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Conserved domains on  [gi|1622849900|ref|XP_028686560|]
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protein TANC1 isoform X3 [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];
1072-1278 3.78e-52

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 185.93  E-value: 3.78e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1072 GETALTAAAGRGKLEVCELLLGRGAAVSRTNRRGVPPLFCAARQGHWQIVRLLLERGCDVNLSDKQGRTPLMVAACEGHL 1151
Cdd:COG0666     54 GALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNL 133

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1152 STVEFLLSKGAALSSLDKEGLSALSWACLKGHRAVVQYLVEEGAAIDQMDKNGRTPLDLAAFYGDAETVLYLVEKGAVIE 1231
Cdd:COG0666    134 EIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVN 213

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1622849900 1232 HVDHSGMRPLDRAIGCRNTSVVVALLRKGAKLGNAAWAMATSKPDIL 1278
Cdd:COG0666    214 AKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAA 260
PHA02876 super family cl31517
ankyrin repeat protein; Provisional
 847-1263 8.57e-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: 8.57e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900  847 LNRQQTMELGHHILKAhifkglskktGISSSHLQALWIGYSTEGLSAALASLRNlytPNVKVSRLLILGGANVNYRtEVL 926
Cdd:PHA02876   112 LNKHKLDEACIHILKE----------AISGNDIHYDKINESIEYMKLIKERIQQ---DELLIAEMLLEGGADVNAK-DIY 177

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900  927 NNAPILCVQSHlGHEEVVTLLLEFGACLDGTSENGMTALCYAAAAGHMKLVCLLTKKGARVDHLDKKGQCALVHSALRGH 1006
Cdd:PHA02876   178 CITPIHYAAER-GNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKNDLSLLKAIRNEDLETS 256

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1007 ------GDILQYLLTCEWSPgppqpgalrknhalqqALTAAASMGHSSVVQCLLgmekEHEVEVNGTDtLWGETALTAAA 1080
Cdd:PHA02876   257 lllydaGFSVNSIDDCKNTP----------------LHHASQAPSLSRLVPKLL----ERGADVNAKN-IKGETPLYLMA 315

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1081 GRG-KLEVCELLLGRGAAVSRTNRRGVPPLFCAARQGHWQ-IVRLLLERGCDVNLSDKQGRTPLMVAACEGHLSTVEFLL 1158
Cdd:PHA02876   316 KNGyDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKdIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLL 395

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1159 SKGAALSSLDKEGLSALSWA-CLKGHRAVVQYLVEEGAAIDQMDKNGRTPLDLAAFYG-DAETVLYLVEKGAVIEHVDHS 1236
Cdd:PHA02876   396 DYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQ 475

                          410       420
                   ....*....|....*....|....*..
gi 1622849900 1237 GMRPLDRAIGCRntSVVVALLRKGAKL 1263
Cdd:PHA02876   476 NQYPLLIALEYH--GIVNILLHYGAEL 500
Spy super family cl27809
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 1266-1403 4.33e-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: 4.33e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1266 AAWAMATSKPDILIILLQKLMEE-----------GNVMYKKGKMKEAAQRYQYALRKFPREgfgedmrpfnelrVSLYLN 1334
Cdd:COG3914     85 ALLLQALGRYEEALALYRRALALnpdnaealfnlGNLLLALGRLEEALAALRRALALNPDF-------------AEAYLN 151

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622849900 1335 LSRCRRKTNDFGMAEEFASKALEMKPKSYEAFYARARAKRNSRQFVAALADLQEAVKLCPTNQEIKRLL 1403
Cdd:COG3914    152 LGEALRRLGRLEEAIAALRRALELDPDNAEALNNLGNALQDLGRLEEAIAAYRRALELDPDNADAHSNL 220
NACHT super family cl26020
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
514-815 3.86e-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: 3.86e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900  514 FVHSIAALLCRSHQLAAYR-DLLIKEPQLQSMLSLRSCVQDPVAAFKRGVLEPLTNLRNEQKIpeeeyIILIDGLNEAEF 592
Cdd:COG5635    196 LLRYLALELAERYLDAEDPiPILIELRDLAEEASLEDLLAEALEKRGGEPEDALERLLRNGRL-----LLLLDGLDEVPD 270

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900  593 hkPDYGDTLSSFITKIISKFPAwLKLIVTVRANFQEIISALPFVKLSLDDFpDNKDIHSDLHAYVQHRVHSSQDILSNIS 672
Cdd:COG5635    271 --EADRDEVLNQLRRFLERYPK-ARVIITSRPEGYDSSELEGFEVLELAPL-SDEQIEEFLKKWFEATERKAERLLEALE 346

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900  673 LNGKadatligkvsshlvLRSL-GSYLYLKLTLDLFQRGHlviksasykVVPVSLSELYLLQCNMkFMTQSAFERALPIL 751
Cdd:COG5635    347 ENPE--------------LRELaRNPLLLTLLALLLRERG---------ELPDTRAELYEQFVEL-LLERWDEQRGLTIY 402

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900  752 N-------------VALASLH----PMTDEQIFQAINAgHIQGEQGWEDFQQRMDALSCFLIKRRDKTRMFCHPSFREWL 814
Cdd:COG5635    403 RelsreelrellseLALAMQEngrtEFAREELEEILRE-YLGRRKDAEALLDELLLRTGLLVERGEGRYSFAHRSFQEYL 481


                   .
gi 1622849900  815 V 815
Cdd:COG5635    482 A 482
PHA03307 super family cl33723
transcriptional regulator ICP4; Provisional
 25-319 1.66e-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: 1.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900   25 GPETSPVLPLDHGADSPVSSLPAAEDTYRVSLAKGVSMSLPSSPLLPRQSHLVQSRANKKSPGPVRKPKYVESPRVPG-D 103
Cdd:PHA03307   131 APDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRrS 210

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900  104 AVIMPFREVSKPTEPDEHEAKADNEPSCSPAAQELLTRLGFLLGEGIPSATHITieDKNETMCTALSQGISPCSTLTSST 183
Cdd:PHA03307   211 SPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPIT--LPTRIWEASGWNGPSSRPGPASSS 288

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900  184 ASPSTDSPCStlnscvSKTAANKSPCETISSPSSTLESKDSGIIATITSSSENDDRSGSSLEWNKDGSLRLGVQKGVL-- 261
Cdd:PHA03307   289 SSPRERSPSP------SPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPAdp 362

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622849900  262 -HDRRADNCSPVAEEETTGSAESTLPKAESSAGDGPVPySQGSSSLIMPRPNSVAATSS 319
Cdd:PHA03307   363 sSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARR-RDATGRFPAGRPRPSPLDAG 420
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1072-1278 3.78e-52

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 185.93  E-value: 3.78e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1072 GETALTAAAGRGKLEVCELLLGRGAAVSRTNRRGVPPLFCAARQGHWQIVRLLLERGCDVNLSDKQGRTPLMVAACEGHL 1151
Cdd:COG0666     54 GALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNL 133

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1152 STVEFLLSKGAALSSLDKEGLSALSWACLKGHRAVVQYLVEEGAAIDQMDKNGRTPLDLAAFYGDAETVLYLVEKGAVIE 1231
Cdd:COG0666    134 EIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVN 213

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1622849900 1232 HVDHSGMRPLDRAIGCRNTSVVVALLRKGAKLGNAAWAMATSKPDIL 1278
Cdd:COG0666    214 AKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAA 260
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1109-1201 2.91e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.87  E-value: 2.91e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1109 LFCAARQGHWQIVRLLLERGCDVNLSDKQGRTPLMVAACEGHLSTVEFLLSKGAAlsSLDKEGLSALSWACLKGHRAVVQ 1188
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 1622849900 1189 YLVEEGAAIDQMD 1201
Cdd:pfam12796   79 LLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 1085-1261 1.25e-21

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 99.74  E-value: 1.25e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1085 LEVCELLLGRGAAVSRTNRRGVPPLFCAA--RQGHWQIVRLLLERGCDVNLSDKQGRTPLMVAA--CEGHLSTVEFLLSK 1160
Cdd:PHA03100    86 KEIVKLLLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLesNKIDLKILKLLIDK 165

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1161 GAALSSLDKeglsalswaclkghravVQYLVEEGAAIDQMDKNGRTPLDLAAFYGDAETVLYLVEKGAVIEHVDHSGMRP 1240
Cdd:PHA03100   166 GVDINAKNR-----------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTP 228

                          170       180
                   ....*....|....*....|.
gi 1622849900 1241 LDRAIGCRNTSVVVALLRKGA 1261
Cdd:PHA03100   229 LHIAILNNNKEIFKLLLNNGP 249
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 847-1263 8.57e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 70.48  E-value: 8.57e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900  847 LNRQQTMELGHHILKAhifkglskktGISSSHLQALWIGYSTEGLSAALASLRNlytPNVKVSRLLILGGANVNYRtEVL 926
Cdd:PHA02876   112 LNKHKLDEACIHILKE----------AISGNDIHYDKINESIEYMKLIKERIQQ---DELLIAEMLLEGGADVNAK-DIY 177

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900  927 NNAPILCVQSHlGHEEVVTLLLEFGACLDGTSENGMTALCYAAAAGHMKLVCLLTKKGARVDHLDKKGQCALVHSALRGH 1006
Cdd:PHA02876   178 CITPIHYAAER-GNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKNDLSLLKAIRNEDLETS 256

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1007 ------GDILQYLLTCEWSPgppqpgalrknhalqqALTAAASMGHSSVVQCLLgmekEHEVEVNGTDtLWGETALTAAA 1080
Cdd:PHA02876   257 lllydaGFSVNSIDDCKNTP----------------LHHASQAPSLSRLVPKLL----ERGADVNAKN-IKGETPLYLMA 315

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1081 GRG-KLEVCELLLGRGAAVSRTNRRGVPPLFCAARQGHWQ-IVRLLLERGCDVNLSDKQGRTPLMVAACEGHLSTVEFLL 1158
Cdd:PHA02876   316 KNGyDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKdIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLL 395

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1159 SKGAALSSLDKEGLSALSWA-CLKGHRAVVQYLVEEGAAIDQMDKNGRTPLDLAAFYG-DAETVLYLVEKGAVIEHVDHS 1236
Cdd:PHA02876   396 DYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQ 475

                          410       420
                   ....*....|....*....|....*..
gi 1622849900 1237 GMRPLDRAIGCRntSVVVALLRKGAKL 1263
Cdd:PHA02876   476 NQYPLLIALEYH--GIVNILLHYGAEL 500
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 1266-1403 4.33e-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: 4.33e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1266 AAWAMATSKPDILIILLQKLMEE-----------GNVMYKKGKMKEAAQRYQYALRKFPREgfgedmrpfnelrVSLYLN 1334
Cdd:COG3914     85 ALLLQALGRYEEALALYRRALALnpdnaealfnlGNLLLALGRLEEALAALRRALALNPDF-------------AEAYLN 151

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622849900 1335 LSRCRRKTNDFGMAEEFASKALEMKPKSYEAFYARARAKRNSRQFVAALADLQEAVKLCPTNQEIKRLL 1403
Cdd:COG3914    152 LGEALRRLGRLEEAIAALRRALELDPDNAEALNNLGNALQDLGRLEEAIAAYRRALELDPDNADAHSNL 220
Ank_2 pfam12796
Ankyrin repeats (3 copies);
939-1014 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 1622849900  939 GHEEVVTLLLEFGACLDGTSENGMTALCYAAAAGHMKLV-CLLTKKGARVDHldkKGQCALVHSALRGHGDILQYLL 1014
Cdd:pfam12796    8 GNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVkLLLEHADVNLKD---NGRTALHYAARSGHLEIVKLLL 81
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
514-815 3.86e-08

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 58.66  E-value: 3.86e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900  514 FVHSIAALLCRSHQLAAYR-DLLIKEPQLQSMLSLRSCVQDPVAAFKRGVLEPLTNLRNEQKIpeeeyIILIDGLNEAEF 592
Cdd:COG5635    196 LLRYLALELAERYLDAEDPiPILIELRDLAEEASLEDLLAEALEKRGGEPEDALERLLRNGRL-----LLLLDGLDEVPD 270

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900  593 hkPDYGDTLSSFITKIISKFPAwLKLIVTVRANFQEIISALPFVKLSLDDFpDNKDIHSDLHAYVQHRVHSSQDILSNIS 672
Cdd:COG5635    271 --EADRDEVLNQLRRFLERYPK-ARVIITSRPEGYDSSELEGFEVLELAPL-SDEQIEEFLKKWFEATERKAERLLEALE 346

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900  673 LNGKadatligkvsshlvLRSL-GSYLYLKLTLDLFQRGHlviksasykVVPVSLSELYLLQCNMkFMTQSAFERALPIL 751
Cdd:COG5635    347 ENPE--------------LRELaRNPLLLTLLALLLRERG---------ELPDTRAELYEQFVEL-LLERWDEQRGLTIY 402

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900  752 N-------------VALASLH----PMTDEQIFQAINAgHIQGEQGWEDFQQRMDALSCFLIKRRDKTRMFCHPSFREWL 814
Cdd:COG5635    403 RelsreelrellseLALAMQEngrtEFAREELEEILRE-YLGRRKDAEALLDELLLRTGLLVERGEGRYSFAHRSFQEYL 481


                   .
gi 1622849900  815 V 815
Cdd:COG5635    482 A 482
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 1072-1191 9.58e-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: 9.58e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1072 GETALTAAAGRGKLEVCELLLGRGAAVS---------RTNRR-----GVPPLFCAARQGHWQIVRLLLERGCDVNLSDKQ 1137
Cdd:cd22192     89 GETALHIAVVNQNLNLVRELIARGADVVspratgtffRPGPKnliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSL 168

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622849900 1138 GRTPLMV--------AACEghlsTVEFLLS--KGAALSSLD----KEGLSALSWACLKGHRAVVQYLV 1191
Cdd:cd22192    169 GNTVLHIlvlqpnktFACQ----MYDLILSydKEDDLQPLDlvpnNQGLTPFKLAAKEGNIVMFQHLV 232
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 1137-1162 3.55e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.49  E-value: 3.55e-04
                            10        20
                    ....*....|....*....|....*.
gi 1622849900  1137 QGRTPLMVAACEGHLSTVEFLLSKGA 1162
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 25-319 1.66e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 43.62  E-value: 1.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900   25 GPETSPVLPLDHGADSPVSSLPAAEDTYRVSLAKGVSMSLPSSPLLPRQSHLVQSRANKKSPGPVRKPKYVESPRVPG-D 103
Cdd:PHA03307   131 APDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRrS 210

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900  104 AVIMPFREVSKPTEPDEHEAKADNEPSCSPAAQELLTRLGFLLGEGIPSATHITieDKNETMCTALSQGISPCSTLTSST 183
Cdd:PHA03307   211 SPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPIT--LPTRIWEASGWNGPSSRPGPASSS 288

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900  184 ASPSTDSPCStlnscvSKTAANKSPCETISSPSSTLESKDSGIIATITSSSENDDRSGSSLEWNKDGSLRLGVQKGVL-- 261
Cdd:PHA03307   289 SSPRERSPSP------SPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPAdp 362

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622849900  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 ...
 1293-1405 1.77e-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: 1.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1293 YKKGKMKEAAQRYQYALRKFPREgfgedmrpfnelrVSLYLNLSRCRRKTNDFGMAEEFASKALEMKPKSYEAFYARARA 1372
Cdd:TIGR02917  510 IQEGNPDDAIQRFEKVLTIDPKN-------------LRAILALAGLYLRTGNEEEAVAWLEKAAELNPQEIEPALALAQY 576

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1622849900 1373 KRNSRQFVAALADLQEAVKLCPTNQEIKRLLAR 1405
Cdd:TIGR02917  577 YLGKGQLKKALAILNEAADAAPDSPEAWLMLGR 609
TPR_14 pfam13428
Tetratricopeptide repeat;
1364-1406 3.00e-03

Tetratricopeptide repeat;


Pssm-ID: 463874 [Multi-domain]  Cd Length: 44  Bit Score: 37.02  E-value: 3.00e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1622849900 1364 EAFYARARAKRNSRQFVAALADLQEAVKLCPTNQEIKRLLARV 1406
Cdd:pfam13428    2 EALLALARALLALGDPDEALALLERALALDPDDPEAWLALAQL 44
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 1072-1155 8.10e-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: 8.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1072 GETALTAAAGRGKLEVCELLLGRGAAVS-RTN-------------RRGVPPLFCAARQGHWQIVRLLLERGCDVNLSDKQ 1137
Cdd:TIGR00870  128 GITALHLAAHRQNYEIVKLLLERGASVPaRACgdffvksqgvdsfYHGESPLNAAACLGSPSIVALLSEDPADILTADSL 207

                           90
                   ....*....|....*...
gi 1622849900 1138 GRTPLmvaacegHLSTVE 1155
Cdd:TIGR00870  208 GNTLL-------HLLVME 218
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1072-1278 3.78e-52

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 185.93  E-value: 3.78e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1072 GETALTAAAGRGKLEVCELLLGRGAAVSRTNRRGVPPLFCAARQGHWQIVRLLLERGCDVNLSDKQGRTPLMVAACEGHL 1151
Cdd:COG0666     54 GALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNL 133

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1152 STVEFLLSKGAALSSLDKEGLSALSWACLKGHRAVVQYLVEEGAAIDQMDKNGRTPLDLAAFYGDAETVLYLVEKGAVIE 1231
Cdd:COG0666    134 EIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVN 213

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1622849900 1232 HVDHSGMRPLDRAIGCRNTSVVVALLRKGAKLGNAAWAMATSKPDIL 1278
Cdd:COG0666    214 AKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAA 260
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1065-1267 1.62e-50

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 181.31  E-value: 1.62e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1065 NGTDTLWGETALTAAAGRGKLEVCELLLGRGAAVSRTNRRGVPPLFCAARQGHWQIVRLLLERGCDVNLSDKQGRTPLMV 1144
Cdd:COG0666     80 INAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHL 159

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1145 AACEGHLSTVEFLLSKGAALSSLDKEGLSALSWACLKGHRAVVQYLVEEGAAIDQMDKNGRTPLDLAAFYGDAETVLYLV 1224
Cdd:COG0666    160 AAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1622849900 1225 EKGAVIEHVDHSGMRPLDRAIGCRNTSVVVALLRKGAKLGNAA 1267
Cdd:COG0666    240 EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
926-1241 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 1622849900  926 LNNAPILCVQSHLGHEEVVTLLLEFGACLDGTSENGMTALCYAAAAGHMKLVCLLTKKGARVDHLDKKGQCALVHSALRG 1005
Cdd:COG0666     19 LLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNG 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1006 HGDILQYLLtcewspgppqpgalrknhalqqaltaaasmghssvvqcllgmekEHEVEVNGTDTlWGETALTAAAGRGKL 1085
Cdd:COG0666     99 DLEIVKLLL--------------------------------------------EAGADVNARDK-DGETPLHLAAYNGNL 133

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1086 EVCELLLGRGAAVSRTNRRGVPPLFCAARQGHWQIVRLLLERGCDVNLSDKQGRTPLMVAACEGHLSTVEFLLSKGAALS 1165
Cdd:COG0666    134 EIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVN 213

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622849900 1166 SLDKEGLSALSWACLKGHRAVVQYLVEEGAAIDQMDKNGRTPLDLAAFYGDAETVLYLVEKGAVIEHVDHSGMRPL 1241
Cdd:COG0666    214 AKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
893-1208 5.27e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 156.65  E-value: 5.27e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900  893 AALASLRNLYTPNVKVSRLLILGGANVNYRTEVLNNAPILCVQSHLGHEEVVTLLLEFGACLDGTSENGMTALCYAAAAG 972
Cdd:COG0666     19 LLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNG 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900  973 HMKLVCLLTKKGARVDHLDKKGQCALVHSALRGHGDILQYLLtcewspgppqpgalrknhalqqaltaaasmghssvvqc 1052
Cdd:COG0666     99 DLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLL-------------------------------------- 140

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1053 llgmekEHEVEVNGTDTlWGETALTAAAGRGKLEVCELLLGRGAAVSRTNRRGVPPLFCAARQGHWQIVRLLLERGCDVN 1132
Cdd:COG0666    141 ------EAGADVNAQDN-DGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVN 213

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622849900 1133 LSDKQGRTPLMVAACEGHLSTVEFLLSKGAALSSLDKEGLSALSWACLKGHRAVVQYLVEEGAAIDQMDKNGRTPL 1208
Cdd:COG0666    214 AKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1053-1311 8.09e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 153.19  E-value: 8.09e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1053 LLGMEKEHEVEVNGTDTLWGETALTAAAGRGKLEVCELLLGRGAAVSRTNRRGVPPLFCAARQGHWQIVRLLLERGCDVN 1132
Cdd:COG0666      2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1133 LSDKQGRTPLMVAACEGHLSTVEFLLSKGAALSSLDKEGLSALSWACLKGHRAVVQYLVEEGAAIDQMDKNGRTPLDLAA 1212
Cdd:COG0666     82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1213 FYGDAETVLYLVEKGAVIEHVDHSGMRPLDRAIGCRNTSVVVALLRKGA------KLGNAA--WAMATSKPDILIILLQK 1284
Cdd:COG0666    162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGAdvnakdNDGKTAldLAAENGNLEIVKLLLEA 241

                          250       260
                   ....*....|....*....|....*..
gi 1622849900 1285 LMEEGNVMYKKGKMKEAAQRYQYALRK 1311
Cdd:COG0666    242 GADLNAKDKDGLTALLLAAAAGAALIV 268
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1085-1284 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 1622849900 1085 LEVCELLLGRGAAVSRTNRRGVPPLFCAARQGHWQIVRLLLERGCDVNLSDKQGRTPLMVAACEGHLSTVEFLLSKGAAL 1164
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1165 SSLDKEGLSALSWACLKGHRAVVQYLVEEGAAIDQMDKNGRTPLDLAAFYGDAETVLYLVEKGAVIEHVDHSGMRPLDRA 1244
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1622849900 1245 IGCRNTSVVVALLRKGA------KLGNAA--WAMATSKPDILIILLQK 1284
Cdd:COG0666    161 AANGNLEIVKLLLEAGAdvnardNDGETPlhLAAENGHLEIVKLLLEA 208
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1109-1201 2.91e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.87  E-value: 2.91e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1109 LFCAARQGHWQIVRLLLERGCDVNLSDKQGRTPLMVAACEGHLSTVEFLLSKGAAlsSLDKEGLSALSWACLKGHRAVVQ 1188
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 1622849900 1189 YLVEEGAAIDQMD 1201
Cdd:pfam12796   79 LLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 1085-1261 1.25e-21

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 99.74  E-value: 1.25e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1085 LEVCELLLGRGAAVSRTNRRGVPPLFCAA--RQGHWQIVRLLLERGCDVNLSDKQGRTPLMVAA--CEGHLSTVEFLLSK 1160
Cdd:PHA03100    86 KEIVKLLLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLesNKIDLKILKLLIDK 165

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1161 GAALSSLDKeglsalswaclkghravVQYLVEEGAAIDQMDKNGRTPLDLAAFYGDAETVLYLVEKGAVIEHVDHSGMRP 1240
Cdd:PHA03100   166 GVDINAKNR-----------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTP 228

                          170       180
                   ....*....|....*....|.
gi 1622849900 1241 LDRAIGCRNTSVVVALLRKGA 1261
Cdd:PHA03100   229 LHIAILNNNKEIFKLLLNNGP 249
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1142-1234 2.49e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 90.18  E-value: 2.49e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1142 LMVAACEGHLSTVEFLLSKGAALSSLDKEGLSALSWACLKGHRAVVQYLVEEGAAidQMDKNGRTPLDLAAFYGDAETVL 1221
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 1622849900 1222 YLVEKGAVIEHVD 1234
Cdd:pfam12796   79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1076-1162 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 1622849900 1076 LTAAAGRGKLEVCELLLGRGAAVSRTNRRGVPPLFCAARQGHWQIVRLLLERgCDVNLSDkQGRTPLMVAACEGHLSTVE 1155
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78


                   ....*..
gi 1622849900 1156 FLLSKGA 1162
Cdd:pfam12796   79 LLLEKGA 85
PHA03095 PHA03095
ankyrin-like protein; Provisional
 899-1259 1.32e-19

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 94.32  E-value: 1.32e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900  899 RNLYTPNVKVS--RLLILGGANVNYRTEvLNNAPiLCVQSHLGHE---EVVTLLLEFGACLDGTSENGMTAL-CYAAAAG 972
Cdd:PHA03095    18 YLLNASNVTVEevRRLLAAGADVNFRGE-YGKTP-LHLYLHYSSEkvkDIVRLLLEAGADVNAPERCGFTPLhLYLYNAT 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900  973 HMKLVCLLTKKGARVDHLDKKGQCALvHSALRG---HGDILQYLLtcewspgppqpgalrknhalqqaltaaasmghssv 1049
Cdd:PHA03095    96 TLDVIKLLIKAGADVNAKDKVGRTPL-HVYLSGfniNPKVIRLLL----------------------------------- 139

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1050 vqcllgmekEHEVEVNGTDtLWGETALTA--AAGRGKLEVCELLLGRGAAVSRTNRRGVPPL-----FCAARQGhwqIVR 1122
Cdd:PHA03095   140 ---------RKGADVNALD-LYGMTPLAVllKSRNANVELLRLLIDAGADVYAVDDRFRSLLhhhlqSFKPRAR---IVR 206

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1123 LLLERGCDVNLSDKQGRTPLMVAACEGhlstvefllskgaalssldkeglsalswAClkgHRAVVQYLVEEGAAIDQMDK 1202
Cdd:PHA03095   207 ELIRAGCDPAATDMLGNTPLHSMATGS----------------------------SC---KRSLVLPLLIAGISINARNR 255

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622849900 1203 NGRTPLDLAAFYGDAETVLYLVEKGAVIEHVDHSGMRPLDRAIGCRNTSVVVALLRK 1259
Cdd:PHA03095   256 YGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAK 312
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 951-1267 3.04e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 86.56  E-value: 3.04e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900  951 GACLDGTSENGMTALCYAAAAGHMKLVCLLTKKGARVDHLDKKGQCALVHSALRGHGDILQYLLTCEWSPGP-PQPGAlr 1029
Cdd:PHA02874    25 GNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSIlPIPCI-- 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1030 knhalqqaltaaasmgHSSVVQCLLgmekEHEVEVNGTDTLwGETALTAAAGRGKLEVCELLLGRGAAVSRTNRRGVPPL 1109
Cdd:PHA02874   103 ----------------EKDMIKTIL----DCGIDVNIKDAE-LKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPI 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1110 FCAARQGHWQIVRLLLERGCDVNLSDKQGRTPLMVAACEGHLSTVEFLLSKGAALSSLDKEGLSALSWACLKgHRAVVQY 1189
Cdd:PHA02874   162 HIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIH-NRSAIEL 240

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622849900 1190 LVEEgAAIDQMDKNGRTPLDLAAFYG-DAETVLYLVEKGAVIEHVDHSGMRPLDRAIGCRNTSVVVALLRKGAKLGNAA 1267
Cdd:PHA02874   241 LINN-ASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTAFKYINKDPVIKDIIANAVLIKEA 318
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1045-1135 7.76e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 71.69  E-value: 7.76e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1045 GHSSVVQCLLgmekEHEVEVNGTDTlWGETALTAAAGRGKLEVCELLLGRGAAVSRTNrrGVPPLFCAARQGHWQIVRLL 1124
Cdd:pfam12796    8 GNLELVKLLL----ENGADANLQDK-NGRTALHLAAKNGHLEIVKLLLEHADVNLKDN--GRTALHYAARSGHLEIVKLL 80

                           90
                   ....*....|.
gi 1622849900 1125 LERGCDVNLSD 1135
Cdd:pfam12796   81 LEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1175-1263 1.50e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.92  E-value: 1.50e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1175 LSWACLKGHRAVVQYLVEEGAAIDQMDKNGRTPLDLAAFYGDAETVLYLVEKGAVieHVDHSGMRPLDRAIGCRNTSVVV 1254
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78


                   ....*....
gi 1622849900 1255 ALLRKGAKL 1263
Cdd:pfam12796   79 LLLEKGADI 87
PHA03095 PHA03095
ankyrin-like protein; Provisional
 1085-1261 2.85e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 77.76  E-value: 2.85e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1085 LEVCELLLGRGAAVSRTNRRGVPPLFCAARQGH-WQIVRLLLERGCDVNLSDKQGRTPLMVAAC--EGHLSTVEFLLSKG 1161
Cdd:PHA03095    63 KDIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAGADVNAKDKVGRTPLHVYLSgfNINPKVIRLLLRKG 142

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1162 AALSSLDKEGLSALSwACLKGHRA---VVQYLVEEGA-----------AIDQM------------------------DKN 1203
Cdd:PHA03095   143 ADVNALDLYGMTPLA-VLLKSRNAnveLLRLLIDAGAdvyavddrfrsLLHHHlqsfkprarivreliragcdpaatDML 221

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1204 GRTPLDLAAFYGDAET--VLYLVEKGAVIEHVDHSGMRPLDRAIGCRNTSVVVALLRKGA 1261
Cdd:PHA03095   222 GNTPLHSMATGSSCKRslVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGA 281
PHA03095 PHA03095
ankyrin-like protein; Provisional
 1120-1263 3.98e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 76.99  E-value: 3.98e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1120 IVRLLLERGCDVNLSDKQGRTPL---MVAACEGHLSTVEFLLSKGAALSSLDKEGLSAL-SWACLKGHRAVVQYLVEEGA 1195
Cdd:PHA03095    29 EVRRLLAAGADVNFRGEYGKTPLhlyLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLhLYLYNATTLDVIKLLIKAGA 108

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622849900 1196 AIDQMDKNGRTPLD--LAAFYGDAETVLYLVEKGAVIEHVDHSGMRPLDRAIGCRNTSV--VVALLRKGAKL 1263
Cdd:PHA03095   109 DVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVelLRLLIDAGADV 180
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 941-1203 5.42e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 73.16  E-value: 5.42e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900  941 EEVVTLLLEFGACLDGTSENGMTALCYAAAAGH-----MKLVCLLTKKGARVDHLDKKGqcalVHsalrghgdILQYLLT 1015
Cdd:PHA03100    48 IDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVNAPDNNG----IT--------PLLYAIS 115

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1016 CEwspgppqpgalrknhalqqaltaaasMGHSSVVQCLLgmekEHEVEVNgTDTLWGETALTAAA--GRGKLEVCELLLG 1093
Cdd:PHA03100   116 KK--------------------------SNSYSIVEYLL----DNGANVN-IKNSDGENLLHLYLesNKIDLKILKLLID 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1094 RGAAVSRTNRrgvpplfcaarqghwqiVRLLLERGCDVNLSDKQGRTPLMVAACEGHLSTVEFLLSKGAALSSLDKEGLS 1173
Cdd:PHA03100   165 KGVDINAKNR-----------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDT 227

                          250       260       270
                   ....*....|....*....|....*....|
gi 1622849900 1174 ALSWACLKGHRAVVQYLVEEGAAIDQMDKN 1203
Cdd:PHA03100   228 PLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 1119-1268 4.06e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 70.68  E-value: 4.06e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1119 QIVRLLLERGCDVNLSDK-QGRTPLMVAACEGHLSTVEFLLSKGAALSSLDKEGLSALSWACLKGHRAVVQYLVEEGAAI 1197
Cdd:PHA02878   148 EITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAST 227

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622849900 1198 DQMDKNGRTPLDLAAFY-GDAETVLYLVEKGAVIEHVDH-SGMRPLDRAIgcRNTSVVVALLRKGAKLGNAAW 1268
Cdd:PHA02878   228 DARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYiLGLTALHSSI--KSERKLKLLLEYGADINSLNS 298
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 847-1263 8.57e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 70.48  E-value: 8.57e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900  847 LNRQQTMELGHHILKAhifkglskktGISSSHLQALWIGYSTEGLSAALASLRNlytPNVKVSRLLILGGANVNYRtEVL 926
Cdd:PHA02876   112 LNKHKLDEACIHILKE----------AISGNDIHYDKINESIEYMKLIKERIQQ---DELLIAEMLLEGGADVNAK-DIY 177

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900  927 NNAPILCVQSHlGHEEVVTLLLEFGACLDGTSENGMTALCYAAAAGHMKLVCLLTKKGARVDHLDKKGQCALVHSALRGH 1006
Cdd:PHA02876   178 CITPIHYAAER-GNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKNDLSLLKAIRNEDLETS 256

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1007 ------GDILQYLLTCEWSPgppqpgalrknhalqqALTAAASMGHSSVVQCLLgmekEHEVEVNGTDtLWGETALTAAA 1080
Cdd:PHA02876   257 lllydaGFSVNSIDDCKNTP----------------LHHASQAPSLSRLVPKLL----ERGADVNAKN-IKGETPLYLMA 315

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1081 GRG-KLEVCELLLGRGAAVSRTNRRGVPPLFCAARQGHWQ-IVRLLLERGCDVNLSDKQGRTPLMVAACEGHLSTVEFLL 1158
Cdd:PHA02876   316 KNGyDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKdIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLL 395

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1159 SKGAALSSLDKEGLSALSWA-CLKGHRAVVQYLVEEGAAIDQMDKNGRTPLDLAAFYG-DAETVLYLVEKGAVIEHVDHS 1236
Cdd:PHA02876   396 DYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQ 475

                          410       420
                   ....*....|....*....|....*..
gi 1622849900 1237 GMRPLDRAIGCRntSVVVALLRKGAKL 1263
Cdd:PHA02876   476 NQYPLLIALEYH--GIVNILLHYGAEL 500
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 1266-1403 4.33e-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: 4.33e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1266 AAWAMATSKPDILIILLQKLMEE-----------GNVMYKKGKMKEAAQRYQYALRKFPREgfgedmrpfnelrVSLYLN 1334
Cdd:COG3914     85 ALLLQALGRYEEALALYRRALALnpdnaealfnlGNLLLALGRLEEALAALRRALALNPDF-------------AEAYLN 151

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622849900 1335 LSRCRRKTNDFGMAEEFASKALEMKPKSYEAFYARARAKRNSRQFVAALADLQEAVKLCPTNQEIKRLL 1403
Cdd:COG3914    152 LGEALRRLGRLEEAIAALRRALELDPDNAEALNNLGNALQDLGRLEEAIAAYRRALELDPDNADAHSNL 220
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
1289-1406 6.88e-11

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 64.64  E-value: 6.88e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1289 GNVMYKKGKMKEAAQRYQYALRKFPREgfgedmrpfnelrVSLYLNLSRCRRKTNDFGMAEEFASKALEMKPKSYEAFYA 1368
Cdd:COG0457     15 GLAYRRLGRYEEAIEDYEKALELDPDD-------------AEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNN 81

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1622849900 1369 RARAKRNSRQFVAALADLQEAVKLCPTNQEIKRLLARV 1406
Cdd:COG0457     82 LGLALQALGRYEEALEDYDKALELDPDDAEALYNLGLA 119
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
1289-1409 1.16e-10

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 63.87  E-value: 1.16e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1289 GNVMYKKGKMKEAAQRYQYALRKFPRegfgedmrpfnelRVSLYLNLSRCRRKTNDFGMAEEFASKALEMKPKSYEAFYA 1368
Cdd:COG0457     49 GLAYLRLGRYEEALADYEQALELDPD-------------DAEALNNLGLALQALGRYEEALEDYDKALELDPDDAEALYN 115

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1622849900 1369 RARAKRNSRQFVAALADLQEAVKLCPTNQEIKRLLARVEEE 1409
Cdd:COG0457    116 LGLALLELGRYDEAIEAYERALELDPDDADALYNLGIALEK 156
Ank_2 pfam12796
Ankyrin repeats (3 copies);
939-1014 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 1622849900  939 GHEEVVTLLLEFGACLDGTSENGMTALCYAAAAGHMKLV-CLLTKKGARVDHldkKGQCALVHSALRGHGDILQYLL 1014
Cdd:pfam12796    8 GNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVkLLLEHADVNLKD---NGRTALHYAARSGHLEIVKLLL 81
Ank_2 pfam12796
Ankyrin repeats (3 copies);
965-1102 2.24e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 58.97  E-value: 2.24e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900  965 LCYAAAAGHMKLVCLLTKKGARVDHLDKKGQCALVHSALRGHGDILQYLLTcewspgppqpgalrknhalqqaltaaasm 1044
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE----------------------------- 51

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622849900 1045 ghssvvqcllgmekehevEVNGTDTLWGETALTAAAGRGKLEVCELLLGRGAAVSRTN 1102
Cdd:pfam12796   52 ------------------HADVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 1282-1409 6.71e-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: 6.71e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1282 LQKLMEEGNVMYKKGKMKEAAQRYQYALRKFPREgfgedmrpfnelrVSLYLNLSRCRRKTNDFGMAEEFASKALEMKPK 1361
Cdd:COG4783      4 AEALYALAQALLLAGDYDEAEALLEKALELDPDN-------------PEAFALLGEILLQLGDLDEAIVLLHEALELDPD 70

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1622849900 1362 SYEAFYARARAKRNSRQFVAALADLQEAVKLCPTNQEIKRLLARVEEE 1409
Cdd:COG4783     71 EPEARLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRA 118
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
1291-1398 8.00e-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: 8.00e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1291 VMYKKGKMKEAAQRYQYALRKFPREGfgedmrpfnelrvSLYLNLSRCRRKTNDFGMAEEFaSKALEMKPKSYEAFYARA 1370
Cdd:COG3063      1 LYLKLGDLEEAEEYYEKALELDPDNA-------------DALNNLGLLLLEQGRYDEAIAL-EKALKLDPNNAEALLNLA 66

                           90       100
                   ....*....|....*....|....*...
gi 1622849900 1371 RAKRNSRQFVAALADLQEAVKLCPTNQE 1398
Cdd:COG3063     67 ELLLELGDYDEALAYLERALELDPSALR 94
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 1076-1242 1.63e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 62.96  E-value: 1.63e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1076 LTAAAGRGKLEVCELLLGRGAAVSRTNRRGVPPLFCAARQGHWQIVRLLLERGCDVNLSDKQGRTPLMVAACEGHlSTVE 1155
Cdd:PLN03192   529 LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKH-HKIF 607

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1156 FLLSKGAALSSLDKEGlSALSWACLKGHRAVVQYLVEEGAAIDQMDKNGRTPLDLAAFYGDAETVLYLVEKGAVIEHVD- 1234
Cdd:PLN03192   608 RILYHFASISDPHAAG-DLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANt 686


                   ....*...
gi 1622849900 1235 HSGMRPLD 1242
Cdd:PLN03192   687 DDDFSPTE 694
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 1289-1408 1.91e-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: 1.91e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1289 GNVMYKKGKMKEAAQRYQYALRKFPREgfgedmrpfnelrVSLYLNLSRCRRKTNDFGMAEEFASKALEMKPKSYEAFYA 1368
Cdd:COG4235     24 GRAYLRLGRYDEALAAYEKALRLDPDN-------------ADALLDLAEALLAAGDTEEAEELLERALALDPDNPEALYL 90

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1622849900 1369 RARAKRNSRQFVAALADLQEAVKLCPTNQEIKRLLARVEE 1408
Cdd:COG4235     91 LGLAAFQQGDYAEAIAAWQKLLALLPADAPARLLEASIAE 130
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 1073-1204 2.32e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 61.55  E-value: 2.32e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1073 ETALTAAAGRGKLEVCELLLGRGAAVSRT-NRRGVPPLFCAARQGHWQIVRLLLERGCDVNLSDKQGRTPLMVAACEGHL 1151
Cdd:PHA02875    69 ESELHDAVEEGDVKAVEELLDLGKFADDVfYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDI 148

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1622849900 1152 STVEFLLSKGAALSSLDKEGLSALSWACLKGHRAVVQYLVEEGAAIDQMDKNG 1204
Cdd:PHA02875   149 KGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNG 201
Ank_4 pfam13637
Ankyrin repeats (many copies);
1105-1158 2.76e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.59  E-value: 2.76e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1622849900 1105 GVPPLFCAARQGHWQIVRLLLERGCDVNLSDKQGRTPLMVAACEGHLSTVEFLL 1158
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 1278-1406 3.19e-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: 3.19e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1278 LIILLQKLMEEGNVMYKKGKMKEAAQRYQYALRKFPREgfgedmrpfnelrVSLYLNLSRCRRKTNDFGMAEEFASKALE 1357
Cdd:COG3914     74 LLLLAALLELAALLLQALGRYEEALALYRRALALNPDN-------------AEALFNLGNLLLALGRLEEALAALRRALA 140

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1622849900 1358 MKPKSYEAFYARARAKRNSRQFVAALADLQEAVKLCPTNQEIKRLLARV 1406
Cdd:COG3914    141 LNPDFAEAYLNLGEALRRLGRLEEAIAALRRALELDPDNAEALNNLGNA 189
PHA03095 PHA03095
ankyrin-like protein; Provisional
 885-1151 3.53e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 61.19  E-value: 3.53e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900  885 GYSTEGLSAALASLRNLYTpnVKVSRLLILGGANVNYRTEVLNNApilcVQSHLG----HEEVVTLLLEFGACLDGTSEN 960
Cdd:PHA03095    78 APERCGFTPLHLYLYNATT--LDVIKLLIKAGADVNAKDKVGRTP----LHVYLSgfniNPKVIRLLLRKGADVNALDLY 151

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900  961 GMTAL-CYAAAAG-HMKLVCLLTKKGARVDHLDKKGQCALVHsalrghgdILQYlltcewspgppqpgaLRKNhalqqal 1038
Cdd:PHA03095   152 GMTPLaVLLKSRNaNVELLRLLIDAGADVYAVDDRFRSLLHH--------HLQS---------------FKPR------- 201

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1039 taaasmghSSVVQCLLgmekEHEVEVNGTDTLwGETALTAAA--GRGKLEVCELLLGRGAAVSRTNRRGVPPLFCAARQG 1116
Cdd:PHA03095   202 --------ARIVRELI----RAGCDPAATDML-GNTPLHSMAtgSSCKRSLVLPLLIAGISINARNRYGQTPLHYAAVFN 268

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1622849900 1117 HWQIVRLLLERGCDVNLSDKQGRTPL--MVAACEGHL 1151
Cdd:PHA03095   269 NPRACRRLIALGADINAVSSDGNTPLslMVRNNNGRA 305
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 1300-1409 3.76e-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: 3.76e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1300 EAAQRYQYALRKFPREGFGedmrpfnelrvslYLNLSRCRRKTNDFGMAEEFASKALEMKPKSYEAFYARARAKRNSRQF 1379
Cdd:COG4235      1 EAIARLRQALAANPNDAEG-------------WLLLGRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDT 67

                           90       100       110
                   ....*....|....*....|....*....|
gi 1622849900 1380 VAALADLQEAVKLCPTNQEIKRLLARVEEE 1409
Cdd:COG4235     68 EEAEELLERALALDPDNPEALYLLGLAAFQ 97
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 1121-1204 6.48e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 61.07  E-value: 6.48e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1121 VRLLLERGCDVNLSDKQGRTPLMVAACEGHLSTVEFLLSKGAALSSLDKEGLSALSWACLKGHRAVVQYLVEEGAAIDQM 1200
Cdd:PTZ00322    98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFEL 177


                   ....
gi 1622849900 1201 DKNG 1204
Cdd:PTZ00322   178 GANA 181
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 1298-1406 6.67e-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: 56.89  E-value: 6.67e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1298 MKEAAQRYQYALRKFPREGFGEDMRPFNELRVSLYLNLSRCRRKTNDFGMAEEFASKALEMKPKSYEAFYARARAKRNSR 1377
Cdd:COG5010     23 LVEKYEAALAGANNTKEDELAAAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQALQLDPNNPELYYNLALLYSRSG 102

                           90       100
                   ....*....|....*....|....*....
gi 1622849900 1378 QFVAALADLQEAVKLCPTNQEIKRLLARV 1406
Cdd:COG5010    103 DKDEAKEYYEKALALSPDNPNAYSNLAAL 131
Ank_4 pfam13637
Ankyrin repeats (many copies);
1171-1224 1.01e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.05  E-value: 1.01e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1622849900 1171 GLSALSWACLKGHRAVVQYLVEEGAAIDQMDKNGRTPLDLAAFYGDAETVLYLV 1224
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
910-991 1.13e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 53.97  E-value: 1.13e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900  910 RLLILGGANVNYRTEVLNNAPILCVQShlGHEEVVTLLLEFgACLDGTsENGMTALCYAAAAGHMKLVCLLTKKGARVDH 989
Cdd:pfam12796   14 KLLLENGADANLQDKNGRTALHLAAKN--GHLEIVKLLLEH-ADVNLK-DNGRTALHYAARSGHLEIVKLLLEKGADINV 89


                   ..
gi 1622849900  990 LD 991
Cdd:pfam12796   90 KD 91
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
1253-1398 1.24e-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: 1.24e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1253 VVALLRKGAKLGNAAWAMATSKPDiliiLLQKLMEEGNVMYKKGKMKEAAQRYQYALRKFPRegfgedmrpfnelRVSLY 1332
Cdd:COG4785     48 LAAAALAAAALAAERIDRALALPD----LAQLYYERGVAYDSLGDYDLAIADFDQALELDPD-------------LAEAY 110

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622849900 1333 LNLSRCRRKTNDFGMAEEFASKALEMKPKSYEAFYARARAKRNSRQFVAALADLQEAVKLCPTNQE 1398
Cdd:COG4785    111 NNRGLAYLLLGDYDAALEDFDRALELDPDYAYAYLNRGIALYYLGRYELAIADLEKALELDPNDPE 176
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 1255-1394 1.42e-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: 1.42e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1255 ALLRKGAKLGNAAWAMATSKPDILIILLQKLMEEGNVMYKKGKMKEAAQRYQYALRKFPREGfgedmrpfnelrvSLYLN 1334
Cdd:COG5010     27 YEAALAGANNTKEDELAAAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQALQLDPNNP-------------ELYYN 93

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1335 LSRCRRKTNDFGMAEEFASKALEMKPKSYEAFYARARAKRNSRQFVAALADLQEAVKLCP 1394
Cdd:COG5010     94 LALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQRALGTSP 153
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 1279-1409 2.10e-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: 2.10e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1279 IILLQKLMEE-----------GNVMYKKGKMKEAAQRYQYALrkfpregfgeDMRPFNElrvSLYLNLSRCRRKTNDFGM 1347
Cdd:COG2956     62 IRIHQKLLERdpdraeallelAQDYLKAGLLDRAEELLEKLL----------ELDPDDA---EALRLLAEIYEQEGDWEK 128

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622849900 1348 AEEFASKALEMKPKSYEAFYARARAKRNSRQFVAALADLQEAVKLCPTNQEIKRLLARVEEE 1409
Cdd:COG2956    129 AIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAELYLE 190
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 1059-1211 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 1622849900 1059 EHEVEVNGTDTLWGETALTAAAGRGKLEVCELLLGRGAAVSRTNRRGVPPLFCAARQGHWQIVRLLLERGCDVNLSDKQG 1138
Cdd:PHA02878   155 SYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCG 234

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622849900 1139 RTPLMVAAceGHL---STVEFLLSKGA---ALSSLdkEGLSALSWAcLKGHRaVVQYLVEEGAAIDQMDKNGRTPLDLA 1211
Cdd:PHA02878   235 NTPLHISV--GYCkdyDILKLLLEHGVdvnAKSYI--LGLTALHSS-IKSER-KLKLLLEYGADINSLNSYKLTPLSSA 307
Ank_4 pfam13637
Ankyrin repeats (many copies);
1074-1125 2.52e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.89  E-value: 2.52e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1622849900 1074 TALTAAAGRGKLEVCELLLGRGAAVSRTNRRGVPPLFCAARQGHWQIVRLLL 1125
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
961-1014 3.04e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.51  E-value: 3.04e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1622849900  961 GMTALCYAAAAGHMKLVCLLTKKGARVDHLDKKGQCALVHSALRGHGDILQYLL 1014
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
514-815 3.86e-08

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 58.66  E-value: 3.86e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900  514 FVHSIAALLCRSHQLAAYR-DLLIKEPQLQSMLSLRSCVQDPVAAFKRGVLEPLTNLRNEQKIpeeeyIILIDGLNEAEF 592
Cdd:COG5635    196 LLRYLALELAERYLDAEDPiPILIELRDLAEEASLEDLLAEALEKRGGEPEDALERLLRNGRL-----LLLLDGLDEVPD 270

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900  593 hkPDYGDTLSSFITKIISKFPAwLKLIVTVRANFQEIISALPFVKLSLDDFpDNKDIHSDLHAYVQHRVHSSQDILSNIS 672
Cdd:COG5635    271 --EADRDEVLNQLRRFLERYPK-ARVIITSRPEGYDSSELEGFEVLELAPL-SDEQIEEFLKKWFEATERKAERLLEALE 346

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900  673 LNGKadatligkvsshlvLRSL-GSYLYLKLTLDLFQRGHlviksasykVVPVSLSELYLLQCNMkFMTQSAFERALPIL 751
Cdd:COG5635    347 ENPE--------------LRELaRNPLLLTLLALLLRERG---------ELPDTRAELYEQFVEL-LLERWDEQRGLTIY 402

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900  752 N-------------VALASLH----PMTDEQIFQAINAgHIQGEQGWEDFQQRMDALSCFLIKRRDKTRMFCHPSFREWL 814
Cdd:COG5635    403 RelsreelrellseLALAMQEngrtEFAREELEEILRE-YLGRRKDAEALLDELLLRTGLLVERGEGRYSFAHRSFQEYL 481


                   .
gi 1622849900  815 V 815
Cdd:COG5635    482 A 482
Ank_4 pfam13637
Ankyrin repeats (many copies);
930-980 4.32e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.12  E-value: 4.32e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1622849900  930 PILCVQSHLGHEEVVTLLLEFGACLDGTSENGMTALCYAAAAGHMKLVCLL 980
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
Ank_4 pfam13637
Ankyrin repeats (many copies);
1138-1191 4.41e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.12  E-value: 4.41e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1622849900 1138 GRTPLMVAACEGHLSTVEFLLSKGAALSSLDKEGLSALSWACLKGHRAVVQYLV 1191
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 1072-1191 9.58e-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: 9.58e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1072 GETALTAAAGRGKLEVCELLLGRGAAVS---------RTNRR-----GVPPLFCAARQGHWQIVRLLLERGCDVNLSDKQ 1137
Cdd:cd22192     89 GETALHIAVVNQNLNLVRELIARGADVVspratgtffRPGPKnliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSL 168

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622849900 1138 GRTPLMV--------AACEghlsTVEFLLS--KGAALSSLD----KEGLSALSWACLKGHRAVVQYLV 1191
Cdd:cd22192    169 GNTVLHIlvlqpnktFACQ----MYDLILSydKEDDLQPLDlvpnNQGLTPFKLAAKEGNIVMFQHLV 232
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 1083-1265 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 1622849900 1083 GKLEVCE-LLLGRGAAVSRTNRRGVPPLFCAARQGHWQIVRLLLERGCDVNLSDKQGRTPLMVAACEGHLSTVEFLLSKG 1161
Cdd:PHA02874    12 GDIEAIEkIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNG 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1162 AALSSL-----------------------DKEGLSALSWACLKGHRAVVQYLVEEGAAIDQMDKNGRTPLDLAAFYGDAE 1218
Cdd:PHA02874    92 VDTSILpipciekdmiktildcgidvnikDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFD 171

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1622849900 1219 TVLYLVEKGAVIEHVDHSGMRPLDRAIGCRNTSVVVALLRKGAKLGN 1265
Cdd:PHA02874   172 IIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMN 218
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 1289-1409 1.66e-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: 1.66e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1289 GNVMYKKGKMKEAAQRYQYALRKfpregfgedmrpfNELRVSLYLNLSRCRRKTNDFGMAEEFASKALEMKPKSYEAFYA 1368
Cdd:COG2956     49 GNLYRRRGEYDRAIRIHQKLLER-------------DPDRAEALLELAQDYLKAGLLDRAEELLEKLLELDPDDAEALRL 115

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1622849900 1369 RARAKRNSRQFVAALADLQEAVKLCPTNQEIKRLLARVEEE 1409
Cdd:COG2956    116 LAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLE 156
Ank_5 pfam13857
Ankyrin repeats (many copies);
1090-1145 3.46e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.50  E-value: 3.46e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622849900 1090 LLLGRGAAVSRTNRRGVPPLFCAARQGHWQIVRLLLERGCDVNLSDKQGRTPLMVA 1145
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
1332-1406 3.61e-07

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 53.47  E-value: 3.61e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622849900 1332 YLNLSRCRRKTNDFGMAEEFASKALEMKPKSYEAFYARARAKRNSRQFVAALADLQEAVKLCPTNQEIKRLLARV 1406
Cdd:COG0457     11 YNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNLGLA 85
PHA02946 PHA02946
ankyin-like protein; Provisional
 1089-1292 4.71e-07

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 54.29  E-value: 4.71e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1089 ELLLGRGAAVSRTNRRGVPPLFCAARQGHWQIVRLLLERGCDVNLSDKQGRTPL--MVAACEGHLSTVEFLLSKGAAL-S 1165
Cdd:PHA02946    56 EELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLyyLSGTDDEVIERINLLVQYGAKInN 135

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1166 SLDKEGLSALsWACLKGHRAVVQYLVEEGAAIDQMDKNGRTPL--DLAAFYGDAETVLYLVEKGAVIEHVDHSGMRPLDr 1243
Cdd:PHA02946   136 SVDEEGCGPL-LACTDPSERVFKKIMSIGFEARIVDKFGKNHIhrHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLH- 213

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1244 aIGC----RNTSVVVALL-----RKGAKLGNAAWAM--ATSKPDILIillQKLMEEGNVM 1292
Cdd:PHA02946   214 -IVCsktvKNVDIINLLLpstdvNKQNKFGDSPLTLliKTLSPAHLI---NKLLSTSNVI 269
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 1085-1171 4.90e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.90  E-value: 4.90e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1085 LEVCEL-----------LLGRGAAVSRTNRRGVPPLFCAARQGHWQIVRLLLERGCDVNLSDKQGRTPLMVAACEGHLST 1153
Cdd:PTZ00322    84 VELCQLaasgdavgariLLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREV 163

                           90
                   ....*....|....*...
gi 1622849900 1154 VEFLLSKGAALSSLDKEG 1171
Cdd:PTZ00322   164 VQLLSRHSQCHFELGANA 181
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 1328-1406 5.39e-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: 5.39e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622849900 1328 RVSLYLNLSRCRRKTNDFGMAEEFASKALEMKPKSYEAFYARARAKRNSRQFVAALADLQEAVKLCPTNQEIKRLLARV 1406
Cdd:COG4783      3 CAEALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLA 81
Ank_4 pfam13637
Ankyrin repeats (many copies);
1204-1257 8.43e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.65  E-value: 8.43e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1622849900 1204 GRTPLDLAAFYGDAETVLYLVEKGAVIEHVDHSGMRPLDRAIGCRNTSVVVALL 1257
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 1109-1261 9.21e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 54.10  E-value: 9.21e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1109 LFCAARQGHWQIVRLLLERGCDVNLSDKQGRTPLMVAACEGHLSTVEFLLSKGAALSSLDKEGLSALSWACLKGHRAVVQ 1188
Cdd:PLN03192   529 LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFR 608

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622849900 1189 YLVEEGAAIDQmdKNGRTPLDLAAFYGDAETVLYLVEKGAVIEHVDHSGMRPLDRAIGCRNTSVVVALLRKGA 1261
Cdd:PLN03192   609 ILYHFASISDP--HAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGA 679
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 1072-1261 9.91e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 53.46  E-value: 9.91e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1072 GETALTAAAGRGKLEVCELLLGRGAaVSRTNRRGV-PPLFCAARQGHWQIVRLLLERGCDVN-LSDKQGRTPLMVAACEG 1149
Cdd:PHA02875    35 GISPIKLAMKFRDSEAIKLLMKHGA-IPDVKYPDIeSELHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILK 113

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1150 HLSTVEFLLSKGA--ALSSLDKegLSALSWACLKGHRAVVQYLVEEGAAIDQMDKNGRTPLDLAAFYGDAETVLYLVEKG 1227
Cdd:PHA02875   114 KLDIMKLLIARGAdpDIPNTDK--FSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSG 191

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1622849900 1228 AVIEHVDHSG-MRPLDRAIGCRNTSVVVALLRKGA 1261
Cdd:PHA02875   192 ANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGA 226
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 903-1133 1.03e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 53.46  E-value: 1.03e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900  903 TPNVKVSRLLILGGANVNYrtEVLNNAPILCVQSHLGHEEVVTLLLEFGACLDGTSENGMTALCYAAAAGHMKLVCLLTK 982
Cdd:PHA02875    12 FGELDIARRLLDIGINPNF--EIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLD 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900  983 KGARVDH-LDKKGQCALVHSALRGHGDILQYLLTCEWSPGPPQPGALRKNHALQQaltaaasMGHSSVVQCLLgmekEHE 1061
Cdd:PHA02875    90 LGKFADDvFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVM-------MGDIKGIELLI----DHK 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622849900 1062 VEVNGTDTlWGETALTAAAGRGKLEVCELLLGRGAAVSRTNRRGVPPLFCAARQGHW-QIVRLLLERGCDVNL 1133
Cdd:PHA02875   159 ACLDIEDC-CGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKiDIVRLFIKRGADCNI 230
Ank_5 pfam13857
Ankyrin repeats (many copies);
1157-1211 1.52e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.96  E-value: 1.52e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622849900 1157 LLSKG-AALSSLDKEGLSALSWACLKGHRAVVQYLVEEGAAIDQMDKNGRTPLDLA 1211
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 1142-1223 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 1622849900 1142 LMVAACE----GHLSTVEFLLSKGAALSSLDKEGLSALSWACLKGHRAVVQYLVEEGAAIDQMDKNGRTPLDLAAFYGDA 1217
Cdd:PTZ00322    82 LTVELCQlaasGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFR 161


                   ....*.
gi 1622849900 1218 ETVLYL 1223
Cdd:PTZ00322   162 EVVQLL 167
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 942-1145 2.45e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 52.19  E-value: 2.45e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900  942 EVVTLLLEFGACLDGTSEN-GMTALCYAAAAGHMKLVCLLTKKGARVDHLDKKGQCALVHSALRGHGDILQYLLtcewsp 1020
Cdd:PHA02878   148 EITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILL------ 221

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1021 gppQPGAlrknhalqqaltaaaSMGHSSvvqcllgmekehevevngtdtLWGETALTAAAGRGK-LEVCELLLGRGAAVS 1099
Cdd:PHA02878   222 ---ENGA---------------STDARD---------------------KCGNTPLHISVGYCKdYDILKLLLEHGVDVN 262

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1622849900 1100 -RTNRRGVPPLFCAARQGhwQIVRLLLERGCDVNLSDKQGRTPLMVA 1145
Cdd:PHA02878   263 aKSYILGLTALHSSIKSE--RKLKLLLEYGADINSLNSYKLTPLSSA 307
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 1289-1374 2.69e-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: 2.69e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1289 GNVMYKKGKMKEAAQRYQYALRKFPREGFGEDMrpfnelrvslYLNLSRCRRKTNDFGMAEEFASKALEMKPKSYEAFYA 1368
Cdd:COG1729     37 GEAYYALGDYDEAAEAFEKLLKRYPDSPKAPDA----------LLKLGLSYLELGDYDKARATLEELIKKYPDSEAAKEA 106


                   ....*.
gi 1622849900 1369 RARAKR 1374
Cdd:COG1729    107 RARLAR 112
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 1293-1408 3.15e-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: 3.15e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1293 YKKGKMKEAAQRYQYALRKFPRegfgedmrpfNELRVSLYLNLSRCRRKTNDFGMAEEFASKALEMKPKSY---EAFYAR 1369
Cdd:COG1729      4 LKAGDYDEAIAAFKAFLKRYPN----------SPLAPDALYWLGEAYYALGDYDEAAEAFEKLLKRYPDSPkapDALLKL 73

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1622849900 1370 ARAKRNSRQFVAALADLQEAVKLCPTNQEIKRLLARVEE 1408
Cdd:COG1729     74 GLSYLELGDYDKARATLEELIKKYPDSEAAKEARARLAR 112
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 1043-1170 3.31e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 52.18  E-value: 3.31e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1043 SMGHSSVVQCLLgmekEHEVEVNGTDtLWGETALTAAAGRGKLEVCELLLgRGAAVSRTNRRGvpPLFC-AARQGHWQIV 1121
Cdd:PLN03192   567 SKGYEDCVLVLL----KHACNVHIRD-ANGNTALWNAISAKHHKIFRILY-HFASISDPHAAG--DLLCtAAKRNDLTAM 638

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1622849900 1122 RLLLERGCDVNLSDKQGRTPLMVAACEGHLSTVEFLLSKGAAL--SSLDKE 1170
Cdd:PLN03192   639 KELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVdkANTDDD 689
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
1338-1409 4.85e-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: 4.85e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622849900 1338 CRRKTNDFGMAEEFASKALEMKPKSYEAFYARARAKRNSRQFVAALAdLQEAVKLCPTNQEIKRLLARVEEE 1409
Cdd:COG3063      1 LYLKLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIA-LEKALKLDPNNAEALLNLAELLLE 71
Ank_5 pfam13857
Ankyrin repeats (many copies);
1124-1175 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 1622849900 1124 LLERG-CDVNLSDKQGRTPLMVAACEGHLSTVEFLLSKGAALSSLDKEGLSAL 1175
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
PHA02798 PHA02798
ankyrin-like protein; Provisional
 1120-1236 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 1622849900 1120 IVRLLLERGCDVNLSDKQGRTPLMVAACEGHLSTVEFLL---SKGAALSSLDKEGLSALSWACLKGHRA---VVQYLVEE 1193
Cdd:PHA02798    91 IVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLfmiENGADTTLLDKDGFTMLQVYLQSNHHIdieIIKLLLEK 170

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1622849900 1194 GAAIDQM-DKNGRTPLDLAAFYG----DAETVLYLVEKGAVIEHVDHS 1236
Cdd:PHA02798   171 GVDINTHnNKEKYDTLHCYFKYNidriDADILKLFVDNGFIINKENKS 218
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 1285-1411 1.92e-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: 1.92e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1285 LMEEGNVMYKKGKMKEAAQRYQYALRKFPREgfgedmrpfnelrVSLYLNLSRCRRKTNDFGMAEEFASKALEMKPKSYE 1364
Cdd:COG2956    147 YCELAELYLEQGDYDEAIEALEKALKLDPDC-------------ARALLLLAELYLEQGDYEEAIAALERALEQDPDYLP 213

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1622849900 1365 AFYARARAKRNSRQFVAALADLQEAVKLCPTNqEIKRLLARVEEECK 1411
Cdd:COG2956    214 ALPRLAELYEKLGDPEEALELLRKALELDPSD-DLLLALADLLERKE 259
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 1085-1213 2.25e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 47.51  E-value: 2.25e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1085 LEVCELLLGRGAAVS-RTNRRGVPPLfcaarqGHW---------QIVRLLLERGCDVNLSDKQGRTPLMV--AACEGHLS 1152
Cdd:PHA02859    66 VEILKFLIENGADVNfKTRDNNLSAL------HHYlsfnknvepEILKILIDSGSSITEEDEDGKNLLHMymCNFNVRIN 139

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622849900 1153 TVEFLLSKGAALSSLDKEGLSAL-SWACLKGHRAVVQYLVEEGAAIDQMDKNGRTPLDLAAF 1213
Cdd:PHA02859   140 VIKLLIDSGVSFLNKDFDNNNILySYILFHSDKKIFDFLTSLGIDINETNKSGYNCYDLIKF 201
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 1096-1226 2.36e-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: 2.36e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1096 AAVSRTNRRGVPPLFCAARQGHWQIVRLLLERGCDVNLSDKQ--------------GRTPLMVAACEGHLSTVEFLLSKG 1161
Cdd:cd22194    132 AEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGvffnpkykhegfyfGETPLALAACTNQPEIVQLLMEKE 211

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622849900 1162 AA-LSSLDKEG---LSALSWAC--LKGHRAVVQYLVE------EGAAIDQM-DKNGRTPLDLAAFYGDAETVLYLVEK 1226
Cdd:cd22194    212 STdITSQDSRGntvLHALVTVAedSKTQNDFVKRMYDmillksENKNLETIrNNEGLTPLQLAAKMGKAEILKYILSR 289
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 1072-1226 6.14e-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: 6.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1072 GETALTAAAGRGKLEVCELLLgrGAAVSRTNR-------RGVPPLFCAARQGHWQIVRLLLERGCDVN----------LS 1134
Cdd:cd22192     51 GETALHVAALYDNLEAAVVLM--EAAPELVNEpmtsdlyQGETALHIAVVNQNLNLVRELIARGADVVspratgtffrPG 128

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1135 DKQ----GRTPLMVAACEGHLSTVEFLLSKGAALSSLDKEGLSALSWACLKGHRAVVQYLVE---------EGAAIDQM- 1200
Cdd:cd22192    129 PKNliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTFACQMYDlilsydkedDLQPLDLVp 208

                          170       180
                   ....*....|....*....|....*.
gi 1622849900 1201 DKNGRTPLDLAAFYGDAETVLYLVEK 1226
Cdd:cd22192    209 NNQGLTPFKLAAKEGNIVMFQHLVQK 234
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 1137-1169 2.18e-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: 2.18e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1622849900 1137 QGRTPLMVAACE-GHLSTVEFLLSKGAALSSLDK 1169
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 1108-1136 2.51e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. 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: 2.51e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1622849900 1108 PLFCAA-RQGHWQIVRLLLERGCDVNLSDK 1136
Cdd:pfam00023    5 PLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 898-1142 2.58e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 46.01  E-value: 2.58e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900  898 LRNLYTPNVKVSRLLI--LGGANVNYRTEVLNNAPILCVQShLGHEEVVTLLLEFGACLDGTSENGMTALCYAAAAGHMK 975
Cdd:PLN03192   494 LKNFLQHHKELHDLNVgdLLGDNGGEHDDPNMASNLLTVAS-TGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYED 572

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900  976 LVCLLTKKGARVDHLDKKGQCALVHSALRGHGDILQYLLTCEWSPGPPQPGALrknhalqqaltaaasmghssvvqcllg 1055
Cdd:PLN03192   573 CVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAGDL--------------------------- 625

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1056 mekehevevngtdtlwgetaLTAAAGRGKLEVCELLLGRGAAVSRTNRRGVPPLFCAARQGHWQIVRLLLERGCDV---N 1132
Cdd:PLN03192   626 --------------------LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVdkaN 685

                          250
                   ....*....|
gi 1622849900 1133 LSDKQGRTPL 1142
Cdd:PLN03192   686 TDDDFSPTEL 695
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 1137-1162 3.55e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.49  E-value: 3.55e-04
                            10        20
                    ....*....|....*....|....*.
gi 1622849900  1137 QGRTPLMVAACEGHLSTVEFLLSKGA 1162
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
PHA02798 PHA02798
ankyrin-like protein; Provisional
 1084-1261 4.83e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 44.83  E-value: 4.83e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1084 KLEVCELLLGRGAAVSRTNRRGVPPLFCAARQGH---WQIVRLLLERGCDVNLSDKQGRTPLMVAACEGH---LSTVEFL 1157
Cdd:PHA02798    88 MLDIVKILIENGADINKKNSDGETPLYCLLSNGYinnLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLL 167

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1158 LSKGAALSSL-DKEGLSAL------SWACLKGHraVVQYLVEEGAAIDQMDKNGRTPL--DLAAFYGDA----ETVLYLV 1224
Cdd:PHA02798   168 LEKGVDINTHnNKEKYDTLhcyfkyNIDRIDAD--ILKLFVDNGFIINKENKSHKKKFmeYLNSLLYDNkrfkKNILDFI 245

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1622849900 1225 EKGAVIEHVDHSGMRPLDRAIGCRNTSVVVALLRKGA 1261
Cdd:PHA02798   246 FSYIDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGG 282
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 1104-1132 6.54e-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: 6.54e-04
                           10        20
                   ....*....|....*....|....*....
gi 1622849900 1104 RGVPPLFCAARQGHWQIVRLLLERGCDVN 1132
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 1072-1243 7.24e-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: 7.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1072 GETALTAAA---GRGKLEVCELLLGRGAAVSRTNRRGVPPLFCAARQGH-----------WQIVRLLLERGCDVNLS--- 1134
Cdd:cd21882     26 GKTCLHKAAlnlNDGVNEAIMLLLEAAPDSGNPKELVNAPCTDEFYQGQtalhiaienrnLNLVRLLVENGADVSARatg 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1135 ---DKQGRT-------PLMVAACEGHLSTVEFLLSKG---AALSSLDKEGLSALSWACLKGHRAVVQY---------LVE 1192
Cdd:cd21882    106 rffRKSPGNlfyfgelPLSLAACTNQEEIVRLLLENGaqpAALEAQDSLGNTVLHALVLQADNTPENSafvcqmynlLLS 185

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622849900 1193 EGAAIDQM-------DKNGRTPLDLAAFYGDAETVLYLVEKGAviehvdHSGMRPLDR 1243
Cdd:cd21882    186 YGAHLDPTqqleeipNHQGLTPLKLAAVEGKIVMFQHILQREF------SGPYQPLSR 237
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 1203-1231 1.14e-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: 1.14e-03
                            10        20
                    ....*....|....*....|....*....
gi 1622849900  1203 NGRTPLDLAAFYGDAETVLYLVEKGAVIE 1231
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 25-319 1.66e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 43.62  E-value: 1.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900   25 GPETSPVLPLDHGADSPVSSLPAAEDTYRVSLAKGVSMSLPSSPLLPRQSHLVQSRANKKSPGPVRKPKYVESPRVPG-D 103
Cdd:PHA03307   131 APDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRrS 210

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900  104 AVIMPFREVSKPTEPDEHEAKADNEPSCSPAAQELLTRLGFLLGEGIPSATHITieDKNETMCTALSQGISPCSTLTSST 183
Cdd:PHA03307   211 SPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPIT--LPTRIWEASGWNGPSSRPGPASSS 288

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900  184 ASPSTDSPCStlnscvSKTAANKSPCETISSPSSTLESKDSGIIATITSSSENDDRSGSSLEWNKDGSLRLGVQKGVL-- 261
Cdd:PHA03307   289 SSPRERSPSP------SPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPAdp 362

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622849900  262 -HDRRADNCSPVAEEETTGSAESTLPKAESSAGDGPVPySQGSSSLIMPRPNSVAATSS 319
Cdd:PHA03307   363 sSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARR-RDATGRFPAGRPRPSPLDAG 420
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 1187-1276 1.69e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 43.35  E-value: 1.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1187 VQYLVEEGAAIDQMDKNGRTPLDLAAFYGDAETVLYLVEKGAVIEHVDHSGMRPLDRAIGCRNTSVVVALLRKGAKLGNA 1266
Cdd:PTZ00322    98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFEL 177

                           90
                   ....*....|
gi 1622849900 1267 AwamATSKPD 1276
Cdd:PTZ00322   178 G---ANAKPD 184
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 1293-1405 1.77e-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: 1.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1293 YKKGKMKEAAQRYQYALRKFPREgfgedmrpfnelrVSLYLNLSRCRRKTNDFGMAEEFASKALEMKPKSYEAFYARARA 1372
Cdd:TIGR02917  510 IQEGNPDDAIQRFEKVLTIDPKN-------------LRAILALAGLYLRTGNEEEAVAWLEKAAELNPQEIEPALALAQY 576

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1622849900 1373 KRNSRQFVAALADLQEAVKLCPTNQEIKRLLAR 1405
Cdd:TIGR02917  577 YLGKGQLKKALAILNEAADAAPDSPEAWLMLGR 609
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 1295-1406 2.99e-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: 2.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1295 KGKMKEAAQRYQYALRKFPRegfgedmrpfnelRVSLYLNLSRCRRKTNDFGMAEEFASKALEMKPKSYEAFYARARAKR 1374
Cdd:COG2956     21 NGQPDKAIDLLEEALELDPE-------------TVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQDYL 87

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1622849900 1375 NSRQFVAALADLQEAVKLCPTNQEIKRLLARV 1406
Cdd:COG2956     88 KAGLLDRAEELLEKLLELDPDDAEALRLLAEI 119
TPR_14 pfam13428
Tetratricopeptide repeat;
1364-1406 3.00e-03

Tetratricopeptide repeat;


Pssm-ID: 463874 [Multi-domain]  Cd Length: 44  Bit Score: 37.02  E-value: 3.00e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1622849900 1364 EAFYARARAKRNSRQFVAALADLQEAVKLCPTNQEIKRLLARV 1406
Cdd:pfam13428    2 EALLALARALLALGDPDEALALLERALALDPDDPEAWLALAQL 44
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 1104-1133 3.02e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.80  E-value: 3.02e-03
                            10        20        30
                    ....*....|....*....|....*....|
gi 1622849900  1104 RGVPPLFCAARQGHWQIVRLLLERGCDVNL 1133
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 1108-1241 3.22e-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: 3.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1108 PLFCAARQGHWQ-IVRLLLERGCDVNLSDKQGRTPLMVAACEGHLSTVEFLLSKGAAL------SSLdKEGLSALSWACL 1180
Cdd:cd22192     20 PLLLAAKENDVQaIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELvnepmtSDL-YQGETALHIAVV 98

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622849900 1181 KGHRAVVQYLVEEGAAI--------------DQMDKNGRTPLDLAAFYGDAETVLYLVEKGAVIEHVDHSGMRPL 1241
Cdd:cd22192     99 NQNLNLVRELIARGADVvspratgtffrpgpKNLIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
TPR_12 pfam13424
Tetratricopeptide repeat;
1289-1361 4.70e-03

Tetratricopeptide repeat;


Pssm-ID: 315987 [Multi-domain]  Cd Length: 77  Bit Score: 37.75  E-value: 4.70e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622849900 1289 GNVMYKKGKMKEAAQRYQYALRKFpREGFGEDmrpfNELRVSLYLNLSRCRRKTNDFGMAEEFASKALEMKPK 1361
Cdd:pfam13424   10 AAVLRRLGRYDEALELLEKALEIA-RRLLGPD----HPLTATTLLNLGRLYLELGRYEEALELLERALALAEK 77
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 932-1016 6.21e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.42  E-value: 6.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900  932 LCVQSHLGHEEVVTLLLEFGACLDGTSENGMTALCYAAAAGHMKLVCLLTKKGARVDHLDKKGQCALVHSALRGHGDILQ 1011
Cdd:PTZ00322    86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165


                   ....*
gi 1622849900 1012 YLLTC 1016
Cdd:PTZ00322   166 LLSRH 170
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 1072-1155 8.10e-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: 8.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849900 1072 GETALTAAAGRGKLEVCELLLGRGAAVS-RTN-------------RRGVPPLFCAARQGHWQIVRLLLERGCDVNLSDKQ 1137
Cdd:TIGR00870  128 GITALHLAAHRQNYEIVKLLLERGASVPaRACgdffvksqgvdsfYHGESPLNAAACLGSPSIVALLSEDPADILTADSL 207

                           90
                   ....*....|....*...
gi 1622849900 1138 GRTPLmvaacegHLSTVE 1155
Cdd:TIGR00870  208 GNTLL-------HLLVME 218
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 960-992 9.73e-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: 9.73e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1622849900  960 NGMTALCYAAA-AGHMKLVCLLTKKGARVDHLDK 992
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 1203-1235 9.82e-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: 9.82e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1622849900 1203 NGRTPLDLAA-FYGDAETVLYLVEKGAVIEHVDH 1235
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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