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Conserved domains on  [gi|2024484393|ref|XP_040547812|]
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protein TANC2 isoform X3 [Gallus gallus]

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];
1075-1274 9.54e-55

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 193.63  E-value: 9.54e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1075 INSFDSLWGETALTAAAGRGKLDVCRLLLEQGAAVAQPNRRGVVPLFSAVRQGHWQIVDLLLTHGADVNMADKQGRTPLM 1154
Cdd:COG0666     46 ALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLH 125

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1155 MAASEGHLGTVEFLLAQGASISLMDKEGLTALSWACLKGHLAVVRALVENGAATDHADKNGRTPLDLAAFYGDAEVVQFL 1234
Cdd:COG0666    126 LAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 2024484393 1235 VDHGAMIEHVDYSGMRPLDRAVGCRNTSVVVTLLKKGAKI 1274
Cdd:COG0666    206 LEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADL 245
PHA03095 super family cl33707
ankyrin-like protein; Provisional
 905-1200 4.47e-20

ankyrin-like protein; Provisional


The actual alignment was detected with superfamily member PHA03095:

Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 95.86  E-value: 4.47e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393  905 RNLYTPNIKVS--RLLILGGANVNYRTEvLNNAPiLCVQSHLG---YTEMVALLLEFGANVDAASESGLTPLG-YAAAAG 978
Cdd:PHA03095    18 YLLNASNVTVEevRRLLAAGADVNFRGE-YGKTP-LHLYLHYSsekVKDIVRLLLEAGADVNAPERCGFTPLHlYLYNAT 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393  979 FLSIVVLLCKKRAKVDHLDKNGQCALvHAALRG---HLEVVKFLIQ-----CDWSMAGQQQ-GVFKKSHAIQQaliaaas 1049
Cdd:PHA03095    96 TLDVIKLLIKAGADVNAKDKVGRTPL-HVYLSGfniNPKVIRLLLRkgadvNALDLYGMTPlAVLLKSRNANV------- 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1050 mgytEIVSYLLDlpeKDEEEVERAqiNSFDSLWGETALTAaagRGKLDVCRLLLEQGAAVAQPNRRGVVPLFSAVRQGHW 1129
Cdd:PHA03095   168 ----ELLRLLID---AGADVYAVD--DRFRSLLHHHLQSF---KPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSC 235

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024484393 1130 Q--IVDLLLTHGADVNMADKQGRTPLMMAASEGHLGTVEFLLAQGASISLMDKEGLTALSWACLKGHLAVVRA 1200
Cdd:PHA03095   236 KrsLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRA 308
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
1310-1424 4.79e-13

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


:

Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 71.19  E-value: 4.79e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1310 GDMFYKKGKVKEAAQRYQYALKKFPREgfgedlktfrelkVSLLLNLSRCRRKMNDFGMAEEFATKALELKPKSYEAYYA 1389
Cdd:COG0457     15 GLAYRRLGRYEEAIEDYEKALELDPDD-------------AEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNN 81

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2024484393 1390 RARAKRSSRQFAAALEDLNEAIKLCPNNREIQRLL 1424
Cdd:COG0457     82 LGLALQALGRYEEALEDYDKALELDPDDAEALYNL 116
Herpes_BLLF1 super family cl37540
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 1541-1840 9.35e-06

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


The actual alignment was detected with superfamily member pfam05109:

Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 51.07  E-value: 9.35e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1541 STSPTLSPTH----QNSHYRPSPPH-----TSPAHQGSSYRF----SPPPVGS-QGKEYQSPPPSPLRRGPQYRA---SP 1603
Cdd:pfam05109  429 TTSPTLNTTGfaapNTTTGLPSSTHvptnlTAPASTGPTVSTadvtSPTPAGTtSGASPVTPSPSPRDNGTESKApdmTS 508

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1604 PADGMSVYRSQSGSPVryqqePSAVSPLPGRPKSPLSKMSQRSFQMPQLPVAV-PQQGLRLQPAKAQI--VRSNQPSSAV 1680
Cdd:pfam05109  509 PTSAVTTPTPNATSPT-----PAVTTPTPNATSPTLGKTSPTSAVTTPTPNATsPTPAVTTPTPNATIptLGKTSPTSAV 583

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1681 HSSTviPTGAYSQVAHSMASKYQAAAGEMGVNQSRLVyqgsiggivgdSRPVQHVQASLSAGaicQHG--GLAKEDLPQR 1758
Cdd:pfam05109  584 TTPT--PNATSPTVGETSPQANTTNHTLGGTSSTPVV-----------TSPPKNATSAVTTG---QHNitSSSTSSMSLR 647

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1759 PSSayrggmrysqtpqIGRSQSASYYPMCHSKLDLERSSLPSGQLGSPDVShlirrPISVNPSEIKPHPPTPRPLLHSQS 1838
Cdd:pfam05109  648 PSS-------------ISETLSPSTSDNSTSHMPLLTSAHPTGGENITQVT-----PASTSTHHVSTSSPAPRPGTTSQA 709


                   ..
gi 2024484393 1839 VG 1840
Cdd:pfam05109  710 SG 711
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1075-1274 9.54e-55

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 193.63  E-value: 9.54e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1075 INSFDSLWGETALTAAAGRGKLDVCRLLLEQGAAVAQPNRRGVVPLFSAVRQGHWQIVDLLLTHGADVNMADKQGRTPLM 1154
Cdd:COG0666     46 ALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLH 125

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1155 MAASEGHLGTVEFLLAQGASISLMDKEGLTALSWACLKGHLAVVRALVENGAATDHADKNGRTPLDLAAFYGDAEVVQFL 1234
Cdd:COG0666    126 LAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 2024484393 1235 VDHGAMIEHVDYSGMRPLDRAVGCRNTSVVVTLLKKGAKI 1274
Cdd:COG0666    206 LEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADL 245
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1153-1239 3.91e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.49  E-value: 3.91e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1153 LMMAASEGHLGTVEFLLAQGASISLMDKEGLTALSWACLKGHLAVVRALVENGAATDhaDKNGRTPLDLAAFYGDAEVVQ 1232
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVK 78


                   ....*..
gi 2024484393 1233 FLVDHGA 1239
Cdd:pfam12796   79 LLLEKGA 85
PHA03095 PHA03095
ankyrin-like protein; Provisional
 905-1200 4.47e-20

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 95.86  E-value: 4.47e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393  905 RNLYTPNIKVS--RLLILGGANVNYRTEvLNNAPiLCVQSHLG---YTEMVALLLEFGANVDAASESGLTPLG-YAAAAG 978
Cdd:PHA03095    18 YLLNASNVTVEevRRLLAAGADVNFRGE-YGKTP-LHLYLHYSsekVKDIVRLLLEAGADVNAPERCGFTPLHlYLYNAT 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393  979 FLSIVVLLCKKRAKVDHLDKNGQCALvHAALRG---HLEVVKFLIQ-----CDWSMAGQQQ-GVFKKSHAIQQaliaaas 1049
Cdd:PHA03095    96 TLDVIKLLIKAGADVNAKDKVGRTPL-HVYLSGfniNPKVIRLLLRkgadvNALDLYGMTPlAVLLKSRNANV------- 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1050 mgytEIVSYLLDlpeKDEEEVERAqiNSFDSLWGETALTAaagRGKLDVCRLLLEQGAAVAQPNRRGVVPLFSAVRQGHW 1129
Cdd:PHA03095   168 ----ELLRLLID---AGADVYAVD--DRFRSLLHHHLQSF---KPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSC 235

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024484393 1130 Q--IVDLLLTHGADVNMADKQGRTPLMMAASEGHLGTVEFLLAQGASISLMDKEGLTALSWACLKGHLAVVRA 1200
Cdd:PHA03095   236 KrsLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRA 308
PHA03095 PHA03095
ankyrin-like protein; Provisional
 1058-1278 8.35e-20

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 95.09  E-value: 8.35e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1058 YLLDLPEKDEEEVER-----AQINsFDSLWGETALTAAAGRGK---LDVCRLLLEQGAAVAQPNRRGVVPLFSAVRQGH- 1128
Cdd:PHA03095    18 YLLNASNVTVEEVRRllaagADVN-FRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATt 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1129 WQIVDLLLTHGADVNMADKQGRTPLMMAAS--EGHLGTVEFLLAQGASISLMDKEGLTALswACL--------------- 1191
Cdd:PHA03095    97 LDVIKLLIKAGADVNAKDKVGRTPLHVYLSgfNINPKVIRLLLRKGADVNALDLYGMTPL--AVLlksrnanvellrlli 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1192 -KG----------------HL-------AVVRALVENGAATDHADKNGRTPLDLAAFYGD--AEVVQFLVDHGAMIEHVD 1245
Cdd:PHA03095   175 dAGadvyavddrfrsllhhHLqsfkpraRIVRELIRAGCDPAATDMLGNTPLHSMATGSSckRSLVLPLLIAGISINARN 254

                          250       260       270
                   ....*....|....*....|....*....|...
gi 2024484393 1246 YSGMRPLDRAVGCRNTSVVVTLLKKGAKIGCQT 1278
Cdd:PHA03095   255 RYGQTPLHYAAVFNNPRACRRLIALGADINAVS 287
Ank_2 pfam12796
Ankyrin repeats (3 copies);
945-1023 4.33e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 69.76  E-value: 4.33e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024484393  945 GYTEMVALLLEFGANVDAASESGLTPLGYAAAAGFLSIVVLLCKKrAKVDHLDkNGQCALVHAALRGHLEVVKFLIQCD 1023
Cdd:pfam12796    8 GNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKLLLEKG 84
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
1310-1424 4.79e-13

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 71.19  E-value: 4.79e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1310 GDMFYKKGKVKEAAQRYQYALKKFPREgfgedlktfrelkVSLLLNLSRCRRKMNDFGMAEEFATKALELKPKSYEAYYA 1389
Cdd:COG0457     15 GLAYRRLGRYEEAIEDYEKALELDPDD-------------AEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNN 81

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2024484393 1390 RARAKRSSRQFAAALEDLNEAIKLCPNNREIQRLL 1424
Cdd:COG0457     82 LGLALQALGRYEEALEDYDKALELDPDDAEALYNL 116
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 1083-1204 2.72e-06

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 52.32  E-value: 2.72e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1083 GETALTAAAGRGKLDVCRLLLEQGAAVAQPNRRGVV--------------PLFSAVRQGHWQIVDLLLTHGADVNMADKQ 1148
Cdd:cd22192     89 GETALHIAVVNQNLNLVRELIARGADVVSPRATGTFfrpgpknliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSL 168

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024484393 1149 GRTPLMMAASEGHLGTV----EFLLAQGASISLM------DKEGLTALSWACLKGHLAVVRALVEN 1204
Cdd:cd22192    169 GNTVLHILVLQPNKTFAcqmyDLILSYDKEDDLQpldlvpNNQGLTPFKLAAKEGNIVMFQHLVQK 234
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 1541-1840 9.35e-06

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 51.07  E-value: 9.35e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1541 STSPTLSPTH----QNSHYRPSPPH-----TSPAHQGSSYRF----SPPPVGS-QGKEYQSPPPSPLRRGPQYRA---SP 1603
Cdd:pfam05109  429 TTSPTLNTTGfaapNTTTGLPSSTHvptnlTAPASTGPTVSTadvtSPTPAGTtSGASPVTPSPSPRDNGTESKApdmTS 508

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1604 PADGMSVYRSQSGSPVryqqePSAVSPLPGRPKSPLSKMSQRSFQMPQLPVAV-PQQGLRLQPAKAQI--VRSNQPSSAV 1680
Cdd:pfam05109  509 PTSAVTTPTPNATSPT-----PAVTTPTPNATSPTLGKTSPTSAVTTPTPNATsPTPAVTTPTPNATIptLGKTSPTSAV 583

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1681 HSSTviPTGAYSQVAHSMASKYQAAAGEMGVNQSRLVyqgsiggivgdSRPVQHVQASLSAGaicQHG--GLAKEDLPQR 1758
Cdd:pfam05109  584 TTPT--PNATSPTVGETSPQANTTNHTLGGTSSTPVV-----------TSPPKNATSAVTTG---QHNitSSSTSSMSLR 647

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1759 PSSayrggmrysqtpqIGRSQSASYYPMCHSKLDLERSSLPSGQLGSPDVShlirrPISVNPSEIKPHPPTPRPLLHSQS 1838
Cdd:pfam05109  648 PSS-------------ISETLSPSTSDNSTSHMPLLTSAHPTGGENITQVT-----PASTSTHHVSTSSPAPRPGTTSQA 709


                   ..
gi 2024484393 1839 VG 1840
Cdd:pfam05109  710 SG 711
PHA03247 PHA03247
large tegument protein UL36; Provisional
 1557-1714 1.95e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 50.32  E-value: 1.95e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1557 PSPPHTSPAHQGSSyRFSPPPVgSQGKEYQSPPPSPLRRGPQYRASPPAdgmsvyrsQSGSPVRYQQEPSAVSPLPGRPK 1636
Cdd:PHA03247  2871 PAAKPAAPARPPVR-RLARPAV-SRSTESFALPPDQPERPPQPQAPPPP--------QPQPQPPPPPQPQPPPPPPPRPQ 2940

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1637 SPLSKMSQRSFQMPQLPVAVPQQGLRLQPAKAQIVRSNQPSSA---------VHSSTVIPTGAYSQVAHSMASKYQAAAG 1707
Cdd:PHA03247  2941 PPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPApsreapassTPPLTGHSLSRVSSWASSLALHEETDPP 3020


                   ....*..
gi 2024484393 1708 EMGVNQS 1714
Cdd:PHA03247  3021 PVSLKQT 3027
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 1065-1242 3.41e-05

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 48.92  E-value: 3.41e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1065 KDEEEVERAQINSFDSLWGETALTAAAGRGKLDVCRLLLEQgaavaqpNRRGVV--PLFSAVRQGHWQIVDLLLTHGADV 1142
Cdd:TIGR00870   35 RDLEEPKKLNINCPDRLGRSALFVAAIENENLELTELLLNL-------SCRGAVgdTLLHAISLEYVDAVEAILLHLLAA 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1143 nmADKQGRTPLMMAASeghlgTVEFllaqgasislmdKEGLTALSWACLKGHLAVVRALVENGAA------------TDH 1210
Cdd:TIGR00870  108 --FRKSGPLELANDQY-----TSEF------------TPGITALHLAAHRQNYEIVKLLLERGASvparacgdffvkSQG 168

                          170       180       190
                   ....*....|....*....|....*....|....
gi 2024484393 1211 AD--KNGRTPLDLAAFYGDAEVVQFLVDHGAMIE 1242
Cdd:TIGR00870  169 VDsfYHGESPLNAAACLGSPSIVALLSEDPADIL 202
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 1311-1426 6.27e-05

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: 48.16  E-value: 6.27e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1311 DMFYKKGKVKEAAQRYQYALKKFPREgfgedlktfrelkVSLLLNLSRCRRKMNDFGMAEEFATKALELKPKSYEAYYAR 1390
Cdd:TIGR02917  507 RIDIQEGNPDDAIQRFEKVLTIDPKN-------------LRAILALAGLYLRTGNEEEAVAWLEKAAELNPQEIEPALAL 573

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2024484393 1391 ARAKRSSRQFAAALEDLNEAIKLCPNNREIQRLLLR 1426
Cdd:TIGR02917  574 AQYYLGKGQLKKALAILNEAADAAPDSPEAWLMLGR 609
TPR_14 pfam13428
Tetratricopeptide repeat;
1385-1427 1.40e-04

Tetratricopeptide repeat;


Pssm-ID: 463874 [Multi-domain]  Cd Length: 44  Bit Score: 41.25  E-value: 1.40e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 2024484393 1385 EAYYARARAKRSSRQFAAALEDLNEAIKLCPNNREIQRLLLRV 1427
Cdd:pfam13428    2 EALLALARALLALGDPDEALALLERALALDPDDPEAWLALAQL 44
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 1214-1242 1.44e-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: 40.65  E-value: 1.44e-04
                            10        20
                    ....*....|....*....|....*....
gi 2024484393  1214 NGRTPLDLAAFYGDAEVVQFLVDHGAMIE 1242
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
PLN03088 PLN03088
SGT1, suppressor of G2 allele of SKP1; Provisional
 1364-1415 2.21e-03

SGT1, suppressor of G2 allele of SKP1; Provisional


Pssm-ID: 215568 [Multi-domain]  Cd Length: 356  Bit Score: 42.47  E-value: 2.21e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2024484393 1364 NDFGMAEEFATKALELKPKSYEAYYARARAKRSSRQFAAALEDLNEAIKLCP 1415
Cdd:PLN03088    16 DDFALAVDLYTQAIDLDPNNAELYADRAQANIKLGNFTEAVADANKAIELDP 67
TPR smart00028
Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum ...
 1384-1417 5.46e-03

Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum of 34 amino acids each and self-associate via a "knobs and holes" mechanism.


Pssm-ID: 197478 [Multi-domain]  Cd Length: 34  Bit Score: 36.27  E-value: 5.46e-03
                            10        20        30
                    ....*....|....*....|....*....|....
gi 2024484393  1384 YEAYYARARAKRSSRQFAAALEDLNEAIKLCPNN 1417
Cdd:smart00028    1 AEALYNLGNAYLKLGDYDEALEYYEKALELDPNN 34
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1075-1274 9.54e-55

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 193.63  E-value: 9.54e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1075 INSFDSLWGETALTAAAGRGKLDVCRLLLEQGAAVAQPNRRGVVPLFSAVRQGHWQIVDLLLTHGADVNMADKQGRTPLM 1154
Cdd:COG0666     46 ALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLH 125

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1155 MAASEGHLGTVEFLLAQGASISLMDKEGLTALSWACLKGHLAVVRALVENGAATDHADKNGRTPLDLAAFYGDAEVVQFL 1234
Cdd:COG0666    126 LAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 2024484393 1235 VDHGAMIEHVDYSGMRPLDRAVGCRNTSVVVTLLKKGAKI 1274
Cdd:COG0666    206 LEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADL 245
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1083-1274 1.74e-53

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 189.78  E-value: 1.74e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1083 GETALTAAAGRGKLDVCRLLLEQGAAVAQPNRRGVVPLFSAVRQGHWQIVDLLLTHGADVNMADKQGRTPLMMAASEGHL 1162
Cdd:COG0666     87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1163 GTVEFLLAQGASISLMDKEGLTALSWACLKGHLAVVRALVENGAATDHADKNGRTPLDLAAFYGDAEVVQFLVDHGAMIE 1242
Cdd:COG0666    167 EIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN 246

                          170       180       190
                   ....*....|....*....|....*....|..
gi 2024484393 1243 HVDYSGMRPLDRAVGCRNTSVVVTLLKKGAKI 1274
Cdd:COG0666    247 AKDKDGLTALLLAAAAGAALIVKLLLLALLLL 278
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
932-1252 2.76e-49

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 177.84  E-value: 2.76e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393  932 LNNAPILCVQSHLGYTEMVALLLEFGANVDAASESGLTPLGYAAAAGFLSIVVLLCKKRAKVDHLDKNGQCALVHAALRG 1011
Cdd:COG0666     19 LLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNG 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1012 HLEVVKFLIQcdwsmAGqqqgvfkkshaiqqaliaaasmgyteivsylldlpekdeeeverAQINSFDSlWGETALTAAA 1091
Cdd:COG0666     99 DLEIVKLLLE-----AG--------------------------------------------ADVNARDK-DGETPLHLAA 128

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1092 GRGKLDVCRLLLEQGAAVAQPNRRGVVPLFSAVRQGHWQIVDLLLTHGADVNMADKQGRTPLMMAASEGHLGTVEFLLAQ 1171
Cdd:COG0666    129 YNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA 208

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1172 GASISLMDKEGLTALSWACLKGHLAVVRALVENGAATDHADKNGRTPLDLAAFYGDAEVVQFLVDHGAMIEHVDYSGMRP 1251
Cdd:COG0666    209 GADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288


                   .
gi 2024484393 1252 L 1252
Cdd:COG0666    289 L 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
900-1219 6.71e-46

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 167.82  E-value: 6.71e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393  900 ALASLRNLYTPNIKVSRLLILGGANVNYRTEVLNNAPILCVQSHLGYTEMVALLLEFGANVDAASESGLTPLGYAAAAGF 979
Cdd:COG0666     20 LLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGD 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393  980 LSIVVLLCKKRAKVDHLDKNGQCALVHAALRGHLEVVKFLIQcdwsmAGqqqgvfkkshaiqqaliaaasmgyteivsyl 1059
Cdd:COG0666    100 LEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLE-----AG------------------------------- 143

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1060 ldlpekdeeeverAQINSFDSlWGETALTAAAGRGKLDVCRLLLEQGAAVAQPNRRGVVPLFSAVRQGHWQIVDLLLTHG 1139
Cdd:COG0666    144 -------------ADVNAQDN-DGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAG 209

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1140 ADVNMADKQGRTPLMMAASEGHLGTVEFLLAQGASISLMDKEGLTALSWACLKGHLAVVRALVENGAATDHADKNGRTPL 1219
Cdd:COG0666    210 ADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1153-1239 3.91e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.49  E-value: 3.91e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1153 LMMAASEGHLGTVEFLLAQGASISLMDKEGLTALSWACLKGHLAVVRALVENGAATDhaDKNGRTPLDLAAFYGDAEVVQ 1232
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVK 78


                   ....*..
gi 2024484393 1233 FLVDHGA 1239
Cdd:pfam12796   79 LLLEKGA 85
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1120-1206 1.27e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 88.25  E-value: 1.27e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1120 LFSAVRQGHWQIVDLLLTHGADVNMADKQGRTPLMMAASEGHLGTVEFLLAQGAsiSLMDKEGLTALSWACLKGHLAVVR 1199
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVK 78


                   ....*..
gi 2024484393 1200 ALVENGA 1206
Cdd:pfam12796   79 LLLEKGA 85
PHA03095 PHA03095
ankyrin-like protein; Provisional
 905-1200 4.47e-20

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 95.86  E-value: 4.47e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393  905 RNLYTPNIKVS--RLLILGGANVNYRTEvLNNAPiLCVQSHLG---YTEMVALLLEFGANVDAASESGLTPLG-YAAAAG 978
Cdd:PHA03095    18 YLLNASNVTVEevRRLLAAGADVNFRGE-YGKTP-LHLYLHYSsekVKDIVRLLLEAGADVNAPERCGFTPLHlYLYNAT 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393  979 FLSIVVLLCKKRAKVDHLDKNGQCALvHAALRG---HLEVVKFLIQ-----CDWSMAGQQQ-GVFKKSHAIQQaliaaas 1049
Cdd:PHA03095    96 TLDVIKLLIKAGADVNAKDKVGRTPL-HVYLSGfniNPKVIRLLLRkgadvNALDLYGMTPlAVLLKSRNANV------- 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1050 mgytEIVSYLLDlpeKDEEEVERAqiNSFDSLWGETALTAaagRGKLDVCRLLLEQGAAVAQPNRRGVVPLFSAVRQGHW 1129
Cdd:PHA03095   168 ----ELLRLLID---AGADVYAVD--DRFRSLLHHHLQSF---KPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSC 235

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024484393 1130 Q--IVDLLLTHGADVNMADKQGRTPLMMAASEGHLGTVEFLLAQGASISLMDKEGLTALSWACLKGHLAVVRA 1200
Cdd:PHA03095   236 KrsLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRA 308
PHA03095 PHA03095
ankyrin-like protein; Provisional
 1058-1278 8.35e-20

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 95.09  E-value: 8.35e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1058 YLLDLPEKDEEEVER-----AQINsFDSLWGETALTAAAGRGK---LDVCRLLLEQGAAVAQPNRRGVVPLFSAVRQGH- 1128
Cdd:PHA03095    18 YLLNASNVTVEEVRRllaagADVN-FRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATt 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1129 WQIVDLLLTHGADVNMADKQGRTPLMMAAS--EGHLGTVEFLLAQGASISLMDKEGLTALswACL--------------- 1191
Cdd:PHA03095    97 LDVIKLLIKAGADVNAKDKVGRTPLHVYLSgfNINPKVIRLLLRKGADVNALDLYGMTPL--AVLlksrnanvellrlli 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1192 -KG----------------HL-------AVVRALVENGAATDHADKNGRTPLDLAAFYGD--AEVVQFLVDHGAMIEHVD 1245
Cdd:PHA03095   175 dAGadvyavddrfrsllhhHLqsfkpraRIVRELIRAGCDPAATDMLGNTPLHSMATGSSckRSLVLPLLIAGISINARN 254

                          250       260       270
                   ....*....|....*....|....*....|...
gi 2024484393 1246 YSGMRPLDRAVGCRNTSVVVTLLKKGAKIGCQT 1278
Cdd:PHA03095   255 RYGQTPLHYAAVFNNPRACRRLIALGADINAVS 287
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1087-1179 9.39e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 82.86  E-value: 9.39e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1087 LTAAAGRGKLDVCRLLLEQGAAVAQPNRRGVVPLFSAVRQGHWQIVDLLLTHgADVNMADkQGRTPLMMAASEGHLGTVE 1166
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 2024484393 1167 FLLAQGASISLMD 1179
Cdd:pfam12796   79 LLLEKGADINVKD 91
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 1084-1305 1.31e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 90.82  E-value: 1.31e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1084 ETALTAAAGRGKLDVCRLLLEQGAavaQPN---RRGVVPLFSAVRQGHWQIVDLLLTHGADVNMADKQGRTPLMMAASEG 1160
Cdd:PHA02875     3 QVALCDAILFGELDIARRLLDIGI---NPNfeiYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEG 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1161 HLGTVEFLLAQGASIS-LMDKEGLTALSWACLKGHLAVVRALVENGAATDHADKNGRTPLDLAAFYGDAEVVQFLVDHGA 1239
Cdd:PHA02875    80 DVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKA 159

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024484393 1240 MIEHVDYSGMRPLDRAVGCRNTSVVVTLLKKGAKI------GCQTLpsrprgpATWAMATSKPDIMIILLSK 1305
Cdd:PHA02875   160 CLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIdyfgknGCVAA-------LCYAIENNKIDIVRLFIKR 224
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 965-1255 3.10e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 86.56  E-value: 3.10e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393  965 ESGLTPLGYAAAAGFLSIVVLLCKKRAKVDHLDKNGQCALVHAALRGHLEVVKFLIQcdwsmagqqQGVfkkshaiqqal 1044
Cdd:PHA02874    33 DETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLID---------NGV----------- 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1045 iaaasmgyteiVSYLLDLPEKDEEEVER-----AQINSFDSLwGETALTAAAGRGKLDVCRLLLEQGAAVAQPNRRGVVP 1119
Cdd:PHA02874    93 -----------DTSILPIPCIEKDMIKTildcgIDVNIKDAE-LKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYP 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1120 LFSAVRQGHWQIVDLLLTHGADVNMADKQGRTPLMMAASEGHLGTVEFLLAQGASISLMDKEGLTALSWACLKGHLAVvr 1199
Cdd:PHA02874   161 IHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAI-- 238

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2024484393 1200 ALVENGAATDHADKNGRTPLDLAAFYG-DAEVVQFLVDHGAMIEHVDYSGMRPLDRA 1255
Cdd:PHA02874   239 ELLINNASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTA 295
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 1095-1274 7.41e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 85.49  E-value: 7.41e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1095 KLDVCRLLLEQGAAVAQPNRRGVVPLFSAVRQGHWQ-----IVDLLLTHGADVNMADKQGRTPLMMAASE--GHLGTVEF 1167
Cdd:PHA03100    47 NIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLtdvkeIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEY 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1168 LLAQGASISLMDKEGLTALSWA--CLKGHLAVVRALVENGA----------------ATDHADKNGRTPLDLAAFYGDAE 1229
Cdd:PHA03100   127 LLDNGANVNIKNSDGENLLHLYleSNKIDLKILKLLIDKGVdinaknrvnyllsygvPINIKDVYGFTPLHYAVYNNNPE 206

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 2024484393 1230 VVQFLVDHGAMIEHVDYSGMRPLDRAVGCRNTSVVVTLLKKGAKI 1274
Cdd:PHA03100   207 FVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSI 251
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 1085-1268 1.22e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 85.02  E-value: 1.22e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1085 TALTAAAGRGKLDVCRLLLEQGAAVAQPNRRGVVPLFSAVRQGHWQIVDLLLTHGAD----------------------- 1141
Cdd:PHA02874    37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDtsilpipciekdmiktildcgid 116

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1142 VNMADKQGRTPLMMAASEGHLGTVEFLLAQGASISLMDKEGLTALSWACLKGHLAVVRALVENGAATDHADKNGRTPLDL 1221
Cdd:PHA02874   117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHN 196

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 2024484393 1222 AAFYGDAEVVQFLVDHGAMIEHVDYSGMRPLDRAVgCRNTSVVVTLL 1268
Cdd:PHA02874   197 AAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI-IHNRSAIELLI 242
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 981-1214 2.51e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 83.95  E-value: 2.51e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393  981 SIVVLLCKKRAKVDHLDKNGQCALVHAALRGH-----LEVVKFLIQcdwsmAGQQQGVFKKSHAIQQALIAAASMGYTEI 1055
Cdd:PHA03100    49 DVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLE-----YGANVNAPDNNGITPLLYAISKKSNSYSI 123

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1056 VSYLLDLpekdeeeveRAQINSFDSlWGETALTAAA--GRGKLDVCRLLLEQGAAVAQPNRrgvvplfsavrqghwqiVD 1133
Cdd:PHA03100   124 VEYLLDN---------GANVNIKNS-DGENLLHLYLesNKIDLKILKLLIDKGVDINAKNR-----------------VN 176

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1134 LLLTHGADVNMADKQGRTPLMMAASEGHLGTVEFLLAQGASISLMDKEGLTALSWACLKGHLAVVRALVENGAATDHADK 1213
Cdd:PHA03100   177 YLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256


                   .
gi 2024484393 1214 N 1214
Cdd:PHA03100   257 T 257
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 912-1274 3.12e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 84.73  E-value: 3.12e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393  912 IKVSRLLILGGANVNYRtEVLNNAPILCVQSHlGYTEMVALLLEFGANVDAASESGLTPLGYAAAAGFLSIVVLLCKKRA 991
Cdd:PHA02876   158 LLIAEMLLEGGADVNAK-DIYCITPIHYAAER-GNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRS 235

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393  992 KVDHLDkngqCALVHAALRGHLEVVKFLIQCDWSMagQQQGVFKKSHAIQQALIAAASmgytEIVSYLLdlpekdeeevE 1071
Cdd:PHA02876   236 NINKND----LSLLKAIRNEDLETSLLLYDAGFSV--NSIDDCKNTPLHHASQAPSLS----RLVPKLL----------E 295

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1072 RAQINSFDSLWGETALTAAAGRG-KLDVCRLLLEQGAAVAQPNRRGVVPLFSAVRQGHWQ-IVDLLLTHGADVNMADKQG 1149
Cdd:PHA02876   296 RGADVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKdIVITLLELGANVNARDYCD 375

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1150 RTPLMMAASEGHLGTVEFLLAQGASISLMDKEGLTALSWA-CLKGHLAVVRALVENGAATDHADKNGRTPLDLAAFYG-D 1227
Cdd:PHA02876   376 KTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcK 455

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*..
gi 2024484393 1228 AEVVQFLVDHGAMIEHVDYSGMRPLDRAVGCRntSVVVTLLKKGAKI 1274
Cdd:PHA02876   456 LDVIEMLLDNGADVNAINIQNQYPLLIALEYH--GIVNILLHYGAEL 500
Ank_2 pfam12796
Ankyrin repeats (3 copies);
945-1023 4.33e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 69.76  E-value: 4.33e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024484393  945 GYTEMVALLLEFGANVDAASESGLTPLGYAAAAGFLSIVVLLCKKrAKVDHLDkNGQCALVHAALRGHLEVVKFLIQCD 1023
Cdd:pfam12796    8 GNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKLLLEKG 84
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1051-1146 2.04e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.83  E-value: 2.04e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1051 GYTEIVSYLLDlpekdeeevERAQINSFDSlWGETALTAAAGRGKLDVCRLLLEQGAAVAQPNrrGVVPLFSAVRQGHWQ 1130
Cdd:pfam12796    8 GNLELVKLLLE---------NGADANLQDK-NGRTALHLAAKNGHLEIVKLLLEHADVNLKDN--GRTALHYAARSGHLE 75

                           90
                   ....*....|....*.
gi 2024484393 1131 IVDLLLTHGADVNMAD 1146
Cdd:pfam12796   76 IVKLLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 1117-1274 2.55e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 74.61  E-value: 2.55e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1117 VVPLFSAVRQGHWQIVDLLLTHGADVNMADKQGRTPLMMAASEGHLGTVEFLLAQGASISLM------------------ 1178
Cdd:PHA02874    36 TTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSILpipciekdmiktildcgi 115

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1179 -----DKEGLTALSWACLKGHLAVVRALVENGAATDHADKNGRTPLDLAAFYGDAEVVQFLVDHGAMIEHVDYSGMRPLD 1253
Cdd:PHA02874   116 dvnikDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLH 195

                          170       180
                   ....*....|....*....|.
gi 2024484393 1254 RAVGCRNTSVVVTLLKKGAKI 1274
Cdd:PHA02874   196 NAAEYGDYACIKLLIDHGNHI 216
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
1310-1424 4.79e-13

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 71.19  E-value: 4.79e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1310 GDMFYKKGKVKEAAQRYQYALKKFPREgfgedlktfrelkVSLLLNLSRCRRKMNDFGMAEEFATKALELKPKSYEAYYA 1389
Cdd:COG0457     15 GLAYRRLGRYEEAIEDYEKALELDPDD-------------AEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNN 81

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2024484393 1390 RARAKRSSRQFAAALEDLNEAIKLCPNNREIQRLL 1424
Cdd:COG0457     82 LGLALQALGRYEEALEDYDKALELDPDDAEALYNL 116
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 1051-1272 8.43e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 72.72  E-value: 8.43e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1051 GYTEIVSYLLDLpekdeeeveraQIN-SFDSLWGETALTAAAGRGKLDVCRLLLEQGAA--VAQPNRRGvvPLFSAVRQG 1127
Cdd:PHA02875    13 GELDIARRLLDI-----------GINpNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIpdVKYPDIES--ELHDAVEEG 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1128 HWQIVDLLLTHGADVN-MADKQGRTPLMMAASEGHLGTVEFLLAQGASISLMDKEGLTALSWACLKGHLAVVRALVENGA 1206
Cdd:PHA02875    80 DVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKA 159

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1207 ATDHADKNGRTPLDLAAFYGDAEVVQFLVDHGAmieHVDYSGMRP----LDRAVGCRNTSVVVTLLKKGA 1272
Cdd:PHA02875   160 CLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGA---NIDYFGKNGcvaaLCYAIENNKIDIVRLFIKRGA 226
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
1310-1424 2.98e-12

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 68.88  E-value: 2.98e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1310 GDMFYKKGKVKEAAQRYQYALKKFPREgfgedlktfrelkVSLLLNLSRCRRKMNDFGMAEEFATKALELKPKSYEAYYA 1389
Cdd:COG0457     49 GLAYLRLGRYEEALADYEQALELDPDD-------------AEALNNLGLALQALGRYEEALEDYDKALELDPDDAEALYN 115

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2024484393 1390 RARAKRSSRQFAAALEDLNEAIKLCPNNREIQRLL 1424
Cdd:COG0457    116 LGLALLELGRYDEAIEAYERALELDPDDADALYNL 150
Ank_2 pfam12796
Ankyrin repeats (3 copies);
971-1107 6.62e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 63.21  E-value: 6.62e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393  971 LGYAAAAGFLSIVVLLCKKRAKVDHLDKNGQCALVHAALRGHLEVVKFLIqcdwsmagqqqgvfkkshaiqqaliaaasm 1050
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL------------------------------ 50

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2024484393 1051 gyteivsylldlpekdeeevERAQINSFDSlwGETALTAAAGRGKLDVCRLLLEQGA 1107
Cdd:pfam12796   51 --------------------EHADVNLKDN--GRTALHYAARSGHLEIVKLLLEKGA 85
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 1096-1245 7.26e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 69.69  E-value: 7.26e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1096 LDVCRLLLEQGAAVAQPNRRGVVPLFSAV--RQGHWQIVDLLLTHGADVNMADKQGRTPLMMAASEGHLGT--------- 1164
Cdd:PHA03100    86 KEIVKLLLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLkilkllidk 165

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1165 ---------VEFLLAQGASISLMDKEGLTALSWACLKGHLAVVRALVENGAATDHADKNGRTPLDLAAFYGDAEVVQFLV 1235
Cdd:PHA03100   166 gvdinaknrVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLL 245

                          170
                   ....*....|
gi 2024484393 1236 DHGAMIEHVD 1245
Cdd:PHA03100   246 NNGPSIKTII 255
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 1130-1256 9.32e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 69.91  E-value: 9.32e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1130 QIVDLLLTHGADVNMADK-QGRTPLMMAASEGHLGTVEFLLAQGASISLMDKEGLTALSWACLKGHLAVVRALVENGAAT 1208
Cdd:PHA02878   148 EITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAST 227

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1209 DHADKNGRTPLDLAAFY---------------------------------GDAEVVQFLVDHGAMIEHVDYSGMRPLDRA 1255
Cdd:PHA02878   228 DARDKCGNTPLHISVGYckdydilklllehgvdvnaksyilgltalhssiKSERKLKLLLEYGADINSLNSYKLTPLSSA 307


                   .
gi 2024484393 1256 V 1256
Cdd:PHA02878   308 V 308
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 1096-1279 9.69e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 70.28  E-value: 9.69e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1096 LDVCRLLLEQGAAVAQPNRRGvvPLFSAVRQGHWQIVDLLLTHGADVNMADKQGRTPLMMAASEGHLGTVEFLLAQGASI 1175
Cdd:PLN03192   507 LNVGDLLGDNGGEHDDPNMAS--NLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNV 584

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1176 SLMDKEGLTALSWACLKGHLAVVRALVENGAATD-HAdknGRTPLDLAAFYGDAEVVQFLVDHGAMIEHVDYSGMRPLDR 1254
Cdd:PLN03192   585 HIRDANGNTALWNAISAKHHKIFRILYHFASISDpHA---AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQV 661

                          170       180
                   ....*....|....*....|....*
gi 2024484393 1255 AVGCRNTSVVVTLLKKGAKIGCQTL 1279
Cdd:PLN03192   662 AMAEDHVDMVRLLIMNGADVDKANT 686
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 1310-1417 1.36e-11

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: 64.06  E-value: 1.36e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1310 GDMFYKKGKVKEAAQRYQYALKKFPREgfgedlktfrelkVSLLLNLSRCRRKMNDFGMAEEFATKALELKPKSYEAYYA 1389
Cdd:COG4783     45 GEILLQLGDLDEAIVLLHEALELDPDE-------------PEARLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLR 111

                           90       100
                   ....*....|....*....|....*...
gi 2024484393 1390 RARAKRSSRQFAAALEDLNEAIKLCPNN 1417
Cdd:COG4783    112 LARAYRALGRPDEAIAALEKALELDPDD 139
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
1313-1419 1.71e-11

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 62.11  E-value: 1.71e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1313 FYKKGKVKEAAQRYQYALKKFPREGfgedlktfrelkvSLLLNLSRCRRKMNDFGMAEEFaTKALELKPKSYEAYYARAR 1392
Cdd:COG3063      2 YLKLGDLEEAEEYYEKALELDPDNA-------------DALNNLGLLLLEQGRYDEAIAL-EKALKLDPNNAEALLNLAE 67

                           90       100
                   ....*....|....*....|....*..
gi 2024484393 1393 AKRSSRQFAAALEDLNEAIKLCPNNRE 1419
Cdd:COG3063     68 LLLELGDYDEALAYLERALELDPSALR 94
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 1310-1426 1.79e-11

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 69.25  E-value: 1.79e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1310 GDMFYKKGKVKEAAQRYQYALKKFPREgfgedlktfrelkVSLLLNLSRCRRKMNDFGMAEEFATKALELKPKSYEAYYA 1389
Cdd:COG3914    119 GNLLLALGRLEEALAALRRALALNPDF-------------AEAYLNLGEALRRLGRLEEAIAALRRALELDPDNAEALNN 185

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2024484393 1390 RARAKRSSRQFAAALEDLNEAIKLCPNNREIQRLLLR 1426
Cdd:COG3914    186 LGNALQDLGRLEEAIAAYRRALELDPDNADAHSNLLF 222
Ank_4 pfam13637
Ankyrin repeats (many copies);
1182-1235 2.04e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 60.75  E-value: 2.04e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2024484393 1182 GLTALSWACLKGHLAVVRALVENGAATDHADKNGRTPLDLAAFYGDAEVVQFLV 1235
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 1303-1424 3.14e-11

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: 62.90  E-value: 3.14e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1303 LSKLMEEGDMFYKKGKVKEAAQRYQYALKKFPREgfgedlktfrelkVSLLLNLSRCRRKMNDFGMAEEFATKALELKPK 1382
Cdd:COG4783      4 AEALYALAQALLLAGDYDEAEALLEKALELDPDN-------------PEAFALLGEILLQLGDLDEAIVLLHEALELDPD 70

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2024484393 1383 SYEAYYARARAKRSSRQFAAALEDLNEAIKLCPNNREIQRLL 1424
Cdd:COG4783     71 EPEARLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRL 112
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 1313-1424 5.54e-11

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 67.71  E-value: 5.54e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1313 FYKKGKVKEAAQRYQYALKKFPREgfgedlktfrelkVSLLLNLSRCRRKMNDFGMAEEFATKALELKPKSYEAYYARAR 1392
Cdd:COG3914     88 LQALGRYEEALALYRRALALNPDN-------------AEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGE 154

                           90       100       110
                   ....*....|....*....|....*....|..
gi 2024484393 1393 AKRSSRQFAAALEDLNEAIKLCPNNREIQRLL 1424
Cdd:COG3914    155 ALRRLGRLEEAIAALRRALELDPDNAEALNNL 186
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 1306-1427 1.26e-10

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: 64.37  E-value: 1.26e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1306 LMEEGDMFYKKGKVKEAAQRYQYALKKFPREgfgedlktfrelkVSLLLNLSRCRRKMNDFGMAEEFATKALELKPKSYE 1385
Cdd:COG2956     79 LLELAQDYLKAGLLDRAEELLEKLLELDPDD-------------AEALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAH 145

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2024484393 1386 AYYARARAKRSSRQFAAALEDLNEAIKLCPNNREIQRLLLRV 1427
Cdd:COG2956    146 AYCELAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAEL 187
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 913-1245 2.55e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 64.98  E-value: 2.55e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393  913 KVSRLLILGGANvnyrTEVLnnaPILCVQShlgytEMVALLLEFGANVDAASESGLTPLGYAAAAGFLSIVVLLCKKRAK 992
Cdd:PHA02874    82 DIIKLLIDNGVD----TSIL---PIPCIEK-----DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGAD 149

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393  993 VDHLDKNGqCALVHAALRGhlevvkfliqcdwsmagqqqgvfkkshaiqqaliaaasmgyteivsylldlpekdeeever 1072
Cdd:PHA02874   150 VNIEDDNG-CYPIHIAIKH------------------------------------------------------------- 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1073 aqiNSFdslwgetaltaaagrgklDVCRLLLEQGAAVAQPNRRGVVPLFSAVRQGHWQIVDLLLTHGADVNMADKQGRTP 1152
Cdd:PHA02874   168 ---NFF------------------DIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTP 226

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1153 LMMAASegHLGTVEFLLAQGASISLMDKEGLTALSWA----CLKGhlaVVRALVENGAATDHADKNGRTPLDLAAFY-GD 1227
Cdd:PHA02874   227 LHNAII--HNRSAIELLINNASINDQDIDGSTPLHHAinppCDID---IIDILLYHKADISIKDNKGENPIDTAFKYiNK 301

                          330
                   ....*....|....*...
gi 2024484393 1228 AEVVQFLVDHGAMIEHVD 1245
Cdd:PHA02874   302 DPVIKDIIANAVLIKEAD 319
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 1095-1274 2.61e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 65.47  E-value: 2.61e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1095 KLDVCRLLLEQGAAVAQPNRRGVVPLFSAVRQGHWQIVDLLLTHGADVNMADKQGRTPLMMAASEGHLGTVE-------- 1166
Cdd:PHA02876   157 ELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKaiidnrsn 236

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1167 ---------------------FLLAQGASISLMDKEGLTALSWACLKGHLA-VVRALVENGAATDHADKNGRTPLDLAAF 1224
Cdd:PHA02876   237 inkndlsllkairnedletslLLYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMAK 316

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2024484393 1225 YG-DAEVVQFLVDHGAMIEHVDYSGMRPLDRAVGC-RNTSVVVTLLKKGAKI 1274
Cdd:PHA02876   317 NGyDTENIRTLIMLGADVNAADRLYITPLHQASTLdRNKDIVITLLELGANV 368
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 1124-1279 2.66e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 65.47  E-value: 2.66e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1124 VRQGHWQIVDLLLTHGADVNMADKQGRTPLMMAASEGHLGTVEFLLAQGASISLMDKEGLTALSWACLKGHLAVVRALVE 1203
Cdd:PHA02876   153 IQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIID 232

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024484393 1204 NGAatdHADKNGRTPLDlAAFYGDAEVVQFLVDHGAMIEHVDYSGMRPLDRAVGCRNTS-VVVTLLKKGAKIGCQTL 1279
Cdd:PHA02876   233 NRS---NINKNDLSLLK-AIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNI 305
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 1321-1424 3.22e-10

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: 60.02  E-value: 3.22e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1321 EAAQRYQYALKKFPREGFGedlktfrelkvslLLNLSRCRRKMNDFGMAEEFATKALELKPKSYEAYYARARAKRSSRQF 1400
Cdd:COG4235      1 EAIARLRQALAANPNDAEG-------------WLLLGRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDT 67

                           90       100
                   ....*....|....*....|....
gi 2024484393 1401 AAALEDLNEAIKLCPNNREIQRLL 1424
Cdd:COG4235     68 EEAEELLERALALDPDNPEALYLL 91
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 1073-1237 3.69e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 64.52  E-value: 3.69e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1073 AQINSFDSLWGETALTAAAGRGKLDVCRLLLEQGAAVAQPNRRGVVPLFSAVRQGHWQIVDLLLTHGADVNMADKQGRTP 1152
Cdd:PHA02878   158 ADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTP 237

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1153 LMMAASE-GHLGTVEFLLAQGASISLMDK-EGLTALswaclkgHLA-----VVRALVENGAATDHADKNGRTPLDLAAF- 1224
Cdd:PHA02878   238 LHISVGYcKDYDILKLLLEHGVDVNAKSYiLGLTAL-------HSSikserKLKLLLEYGADINSLNSYKLTPLSSAVKq 310

                          170
                   ....*....|...
gi 2024484393 1225 YGDAEVVQFLVDH 1237
Cdd:PHA02878   311 YLCINIGRILISN 323
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 1310-1423 4.23e-10

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: 59.63  E-value: 4.23e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1310 GDMFYKKGKVKEAAQRYQYALKKFPREgfgedlktfrelkVSLLLNLSRCRRKMNDFGMAEEFATKALELKPKSYEAYYA 1389
Cdd:COG4235     24 GRAYLRLGRYDEALAAYEKALRLDPDN-------------ADALLDLAEALLAAGDTEEAEELLERALALDPDNPEALYL 90

                           90       100       110
                   ....*....|....*....|....*....|....
gi 2024484393 1390 RARAKRSSRQFAAALEDLNEAIKLCPNNREIQRL 1423
Cdd:COG4235     91 LGLAAFQQGDYAEAIAAWQKLLALLPADAPARLL 124
PHA02798 PHA02798
ankyrin-like protein; Provisional
 1095-1247 4.75e-10

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 64.47  E-value: 4.75e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1095 KLDVCRLLLEQGAAVAQPNRRGVVPLFSAVR-----QGHWQIVDLLLTHGADVNMADKQGRTPLMMAASEGHLGTVEFLL 1169
Cdd:PHA02798    50 STDIVKLFINLGANVNGLDNEYSTPLCTILSnikdyKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILL 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1170 ---AQGASISLMDKEGLTALSWACLKGH---LAVVRALVENGAATD-HADKNGRTPLDLAAFYG----DAEVVQFLVDHG 1238
Cdd:PHA02798   130 fmiENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDINtHNNKEKYDTLHCYFKYNidriDADILKLFVDNG 209


                   ....*....
gi 2024484393 1239 AMIEHVDYS 1247
Cdd:PHA02798   210 FIINKENKS 218
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 1155-1237 5.18e-10

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 64.53  E-value: 5.18e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1155 MAASEGHLGtVEFLLAQGASISLMDKEGLTALSWACLKGHLAVVRALVENGAATDHADKNGRTPLDLAAFYGDAEVVQFL 1234
Cdd:PTZ00322    89 LAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167


                   ...
gi 2024484393 1235 VDH 1237
Cdd:PTZ00322   168 SRH 170
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 1321-1427 7.77e-10

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: 59.59  E-value: 7.77e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1321 EAAQRYQYALKKFPREGFGEDLKTFRELKVSLLLNLSRCRRKMNDFGMAEEFATKALELKPKSYEAYYARARAKRSSRQF 1400
Cdd:COG5010     25 EKYEAALAGANNTKEDELAAAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQALQLDPNNPELYYNLALLYSRSGDK 104

                           90       100
                   ....*....|....*....|....*..
gi 2024484393 1401 AAALEDLNEAIKLCPNNREIQRLLLRV 1427
Cdd:COG5010    105 DEAKEYYEKALALSPDNPNAYSNLAAL 131
Ank_4 pfam13637
Ankyrin repeats (many copies);
1119-1169 1.01e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.74  E-value: 1.01e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2024484393 1119 PLFSAVRQGHWQIVDLLLTHGADVNMADKQGRTPLMMAASEGHLGTVEFLL 1169
Cdd:pfam13637    4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
1353-1417 1.14e-09

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 61.18  E-value: 1.14e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024484393 1353 LLNLSRCRRKMNDFGMAEEFATKALELKPKSYEAYYARARAKRSSRQFAAALEDLNEAIKLCPNN 1417
Cdd:COG0457     11 YNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDD 75
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 909-1148 1.32e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 62.76  E-value: 1.32e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393  909 TPNIKVSRLLILGGANVNYRTEVLNNAPILCVQSHLGYTEMVALLLEFGANVDAASESGLTPLGYAAAAGF--LSIVVLL 986
Cdd:PHA03100    83 TDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLL 162

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393  987 CKKRAKVDHLDKngqcalvhaalrghlevVKFLIqcdwsmagqqqgvfkkshaiqqaliaaasmgyteivSYLLDLPEKD 1066
Cdd:PHA03100   163 IDKGVDINAKNR-----------------VNYLL------------------------------------SYGVPINIKD 189

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1067 EeeveraqinsfdslWGETALTAAAGRGKLDVCRLLLEQGAAVAQPNRRGVVPLFSAVRQGHWQIVDLLLTHGADVNMAD 1146
Cdd:PHA03100   190 V--------------YGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTII 255


                   ..
gi 2024484393 1147 KQ 1148
Cdd:PHA03100   256 ET 257
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 1132-1252 1.85e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 62.99  E-value: 1.85e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1132 VDLLLTHGADVNMADKQGRTPLMMAASEGHLGTVEFLLAQGASISLMDKEGLTALSWACLKGHLAVVRALVenGAATDHA 1211
Cdd:PTZ00322    98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS--RHSQCHF 175

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2024484393 1212 DKNGRTPLDlaAFYGdaeVVQFLVDHGAMIEHVDYSGM-RPL 1252
Cdd:PTZ00322   176 ELGANAKPD--SFTG---KPPSLEDSPISSHHPDFSAVpQPM 212
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 1312-1415 2.30e-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: 58.05  E-value: 2.30e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1312 MFYKKGKVKEAAQRYQYALKKFPREGfgedlktfrelkvSLLLNLSRCRRKMNDFGMAEEFATKALELKPKSYEAYYARA 1391
Cdd:COG5010     63 LYNKLGDFEESLALLEQALQLDPNNP-------------ELYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLA 129

                           90       100
                   ....*....|....*....|....
gi 2024484393 1392 RAKRSSRQFAAALEDLNEAIKLCP 1415
Cdd:COG5010    130 ALLLSLGQDDEAKAALQRALGTSP 153
Ank_4 pfam13637
Ankyrin repeats (many copies);
1149-1202 2.74e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.59  E-value: 2.74e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2024484393 1149 GRTPLMMAASEGHLGTVEFLLAQGASISLMDKEGLTALSWACLKGHLAVVRALV 1202
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
1310-1478 5.60e-09

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 58.86  E-value: 5.60e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1310 GDMFYKKGKVKEAAQRYQYALKKFPREgfgedlktfrelkVSLLLNLSRCRRKMNDFGMAEEFATKALELKPKSYEAYYA 1389
Cdd:COG0457     83 GLALQALGRYEEALEDYDKALELDPDD-------------AEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYN 149

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1390 RARAKRSSRQFAAALEDLNEAIKLCPNNREIQRLLLRVEEECRQVQQQQQQQQQQPPPLPAEPEPEAQHEELYSVQDIFE 1469
Cdd:COG0457    150 LGIALEKLGRYEEALELLEKLEAAALAALLAAALGEAALALAAAEVLLALLLALEQALRKKLAILTLAALAELLLLALAL 229


                   ....*....
gi 2024484393 1470 EEYLEQDVE 1478
Cdd:COG0457    230 LLALRLAAL 238
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
1306-1419 9.90e-09

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


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 58.00  E-value: 9.90e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1306 LMEEGDMFYKKGKVKEAAQRYQYALKKFPRegfgedlktfrelKVSLLLNLSRCRRKMNDFGMAEEFATKALELKPKSYE 1385
Cdd:COG4785     76 YYERGVAYDSLGDYDLAIADFDQALELDPD-------------LAEAYNNRGLAYLLLGDYDAALEDFDRALELDPDYAY 142

                           90       100       110
                   ....*....|....*....|....*....|....
gi 2024484393 1386 AYYARARAKRSSRQFAAALEDLNEAIKLCPNNRE 1419
Cdd:COG4785    143 AYLNRGIALYYLGRYELAIADLEKALELDPNDPE 176
Ank_4 pfam13637
Ankyrin repeats (many copies);
1215-1268 3.50e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.51  E-value: 3.50e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2024484393 1215 GRTPLDLAAFYGDAEVVQFLVDHGAMIEHVDYSGMRPLDRAVGCRNTSVVVTLL 1268
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
1279-1417 3.75e-08

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


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 56.08  E-value: 3.75e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1279 LPSRPRGPATWAMATSKPDIMiillSKLMEEGDMFYKkgkVKEAAQRYQYALKKFPREGFGEDLKTFRELK----VSLLL 1354
Cdd:COG4785      5 ALALLLALALAAAAASKAAIL----LAALLFAAVLAL---AIALADLALALAAAALAAAALAAERIDRALAlpdlAQLYY 77

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024484393 1355 NLSRCRRKMNDFGMAEEFATKALELKPKSYEAYYARARAKRSSRQFAAALEDLNEAIKLCPNN 1417
Cdd:COG4785     78 ERGVAYDSLGDYDLAIADFDQALELDPDLAEAYNNRGLAYLLLGDYDAALEDFDRALELDPDY 140
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 1310-1424 3.99e-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: 56.66  E-value: 3.99e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1310 GDMFYKKGKVKEAAQRYQYALKKFPRegfgedlktfrelKVSLLLNLSRCRRKMNDFGMAEEFATKALELKPKSYEAYYA 1389
Cdd:COG2956     49 GNLYRRRGEYDRAIRIHQKLLERDPD-------------RAEALLELAQDYLKAGLLDRAEELLEKLLELDPDDAEALRL 115

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2024484393 1390 RARAKRSSRQFAAALEDLNEAIKLCPNNREIQRLL 1424
Cdd:COG2956    116 LAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCEL 150
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 1298-1427 4.87e-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: 56.66  E-value: 4.87e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1298 IMIILLSKLMEEGDMFYKKGKVKEAAQRYQYALKKFPREgfgedlktfrelkVSLLLNLSRCRRKMNDFGMAEEFATKAL 1377
Cdd:COG2956      3 LPVAAALGWYFKGLNYLLNGQPDKAIDLLEEALELDPET-------------VEAHLALGNLYRRRGEYDRAIRIHQKLL 69

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1378 ELKPKSYEAYYARARAKRSSRQFAAALEDLNEAIKLCPNNREIQRLLLRV 1427
Cdd:COG2956     70 ERDPDRAEALLELAQDYLKAGLLDRAEELLEKLLELDPDDAEALRLLAEI 119
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 1310-1395 5.54e-08

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: 53.07  E-value: 5.54e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1310 GDMFYKKGKVKEAAQRYQYALKKFPREGFGEDLktfrelkvslLLNLSRCRRKMNDFGMAEEFATKALELKPKSYEAYYA 1389
Cdd:COG1729     37 GEAYYALGDYDEAAEAFEKLLKRYPDSPKAPDA----------LLKLGLSYLELGDYDKARATLEELIKKYPDSEAAKEA 106


                   ....*.
gi 2024484393 1390 RARAKR 1395
Cdd:COG1729    107 RARLAR 112
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 1349-1424 7.13e-08

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: 53.27  E-value: 7.13e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024484393 1349 KVSLLLNLSRCRRKMNDFGMAEEFATKALELKPKSYEAYYARARAKRSSRQFAAALEDLNEAIKLCPNNREIQRLL 1424
Cdd:COG4783      3 CAEALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNL 78
Ank_5 pfam13857
Ankyrin repeats (many copies);
1135-1186 8.72e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 50.42  E-value: 8.72e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2024484393 1135 LLTHG-ADVNMADKQGRTPLMMAASEGHLGTVEFLLAQGASISLMDKEGLTAL 1186
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 911-1146 1.74e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 56.41  E-value: 1.74e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393  911 NIKVSRLLilgGANVNYRTEVLNNAPILCVQShLGYTEMVALLLEFGANVDAASESGLTPLGYAAAAGFLSIVVLLCKKR 990
Cdd:PLN03192   506 DLNVGDLL---GDNGGEHDDPNMASNLLTVAS-TGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHA 581

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393  991 AKVDHLDKNGQCALVHAALRGHLEVVKFLIQCdwsmagqqqgvfkkshaiqqaliaaasmgyteivsylldlpekdeeev 1070
Cdd:PLN03192   582 CNVHIRDANGNTALWNAISAKHHKIFRILYHF------------------------------------------------ 613

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024484393 1071 erAQINsfDSLWGETALTAAAGRGKLDVCRLLLEQGAAVAQPNRRGVVPLFSAVRQGHWQIVDLLLTHGADVNMAD 1146
Cdd:PLN03192   614 --ASIS--DPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
Ank_4 pfam13637
Ankyrin repeats (many copies);
967-1020 1.91e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.58  E-value: 1.91e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2024484393  967 GLTPLGYAAAAGFLSIVVLLCKKRAKVDHLDKNGQCALVHAALRGHLEVVKFLI 1020
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
916-997 3.11e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 50.11  E-value: 3.11e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393  916 RLLILGGANVNYRTEVLNNAPILCVQShlGYTEMVALLLEFgANVDAaSESGLTPLGYAAAAGFLSIVVLLCKKRAKVDH 995
Cdd:pfam12796   14 KLLLENGADANLQDKNGRTALHLAAKN--GHLEIVKLLLEH-ADVNL-KDNGRTALHYAARSGHLEIVKLLLEKGADINV 89


                   ..
gi 2024484393  996 LD 997
Cdd:pfam12796   90 KD 91
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
1359-1427 4.22e-07

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 49.78  E-value: 4.22e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024484393 1359 CRRKMNDFGMAEEFATKALELKPKSYEAYYARARAKRSSRQFAAALEdLNEAIKLCPNNREIQRLLLRV 1427
Cdd:COG3063      1 LYLKLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIA-LEKALKLDPNNAEALLNLAEL 68
Ank_4 pfam13637
Ankyrin repeats (many copies);
936-986 4.70e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.42  E-value: 4.70e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2024484393  936 PILCVQSHLGYTEMVALLLEFGANVDAASESGLTPLGYAAAAGFLSIVVLL 986
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 1306-1423 9.97e-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: 52.42  E-value: 9.97e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1306 LMEEGDMFYKKGKVKEAAQRYQYALKKFPRegfgedlktfrelKVSLLLNLSRCRRKMNDFGMAEEFATKALELKPKSYE 1385
Cdd:COG2956    147 YCELAELYLEQGDYDEAIEALEKALKLDPD-------------CARALLLLAELYLEQGDYEEAIAALERALEQDPDYLP 213

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2024484393 1386 AYYARARAKRSSRQFAAALEDLNEAIKLCPNNREIQRL 1423
Cdd:COG2956    214 ALPRLAELYEKLGDPEEALELLRKALELDPSDDLLLAL 251
Ank_5 pfam13857
Ankyrin repeats (many copies);
1179-1222 1.04e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.34  E-value: 1.04e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2024484393 1179 DKEGLTALSWACLKGHLAVVRALVENGAATDHADKNGRTPLDLA 1222
Cdd:pfam13857   13 DGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 1313-1422 2.61e-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: 2.61e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1313 FYKKGKVKEAAQRYQYALKKFPREgfgedlktfrELKVSLLLNLSRCRRKMNDFGMAEEFATKALELKPKSY---EAYYA 1389
Cdd:COG1729      3 LLKAGDYDEAIAAFKAFLKRYPNS----------PLAPDALYWLGEAYYALGDYDEAAEAFEKLLKRYPDSPkapDALLK 72

                           90       100       110
                   ....*....|....*....|....*....|...
gi 2024484393 1390 RARAKRSSRQFAAALEDLNEAIKLCPNNREIQR 1422
Cdd:COG1729     73 LGLSYLELGDYDKARATLEELIKKYPDSEAAKE 105
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 1083-1204 2.72e-06

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 52.32  E-value: 2.72e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1083 GETALTAAAGRGKLDVCRLLLEQGAAVAQPNRRGVV--------------PLFSAVRQGHWQIVDLLLTHGADVNMADKQ 1148
Cdd:cd22192     89 GETALHIAVVNQNLNLVRELIARGADVVSPRATGTFfrpgpknliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSL 168

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024484393 1149 GRTPLMMAASEGHLGTV----EFLLAQGASISLM------DKEGLTALSWACLKGHLAVVRALVEN 1204
Cdd:cd22192    169 GNTVLHILVLQPNKTFAcqmyDLILSYDKEDDLQpldlvpNNQGLTPFKLAAKEGNIVMFQHLVQK 234
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 1118-1274 2.77e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 52.19  E-value: 2.77e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1118 VPLFSAVRQGHWQIVDLLLTHGADVNMADKQGRTPLMMAASEGHLGTVEFLLAQGASISL-------------------- 1177
Cdd:PHA02878    39 IPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVfytlvaikdafnnrnveifk 118

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1178 ------MDKEGLTALSWACLKGH-----LAVVRALVENGAATDHADKN-GRTPLDLAAFYGDAEVVQFLVDHGAMIEHVD 1245
Cdd:PHA02878   119 iiltnrYKNIQTIDLVYIDKKSKddiieAEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPD 198

                          170       180
                   ....*....|....*....|....*....
gi 2024484393 1246 YSGMRPLDRAVGCRNTSVVVTLLKKGAKI 1274
Cdd:PHA02878   199 KTNNSPLHHAVKHYNKPIVHILLENGAST 227
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 909-1142 6.87e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 51.22  E-value: 6.87e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393  909 TPNIkvsRLLILGGANVNyRTEVLNNAPILCVQSHLGYTEMVALLLEFGANVDAASESGLTPLGYAAAAGFLSIVVLLCK 988
Cdd:PHA02876   321 TENI---RTLIMLGADVN-AADRLYITPLHQASTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLD 396

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393  989 KRAKVDHLDKNGQCALvHAALRGhlevvkfliqcdwsmagqqqgvfkkshaiqqaliaaaSMGYTEiVSYLLDlpekdee 1068
Cdd:PHA02876   397 YGADIEALSQKIGTAL-HFALCG-------------------------------------TNPYMS-VKTLID------- 430

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024484393 1069 evERAQINSFDSLWGETALTAAAGRGKLDVCRLLLEQGAAVAQPNRRGVVPLFSAVrqGHWQIVDLLLTHGADV 1142
Cdd:PHA02876   431 --RGANVNSKNKDLSTPLHYACKKNCKLDVIEMLLDNGADVNAINIQNQYPLLIAL--EYHGIVNILLHYGAEL 500
Ank_5 pfam13857
Ankyrin repeats (many copies);
1102-1156 8.02e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.03  E-value: 8.02e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2024484393 1102 LLEQG-AAVAQPNRRGVVPLFSAVRQGHWQIVDLLLTHGADVNMADKQGRTPLMMA 1156
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 1100-1169 8.95e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.67  E-value: 8.95e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024484393 1100 RLLLEQGAavaQPNRR---GVVPLFSAVRQGHWQIVDLLLTHGADVNMADKQGRTPLMMAASEGHLGTVEFLL 1169
Cdd:PTZ00322    99 RILLTGGA---DPNCRdydGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 1541-1840 9.35e-06

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 51.07  E-value: 9.35e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1541 STSPTLSPTH----QNSHYRPSPPH-----TSPAHQGSSYRF----SPPPVGS-QGKEYQSPPPSPLRRGPQYRA---SP 1603
Cdd:pfam05109  429 TTSPTLNTTGfaapNTTTGLPSSTHvptnlTAPASTGPTVSTadvtSPTPAGTtSGASPVTPSPSPRDNGTESKApdmTS 508

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1604 PADGMSVYRSQSGSPVryqqePSAVSPLPGRPKSPLSKMSQRSFQMPQLPVAV-PQQGLRLQPAKAQI--VRSNQPSSAV 1680
Cdd:pfam05109  509 PTSAVTTPTPNATSPT-----PAVTTPTPNATSPTLGKTSPTSAVTTPTPNATsPTPAVTTPTPNATIptLGKTSPTSAV 583

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1681 HSSTviPTGAYSQVAHSMASKYQAAAGEMGVNQSRLVyqgsiggivgdSRPVQHVQASLSAGaicQHG--GLAKEDLPQR 1758
Cdd:pfam05109  584 TTPT--PNATSPTVGETSPQANTTNHTLGGTSSTPVV-----------TSPPKNATSAVTTG---QHNitSSSTSSMSLR 647

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1759 PSSayrggmrysqtpqIGRSQSASYYPMCHSKLDLERSSLPSGQLGSPDVShlirrPISVNPSEIKPHPPTPRPLLHSQS 1838
Cdd:pfam05109  648 PSS-------------ISETLSPSTSDNSTSHMPLLTSAHPTGGENITQVT-----PASTSTHHVSTSSPAPRPGTTSQA 709


                   ..
gi 2024484393 1839 VG 1840
Cdd:pfam05109  710 SG 711
PHA03247 PHA03247
large tegument protein UL36; Provisional
 1557-1714 1.95e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 50.32  E-value: 1.95e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1557 PSPPHTSPAHQGSSyRFSPPPVgSQGKEYQSPPPSPLRRGPQYRASPPAdgmsvyrsQSGSPVRYQQEPSAVSPLPGRPK 1636
Cdd:PHA03247  2871 PAAKPAAPARPPVR-RLARPAV-SRSTESFALPPDQPERPPQPQAPPPP--------QPQPQPPPPPQPQPPPPPPPRPQ 2940

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1637 SPLSKMSQRSFQMPQLPVAVPQQGLRLQPAKAQIVRSNQPSSA---------VHSSTVIPTGAYSQVAHSMASKYQAAAG 1707
Cdd:PHA03247  2941 PPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPApsreapassTPPLTGHSLSRVSSWASSLALHEETDPP 3020


                   ....*..
gi 2024484393 1708 EMGVNQS 1714
Cdd:PHA03247  3021 PVSLKQT 3027
PHA02946 PHA02946
ankyin-like protein; Provisional
 1102-1252 2.18e-05

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 49.28  E-value: 2.18e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1102 LLEQGAAVAQPNRRGVVPLFSAVRQGHWQIVDLLLTHGADVNMADKQGRTPL--MMAASEGHLGTVEFLLAQGASI-SLM 1178
Cdd:PHA02946    58 LLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLyyLSGTDDEVIERINLLVQYGAKInNSV 137

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024484393 1179 DKEGLTALsWACLKGHLAVVRALVENGAATDHADKNGRTPL--DLAAFYGDAEVVQFLVDHGAMIEHVDYSGMRPL 1252
Cdd:PHA02946   138 DEEGCGPL-LACTDPSERVFKKIMSIGFEARIVDKFGKNHIhrHLMSDNPKASTISWMMKLGISPSKPDHDGNTPL 212
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 1065-1242 3.41e-05

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 48.92  E-value: 3.41e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1065 KDEEEVERAQINSFDSLWGETALTAAAGRGKLDVCRLLLEQgaavaqpNRRGVV--PLFSAVRQGHWQIVDLLLTHGADV 1142
Cdd:TIGR00870   35 RDLEEPKKLNINCPDRLGRSALFVAAIENENLELTELLLNL-------SCRGAVgdTLLHAISLEYVDAVEAILLHLLAA 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1143 nmADKQGRTPLMMAASeghlgTVEFllaqgasislmdKEGLTALSWACLKGHLAVVRALVENGAA------------TDH 1210
Cdd:TIGR00870  108 --FRKSGPLELANDQY-----TSEF------------TPGITALHLAAHRQNYEIVKLLLERGASvparacgdffvkSQG 168

                          170       180       190
                   ....*....|....*....|....*....|....
gi 2024484393 1211 AD--KNGRTPLDLAAFYGDAEVVQFLVDHGAMIE 1242
Cdd:TIGR00870  169 VDsfYHGESPLNAAACLGSPSIVALLSEDPADIL 202
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 1529-1708 3.77e-05

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 49.00  E-value: 3.77e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1529 SSVGSPTRQGYQSTSPtlsPTHQNSHYRPSPPHTSPAHQGSSYRFSPPPVGSQGKEYQSPPPSPLRRGPQYRASPPAdgm 1608
Cdd:pfam03154  156 SDSDSSAQQQILQTQP---PVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHT--- 229

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1609 svyRSQSGSPVRYQQEPSAVSPLPGRPK-SPLSKMSQRSFQMPQLPVAVPQQGLRLQ--PAKAQIVRSNQP--SSAVHSS 1683
Cdd:pfam03154  230 ---LIQQTPTLHPQRLPSPHPPLQPMTQpPPPSQVSPQPLPQPSLHGQMPPMPHSLQtgPSHMQHPVPPQPfpLTPQSSQ 306

                          170       180
                   ....*....|....*....|....*
gi 2024484393 1684 TVIPTGAYSQVAHSMASKYQAAAGE 1708
Cdd:pfam03154  307 SQVPPGPSPAAPGQSQQRIHTPPSQ 331
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 1149-1241 5.54e-05

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: 48.34  E-value: 5.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1149 GRTPLMMAASEGHLGTVE--FLLAQGASISLMDKE------------GLTALSWACLKGHLAVVRALVENGAATdHADKN 1214
Cdd:cd21882     26 GKTCLHKAALNLNDGVNEaiMLLLEAAPDSGNPKElvnapctdefyqGQTALHIAIENRNLNLVRLLVENGADV-SARAT 104

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 2024484393 1215 GRT--------------PLDLAAFYGDAEVVQFLVDHGAMI 1241
Cdd:cd21882    105 GRFfrkspgnlfyfgelPLSLAACTNQEEIVRLLLENGAQP 145
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 1311-1426 6.27e-05

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: 48.16  E-value: 6.27e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1311 DMFYKKGKVKEAAQRYQYALKKFPREgfgedlktfrelkVSLLLNLSRCRRKMNDFGMAEEFATKALELKPKSYEAYYAR 1390
Cdd:TIGR02917  507 RIDIQEGNPDDAIQRFEKVLTIDPKN-------------LRAILALAGLYLRTGNEEEAVAWLEKAAELNPQEIEPALAL 573

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2024484393 1391 ARAKRSSRQFAAALEDLNEAIKLCPNNREIQRLLLR 1426
Cdd:TIGR02917  574 AQYYLGKGQLKKALAILNEAADAAPDSPEAWLMLGR 609
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 1148-1180 6.67e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 41.51  E-value: 6.67e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 2024484393 1148 QGRTPLMMAA-SEGHLGTVEFLLAQGASISLMDK 1180
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
1378-1426 1.18e-04

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


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 45.68  E-value: 1.18e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2024484393 1378 ELKPKSYEAYYARARAKRSSRQFAAALEDLNEAIKLCP------NNREIQRLLLR 1426
Cdd:COG4785     67 LALPDLAQLYYERGVAYDSLGDYDLAIADFDQALELDPdlaeayNNRGLAYLLLG 121
TPR_14 pfam13428
Tetratricopeptide repeat;
1385-1427 1.40e-04

Tetratricopeptide repeat;


Pssm-ID: 463874 [Multi-domain]  Cd Length: 44  Bit Score: 41.25  E-value: 1.40e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 2024484393 1385 EAYYARARAKRSSRQFAAALEDLNEAIKLCPNNREIQRLLLRV 1427
Cdd:pfam13428    2 EALLALARALLALGDPDEALALLERALALDPDDPEAWLALAQL 44
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 1214-1242 1.44e-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: 40.65  E-value: 1.44e-04
                            10        20
                    ....*....|....*....|....*....
gi 2024484393  1214 NGRTPLDLAAFYGDAEVVQFLVDHGAMIE 1242
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
HemYx COG3071
Uncharacterized protein HemY, contains HemY_N domain and TPR repeats (unrelated to ...
 1347-1427 2.04e-04

Uncharacterized protein HemY, contains HemY_N domain and TPR repeats (unrelated to protoporphyrinogen oxidase HemY) [Function unknown];


Pssm-ID: 442305 [Multi-domain]  Cd Length: 323  Bit Score: 45.67  E-value: 2.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1347 ELKVSLLLNLSRCRRKMNDFGMAEEFATKALELKPKSYEA-YYARARAKRSSRQFAAALEDLNEAIKLCPNNREIQRLLL 1425
Cdd:COG3071     47 EAPLLAYLLAARAAQALGDYERRDEYLAQALELAPEAELAvLLTRAELLLDQGQAEQALATLEALRAGAPRHPQVLRLLL 126


                   ..
gi 2024484393 1426 RV 1427
Cdd:COG3071    127 QA 128
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 1214-1245 2.30e-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: 40.35  E-value: 2.30e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 2024484393 1214 NGRTPLDLAA-FYGDAEVVQFLVDHGAMIEHVD 1245
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 1198-1268 2.57e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.04  E-value: 2.57e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024484393 1198 VRALVENGAATDHADKNGRTPLDLAAFYGDAEVVQFLVDHGAMIEHVDYSGMRPLDRAVGcRNTSVVVTLL 1268
Cdd:PTZ00322    98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEE-NGFREVVQLL 167
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
1377-1424 2.99e-04

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 44.61  E-value: 2.99e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 2024484393 1377 LELKPKSYEAYYARARAKRSSRQFAAALEDLNEAIKLCPNNREIQRLL 1424
Cdd:COG0457      1 LELDPDDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNL 48
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 1083-1235 5.56e-04

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 45.07  E-value: 5.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1083 GETALTAAAGRGKLDVCRLLLEQGAAV-AQPN-------------RRGVVPLFSAVRQGHWQIVDLLLTHGADVNMADKQ 1148
Cdd:TIGR00870  128 GITALHLAAHRQNYEIVKLLLERGASVpARACgdffvksqgvdsfYHGESPLNAAACLGSPSIVALLSEDPADILTADSL 207

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1149 GRTPLMMAASEGhlgtvEFllaqgasislmdKEGLTALSWAC---LKGHLAVVRALVENGAATDHadkNGRTPLDLAAFY 1225
Cdd:TIGR00870  208 GNTLLHLLVMEN-----EF------------KAEYEELSCQMynfALSLLDKLRDSKELEVILNH---QGLTPLKLAAKE 267

                          170
                   ....*....|
gi 2024484393 1226 GDAEVVQFLV 1235
Cdd:TIGR00870  268 GRIVLFRLKL 277
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 1148-1177 6.23e-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: 38.72  E-value: 6.23e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 2024484393  1148 QGRTPLMMAASEGHLGTVEFLLAQGASISL 1177
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 916-1000 6.32e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.89  E-value: 6.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393  916 RLLILGGANVNYRTevLNNAPILCVQSHLGYTEMVALLLEFGANVDAASESGLTPLGYAAAAGFLSIVVLLCKKRAKVDH 995
Cdd:PTZ00322    99 RILLTGGADPNCRD--YDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFE 176


                   ....*
gi 2024484393  996 LDKNG 1000
Cdd:PTZ00322   177 LGANA 181
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 910-974 7.32e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 44.49  E-value: 7.32e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024484393  910 PNIKVSRLLILGGANVNYrTEVLNNAPILCVQSHLGyTEMVALLLEFGANVDAASESGLTPLGYA 974
Cdd:PHA02878   179 KDQRLTELLLSYGANVNI-PDKTNNSPLHHAVKHYN-KPIVHILLENGASTDARDKCGNTPLHIS 241
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 1557-1661 7.75e-04

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 44.69  E-value: 7.75e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1557 PSPPHTSPAHQGSSYRFSPPPVGSQGKEYQSP-PPSPLRRGPQYRASPPADGMSVYRSQSGSPVRYQ-QEPSAVSPLPGR 1634
Cdd:PRK10263   740 PHEPLFTPIVEPVQQPQQPVAPQQQYQQPQQPvAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQpQQPVAPQPQYQQ 819

                           90       100
                   ....*....|....*....|....*...
gi 2024484393 1635 PKSPLSkmSQRSFQMPQLPVA-VPQQGL 1661
Cdd:PRK10263   820 PQQPVA--PQPQYQQPQQPVApQPQDTL 845
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 1310-1425 8.18e-04

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 44.60  E-value: 8.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1310 GDMFYKKGKVKEAAQRYQYALKKFPREgfgedlktfrelkVSLLLNLSRCRRKMNDFGMAEEFATKALELKPKSYEAYYA 1389
Cdd:COG3914    153 GEALRRLGRLEEAIAALRRALELDPDN-------------AEALNNLGNALQDLGRLEEAIAAYRRALELDPDNADAHSN 219

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2024484393 1390 RARAKRSSRQFAAALEDLNEAIKLCPNNREIQRLLL 1425
Cdd:COG3914    220 LLFALRQACDWEVYDRFEELLAALARGPSELSPFAL 255
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 1361-1427 8.18e-04

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 44.60  E-value: 8.18e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024484393 1361 RKMNDFGMAEEFATKALELKPKSYEAYYARARAKRSSRQFAAALEDLNEAIKLCPNNREIQRLLLRV 1427
Cdd:COG3914     89 QALGRYEEALALYRRALALNPDNAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEA 155
Ank_5 pfam13857
Ankyrin repeats (many copies);
1201-1255 8.80e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.25  E-value: 8.80e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2024484393 1201 LVENG-AATDHADKNGRTPLDLAAFYGDAEVVQFLVDHGAMIEHVDYSGMRPLDRA 1255
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 1310-1427 1.18e-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: 43.92  E-value: 1.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1310 GDMFYKKGKVKEAAQRYQYALKKFPREGfgedlktfrelkvSLLLNLSRCRRKMNDFGMAEEFATKALELKPKSYEAYYA 1389
Cdd:TIGR02917  132 GLAYLGLGQLELAQKSYEQALAIDPRSL-------------YAKLGLAQLALAENRFDEARALIDEVLTADPGNVDALLL 198

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2024484393 1390 RARAKRSSRQFAAALEDLNEAIKLCPNNreIQRLLLRV 1427
Cdd:TIGR02917  199 KGDLLLSLGNIELALAAYRKAIALRPNN--IAVLLALA 234
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 1083-1270 1.21e-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: 43.85  E-value: 1.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1083 GETALTAAAGRGKLDVCRLLLEqgAA---VAQPNR----RGVVPLFSAVRQGHWQIVDLLLTHGADVNMAdkqgRTplmm 1155
Cdd:cd22192     51 GETALHVAALYDNLEAAVVLME--AApelVNEPMTsdlyQGETALHIAVVNQNLNLVRELIARGADVVSP----RA---- 120

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1156 aaseghLGTVeFLLAQGASISLmdkeGLTALSWACLKGHLAVVRALVENGAATDHADKNGRTPLDLAAFYGDA----EVV 1231
Cdd:cd22192    121 ------TGTF-FRPGPKNLIYY----GEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKtfacQMY 189

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 2024484393 1232 QFLV-----DHGAMIEHV-DYSGMRPLDRAVGCRNTSVVVTLLKK 1270
Cdd:cd22192    190 DLILsydkeDDLQPLDLVpNNQGLTPFKLAAKEGNIVMFQHLVQK 234
TPR_1 pfam00515
Tetratricopeptide repeat;
1384-1417 1.25e-03

Tetratricopeptide repeat;


Pssm-ID: 459840 [Multi-domain]  Cd Length: 34  Bit Score: 38.17  E-value: 1.25e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 2024484393 1384 YEAYYARARAKRSSRQFAAALEDLNEAIKLCPNN 1417
Cdd:pfam00515    1 AKALYNLGNAYFKLGKYDEALEYYEKALELNPNN 34
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 1051-1235 1.70e-03

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: 43.59  E-value: 1.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1051 GYTEIVSYLLDLPEKDEEEVEraqinsfdslwgeTALTAAAGRGKLDvcRLLleqGAAVAQPNRRGVVPLFSAVRQGHWQ 1130
Cdd:cd22194     94 GKTCLMKALLNINENTKEIVR-------------ILLAFAEENGILD--RFI---NAEYTEEAYEGQTALNIAIERRQGD 155

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1131 IVDLLLTHGADVNMADKQ--------------GRTPLMMAASEGHLGTVEFLLAQGAS-ISLMDKEG---LTALSWAC-- 1190
Cdd:cd22194    156 IVKLLIAKGADVNAHAKGvffnpkykhegfyfGETPLALAACTNQPEIVQLLMEKESTdITSQDSRGntvLHALVTVAed 235

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2024484393 1191 LKGHLAVVRALVENgAATDHADKN--------GRTPLDLAAFYGDAEVVQFLV 1235
Cdd:cd22194    236 SKTQNDFVKRMYDM-ILLKSENKNletirnneGLTPLQLAAKMGKAEILKYIL 287
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 1214-1239 1.97e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.62  E-value: 1.97e-03
                           10        20
                   ....*....|....*....|....*.
gi 2024484393 1214 NGRTPLDLAAFYGDAEVVQFLVDHGA 1239
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGA 26
PHA03247 PHA03247
large tegument protein UL36; Provisional
 1534-1888 2.03e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.39  E-value: 2.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1534 PTRQGYQSTSPTLSPTHQNSHYRPSPPHTSPAHQGSSYRFSPPPVGSQGKEYQSPPPSPlrrGPQYRASPPADGMSVYRS 1613
Cdd:PHA03247  2648 PPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPP---TPEPAPHALVSATPLPPG 2724

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1614 QSGSPVRYQQEPSAVSPlPGRPKSPLSKMSQRSFQMPQLPVAVPQQGLRLQPAKAQIVRSNQP--SSAVHSSTVIPTgAY 1691
Cdd:PHA03247  2725 PAAARQASPALPAAPAP-PAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPavASLSESRESLPS-PW 2802

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1692 SQVAHSMASKYQAAAGEMGVNQSRLVYQGSIGGIVGDSRPVQHVQASLSAGAICQHGGLAKEDLPQRPSSAYRGGMRYSQ 1771
Cdd:PHA03247  2803 DPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPP 2882

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1772 TPQIGRSQ-SASYYPMCHSKLDLERSSLPSGQLGSPDVSHLIRRPISVNPSEIKPHP-----PTPRPLLHSQSVGLRFSP 1845
Cdd:PHA03247  2883 VRRLARPAvSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPqpplaPTTDPAGAGEPSGAVPQP 2962

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|...
gi 2024484393 1846 SSNSISSTSNLTPNFRPSASIQQMEIPLKPAYDRACDELSPVS 1888
Cdd:PHA03247  2963 WLGALVPGRVAVPRFRVPQPAPSREAPASSTPPLTGHSLSRVS 3005
PLN03088 PLN03088
SGT1, suppressor of G2 allele of SKP1; Provisional
 1364-1415 2.21e-03

SGT1, suppressor of G2 allele of SKP1; Provisional


Pssm-ID: 215568 [Multi-domain]  Cd Length: 356  Bit Score: 42.47  E-value: 2.21e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2024484393 1364 NDFGMAEEFATKALELKPKSYEAYYARARAKRSSRQFAAALEDLNEAIKLCP 1415
Cdd:PLN03088    16 DDFALAVDLYTQAIDLDPNNAELYADRAQANIKLGNFTEAVADANKAIELDP 67
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
 1532-1638 2.34e-03

Proline-rich protein; This family includes several eukaryotic proline-rich proteins.


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 40.79  E-value: 2.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1532 GSPTRQGYQStsPTLSPTHQNSHYRPSPPHTSPAHQGSSYRFSPPPVGSQGKEYQSPPPSPLRRGPQYRASPPAdgmsvy 1611
Cdd:pfam15240   75 QPPPQGGKQK--PQGPPPQGGPRPPPGKPQGPPPQGGNQQQGPPPPGKPQGPPPQGGGPPPQGGNQQGPPPPPP------ 146

                           90       100
                   ....*....|....*....|....*..
gi 2024484393 1612 RSQSGSPVRyqqepsavSPLPGRPKSP 1638
Cdd:pfam15240  147 GNPQGPPQR--------PPQPGNPQGP 165
TPR_2 pfam07719
Tetratricopeptide repeat; This Pfam entry includes outlying Tetratricopeptide-like repeats ...
 1385-1416 2.50e-03

Tetratricopeptide repeat; This Pfam entry includes outlying Tetratricopeptide-like repeats (TPR) that are not matched by pfam00515.


Pssm-ID: 429619 [Multi-domain]  Cd Length: 33  Bit Score: 37.12  E-value: 2.50e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 2024484393 1385 EAYYARARAKRSSRQFAAALEDLNEAIKLCPN 1416
Cdd:pfam07719    2 EALYNLGLAYYKLGDYEEALEAYEKALELDPN 33
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 1119-1147 2.66e-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: 37.27  E-value: 2.66e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 2024484393 1119 PLFSAV-RQGHWQIVDLLLTHGADVNMADK 1147
Cdd:pfam00023    5 PLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 938-1022 3.02e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.58  E-value: 3.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393  938 LCVQSHLGYTEMVALLLEFGANVDAASESGLTPLGYAAAAGFLSIVVLLCKKRAKVDHLDKNGQCALVHAALRGHLEVVK 1017
Cdd:PTZ00322    86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165


                   ....*
gi 2024484393 1018 FLIQC 1022
Cdd:PTZ00322   166 LLSRH 170
TPR_12 pfam13424
Tetratricopeptide repeat;
1351-1413 3.59e-03

Tetratricopeptide repeat;


Pssm-ID: 315987 [Multi-domain]  Cd Length: 77  Bit Score: 38.14  E-value: 3.59e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024484393 1351 SLLLNLSRCRRKMNDFGMAEEFATKALEL--------KPKSYEAYYARARAKRSSRQFAAALEDLNEAIKL 1413
Cdd:pfam13424    4 TALNNLAAVLRRLGRYDEALELLEKALEIarrllgpdHPLTATTLLNLGRLYLELGRYEEALELLERALAL 74
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 1513-1695 3.82e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 42.45  E-value: 3.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1513 SGSPLGSH----QVFDFRSNSSvgsptrQGYQSTSPTLSPTHQNSHYRPSPPHTSPAHQGSSYRFSPPPVGSQGKEYQSP 1588
Cdd:pfam03154  284 TGPSHMQHpvppQPFPLTPQSS------QSQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPAPLSMPHIKP 357

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1589 PPS---PLRRGPQYRASPPadgmsvyrsQSGSPVRYQQePSAVSPLPG-RPKSPLSKMSQRSFQMPqlPVAVPQQGLRLQ 1664
Cdd:pfam03154  358 PPTtpiPQLPNPQSHKHPP---------HLSGPSPFQM-NSNLPPPPAlKPLSSLSTHHPPSAHPP--PLQLMPQSQQLP 425

                          170       180       190
                   ....*....|....*....|....*....|..
gi 2024484393 1665 PAKAQ-IVRSNQPSSAVHSSTVIPTGAYSQVA 1695
Cdd:pfam03154  426 PPPAQpPVLTQSQSLPPPAASHPPTSGLHQVP 457
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 912-1020 4.30e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 41.90  E-value: 4.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393  912 IKVSRLLILGganvNYRTEVL---NNAPiLCVQSHLGYTEMVALLLEFGANVDAASESGLTPLGYAAAAGFLSIVVLLCK 988
Cdd:PHA02875    82 KAVEELLDLG----KFADDVFykdGMTP-LHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLID 156

                           90       100       110
                   ....*....|....*....|....*....|..
gi 2024484393  989 KRAKVDHLDKNGQCALVHAALRGHLEVVKFLI 1020
Cdd:PHA02875   157 HKACLDIEDCCGCTPLIIAMAKGDIAICKMLL 188
PRK09782 PRK09782
bacteriophage N4 receptor, outer membrane subunit; Provisional
 1360-1421 4.51e-03

bacteriophage N4 receptor, outer membrane subunit; Provisional


Pssm-ID: 236624 [Multi-domain]  Cd Length: 987  Bit Score: 42.21  E-value: 4.51e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024484393 1360 RRKMNDFGMAEEFATKALELKPkSYEAYYARARAKRSSRQFAAALEDLNEAIKLCPNNREIQ 1421
Cdd:PRK09782   586 RYIPGQPELALNDLTRSLNIAP-SANAYVARATIYRQRHNVPAAVSDLRAALELEPNNSNYQ 646
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 1149-1176 4.54e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 36.47  E-value: 4.54e-03
                           10        20
                   ....*....|....*....|....*...
gi 2024484393 1149 GRTPLMMAASEGHLGTVEFLLAQGASIS 1176
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADIN 29
TPR_19 pfam14559
Tetratricopeptide repeat;
1364-1424 4.88e-03

Tetratricopeptide repeat;


Pssm-ID: 434038 [Multi-domain]  Cd Length: 65  Bit Score: 37.18  E-value: 4.88e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024484393 1364 NDFGMAEEFATKALELKPKSYEAYYARARAKRSSRQFAAALEDLNEAIKLCPNNREIQRLL 1424
Cdd:pfam14559    2 GDYAEALELLEQALAEDPDNAEARLGLAEALLALGRLDEAEALLAALPAADPDDPRYAALL 62
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 1181-1210 5.16e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 36.08  E-value: 5.16e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 2024484393 1181 EGLTALSWACLKGHLAVVRALVENGAATDH 1210
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
TPR_12 pfam13424
Tetratricopeptide repeat;
1310-1382 5.21e-03

Tetratricopeptide repeat;


Pssm-ID: 315987 [Multi-domain]  Cd Length: 77  Bit Score: 37.75  E-value: 5.21e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024484393 1310 GDMFYKKGKVKEAAQRYQYALKKFpREGFGEDlktfRELKVSLLLNLSRCRRKMNDFGMAEEFATKALELKPK 1382
Cdd:pfam13424   10 AAVLRRLGRYDEALELLEKALEIA-RRLLGPD----HPLTATTLLNLGRLYLELGRYEEALELLERALALAEK 77
TPR smart00028
Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum ...
 1384-1417 5.46e-03

Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum of 34 amino acids each and self-associate via a "knobs and holes" mechanism.


Pssm-ID: 197478 [Multi-domain]  Cd Length: 34  Bit Score: 36.27  E-value: 5.46e-03
                            10        20        30
                    ....*....|....*....|....*....|....
gi 2024484393  1384 YEAYYARARAKRSSRQFAAALEDLNEAIKLCPNN 1417
Cdd:smart00028    1 AEALYNLGNAYLKLGDYDEALEYYEKALELDPNN 34
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 1095-1175 6.03e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 41.65  E-value: 6.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1095 KLDVCRLLLEQGAAVaqpNRRGVV--PLFSAVRQGHW------QIVDLLLTHGADVNMADKQGRTPLMMAASEGHLGTVE 1166
Cdd:PHA02989    49 KIKIVKLLIDNGADV---NYKGYIetPLCAVLRNREItsnkikKIVKLLLKFGADINLKTFNGVSPIVCFIYNSNINNCD 125

                           90
                   ....*....|..
gi 2024484393 1167 ---FLLAQGASI 1175
Cdd:PHA02989   126 mlrFLLSKGINV 137
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 1119-1144 6.04e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.03  E-value: 6.04e-03
                            10        20
                    ....*....|....*....|....*.
gi 2024484393  1119 PLFSAVRQGHWQIVDLLLTHGADVNM 1144
Cdd:smart00248    5 PLHLAAENGNLEVVKLLLDKGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 1083-1157 6.87e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.42  E-value: 6.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1083 GETALTAAAGRGKLDVCRLLLEQGAAVAQPNRRGVVPLFSAVRQGHWQIVDLLLTHGADVNMADKQGR------------ 1150
Cdd:PTZ00322   115 GRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGANAKpdsftgkppsle 194


                   ....*...
gi 2024484393 1151 -TPLMMAA 1157
Cdd:PTZ00322   195 dSPISSHH 202
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 1181-1213 7.05e-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: 36.11  E-value: 7.05e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 2024484393 1181 EGLTALSWACLK-GHLAVVRALVENGAATDHADK 1213
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 912-1198 7.93e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 41.27  E-value: 7.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393  912 IKVSRLLILGGANVNYR-------TEVLNNAPIlcvqSHLGYTEMVALLLEFGANVDAASESGLTPLG---YAAAAGFLS 981
Cdd:PHA02989    50 IKIVKLLIDNGADVNYKgyietplCAVLRNREI----TSNKIKKIVKLLLKFGADINLKTFNGVSPIVcfiYNSNINNCD 125

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393  982 IVVLLCKKRAKVDHLDKNGQCALVHAALRG---HLEVVKFLIQcdwsmAGqqQGVFKKSHAiqqaliaaasMGYTEIVSY 1058
Cdd:PHA02989   126 MLRFLLSKGINVNDVKNSRGYNLLHMYLESfsvKKDVIKILLS-----FG--VNLFEKTSL----------YGLTPMNIY 188

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1059 LldlpekdeeeveRAQINSFDslwgetaltaaagrgkLDVCRLLLEQGAAVAQPNRRGVVPLFSAVR------QGHWQIV 1132
Cdd:PHA02989   189 L------------RNDIDVIS----------------IKVIKYLIKKGVNIETNNNGSESVLESFLDnnkilsKKEFKVL 240

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024484393 1133 DLLLTHgADVNMADKQGRTPLMMAASEGHLGTVEFLLAQGASISLMDKEGLTALSWACLKGHLAVV 1198
Cdd:PHA02989   241 NFILKY-IKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDML 305
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 1051-1235 8.19e-03

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: 41.02  E-value: 8.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1051 GYTEIVSYLLDLPEKDEEEVERAQINSFDSLW-GETALTAAAGRGKLDVCRLLLEQGAAV-AQPNRR------------G 1116
Cdd:cd21882     40 GVNEAIMLLLEAAPDSGNPKELVNAPCTDEFYqGQTALHIAIENRNLNLVRLLVENGADVsARATGRffrkspgnlfyfG 119

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024484393 1117 VVPLFSAVRQGHWQIVDLLLTHGAD---VNMADKQGRTPL--MMAASEGHLGTVEFLLAQGASISLMDKegltalswacl 1191
Cdd:cd21882    120 ELPLSLAACTNQEEIVRLLLENGAQpaaLEAQDSLGNTVLhaLVLQADNTPENSAFVCQMYNLLLSYGA----------- 188

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 2024484393 1192 KGHLAVVRALVENgaatdhadKNGRTPLDLAAFYGDAEVVQFLV 1235
Cdd:cd21882    189 HLDPTQQLEEIPN--------HQGLTPLKLAAVEGKIVMFQHIL 224
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 1119-1144 9.14e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 35.70  E-value: 9.14e-03
                           10        20
                   ....*....|....*....|....*.
gi 2024484393 1119 PLFSAVRQGHWQIVDLLLTHGADVNM 1144
Cdd:pfam13606    5 PLHLAARNGRLEIVKLLLENGADINA 30
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 1217-1280 9.95e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 40.72  E-value: 9.95e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024484393 1217 TPLDLAAFYGDAEVVQFLVDHGAMIEHVDYSGMRPLDRAVGCRNTSVVVTLLKKGAKIGCQTLP 1280
Cdd:PHA02874    37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSILPIP 100
 
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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