKAAlnlNDGVNEAIMLLLEAAPDSGNPKELVNAPCTDEFYQGQtalhiaienrnLNLVRLLVENGADVSARatg 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1142 ---DKQGRT-------PLMVAACEGHLSTVEFLLSKG---AALSSLDKEGLSALSWACLKGHRAVVQY---------LVE 1199
Cdd:cd21882    106 rffRKSPGNlfyfgelPLSLAACTNQEEIVRLLLENGaqpAALEAQDSLGNTVLHALVLQADNTPENSafvcqmynlLLS 185

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622849896 1200 EGAAIDQM-------DKNGRTPLDLAAFYGDAETVLYLVEKGAviehvdHSGMRPLDR 1250
Cdd:cd21882    186 YGAHLDPTqqleeipNHQGLTPLKLAAVEGKIVMFQHILQREF------SGPYQPLSR 237
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 1210-1238 1.15e-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: 37.95  E-value: 1.15e-03
                            10        20
                    ....*....|....*....|....*....
gi 1622849896  1210 NGRTPLDLAAFYGDAETVLYLVEKGAVIE 1238
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 25-319 1.69e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 43.62  E-value: 1.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896   25 GPETSPVLPLDHGADSPVSSLPAAEDTYRVSLAKGVSMSLPSSPLLPRQSHLVQSRANKKSPGPVRKPKYVESPRVPG-D 103
Cdd:PHA03307   131 APDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRrS 210

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896  104 AVIMPFREVSKPTEPDEHEAKADNEPSCSPAAQELLTRLGFLLGEGIPSATHITieDKNETMCTALSQGISPCSTLTSST 183
Cdd:PHA03307   211 SPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPIT--LPTRIWEASGWNGPSSRPGPASSS 288

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896  184 ASPSTDSPCStlnscvSKTAANKSPCETISSPSSTLESKDSGIIATITSSSENDDRSGSSLEWNKDGSLRLGVQKGVL-- 261
Cdd:PHA03307   289 SSPRERSPSP------SPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPAdp 362

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622849896  262 -HDRRADNCSPVAEEETTGSAESTLPKAESSAGDGPVPySQGSSSLIMPRPNSVAATSS 319
Cdd:PHA03307   363 sSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARR-RDATGRFPAGRPRPSPLDAG 420
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 1194-1283 1.70e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 43.35  E-value: 1.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1194 VQYLVEEGAAIDQMDKNGRTPLDLAAFYGDAETVLYLVEKGAVIEHVDHSGMRPLDRAIGCRNTSVVVALLRKGAKLGNA 1273
Cdd:PTZ00322    98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFEL 177

                           90
                   ....*....|
gi 1622849896 1274 AwamATSKPD 1283
Cdd:PTZ00322   178 G---ANAKPD 184
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 1300-1412 1.81e-03

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 43.15  E-value: 1.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1300 YKKGKMKEAAQRYQYALRKFPREgfgedmrpfnelrVSLYLNLSRCRRKTNDFGMAEEFASKALEMKPKSYEAFYARARA 1379
Cdd:TIGR02917  510 IQEGNPDDAIQRFEKVLTIDPKN-------------LRAILALAGLYLRTGNEEEAVAWLEKAAELNPQEIEPALALAQY 576

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1622849896 1380 KRNSRQFVAALADLQEAVKLCPTNQEIKRLLAR 1412
Cdd:TIGR02917  577 YLGKGQLKKALAILNEAADAAPDSPEAWLMLGR 609
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 1111-1140 3.04e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.80  E-value: 3.04e-03
                            10        20        30
                    ....*....|....*....|....*....|
gi 1622849896  1111 RGVPPLFCAARQGHWQIVRLLLERGCDVNL 1140
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 1302-1413 3.05e-03

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 41.64  E-value: 3.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1302 KGKMKEAAQRYQYALRKFPRegfgedmrpfnelRVSLYLNLSRCRRKTNDFGMAEEFASKALEMKPKSYEAFYARARAKR 1381
Cdd:COG2956     21 NGQPDKAIDLLEEALELDPE-------------TVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQDYL 87

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1622849896 1382 NSRQFVAALADLQEAVKLCPTNQEIKRLLARV 1413
Cdd:COG2956     88 KAGLLDRAEELLEKLLELDPDDAEALRLLAEI 119
TPR_14 pfam13428
Tetratricopeptide repeat;
1371-1413 3.16e-03

Tetratricopeptide repeat;


Pssm-ID: 463874 [Multi-domain]  Cd Length: 44  Bit Score: 37.02  E-value: 3.16e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1622849896 1371 EAFYARARAKRNSRQFVAALADLQEAVKLCPTNQEIKRLLARV 1413
Cdd:pfam13428    2 EALLALARALLALGDPDEALALLERALALDPDDPEAWLALAQL 44
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 1115-1248 3.23e-03

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: 42.31  E-value: 3.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1115 PLFCAARQGHWQ-IVRLLLERGCDVNLSDKQGRTPLMVAACEGHLSTVEFLLSKGAAL------SSLdKEGLSALSWACL 1187
Cdd:cd22192     20 PLLLAAKENDVQaIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELvnepmtSDL-YQGETALHIAVV 98

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622849896 1188 KGHRAVVQYLVEEGAAI--------------DQMDKNGRTPLDLAAFYGDAETVLYLVEKGAVIEHVDHSGMRPL 1248
Cdd:cd22192     99 NQNLNLVRELIARGADVvspratgtffrpgpKNLIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
TPR_12 pfam13424
Tetratricopeptide repeat;
1296-1368 4.72e-03

Tetratricopeptide repeat;


Pssm-ID: 315987 [Multi-domain]  Cd Length: 77  Bit Score: 37.75  E-value: 4.72e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622849896 1296 GNVMYKKGKMKEAAQRYQYALRKFpREGFGEDmrpfNELRVSLYLNLSRCRRKTNDFGMAEEFASKALEMKPK 1368
Cdd:pfam13424   10 AAVLRRLGRYDEALELLEKALEIA-RRLLGPD----HPLTATTLLNLGRLYLELGRYEEALELLERALALAEK 77
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 939-1023 6.18e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.42  E-value: 6.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896  939 LCVQSHLGHEEVVTLLLEFGACLDGTSENGMTALCYAAAAGHMKLVCLLTKKGARVDHLDKKGQCALVHSALRGHGDILQ 1018
Cdd:PTZ00322    86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165


                   ....*
gi 1622849896 1019 YLLTC 1023
Cdd:PTZ00322   166 LLSRH 170
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 1079-1162 8.13e-03

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 41.22  E-value: 8.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849896 1079 GETALTAAAGRGKLEVCELLLGRGAAVS-RTN-------------RRGVPPLFCAARQGHWQIVRLLLERGCDVNLSDKQ 1144
Cdd:TIGR00870  128 GITALHLAAHRQNYEIVKLLLERGASVPaRACgdffvksqgvdsfYHGESPLNAAACLGSPSIVALLSEDPADILTADSL 207

                           90
                   ....*....|....*...
gi 1622849896 1145 GRTPLmvaacegHLSTVE 1162
Cdd:TIGR00870  208 GNTLL-------HLLVME 218
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 967-999 9.57e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. 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: 35.34  E-value: 9.57e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1622849896  967 NGMTALCYAAA-AGHMKLVCLLTKKGARVDHLDK 999
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 1210-1242 9.67e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. 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: 35.34  E-value: 9.67e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1622849896 1210 NGRTPLDLAA-FYGDAETVLYLVEKGAVIEHVDH 1242
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
 
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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