NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|767950366|ref|XP_011542147|]
View 

poly [ADP-ribose] polymerase tankyrase-1 isoform X1 [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
tankyrase_like cd01438
Tankyrases interact with the telomere reverse transcriptase complex (TERT). Tankyrase 1 ...
1091-1299 2.98e-151

Tankyrases interact with the telomere reverse transcriptase complex (TERT). Tankyrase 1 poly-ADP-ribosylates Telomere Repeat Binding Factor 1 (TRF1) while Tankyrase 2 can poly-ADP-ribosylate itself or TRF1. The tankyrases also contain multiple ankyrin repeats that mediate protein-protein interaction (binding TRF1 and insulin-responsive aminopeptidase) and may function as a complex. Overexpression of Tank1 promotes increased telomere length when overexpressed, while overexpressed Tank2 has been shown to promote PARP cleavage- independent cell death (necrosis).


:

Pssm-ID: 238718 [Multi-domain]  Cd Length: 223  Bit Score: 454.74  E-value: 2.98e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366 1091 QGTNPYLTFHCVNQGTILLDLAPEDKEYQSVEEEMQSTIREHRDGGNAGGIFNRYNVIRIQKVVNKKLRERFCHRQKEVS 1170
Cdd:cd01438     1 QGRNPYLTFHCVNQGTILLDLAPDDKEYQSVEEEMQSTIREHRDGGNAGGIFNRYNIIRIQKVVNKKLRERYCHRQKEIA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366 1171 EENHNHHNERMLFHGSPFINAIIHKGFDERHAYIGGMFGAGIYFAENSSKSNQYVYGIGGGTGCPTHKDRSCYICHRQML 1250
Cdd:cd01438    81 EENHNHHNERMLFHGSPFINAIIHKGFDERHAYIGGMFGAGIYFAENSSKSNQYVYGIGGGTGCPTHKDRSCYVCHRQML 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 767950366 1251 FCRVTLGKSFLQFSTMKMAHAPPGHHSVIGRPSVNGLAYAEYVIYRGEQ 1299
Cdd:cd01438   161 FCRVTLGKSFLQFSAMKMAHAPPGHHSVIGRPSVNGLAYAEYVIYRGEQ 209
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
645-953 2.96e-47

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 171.29  E-value: 2.96e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  645 IRTSDVDYRLLEASKAGDLETVKQLCSSQNVNCRDLEGRHSTPLHFAAGYNRVSVVEYLLHHGADVHAKDKGGLVPLHNA 724
Cdd:COG0666    15 LLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAA 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  725 CSYGHYEVAELLVRHGASVNVADLWKFTPLHEAAAKGKYEICKLLLKHGADPTKKNRDGNtpldlvkegdtdiqdllrgd 804
Cdd:COG0666    95 ARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGN-------------------- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  805 aalldaakkgclarvqklctpenincrdtqgrnsTPLHLAAGYNNLEVAEYLLEHGADVNAQDKGGLIPLHNAASYGHVD 884
Cdd:COG0666   155 ----------------------------------TPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLE 200
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767950366  885 IAALLIKYNTCVNATDKWAFTPLHEAAQKGRTQLCALLLAHGADPTMKNQEGQTPLDLATADDIRALLI 953
Cdd:COG0666   201 IVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVK 269
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
182-504 2.85e-46

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 168.59  E-value: 2.85e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  182 ALRELLEACRNGDVSRVKRLVDAANVNAKDMAGRKSSPLHFAAGFGRKDVVEHLLQMGANVHARDDGGLIPLHNACSFGH 261
Cdd:COG0666    20 LLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGD 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  262 AEVVSLLLCQGADPNARDNWNYTPLHEAAIKGKIDVCIVLLQHGADPNIRNTDGKsaldladpsakavltgeykkdelle 341
Cdd:COG0666   100 LEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGN------------------------- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  342 aarsgneeklmalltplnvnchasdgrksTPLHLAAGYNRVRIVQLLLQHGADVHAKDKGGLVPLHNACSYGHYEVTELL 421
Cdd:COG0666   155 -----------------------------TPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  422 LKHGACVNAMDLWQFTPLHEAASKNRVEVCSLLLSHGADPTLVNCHGKSAVDMAPTPELRERLTYEFKGHSLLQAAREAD 501
Cdd:COG0666   206 LEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDL 285

                  ...
gi 767950366  502 LAK 504
Cdd:COG0666   286 LTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
288-628 2.93e-42

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 157.04  E-value: 2.93e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  288 EAAIKGKIDVCIVLLQHGADPNIRNTDGKSALDLADPSAKAVLTGEYKKDELLEAARSGNEEKLMALLTPLNVNCHASDG 367
Cdd:COG0666     6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  368 RKSTPLHLAAGYNRVRIVQLLLQHGADVHAKDKGGLVPLHNACSYGHYEVTELLLKHGACVNAMDLWQFTPLHEAASKNR 447
Cdd:COG0666    86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  448 VEVCSLLLSHGADPTLVNCHGksavdmaptpelrerltyefkghsllqaareadlakvkktlaleiinfkqpqshETALH 527
Cdd:COG0666   166 LEIVKLLLEAGADVNARDNDG------------------------------------------------------ETPLH 191
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  528 CAVASLHPKrkqVTELLLRKGANVNEKNKDFMTPLHVAAERAHNDVMEVLHKHGAKMNALDTLGQTALHRAALAGHLQTC 607
Cdd:COG0666   192 LAAENGHLE---IVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIV 268
                         330       340
                  ....*....|....*....|.
gi 767950366  608 RLLLSYGSDPSIISLQGFTAA 628
Cdd:COG0666   269 KLLLLALLLLAAALLDLLTLL 289
SAM_tankyrase1,2 cd09524
SAM domain of tankyrase1,2 subfamily; SAM (sterile alpha motif) domain of Tankyrase1,2 ...
1024-1089 1.48e-37

SAM domain of tankyrase1,2 subfamily; SAM (sterile alpha motif) domain of Tankyrase1,2 subfamily is a protein-protein interaction domain. In addition to the SAM domain, proteins of this group have ankyrin repeats and a ADP- ribosyltransferase (poly-(ADP-ribose) synthase) domain. Tankyrases can polymerize through their SAM domains forming homoligomers and these complexes are disrupted by autoribosylation. Tankyrases apparently act as master scaffolding proteins and thus may interact simultaneously with multiple proteins, in particular with TRF1, NuMA, IRAP and Grb14 (ankyrin repeats are involved in these interactions). Tankyrases participate in a variety of cell signaling pathways as effector molecules. Their functions are different depending on the intracellular location: at telomeres they play a role in the regulation of telomere length via control of telomerase access to telomeres, at centrosomes they promote spindle assembly/disassembly, in Golgi vesicles they participate in the regulation of vesicle trafficking and Golgi dynamics. Tankyrase 1 may be of interest as new potential target for telomerase-directed cancer therapy.


:

Pssm-ID: 188923  Cd Length: 66  Bit Score: 135.15  E-value: 1.48e-37
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767950366 1024 VAGLDMNISQFLKSLGLEHLRDIFETEQITLDVLADMGHEELKEIGINAYGHRHKLIKGVERLLGG 1089
Cdd:cd09524     1 VNGTDFSISQFLSSLGLEHLREIFEREQITLDVLAEMGHEELKEIGINAYGHRHKLIKGVERLISG 66
Ank_4 pfam13637
Ankyrin repeats (many copies);
806-857 5.97e-05

Ankyrin repeats (many copies);


:

Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.88  E-value: 5.97e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 767950366   806 ALLDAAKKGCLARVQKL-CTPENINCRDTQGRnsTPLHLAAGYNNLEVAEYLL 857
Cdd:pfam13637    4 ALHAAAASGHLELLRLLlEKGADINAVDGNGE--TALHFAASNGNVEVLKLLL 54
 
Name Accession Description Interval E-value
tankyrase_like cd01438
Tankyrases interact with the telomere reverse transcriptase complex (TERT). Tankyrase 1 ...
1091-1299 2.98e-151

Tankyrases interact with the telomere reverse transcriptase complex (TERT). Tankyrase 1 poly-ADP-ribosylates Telomere Repeat Binding Factor 1 (TRF1) while Tankyrase 2 can poly-ADP-ribosylate itself or TRF1. The tankyrases also contain multiple ankyrin repeats that mediate protein-protein interaction (binding TRF1 and insulin-responsive aminopeptidase) and may function as a complex. Overexpression of Tank1 promotes increased telomere length when overexpressed, while overexpressed Tank2 has been shown to promote PARP cleavage- independent cell death (necrosis).


Pssm-ID: 238718 [Multi-domain]  Cd Length: 223  Bit Score: 454.74  E-value: 2.98e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366 1091 QGTNPYLTFHCVNQGTILLDLAPEDKEYQSVEEEMQSTIREHRDGGNAGGIFNRYNVIRIQKVVNKKLRERFCHRQKEVS 1170
Cdd:cd01438     1 QGRNPYLTFHCVNQGTILLDLAPDDKEYQSVEEEMQSTIREHRDGGNAGGIFNRYNIIRIQKVVNKKLRERYCHRQKEIA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366 1171 EENHNHHNERMLFHGSPFINAIIHKGFDERHAYIGGMFGAGIYFAENSSKSNQYVYGIGGGTGCPTHKDRSCYICHRQML 1250
Cdd:cd01438    81 EENHNHHNERMLFHGSPFINAIIHKGFDERHAYIGGMFGAGIYFAENSSKSNQYVYGIGGGTGCPTHKDRSCYVCHRQML 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 767950366 1251 FCRVTLGKSFLQFSTMKMAHAPPGHHSVIGRPSVNGLAYAEYVIYRGEQ 1299
Cdd:cd01438   161 FCRVTLGKSFLQFSAMKMAHAPPGHHSVIGRPSVNGLAYAEYVIYRGEQ 209
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
645-953 2.96e-47

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 171.29  E-value: 2.96e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  645 IRTSDVDYRLLEASKAGDLETVKQLCSSQNVNCRDLEGRHSTPLHFAAGYNRVSVVEYLLHHGADVHAKDKGGLVPLHNA 724
Cdd:COG0666    15 LLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAA 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  725 CSYGHYEVAELLVRHGASVNVADLWKFTPLHEAAAKGKYEICKLLLKHGADPTKKNRDGNtpldlvkegdtdiqdllrgd 804
Cdd:COG0666    95 ARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGN-------------------- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  805 aalldaakkgclarvqklctpenincrdtqgrnsTPLHLAAGYNNLEVAEYLLEHGADVNAQDKGGLIPLHNAASYGHVD 884
Cdd:COG0666   155 ----------------------------------TPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLE 200
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767950366  885 IAALLIKYNTCVNATDKWAFTPLHEAAQKGRTQLCALLLAHGADPTMKNQEGQTPLDLATADDIRALLI 953
Cdd:COG0666   201 IVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVK 269
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
182-504 2.85e-46

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 168.59  E-value: 2.85e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  182 ALRELLEACRNGDVSRVKRLVDAANVNAKDMAGRKSSPLHFAAGFGRKDVVEHLLQMGANVHARDDGGLIPLHNACSFGH 261
Cdd:COG0666    20 LLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGD 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  262 AEVVSLLLCQGADPNARDNWNYTPLHEAAIKGKIDVCIVLLQHGADPNIRNTDGKsaldladpsakavltgeykkdelle 341
Cdd:COG0666   100 LEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGN------------------------- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  342 aarsgneeklmalltplnvnchasdgrksTPLHLAAGYNRVRIVQLLLQHGADVHAKDKGGLVPLHNACSYGHYEVTELL 421
Cdd:COG0666   155 -----------------------------TPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  422 LKHGACVNAMDLWQFTPLHEAASKNRVEVCSLLLSHGADPTLVNCHGKSAVDMAPTPELRERLTYEFKGHSLLQAAREAD 501
Cdd:COG0666   206 LEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDL 285

                  ...
gi 767950366  502 LAK 504
Cdd:COG0666   286 LTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
288-628 2.93e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 157.04  E-value: 2.93e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  288 EAAIKGKIDVCIVLLQHGADPNIRNTDGKSALDLADPSAKAVLTGEYKKDELLEAARSGNEEKLMALLTPLNVNCHASDG 367
Cdd:COG0666     6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  368 RKSTPLHLAAGYNRVRIVQLLLQHGADVHAKDKGGLVPLHNACSYGHYEVTELLLKHGACVNAMDLWQFTPLHEAASKNR 447
Cdd:COG0666    86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  448 VEVCSLLLSHGADPTLVNCHGksavdmaptpelrerltyefkghsllqaareadlakvkktlaleiinfkqpqshETALH 527
Cdd:COG0666   166 LEIVKLLLEAGADVNARDNDG------------------------------------------------------ETPLH 191
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  528 CAVASLHPKrkqVTELLLRKGANVNEKNKDFMTPLHVAAERAHNDVMEVLHKHGAKMNALDTLGQTALHRAALAGHLQTC 607
Cdd:COG0666   192 LAAENGHLE---IVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIV 268
                         330       340
                  ....*....|....*....|.
gi 767950366  608 RLLLSYGSDPSIISLQGFTAA 628
Cdd:COG0666   269 KLLLLALLLLAAALLDLLTLL 289
SAM_tankyrase1,2 cd09524
SAM domain of tankyrase1,2 subfamily; SAM (sterile alpha motif) domain of Tankyrase1,2 ...
1024-1089 1.48e-37

SAM domain of tankyrase1,2 subfamily; SAM (sterile alpha motif) domain of Tankyrase1,2 subfamily is a protein-protein interaction domain. In addition to the SAM domain, proteins of this group have ankyrin repeats and a ADP- ribosyltransferase (poly-(ADP-ribose) synthase) domain. Tankyrases can polymerize through their SAM domains forming homoligomers and these complexes are disrupted by autoribosylation. Tankyrases apparently act as master scaffolding proteins and thus may interact simultaneously with multiple proteins, in particular with TRF1, NuMA, IRAP and Grb14 (ankyrin repeats are involved in these interactions). Tankyrases participate in a variety of cell signaling pathways as effector molecules. Their functions are different depending on the intracellular location: at telomeres they play a role in the regulation of telomere length via control of telomerase access to telomeres, at centrosomes they promote spindle assembly/disassembly, in Golgi vesicles they participate in the regulation of vesicle trafficking and Golgi dynamics. Tankyrase 1 may be of interest as new potential target for telomerase-directed cancer therapy.


Pssm-ID: 188923  Cd Length: 66  Bit Score: 135.15  E-value: 1.48e-37
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767950366 1024 VAGLDMNISQFLKSLGLEHLRDIFETEQITLDVLADMGHEELKEIGINAYGHRHKLIKGVERLLGG 1089
Cdd:cd09524     1 VNGTDFSISQFLSSLGLEHLREIFEREQITLDVLAEMGHEELKEIGINAYGHRHKLIKGVERLISG 66
PHA03095 PHA03095
ankyrin-like protein; Provisional
652-976 3.20e-33

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 135.15  E-value: 3.20e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  652 YRLLEASKAGDLETVKQLCS-SQNVNCRDLEGRhsTPLHFAAGYN---RVSVVEYLLHHGADVHAKDKGGLVPLH----N 723
Cdd:PHA03095   16 YDYLLNASNVTVEEVRRLLAaGADVNFRGEYGK--TPLHLYLHYSsekVKDIVRLLLEAGADVNAPERCGFTPLHlylyN 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  724 ACSYghyEVAELLVRHGASVNVADLWKFTPLHeAAAKGK---YEICKLLLKHGADPTKKNRDGNTPLD-LVKEGDTDIqD 799
Cdd:PHA03095   94 ATTL---DVIKLLIKAGADVNAKDKVGRTPLH-VYLSGFninPKVIRLLLRKGADVNALDLYGMTPLAvLLKSRNANV-E 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  800 LLRgdaALLDAakkGClarvqklctpeniNCRDTQGRNSTPLHLAAGY--NNLEVAEYLLEHGADVNAQDKGGLIPLHNA 877
Cdd:PHA03095  169 LLR---LLIDA---GA-------------DVYAVDDRFRSLLHHHLQSfkPRARIVRELIRAGCDPAATDMLGNTPLHSM 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  878 ASYG---HVDIAALLIKyNTCVNATDKWAFTPLHEAAQKGRTQLCALLLAHGADPTMKNQEGQTPLDLATAD-DIRALli 953
Cdd:PHA03095  230 ATGSsckRSLVLPLLIA-GISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNnNGRAV-- 306
                         330       340
                  ....*....|....*....|...
gi 767950366  954 DAmppeALPTcfKPQATVVSASL 976
Cdd:PHA03095  307 RA----ALAK--NPSAETVAATL 323
PHA02876 PHA02876
ankyrin repeat protein; Provisional
231-616 4.98e-32

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 134.42  E-value: 4.98e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  231 VVEHLLQMGANVHARDDGGLIPLHNACSFGHAEVVSLLLCQGADPNARDNWNYTPLHEAAIKGKIDVCIVLLQHGADPN- 309
Cdd:PHA02876  160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINk 239
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  310 --------IRNTDGKSALDLADPSAKAVLTGEYKKDELLEAARSGNEEKLMALLTPLNVNCHASDGRKSTPLHLAA--GY 379
Cdd:PHA02876  240 ndlsllkaIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAknGY 319
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  380 NRVRIvQLLLQHGADVHAKDKGGLVPLHNACSYGHYEVTEL-LLKHGACVNAMDLWQFTPLHEAASKNRVEVCSLLLSHG 458
Cdd:PHA02876  320 DTENI-RTLIMLGADVNAADRLYITPLHQASTLDRNKDIVItLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYG 398
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  459 ADptlvnchgksavdmaptpelrerltyefkghsllqaareadlakvkktlaLEIINfkqpQSHETALHCAVASLHPKRK 538
Cdd:PHA02876  399 AD--------------------------------------------------IEALS----QKIGTALHFALCGTNPYMS 424
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767950366  539 QVTelLLRKGANVNEKNKDFMTPLHVAAER-AHNDVMEVLHKHGAKMNALDTLGQTALHRAalAGHLQTCRLLLSYGSD 616
Cdd:PHA02876  425 VKT--LIDRGANVNSKNKDLSTPLHYACKKnCKLDVIEMLLDNGADVNAINIQNQYPLLIA--LEYHGIVNILLHYGAE 499
PHA02876 PHA02876
ankyrin repeat protein; Provisional
417-810 7.52e-28

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 121.32  E-value: 7.52e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  417 VTELLLKHGACVNAMDLWQFTPLHEAASKNRVEVCSLLLSHGADPTLVNCHGKSAVDMAPTPE--------LRERLTYEF 488
Cdd:PHA02876  160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKnidtikaiIDNRSNINK 239
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  489 KGHSLLQAAREADLakvKKTLALEIINFKQPQ---SHETALHCAVASlhPKRKQVTELLLRKGANVNEKNKDFMTPLHVA 565
Cdd:PHA02876  240 NDLSLLKAIRNEDL---ETSLLLYDAGFSVNSiddCKNTPLHHASQA--PSLSRLVPKLLERGADVNAKNIKGETPLYLM 314
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  566 AERAHN-DVMEVLHKHGAKMNALDTLGQTALHRAalaghlqtcrlllsygsdpsiislqgftaaqmgneavqqilseSTP 644
Cdd:PHA02876  315 AKNGYDtENIRTLIMLGADVNAADRLYITPLHQA-------------------------------------------STL 351
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  645 IRTSDVDYRLLEASKagdletvkqlcssqNVNCRDLEGRhsTPLHFAAGYNRVSVVEYLLHHGADVHAKDKGGLVPLHNA 724
Cdd:PHA02876  352 DRNKDIVITLLELGA--------------NVNARDYCDK--TPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFA 415
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  725 -CSYGHYEVAELLVRHGASVNVADLWKFTPLHEAAAKG-KYEICKLLLKHGADPTKKNRDGNTPLDLVKEGDTDIQDLLR 802
Cdd:PHA02876  416 lCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIALEYHGIVNILLH 495

                  ....*...
gi 767950366  803 GDAALLDA 810
Cdd:PHA02876  496 YGAELRDS 503
PHA03095 PHA03095
ankyrin-like protein; Provisional
337-628 4.69e-26

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 113.58  E-value: 4.69e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  337 DELLEAARSGNEEKLMALLTPLNVNChaSDGRKSTPLHLAAGYN---RVRIVQLLLQHGADVHAKDKGGLVPLH----NA 409
Cdd:PHA03095   17 DYLLNASNVTVEEVRRLLAAGADVNF--RGEYGKTPLHLYLHYSsekVKDIVRLLLEAGADVNAPERCGFTPLHlylyNA 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  410 CSYghyEVTELLLKHGACVNAMDLWQFTPLHE-AASKN-RVEVCSLLLSHGADPTLVNCHGKSAVDM-----APTPELRE 482
Cdd:PHA03095   95 TTL---DVIKLLIKAGADVNAKDKVGRTPLHVyLSGFNiNPKVIRLLLRKGADVNALDLYGMTPLAVllksrNANVELLR 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  483 RLtyefkghsllqaareadLAKVKKTLALEIINFkqpqsheTALHCAVASLHPkRKQVTELLLRKGANVNEKNKDFMTPL 562
Cdd:PHA03095  172 LL-----------------IDAGADVYAVDDRFR-------SLLHHHLQSFKP-RARIVRELIRAGCDPAATDMLGNTPL 226
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767950366  563 HVAA--ERAHNDVMEVLHKHGAKMNALDTLGQTALHRAALAGHLQTCRLLLSYGSDPSIISLQGFTAA 628
Cdd:PHA03095  227 HSMAtgSSCKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPL 294
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
1116-1300 6.75e-23

Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the covalent attachment of ADP-ribose units from NAD+ to itself and to a limited number of other DNA binding proteins, which decreases their affinity for DNA. Poly(ADP-ribose) polymerase is a regulatory component induced by DNA damage. The carboxyl-terminal region is the most highly conserved region of the protein. Experiments have shown that a carboxyl 40 kDa fragment is still catalytically active.


Pssm-ID: 395519 [Multi-domain]  Cd Length: 195  Bit Score: 97.79  E-value: 6.75e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  1116 KEYQSVEEEMQSTirehRDGGNAGGIFnrynVIRIQKVVNKKLRERFChrqkevseENHNHHNERMLFHGSP--FINAII 1193
Cdd:pfam00644    2 EEYQIIEKYFLST----HDPTHGYPLF----ILEIFRVQRDGEWERFQ--------PKKKLRNRRLLWHGSRltNFLGIL 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  1194 HKGF--DERHAYIGG-MFGAGIYFAENSSKSNQYvygigggtgCPTHKDRScyicHRQMLFCRVTLGKSFLQFSTMKMAH 1270
Cdd:pfam00644   66 SQGLriAPPEAPVTGyMFGKGIYFADDASKSANY---------CPPSEAHG----NGLMLLSEVALGDMNELKKADYAEK 132
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 767950366  1271 APPGHHSVIG------------------RPSVNG-----LAYAEYVIYRGEQV 1300
Cdd:pfam00644  133 LPPGKHSVKGlgktapesfvdldgvplgKLVATGydssvLLYNEYVVYNVNQV 185
Ank_2 pfam12796
Ankyrin repeats (3 copies);
841-933 1.53e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 90.18  E-value: 1.53e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366   841 LHLAAGYNNLEVAEYLLEHGADVNAQDKGGLIPLHNAASYGHVDIAALLIKYNTCVNATDKWafTPLHEAAQKGRTQLCA 920
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGR--TALHYAARSGHLEIVK 78
                           90
                   ....*....|...
gi 767950366   921 LLLAHGADPTMKN 933
Cdd:pfam12796   79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
220-312 4.02e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 89.02  E-value: 4.02e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366   220 LHFAAGFGRKDVVEHLLQMGANVHARDDGGLIPLHNACSFGHAEVVSLLLcQGADPNARDNwNYTPLHEAAIKGKIDVCI 299
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKDN-GRTALHYAARSGHLEIVK 78
                           90
                   ....*....|...
gi 767950366   300 VLLQHGADPNIRN 312
Cdd:pfam12796   79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
526-619 1.79e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.14  E-value: 1.79e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366   526 LHCAVASlhpKRKQVTELLLRKGANVNEKNKDFMTPLHVAAERAHNDVMEVLHKHGAKMNALDtlGQTALHRAALAGHLQ 605
Cdd:pfam12796    1 LHLAAKN---GNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN--GRTALHYAARSGHLE 75
                           90
                   ....*....|....
gi 767950366   606 TCRLLLSYGSDPSI 619
Cdd:pfam12796   76 IVKLLLEKGADINV 89
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
1030-1087 5.47e-14

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 67.68  E-value: 5.47e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 767950366  1030 NISQFLKSLGLEHLRDIFETEQIT-LDVLADMGHEELKEIGINAYGHRHKLIKGVERLL 1087
Cdd:pfam07647    8 SVADWLRSIGLEQYTDNFRDQGITgAELLLRLTLEDLKRLGITSVGHRRKILKKIQELK 66
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
1030-1087 3.23e-12

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735  Cd Length: 68  Bit Score: 62.70  E-value: 3.23e-12
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 767950366   1030 NISQFLKSLGLEHLRDIFETEQIT-LDVLADMGHEELKEIGINAYGHRHKLIKGVERLL 1087
Cdd:smart00454    8 SVADWLESIGLEQYADNFRKNGIDgALLLLLTSEEDLKELGITKLGHRKKILKAIQKLK 66
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
752-946 4.14e-11

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: 67.35  E-value: 4.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  752 TPLHEAAAKGKYE-ICKLLLKHGADPTKKNRDGNTPLDLVKEGDTDiqdllrgDAA--LLDAAkkgclarvqklctPENI 828
Cdd:cd22192    19 SPLLLAAKENDVQaIKKLLKCPSCDLFQRGALGETALHVAALYDNL-------EAAvvLMEAA-------------PELV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  829 NCRDT----QGRnsTPLHLAAGYNNLEVAEYLLEHGADVNA---------QDKGGLI-----PLHNAASYGHVDIAALLI 890
Cdd:cd22192    79 NEPMTsdlyQGE--TALHIAVVNQNLNLVRELIARGADVVSpratgtffrPGPKNLIyygehPLSFAACVGNEEIVRLLI 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767950366  891 KYNTCVNATDKWAFTPLH----EAAQKGRTQLCALLLAhgADP--------TMKNQEGQTPLDLATAD 946
Cdd:cd22192   157 EHGADIRAQDSLGNTVLHilvlQPNKTFACQMYDLILS--YDKeddlqpldLVPNNQGLTPFKLAAKE 222
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
729-944 1.90e-08

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: 58.94  E-value: 1.90e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366   729 HYEVAELLVRHGASVNVADlwkfTPLHeAAAKGKYEICKLLLKHgadpTKKNRDGNTPLDLVKEGDTDiqDLLRGdaall 808
Cdd:TIGR00870   65 NLELTELLLNLSCRGAVGD----TLLH-AISLEYVDAVEAILLH----LLAAFRKSGPLELANDQYTS--EFTPG----- 128
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366   809 daakkgclarvqklctpenincrdtqgrnSTPLHLAAGYNNLEVAEYLLEHGADVNAQDKG--------------GLIPL 874
Cdd:TIGR00870  129 -----------------------------ITALHLAAHRQNYEIVKLLLERGASVPARACGdffvksqgvdsfyhGESPL 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366   875 HNAASYGHVDIAALLIKYNTCVNATDKWAFTPLHEAA---------QKGRTQLCALLLAHGA--DPTMK-----NQEGQT 938
Cdd:TIGR00870  180 NAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVmenefkaeyEELSCQMYNFALSLLDklRDSKElevilNHQGLT 259

                   ....*.
gi 767950366   939 PLDLAT 944
Cdd:TIGR00870  260 PLKLAA 265
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
284-440 3.78e-08

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 57.72  E-value: 3.78e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  284 TPLHEAAIKGKID-VCIVLLQHGADPNIRNTDGKSALDLAdpsakaVLtgeYKKDE----LLEAARsgneeklmallTPL 358
Cdd:cd22192    19 SPLLLAAKENDVQaIKKLLKCPSCDLFQRGALGETALHVA------AL---YDNLEaavvLMEAAP-----------ELV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  359 NVNCHASDGRKSTPLHLAAGYNRVRIVQLLLQHGADVHA---------KDKGGLV-----PLHNACSYGHYEVTELLLKH 424
Cdd:cd22192    79 NEPMTSDLYQGETALHIAVVNQNLNLVRELIARGADVVSpratgtffrPGPKNLIyygehPLSFAACVGNEEIVRLLIEH 158
                         170
                  ....*....|....*.
gi 767950366  425 GACVNAMDLWQFTPLH 440
Cdd:cd22192   159 GADIRAQDSLGNTVLH 174
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
437-705 1.40e-07

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: 55.79  E-value: 1.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  437 TPLHEAASKNRVE-VCSLLLSHGADPTLVNCHGKSAVDMAPTPELRERLTYefkghsLLQAAREadLAKVKKTLALeiin 515
Cdd:cd22192    19 SPLLLAAKENDVQaIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVV------LMEAAPE--LVNEPMTSDL---- 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  516 fkqpQSHETALHCAVASlhpKRKQVTELLLRKGANV------------NEKNKDFMT--PLHVAAERAHNDVMEVLHKHG 581
Cdd:cd22192    87 ----YQGETALHIAVVN---QNLNLVRELIARGADVvspratgtffrpGPKNLIYYGehPLSFAACVGNEEIVRLLIEHG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  582 AKMNALDTLGQTALHRAAL-AGHLQTCR---LLLSYGSDPSIISL------QGFT----AAQMGN-EAVQQILS------ 640
Cdd:cd22192   160 ADIRAQDSLGNTVLHILVLqPNKTFACQmydLILSYDKEDDLQPLdlvpnnQGLTpfklAAKEGNiVMFQHLVQkrrhiq 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  641 -----------ESTPIRTSDVDYRLLE---------ASKAGDLETVKQLCSSQnvncRDLEGRHstplhfaagYNRVSVV 700
Cdd:cd22192   240 wtygpltstlyDLTEIDSWGDEQSVLElivsskkreARKILDVTPVKELVSLK----WKRYGRP---------YFRILAL 306

                  ....*
gi 767950366  701 EYLLH 705
Cdd:cd22192   307 LYLLY 311
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
839-865 1.86e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.57  E-value: 1.86e-05
                            10        20
                    ....*....|....*....|....*..
gi 767950366    839 TPLHLAAGYNNLEVAEYLLEHGADVNA 865
Cdd:smart00248    4 TPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
371-459 5.09e-05

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 47.77  E-value: 5.09e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366   371 TPLHLAAGYNRVRIVQLLLQHGADVHAKDKGGLV---PLHNACSYGHY-----------EVTELLLKHGACVNAMDLWQF 436
Cdd:TIGR00870  130 TALHLAAHRQNYEIVKLLLERGASVPARACGDFFvksQGVDSFYHGESplnaaaclgspSIVALLSEDPADILTADSLGN 209
                           90       100       110
                   ....*....|....*....|....*....|..
gi 767950366   437 TPLH------EAASKNRVEVCS---LLLSHGA 459
Cdd:TIGR00870  210 TLLHllvmenEFKAEYEELSCQmynFALSLLD 241
Ank_4 pfam13637
Ankyrin repeats (many copies);
806-857 5.97e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.88  E-value: 5.97e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 767950366   806 ALLDAAKKGCLARVQKL-CTPENINCRDTQGRnsTPLHLAAGYNNLEVAEYLL 857
Cdd:pfam13637    4 ALHAAAASGHLELLRLLlEKGADINAVDGNGE--TALHFAASNGNVEVLKLLL 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
282-310 3.46e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.11  E-value: 3.46e-04
                            10        20
                    ....*....|....*....|....*....
gi 767950366    282 NYTPLHEAAIKGKIDVCIVLLQHGADPNI 310
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
557-586 2.86e-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: 36.41  E-value: 2.86e-03
                            10        20        30
                    ....*....|....*....|....*....|
gi 767950366    557 DFMTPLHVAAERAHNDVMEVLHKHGAKMNA 586
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
tankyrase_like cd01438
Tankyrases interact with the telomere reverse transcriptase complex (TERT). Tankyrase 1 ...
1091-1299 2.98e-151

Tankyrases interact with the telomere reverse transcriptase complex (TERT). Tankyrase 1 poly-ADP-ribosylates Telomere Repeat Binding Factor 1 (TRF1) while Tankyrase 2 can poly-ADP-ribosylate itself or TRF1. The tankyrases also contain multiple ankyrin repeats that mediate protein-protein interaction (binding TRF1 and insulin-responsive aminopeptidase) and may function as a complex. Overexpression of Tank1 promotes increased telomere length when overexpressed, while overexpressed Tank2 has been shown to promote PARP cleavage- independent cell death (necrosis).


Pssm-ID: 238718 [Multi-domain]  Cd Length: 223  Bit Score: 454.74  E-value: 2.98e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366 1091 QGTNPYLTFHCVNQGTILLDLAPEDKEYQSVEEEMQSTIREHRDGGNAGGIFNRYNVIRIQKVVNKKLRERFCHRQKEVS 1170
Cdd:cd01438     1 QGRNPYLTFHCVNQGTILLDLAPDDKEYQSVEEEMQSTIREHRDGGNAGGIFNRYNIIRIQKVVNKKLRERYCHRQKEIA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366 1171 EENHNHHNERMLFHGSPFINAIIHKGFDERHAYIGGMFGAGIYFAENSSKSNQYVYGIGGGTGCPTHKDRSCYICHRQML 1250
Cdd:cd01438    81 EENHNHHNERMLFHGSPFINAIIHKGFDERHAYIGGMFGAGIYFAENSSKSNQYVYGIGGGTGCPTHKDRSCYVCHRQML 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 767950366 1251 FCRVTLGKSFLQFSTMKMAHAPPGHHSVIGRPSVNGLAYAEYVIYRGEQ 1299
Cdd:cd01438   161 FCRVTLGKSFLQFSAMKMAHAPPGHHSVIGRPSVNGLAYAEYVIYRGEQ 209
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
645-953 2.96e-47

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 171.29  E-value: 2.96e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  645 IRTSDVDYRLLEASKAGDLETVKQLCSSQNVNCRDLEGRHSTPLHFAAGYNRVSVVEYLLHHGADVHAKDKGGLVPLHNA 724
Cdd:COG0666    15 LLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAA 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  725 CSYGHYEVAELLVRHGASVNVADLWKFTPLHEAAAKGKYEICKLLLKHGADPTKKNRDGNtpldlvkegdtdiqdllrgd 804
Cdd:COG0666    95 ARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGN-------------------- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  805 aalldaakkgclarvqklctpenincrdtqgrnsTPLHLAAGYNNLEVAEYLLEHGADVNAQDKGGLIPLHNAASYGHVD 884
Cdd:COG0666   155 ----------------------------------TPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLE 200
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767950366  885 IAALLIKYNTCVNATDKWAFTPLHEAAQKGRTQLCALLLAHGADPTMKNQEGQTPLDLATADDIRALLI 953
Cdd:COG0666   201 IVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVK 269
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
182-504 2.85e-46

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 168.59  E-value: 2.85e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  182 ALRELLEACRNGDVSRVKRLVDAANVNAKDMAGRKSSPLHFAAGFGRKDVVEHLLQMGANVHARDDGGLIPLHNACSFGH 261
Cdd:COG0666    20 LLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGD 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  262 AEVVSLLLCQGADPNARDNWNYTPLHEAAIKGKIDVCIVLLQHGADPNIRNTDGKsaldladpsakavltgeykkdelle 341
Cdd:COG0666   100 LEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGN------------------------- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  342 aarsgneeklmalltplnvnchasdgrksTPLHLAAGYNRVRIVQLLLQHGADVHAKDKGGLVPLHNACSYGHYEVTELL 421
Cdd:COG0666   155 -----------------------------TPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  422 LKHGACVNAMDLWQFTPLHEAASKNRVEVCSLLLSHGADPTLVNCHGKSAVDMAPTPELRERLTYEFKGHSLLQAAREAD 501
Cdd:COG0666   206 LEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDL 285

                  ...
gi 767950366  502 LAK 504
Cdd:COG0666   286 LTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
686-955 1.04e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 158.19  E-value: 1.04e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  686 TPLHFAAGYNRVSVVEYLLHHGADVHAKDKGGLVPLHNACSYGHYEVAELLVRHGASVNVADLWKFTPLHEAAAKGKYEI 765
Cdd:COG0666    23 LLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEI 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  766 CKLLLKHGADPTKKNRDGNTPLdlvkegdtdiqdllrgdaalldaakkgclarvqklctpenincrdtqgrnstplHLAA 845
Cdd:COG0666   103 VKLLLEAGADVNARDKDGETPL------------------------------------------------------HLAA 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  846 GYNNLEVAEYLLEHGADVNAQDKGGLIPLHNAASYGHVDIAALLIKYNTCVNATDKWAFTPLHEAAQKGRTQLCALLLAH 925
Cdd:COG0666   129 YNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA 208
                         250       260       270
                  ....*....|....*....|....*....|...
gi 767950366  926 GADPTMKNQEGQTPLDLATA---DDIRALLIDA 955
Cdd:COG0666   209 GADVNAKDNDGKTALDLAAEngnLEIVKLLLEA 241
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
288-628 2.93e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 157.04  E-value: 2.93e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  288 EAAIKGKIDVCIVLLQHGADPNIRNTDGKSALDLADPSAKAVLTGEYKKDELLEAARSGNEEKLMALLTPLNVNCHASDG 367
Cdd:COG0666     6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  368 RKSTPLHLAAGYNRVRIVQLLLQHGADVHAKDKGGLVPLHNACSYGHYEVTELLLKHGACVNAMDLWQFTPLHEAASKNR 447
Cdd:COG0666    86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  448 VEVCSLLLSHGADPTLVNCHGksavdmaptpelrerltyefkghsllqaareadlakvkktlaleiinfkqpqshETALH 527
Cdd:COG0666   166 LEIVKLLLEAGADVNARDNDG------------------------------------------------------ETPLH 191
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  528 CAVASLHPKrkqVTELLLRKGANVNEKNKDFMTPLHVAAERAHNDVMEVLHKHGAKMNALDTLGQTALHRAALAGHLQTC 607
Cdd:COG0666   192 LAAENGHLE---IVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIV 268
                         330       340
                  ....*....|....*....|.
gi 767950366  608 RLLLSYGSDPSIISLQGFTAA 628
Cdd:COG0666   269 KLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
542-874 4.29e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 156.27  E-value: 4.29e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  542 ELLLRKGANVNEKNKDFMTPLHVAAERAHNDVMEVLHKHGAKMNALDTLGQTALHRAALAGHLQTCRLLLSYGSDPSIIS 621
Cdd:COG0666     5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  622 LQGFTAaqmgneavqqilsestpirtsdvdyrLLEASKAGDLETVKQLCSSQ-NVNCRDLEGRhsTPLHFAAGYNRVSVV 700
Cdd:COG0666    85 DGGNTL--------------------------LHAAARNGDLEIVKLLLEAGaDVNARDKDGE--TPLHLAAYNGNLEIV 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  701 EYLLHHGADVHAKDKGGLVPLHNACSYGHYEVAELLVRHGASVNVADLWKFTPLHEAAAKGKYEICKLLLKHGADPTKKN 780
Cdd:COG0666   137 KLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKD 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  781 RDGNTPLDL-VKEGDTDIQDLLRGDAALLDAAKKgclarvqklctpenincrdtqgRNSTPLHLAAGYNNLEVAEYLLEH 859
Cdd:COG0666   217 NDGKTALDLaAENGNLEIVKLLLEAGADLNAKDK----------------------DGLTALLLAAAAGAALIVKLLLLA 274
                         330
                  ....*....|....*
gi 767950366  860 GADVNAQDKGGLIPL 874
Cdd:COG0666   275 LLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
201-559 1.59e-40

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 151.65  E-value: 1.59e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  201 LVDAANVNAKDMAGRKSSPLHFAAGFGRKDVVEHLLQMGANVHARDDGGLIPLHNACSFGHAEVVSLLLCQGADPNARDN 280
Cdd:COG0666     6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  281 WNYTPLHEAAIKGKIDVCIVLLQHGADPNIRNTDGKsaldladpsakavltgeykkdelleaarsgneeklmalltplnv 360
Cdd:COG0666    86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGE-------------------------------------------- 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  361 nchasdgrksTPLHLAAGYNRVRIVQLLLQHGADVHAKDKGGLVPLHNACSYGHYEVTELLLKHGACVNAMDLWQFTPLH 440
Cdd:COG0666   122 ----------TPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLH 191
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  441 EAASKNRVEVCSLLLSHGADPTLVNCHGKSAVDMaptpelrerltyefkghsllqAAREADLAKVKKTLALEIINFKQPQ 520
Cdd:COG0666   192 LAAENGHLEIVKLLLEAGADVNAKDNDGKTALDL---------------------AAENGNLEIVKLLLEAGADLNAKDK 250
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 767950366  521 SHETALHCAVASLHPKRKQVTELLLRKGANVNEKNKDFM 559
Cdd:COG0666   251 DGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
SAM_tankyrase1,2 cd09524
SAM domain of tankyrase1,2 subfamily; SAM (sterile alpha motif) domain of Tankyrase1,2 ...
1024-1089 1.48e-37

SAM domain of tankyrase1,2 subfamily; SAM (sterile alpha motif) domain of Tankyrase1,2 subfamily is a protein-protein interaction domain. In addition to the SAM domain, proteins of this group have ankyrin repeats and a ADP- ribosyltransferase (poly-(ADP-ribose) synthase) domain. Tankyrases can polymerize through their SAM domains forming homoligomers and these complexes are disrupted by autoribosylation. Tankyrases apparently act as master scaffolding proteins and thus may interact simultaneously with multiple proteins, in particular with TRF1, NuMA, IRAP and Grb14 (ankyrin repeats are involved in these interactions). Tankyrases participate in a variety of cell signaling pathways as effector molecules. Their functions are different depending on the intracellular location: at telomeres they play a role in the regulation of telomere length via control of telomerase access to telomeres, at centrosomes they promote spindle assembly/disassembly, in Golgi vesicles they participate in the regulation of vesicle trafficking and Golgi dynamics. Tankyrase 1 may be of interest as new potential target for telomerase-directed cancer therapy.


Pssm-ID: 188923  Cd Length: 66  Bit Score: 135.15  E-value: 1.48e-37
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767950366 1024 VAGLDMNISQFLKSLGLEHLRDIFETEQITLDVLADMGHEELKEIGINAYGHRHKLIKGVERLLGG 1089
Cdd:cd09524     1 VNGTDFSISQFLSSLGLEHLREIFEREQITLDVLAEMGHEELKEIGINAYGHRHKLIKGVERLISG 66
PHA03095 PHA03095
ankyrin-like protein; Provisional
652-976 3.20e-33

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 135.15  E-value: 3.20e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  652 YRLLEASKAGDLETVKQLCS-SQNVNCRDLEGRhsTPLHFAAGYN---RVSVVEYLLHHGADVHAKDKGGLVPLH----N 723
Cdd:PHA03095   16 YDYLLNASNVTVEEVRRLLAaGADVNFRGEYGK--TPLHLYLHYSsekVKDIVRLLLEAGADVNAPERCGFTPLHlylyN 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  724 ACSYghyEVAELLVRHGASVNVADLWKFTPLHeAAAKGK---YEICKLLLKHGADPTKKNRDGNTPLD-LVKEGDTDIqD 799
Cdd:PHA03095   94 ATTL---DVIKLLIKAGADVNAKDKVGRTPLH-VYLSGFninPKVIRLLLRKGADVNALDLYGMTPLAvLLKSRNANV-E 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  800 LLRgdaALLDAakkGClarvqklctpeniNCRDTQGRNSTPLHLAAGY--NNLEVAEYLLEHGADVNAQDKGGLIPLHNA 877
Cdd:PHA03095  169 LLR---LLIDA---GA-------------DVYAVDDRFRSLLHHHLQSfkPRARIVRELIRAGCDPAATDMLGNTPLHSM 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  878 ASYG---HVDIAALLIKyNTCVNATDKWAFTPLHEAAQKGRTQLCALLLAHGADPTMKNQEGQTPLDLATAD-DIRALli 953
Cdd:PHA03095  230 ATGSsckRSLVLPLLIA-GISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNnNGRAV-- 306
                         330       340
                  ....*....|....*....|...
gi 767950366  954 DAmppeALPTcfKPQATVVSASL 976
Cdd:PHA03095  307 RA----ALAK--NPSAETVAATL 323
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
186-352 7.34e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 129.69  E-value: 7.34e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  186 LLEACRNGDVSRVKRLVDA-ANVNAKDMAGRksSPLHFAAGFGRKDVVEHLLQMGANVHARDDGGLIPLHNACSFGHAEV 264
Cdd:COG0666   124 LHLAAYNGNLEIVKLLLEAgADVNAQDNDGN--TPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEI 201
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  265 VSLLLCQGADPNARDNWNYTPLHEAAIKGKIDVCIVLLQHGADPNIRNTDGKSALDLADPSAKAVLTGEYKKDELLEAAR 344
Cdd:COG0666   202 VKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAA 281

                  ....*...
gi 767950366  345 SGNEEKLM 352
Cdd:COG0666   282 LLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
349-787 1.13e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 128.92  E-value: 1.13e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  349 EKLMALLTPLNVNCHASDGRKSTPLHLAAGYNRVRIVQLLLQHGADVHAKDKGGLVPLHNACSYGHYEVTELLLKHGACV 428
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  429 NAMDLWQFTPLHEAASKNRVEVCSLLLSHGADptlvnchgksavdmaptpelrerltyefkghsllqaareadlakvkkt 508
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGAD------------------------------------------------ 112
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  509 laleiinfkqpqshetalhcavaslhpkrkqvtelllrkganVNEKNKDFMTPLHVAAERAHNDVMEVLHKHGAKMNALD 588
Cdd:COG0666   113 ------------------------------------------VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQD 150
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  589 TLGQTALHRAALAGHLQTCRLLLSYGSDpsiislqgftaaqmgneavqqilsestpirtsdvdyrlleaskagdletvkq 668
Cdd:COG0666   151 NDGNTPLHLAAANGNLEIVKLLLEAGAD---------------------------------------------------- 178
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  669 lcssqnVNCRDLEGRhsTPLHFAAGYNRVSVVEYLLHHGADVHAKDKGGLVPLHNACSYGHYEVAELLVRHGASVNVADL 748
Cdd:COG0666   179 ------VNARDNDGE--TPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250
                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 767950366  749 WKFTPLHEAAAKGKYEICKLLLKHGADPTKKNRDGNTPL 787
Cdd:COG0666   251 DGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA02876 PHA02876
ankyrin repeat protein; Provisional
231-616 4.98e-32

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 134.42  E-value: 4.98e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  231 VVEHLLQMGANVHARDDGGLIPLHNACSFGHAEVVSLLLCQGADPNARDNWNYTPLHEAAIKGKIDVCIVLLQHGADPN- 309
Cdd:PHA02876  160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINk 239
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  310 --------IRNTDGKSALDLADPSAKAVLTGEYKKDELLEAARSGNEEKLMALLTPLNVNCHASDGRKSTPLHLAA--GY 379
Cdd:PHA02876  240 ndlsllkaIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAknGY 319
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  380 NRVRIvQLLLQHGADVHAKDKGGLVPLHNACSYGHYEVTEL-LLKHGACVNAMDLWQFTPLHEAASKNRVEVCSLLLSHG 458
Cdd:PHA02876  320 DTENI-RTLIMLGADVNAADRLYITPLHQASTLDRNKDIVItLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYG 398
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  459 ADptlvnchgksavdmaptpelrerltyefkghsllqaareadlakvkktlaLEIINfkqpQSHETALHCAVASLHPKRK 538
Cdd:PHA02876  399 AD--------------------------------------------------IEALS----QKIGTALHFALCGTNPYMS 424
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767950366  539 QVTelLLRKGANVNEKNKDFMTPLHVAAER-AHNDVMEVLHKHGAKMNALDTLGQTALHRAalAGHLQTCRLLLSYGSD 616
Cdd:PHA02876  425 VKT--LIDRGANVNSKNKDLSTPLHYACKKnCKLDVIEMLLDNGADVNAINIQNQYPLLIA--LEYHGIVNILLHYGAE 499
PHA03100 PHA03100
ankyrin repeat protein; Provisional
683-901 4.80e-29

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 121.70  E-value: 4.80e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  683 RHSTPLHFAAGYNRVSVVEYLLHHGADVHAKDKGGLVPLHNACSYGHY-----EVAELLVRHGASVNVADLWKFTPLHEA 757
Cdd:PHA03100   34 KPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYA 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  758 AAK--GKYEICKLLLKHGADPTKKNRDGNTPLDLVKEG---DTDIQDLLRGDAALLDAA-------KKGClarvqklctp 825
Cdd:PHA03100  114 ISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESnkiDLKILKLLIDKGVDINAKnrvnyllSYGV---------- 183
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767950366  826 eNINCRDTqgRNSTPLHLAAGYNNLEVAEYLLEHGADVNAQDKGGLIPLHNAASYGHVDIAALLIKYNTCVNATDK 901
Cdd:PHA03100  184 -PINIKDV--YGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256
PHA02876 PHA02876
ankyrin repeat protein; Provisional
567-943 1.73e-28

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 123.25  E-value: 1.73e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  567 ERAHND---VMEVLHKHGAKMNALDTLGQTALHRAALAGHLQTCRLLLSYGSDPSIISLQGFT----AAQMGN-EAVQQI 638
Cdd:PHA02876  151 ERIQQDellIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSvlecAVDSKNiDTIKAI 230
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  639 LSESTPIRTSDVDyrLLEASKAGDLETVKQLCSSQ-NVNCRDLegRHSTPLHFAAGYNRVS-VVEYLLHHGADVHAKDKG 716
Cdd:PHA02876  231 IDNRSNINKNDLS--LLKAIRNEDLETSLLLYDAGfSVNSIDD--CKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIK 306
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  717 GLVPLHNACSYGH-YEVAELLVRHGASVNVADLWKFTPLHEAAAKGKY-EICKLLLKHGAdptkknrdgntpldlvkegd 794
Cdd:PHA02876  307 GETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDRNkDIVITLLELGA-------------------- 366
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  795 tdiqdllrgdaalldaakkgclarvqklctpeNINCRDTQGRnsTPLHLAAGYNNLEVAEYLLEHGADVNAQDKGGLIPL 874
Cdd:PHA02876  367 --------------------------------NVNARDYCDK--TPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTAL 412
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767950366  875 HNAAsYGHVDIAAL--LIKYNTCVNATDKWAFTPLHEAAQKG-RTQLCALLLAHGADPTMKNQEGQTPLDLA 943
Cdd:PHA02876  413 HFAL-CGTNPYMSVktLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIA 483
PHA02876 PHA02876
ankyrin repeat protein; Provisional
417-810 7.52e-28

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 121.32  E-value: 7.52e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  417 VTELLLKHGACVNAMDLWQFTPLHEAASKNRVEVCSLLLSHGADPTLVNCHGKSAVDMAPTPE--------LRERLTYEF 488
Cdd:PHA02876  160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKnidtikaiIDNRSNINK 239
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  489 KGHSLLQAAREADLakvKKTLALEIINFKQPQ---SHETALHCAVASlhPKRKQVTELLLRKGANVNEKNKDFMTPLHVA 565
Cdd:PHA02876  240 NDLSLLKAIRNEDL---ETSLLLYDAGFSVNSiddCKNTPLHHASQA--PSLSRLVPKLLERGADVNAKNIKGETPLYLM 314
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  566 AERAHN-DVMEVLHKHGAKMNALDTLGQTALHRAalaghlqtcrlllsygsdpsiislqgftaaqmgneavqqilseSTP 644
Cdd:PHA02876  315 AKNGYDtENIRTLIMLGADVNAADRLYITPLHQA-------------------------------------------STL 351
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  645 IRTSDVDYRLLEASKagdletvkqlcssqNVNCRDLEGRhsTPLHFAAGYNRVSVVEYLLHHGADVHAKDKGGLVPLHNA 724
Cdd:PHA02876  352 DRNKDIVITLLELGA--------------NVNARDYCDK--TPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFA 415
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  725 -CSYGHYEVAELLVRHGASVNVADLWKFTPLHEAAAKG-KYEICKLLLKHGADPTKKNRDGNTPLDLVKEGDTDIQDLLR 802
Cdd:PHA02876  416 lCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIALEYHGIVNILLH 495

                  ....*...
gi 767950366  803 GDAALLDA 810
Cdd:PHA02876  496 YGAELRDS 503
PHA02874 PHA02874
ankyrin repeat protein; Provisional
540-880 2.49e-26

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 113.91  E-value: 2.49e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  540 VTELLLRKGANVNEKNKDFMTPLHVAAERAHNDVMEVLHKHGAKMNALDTLGQTALHRAALAGHLQTCRLLLSYGSDPSI 619
Cdd:PHA02874   17 IEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSI 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  620 ISLqgftaAQMGNEAVQQILSestpirtsdvdyrlleaskagdletvkqlcSSQNVNCRDLEGRhsTPLHFAAGYNRVSV 699
Cdd:PHA02874   97 LPI-----PCIEKDMIKTILD------------------------------CGIDVNIKDAELK--TFLHYAIKKGDLES 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  700 VEYLLHHGADVHAKDKGGLVPLHNACSYGHYEVAELLVRHGASVNVADLWKFTPLHEAAAKGKYEICKLLLKHGADPTKK 779
Cdd:PHA02874  140 IKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNK 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  780 NRDGNTPLDLVKEGDTDIQDLLRGDAAlldaakkgclarvqklctpenINCRDTQGrnSTPLHLAAGYN-NLEVAEYLLE 858
Cdd:PHA02874  220 CKNGFTPLHNAIIHNRSAIELLINNAS---------------------INDQDIDG--STPLHHAINPPcDIDIIDILLY 276
                         330       340
                  ....*....|....*....|..
gi 767950366  859 HGADVNAQDKGGLIPLHNAASY 880
Cdd:PHA02874  277 HKADISIKDNKGENPIDTAFKY 298
PHA03095 PHA03095
ankyrin-like protein; Provisional
337-628 4.69e-26

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 113.58  E-value: 4.69e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  337 DELLEAARSGNEEKLMALLTPLNVNChaSDGRKSTPLHLAAGYN---RVRIVQLLLQHGADVHAKDKGGLVPLH----NA 409
Cdd:PHA03095   17 DYLLNASNVTVEEVRRLLAAGADVNF--RGEYGKTPLHLYLHYSsekVKDIVRLLLEAGADVNAPERCGFTPLHlylyNA 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  410 CSYghyEVTELLLKHGACVNAMDLWQFTPLHE-AASKN-RVEVCSLLLSHGADPTLVNCHGKSAVDM-----APTPELRE 482
Cdd:PHA03095   95 TTL---DVIKLLIKAGADVNAKDKVGRTPLHVyLSGFNiNPKVIRLLLRKGADVNALDLYGMTPLAVllksrNANVELLR 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  483 RLtyefkghsllqaareadLAKVKKTLALEIINFkqpqsheTALHCAVASLHPkRKQVTELLLRKGANVNEKNKDFMTPL 562
Cdd:PHA03095  172 LL-----------------IDAGADVYAVDDRFR-------SLLHHHLQSFKP-RARIVRELIRAGCDPAATDMLGNTPL 226
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767950366  563 HVAA--ERAHNDVMEVLHKHGAKMNALDTLGQTALHRAALAGHLQTCRLLLSYGSDPSIISLQGFTAA 628
Cdd:PHA03095  227 HSMAtgSSCKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPL 294
PHA03095 PHA03095
ankyrin-like protein; Provisional
180-475 5.14e-26

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 113.58  E-value: 5.14e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  180 SGALRELLEACRNGDVSRVKRLVDA-ANVNAKDmaGRKSSPLHFAAGFG---RKDVVEHLLQMGANVHARDDGGLIPLH- 254
Cdd:PHA03095   12 EAALYDYLLNASNVTVEEVRRLLAAgADVNFRG--EYGKTPLHLYLHYSsekVKDIVRLLLEAGADVNAPERCGFTPLHl 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  255 ---NACSfghAEVVSLLLCQGADPNARDNWNYTPLHeAAIKGK-IDVCIV--LLQHGADPNIRNTDGKSALDladpsaka 328
Cdd:PHA03095   90 ylyNATT---LDVIKLLIKAGADVNAKDKVGRTPLH-VYLSGFnINPKVIrlLLRKGADVNALDLYGMTPLA-------- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  329 VLTgeykkdelleaaRSGN-EEKLMALLTPLNVNCHASDGRKSTPLHLAAGYNRVR--IVQLLLQHGADVHAKDKGGLVP 405
Cdd:PHA03095  158 VLL------------KSRNaNVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTP 225
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767950366  406 LHNACSYGHYEVTEL--LLKHGACVNAMDLWQFTPLHEAASKNRVEVCSLLLSHGADPTLVNCHGKSAVDMA 475
Cdd:PHA03095  226 LHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLM 297
PHA03100 PHA03100
ankyrin repeat protein; Provisional
215-475 7.15e-26

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 112.07  E-value: 7.15e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  215 RKSSPLHFAAGFGRKDVVEHLLQMGANVHARDDGGLIPLHNACSFGHA-----EVVSLLLCQGADPNARDNWNYTPLHEA 289
Cdd:PHA03100   34 KPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYA 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  290 AIKGKIDVCIV--LLQHGADPNIRNTDGKSaldladpsakavltgeykkdeLLEAARSGNEEKLmalltplnvnchasdg 367
Cdd:PHA03100  114 ISKKSNSYSIVeyLLDNGANVNIKNSDGEN---------------------LLHLYLESNKIDL---------------- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  368 rkstplhlaagynrvRIVQLLLQHGADVHAKDKgglvplhnacsyghyevTELLLKHGACVNAMDLWQFTPLHEAASKNR 447
Cdd:PHA03100  157 ---------------KILKLLIDKGVDINAKNR-----------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNN 204
                         250       260
                  ....*....|....*....|....*...
gi 767950366  448 VEVCSLLLSHGADPTLVNCHGKSAVDMA 475
Cdd:PHA03100  205 PEFVKYLLDLGANPNLVNKYGDTPLHIA 232
PHA03095 PHA03095
ankyrin-like protein; Provisional
543-893 2.17e-24

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 108.57  E-value: 2.17e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  543 LLLRKGANVNEKNKDFMTPLHVAAERAHNDVMEV---LHKHGAKMNALDTLGQTALHraalaghlqtcrLLLSYGSDPSI 619
Cdd:PHA03095   32 RLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIvrlLLEAGADVNAPERCGFTPLH------------LYLYNATTLDV 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  620 IslqgftaaqmgneavqqilsestpirtsdvdyRLLEASKAgdletvkqlcssqNVNCRDLEGRhsTPLH-FAAGYN-RV 697
Cdd:PHA03095  100 I--------------------------------KLLIKAGA-------------DVNAKDKVGR--TPLHvYLSGFNiNP 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  698 SVVEYLLHHGADVHAKDKGGLVPLH------NACSyghyEVAELLVRHGASVNVADLWKFTPLHEAA--AKGKYEICKLL 769
Cdd:PHA03095  133 KVIRLLLRKGADVNALDLYGMTPLAvllksrNANV----ELLRLLIDAGADVYAVDDRFRSLLHHHLqsFKPRARIVREL 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  770 LKHGADPTKKNRDGNTPLDLVKEG----DTDIQDLLRGDAAlldaakkgclarvqklctpenINCRDTQGRnsTPLHLAA 845
Cdd:PHA03095  209 IRAGCDPAATDMLGNTPLHSMATGssckRSLVLPLLIAGIS---------------------INARNRYGQ--TPLHYAA 265
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 767950366  846 GYNNLEVAEYLLEHGADVNAQDKGGLIPLHNAASYGHVDIAALLIKYN 893
Cdd:PHA03095  266 VFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKN 313
PHA03095 PHA03095
ankyrin-like protein; Provisional
375-730 2.87e-24

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 108.19  E-value: 2.87e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  375 LAAGYNRVRIVQLLLQHGADVHAKDKGGLVPLHnacSYGHY------EVTELLLKHGACVNAMDLWQFTPLH-EAASKNR 447
Cdd:PHA03095   20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLH---LYLHYssekvkDIVRLLLEAGADVNAPERCGFTPLHlYLYNATT 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  448 VEVCSLLLSHGADptlVNchGKSAVDMAPtpelrerltyefkghslLQAareadlakvkktlaleiinfkqpqshetalH 527
Cdd:PHA03095   97 LDVIKLLIKAGAD---VN--AKDKVGRTP-----------------LHV------------------------------Y 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  528 CAVASLHPKrkqVTELLLRKGANVNEKNKDFMTPLHVAAeRAHN---DVMEVLHKHGAKMNALDTLGQTALHRaalagHL 604
Cdd:PHA03095  125 LSGFNINPK---VIRLLLRKGADVNALDLYGMTPLAVLL-KSRNanvELLRLLIDAGADVYAVDDRFRSLLHH-----HL 195
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  605 QTCR-------LLLSYGSDPSIISLQGFTAAQMgneavqqiLSESTPIRTSDVDYRLLEASKagdletvkqlcssqnVNC 677
Cdd:PHA03095  196 QSFKprarivrELIRAGCDPAATDMLGNTPLHS--------MATGSSCKRSLVLPLLIAGIS---------------INA 252
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767950366  678 RDLEGRhsTPLHFAAGYNRVSVVEYLLHHGADVHAKDKGGLVPLHNACSYGHY 730
Cdd:PHA03095  253 RNRYGQ--TPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNG 303
PHA02874 PHA02874
ankyrin repeat protein; Provisional
650-943 5.90e-24

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 106.59  E-value: 5.90e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  650 VDYRLLEASkaGDLETVKQLCSSQNvNCRDLEGRHS-TPLHFAAGYNRVSVVEYLLHHGADVHAKDKGGLVPLHNACSYG 728
Cdd:PHA02874    3 QDLRMCIYS--GDIEAIEKIIKNKG-NCINISVDETtTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  729 HYEVAELLVRHGA-----------------------SVNVADLWKFTPLHEAAAKGKYEICKLLLKHGADPTKKNRDGNT 785
Cdd:PHA02874   80 AHDIIKLLIDNGVdtsilpipciekdmiktildcgiDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCY 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  786 PLDL-VKEGDTDIQDLLrgdaalldaAKKGCLARVQKlctpENINcrdtqgrnsTPLHLAAGYNNLEVAEYLLEHGADVN 864
Cdd:PHA02874  160 PIHIaIKHNFFDIIKLL---------LEKGAYANVKD----NNGE---------SPLHNAAEYGDYACIKLLIDHGNHIM 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  865 AQDKGGLIPLHNAASYGHvDIAALLIKyNTCVNATDKWAFTPLHEAAQKG-RTQLCALLLAHGADPTMKNQEGQTPLDLA 943
Cdd:PHA02874  218 NKCKNGFTPLHNAIIHNR-SAIELLIN-NASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTA 295
ADP_ribosyl cd01341
ADP_ribosylating enzymes catalyze the transfer of ADP_ribose from NAD+ to substrates. ...
1181-1304 9.66e-24

ADP_ribosylating enzymes catalyze the transfer of ADP_ribose from NAD+ to substrates. Bacterial toxins are cytoplasmic and catalyze the transfer of a single ADP_ribose unit to eukaryotic elongation factor 2, halting protein synthesis and killing the cell. Poly(ADP-ribose) polymerases (PARPS 1-3, VPARP, tankyrase) catalyze the addition of up to 100 ADP_ribose units from NAD+. PARPs 1 and 2 are localized in the nucleaus, bind DNA, and are activated by DNA damage. VPARP is part of the vault ribonucleoprotein complex. Tankyrases regulates telomere length in part through poy(ADP_ribosylation) of telomere repeat binding factor 1 (TRF1). Poly(ADP-ribose) polymerase catalyses the covalent attachment of ADP-ribose units from NAD+ to itself and to a limited number of other DNA binding proteins, which decreases their affinity for DNA. Poly(ADP-ribose) polymerase is a regulatory component induced by DNA damage. The carboxyl-terminal region is the most highly conserved region of the protein. Experiments have shown that a carboxyl 40 kDa fragment is still catalytically active.


Pssm-ID: 238651 [Multi-domain]  Cd Length: 137  Bit Score: 98.02  E-value: 9.66e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366 1181 MLFHGSPFINAIIHKGFDERHAYIG-----GMFGAGIYFAENSSKSNQYVYGIGGGTGCPTHKdrscyichrQMLFCRVT 1255
Cdd:cd01341     1 FLFHGSPPGNVISILKLGLRPASYGvllngGMFGKGIYSAPNISKSNGYSVGCDGQHVFQNGK---------PKVCGREL 71
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767950366 1256 LGKSFLQFSTMKMAHA-------------PPGHHSVIGRPSV---NGLAYAEYVIYRGEQVDTLK 1304
Cdd:cd01341    72 CVFGFLTLGVMSGATEessrvlfprnfrgATGAEVVDLLVAMcrdALLLPREYIIFEPYSQVSIR 136
PHA03095 PHA03095
ankyrin-like protein; Provisional
523-811 1.35e-23

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 105.88  E-value: 1.35e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  523 ETALHCAVASLHPKRKQVTELLLRKGANVNEKNKDFMTPLHVAAERAHN-DVMEVLHKHGAKMNALDTLGQTALHrAALA 601
Cdd:PHA03095   48 KTPLHLYLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKAGADVNAKDKVGRTPLH-VYLS 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  602 G---HLQTCRLLLSYGSDPSIISLQGFTAAqmgneavqQILsestpIRTSDVdyrlleaskagDLETVKQLCS-SQNVNC 677
Cdd:PHA03095  127 GfniNPKVIRLLLRKGADVNALDLYGMTPL--------AVL-----LKSRNA-----------NVELLRLLIDaGADVYA 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  678 RDLEGRhsTPLHFAAGY--NRVSVVEYLLHHGADVHAKDKGGLVPLHNACSYGHYEVAEL--LVRHGASVNVADLWKFTP 753
Cdd:PHA03095  183 VDDRFR--SLLHHHLQSfkPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTP 260
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767950366  754 LHEAAAKGKYEICKLLLKHGADPTKKNRDGNTPLDLVkegdtdiqdLLRGDAALLDAA 811
Cdd:PHA03095  261 LHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLM---------VRNNNGRAVRAA 309
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
1116-1300 6.75e-23

Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the covalent attachment of ADP-ribose units from NAD+ to itself and to a limited number of other DNA binding proteins, which decreases their affinity for DNA. Poly(ADP-ribose) polymerase is a regulatory component induced by DNA damage. The carboxyl-terminal region is the most highly conserved region of the protein. Experiments have shown that a carboxyl 40 kDa fragment is still catalytically active.


Pssm-ID: 395519 [Multi-domain]  Cd Length: 195  Bit Score: 97.79  E-value: 6.75e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  1116 KEYQSVEEEMQSTirehRDGGNAGGIFnrynVIRIQKVVNKKLRERFChrqkevseENHNHHNERMLFHGSP--FINAII 1193
Cdd:pfam00644    2 EEYQIIEKYFLST----HDPTHGYPLF----ILEIFRVQRDGEWERFQ--------PKKKLRNRRLLWHGSRltNFLGIL 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  1194 HKGF--DERHAYIGG-MFGAGIYFAENSSKSNQYvygigggtgCPTHKDRScyicHRQMLFCRVTLGKSFLQFSTMKMAH 1270
Cdd:pfam00644   66 SQGLriAPPEAPVTGyMFGKGIYFADDASKSANY---------CPPSEAHG----NGLMLLSEVALGDMNELKKADYAEK 132
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 767950366  1271 APPGHHSVIG------------------RPSVNG-----LAYAEYVIYRGEQV 1300
Cdd:pfam00644  133 LPPGKHSVKGlgktapesfvdldgvplgKLVATGydssvLLYNEYVVYNVNQV 185
PHA03100 PHA03100
ankyrin repeat protein; Provisional
365-626 1.25e-22

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 102.44  E-value: 1.25e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  365 SDGRKSTPLHLAAGYNRVRIVQLLLQHGADVHAKDKGGLVPLHNACSYGHY-----EVTELLLKHGACVNAMDLWQFTPL 439
Cdd:PHA03100   31 SYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPL 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  440 HEAASK--NRVEVCSLLLSHGADPTLVNCHGksavdmaptpelrerltyefkghsllqaareadlakvkktlaleiinfk 517
Cdd:PHA03100  111 LYAISKksNSYSIVEYLLDNGANVNIKNSDG------------------------------------------------- 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  518 qpqshETALHCAVASLHPKRKqVTELLLRKGANVNEKNKdfmtplhvaaerahndvMEVLHKHGAKMNALDTLGQTALHR 597
Cdd:PHA03100  142 -----ENLLHLYLESNKIDLK-ILKLLIDKGVDINAKNR-----------------VNYLLSYGVPINIKDVYGFTPLHY 198
                         250       260
                  ....*....|....*....|....*....
gi 767950366  598 AALAGHLQTCRLLLSYGSDPSIISLQGFT 626
Cdd:PHA03100  199 AVYNNNPEFVKYLLDLGANPNLVNKYGDT 227
PHA02878 PHA02878
ankyrin repeat protein; Provisional
219-475 1.10e-21

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 100.34  E-value: 1.10e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  219 PLHFAAGFGRKDVVEHLLQMGANVHARDDGGLIPLH------------------NACSFGHAEVVSLLLCQGADPNA--- 277
Cdd:PHA02878   40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHiickepnklgmkemirsiNKCSVFYTLVAIKDAFNNRNVEIfki 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  278 ----RDNWNYT----PLHEAAIKGKIDVCIV--LLQHGADPNIRNTD-GKSALDLADpsakavltgeykkdelleaarSG 346
Cdd:PHA02878  120 iltnRYKNIQTidlvYIDKKSKDDIIEAEITklLLSYGADINMKDRHkGNTALHYAT---------------------EN 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  347 NEEKLMALLTPLNVNCHASDGRKSTPLHLAAGYNRVRIVQLLLQHGADVHAKDKGGLVPLHNACSY-GHYEVTELLLKHG 425
Cdd:PHA02878  179 KDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHG 258
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767950366  426 ACVNAMD-LWQFTPLHEAASKNRVevCSLLLSHGADPTLVNCHGKSAVDMA 475
Cdd:PHA02878  259 VDVNAKSyILGLTALHSSIKSERK--LKLLLEYGADINSLNSYKLTPLSSA 307
Ank_2 pfam12796
Ankyrin repeats (3 copies);
841-933 1.53e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 90.18  E-value: 1.53e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366   841 LHLAAGYNNLEVAEYLLEHGADVNAQDKGGLIPLHNAASYGHVDIAALLIKYNTCVNATDKWafTPLHEAAQKGRTQLCA 920
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGR--TALHYAARSGHLEIVK 78
                           90
                   ....*....|...
gi 767950366   921 LLLAHGADPTMKN 933
Cdd:pfam12796   79 LLLEKGADINVKD 91
PHA02875 PHA02875
ankyrin repeat protein; Provisional
251-468 2.31e-21

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 98.52  E-value: 2.31e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  251 IPLHNACSFGHAEVVSLLLCQGADPNARDNWNYTPLhEAAIKGKIDVCI-VLLQHGADPNIRNTDGKSALDladpsaKAV 329
Cdd:PHA02875    4 VALCDAILFGELDIARRLLDIGINPNFEIYDGISPI-KLAMKFRDSEAIkLLMKHGAIPDVKYPDIESELH------DAV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  330 LTGEYKKDELLeaarsgneeklmalltpLNVNCHASD---GRKSTPLHLAAGYNRVRIVQLLLQHGADVHAKDKGGLVPL 406
Cdd:PHA02875   77 EEGDVKAVEEL-----------------LDLGKFADDvfyKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPL 139
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767950366  407 HNACSYGHYEVTELLLKHGACVNAMDLWQFTPLHEAASKNRVEVCSLLLSHGADPTLVNCHG 468
Cdd:PHA02875  140 HLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNG 201
PHA03100 PHA03100
ankyrin repeat protein; Provisional
536-775 2.35e-21

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 98.58  E-value: 2.35e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  536 KRKQVTELLLRKGANVNEKNKDFMTPLHVAAERAHN--DVME---VLHKHGAKMNALDTLGQTALHRAALA--GHLQTCR 608
Cdd:PHA03100   46 RNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltDVKEivkLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVE 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  609 LLLSYGSDPSIISLQGFTAaqmgneaVQQILSESTPirtsdvdyrlleaskagDLETVKQLCSSQ-NVNCRDlegrhstp 687
Cdd:PHA03100  126 YLLDNGANVNIKNSDGENL-------LHLYLESNKI-----------------DLKILKLLIDKGvDINAKN-------- 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  688 lhfaagynrvsVVEYLLHHGADVHAKDKGGLVPLHNACSYGHYEVAELLVRHGASVNVADLWKFTPLHEAAAKGKYEICK 767
Cdd:PHA03100  174 -----------RVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFK 242

                  ....*...
gi 767950366  768 LLLKHGAD 775
Cdd:PHA03100  243 LLLNNGPS 250
Ank_2 pfam12796
Ankyrin repeats (3 copies);
688-780 3.64e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 89.02  E-value: 3.64e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366   688 LHFAAGYNRVSVVEYLLHHGADVHAKDKGGLVPLHNACSYGHYEVAELLVRHGASVNVADLWkfTPLHEAAAKGKYEICK 767
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGR--TALHYAARSGHLEIVK 78
                           90
                   ....*....|...
gi 767950366   768 LLLKHGADPTKKN 780
Cdd:pfam12796   79 LLLEKGADINVKD 91
PHA02878 PHA02878
ankyrin repeat protein; Provisional
687-943 3.83e-21

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 98.41  E-value: 3.83e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  687 PLHFAAGYNRVSVVEYLLHHGADVHAKDKGGLVPLHNAC-------------SYGHYEVAELLVRHGASVNVADLWKFTP 753
Cdd:PHA02878   40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICkepnklgmkemirSINKCSVFYTLVAIKDAFNNRNVEIFKI 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  754 LHEAAAKGKY------------------EICKLLLKHGADPTKKNRD-GNTPLDLVKEG-DTDIQDLLrgdaaLLDAAKK 813
Cdd:PHA02878  120 ILTNRYKNIQtidlvyidkkskddiieaEITKLLLSYGADINMKDRHkGNTALHYATENkDQRLTELL-----LSYGANV 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  814 GCLARVqklctpenincrdtqgrNSTPLHLAAGYNNLEVAEYLLEHGADVNAQDKGGLIPLHNAASY-GHVDIAALLIKY 892
Cdd:PHA02878  195 NIPDKT-----------------NNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEH 257
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 767950366  893 NTCVNATDK-WAFTPLHEAAQKgrTQLCALLLAHGADPTMKNQEGQTPLDLA 943
Cdd:PHA02878  258 GVDVNAKSYiLGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSA 307
Ank_2 pfam12796
Ankyrin repeats (3 copies);
220-312 4.02e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 89.02  E-value: 4.02e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366   220 LHFAAGFGRKDVVEHLLQMGANVHARDDGGLIPLHNACSFGHAEVVSLLLcQGADPNARDNwNYTPLHEAAIKGKIDVCI 299
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKDN-GRTALHYAARSGHLEIVK 78
                           90
                   ....*....|...
gi 767950366   300 VLLQHGADPNIRN 312
Cdd:pfam12796   79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
373-465 7.48e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 88.25  E-value: 7.48e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366   373 LHLAAGYNRVRIVQLLLQHGADVHAKDKGGLVPLHNACSYGHYEVTELLLKHgACVNaMDLWQFTPLHEAASKNRVEVCS 452
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVN-LKDNGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|...
gi 767950366   453 LLLSHGADPTLVN 465
Cdd:pfam12796   79 LLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
307-589 1.72e-20

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 95.89  E-value: 1.72e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  307 DPNIRNTDGKSALDLADpsakAVLTGEYKKDELLEAARSGNEEKLMALLTPLNVNCHASDGRKSTPLHLAAGYNRV---- 382
Cdd:PHA03100   10 SRIIKVKNIKYIIMEDD----LNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdv 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  383 -RIVQLLLQHGADVHAKDKGGLVPLHNACSY--GHYEVTELLLKHGACVNAMDLWQFTPLHEAASKNRV--EVCSLLLSH 457
Cdd:PHA03100   86 kEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDK 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  458 GADptlVNchGKSAVDMAptpelrerLTYEFKghsllqaareadlakvkktlaleiINFKQPQShETALHCAVASLHPkr 537
Cdd:PHA03100  166 GVD---IN--AKNRVNYL--------LSYGVP------------------------INIKDVYG-FTPLHYAVYNNNP-- 205
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 767950366  538 kQVTELLLRKGANVNEKNKDFMTPLHVAAERAHNDVMEVLHKHGAKMNALDT 589
Cdd:PHA03100  206 -EFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256
PHA02878 PHA02878
ankyrin repeat protein; Provisional
561-898 3.62e-20

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 95.33  E-value: 3.62e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  561 PLHVAAERAHNDVMEVLHKHGAKMNALDTLGQTALHRAALAGHLQTCRLLLSygsdpSIISLQGFTAAQMGNEAVQQ--- 637
Cdd:PHA02878   40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIR-----SINKCSVFYTLVAIKDAFNNrnv 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  638 ------ILSESTPIRTSDVDYrLLEASKAGDLET--VKQLCS-SQNVNCRDlEGRHSTPLHFAAGYNRVSVVEYLLHHGA 708
Cdd:PHA02878  115 eifkiiLTNRYKNIQTIDLVY-IDKKSKDDIIEAeiTKLLLSyGADINMKD-RHKGNTALHYATENKDQRLTELLLSYGA 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  709 DVHAKDKGGLVPLHNACSYGHYEVAELLVRHGASVNVADLWKFTPLHEAAAKGK-YEICKLLLKHGADptkknrdgntpl 787
Cdd:PHA02878  193 NVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKdYDILKLLLEHGVD------------ 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  788 dlvkegdtdiqdllrgdaalldaakkgclarvqklctpenINCRDTQgRNSTPLHLAagYNNLEVAEYLLEHGADVNAQD 867
Cdd:PHA02878  261 ----------------------------------------VNAKSYI-LGLTALHSS--IKSERKLKLLLEYGADINSLN 297
                         330       340       350
                  ....*....|....*....|....*....|..
gi 767950366  868 KGGLIPLHNAA-SYGHVDIAALLIkYNTCVNA 898
Cdd:PHA02878  298 SYKLTPLSSAVkQYLCINIGRILI-SNICLLK 328
PHA02874 PHA02874
ankyrin repeat protein; Provisional
186-518 4.10e-20

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 95.03  E-value: 4.10e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  186 LLEACRNGDVSRVKRLVD-AANVNakDMAGRKSSPLHFAAGFGRKDVVEHLLQMGAnvhardDGGLIPLHNAcsfgHAEV 264
Cdd:PHA02874   39 LIDAIRSGDAKIVELFIKhGADIN--HINTKIPHPLLTAIKIGAHDIIKLLIDNGV------DTSILPIPCI----EKDM 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  265 VSLLLCQGADPNARDNWNYTPLHEAAIKGKIDVCIVLLQHGADPNIRNTDGKSALDLADPSakavltgeykkdelleaar 344
Cdd:PHA02874  107 IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKH------------------- 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  345 sgNEEKLMALLTPLNVNCHASDGRKSTPLHLAAGYNRVRIVQLLLQHGADVHAKDKGGLVPLHNACSYGHyEVTELLLKH 424
Cdd:PHA02874  168 --NFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLINN 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  425 gACVNAMDLWQFTPLHEAASKN-RVEVCSLLLSHGADPTLVNCHGKSAVDMAPTPELRERLTYEFKGHSLLQaaREADla 503
Cdd:PHA02874  245 -ASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTAFKYINKDPVIKDIIANAVLI--KEAD-- 319
                         330
                  ....*....|....*
gi 767950366  504 KVKKTLALEIINFKQ 518
Cdd:PHA02874  320 KLKDSDFLEHIEIKD 334
PHA02874 PHA02874
ankyrin repeat protein; Provisional
405-727 2.93e-19

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 92.33  E-value: 2.93e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  405 PLHNACSYGHYEVTELLLKHGACVNAMDLWQFTPLHEAASKNRVEVCSLLLSHGADPTLVnchgksavdmaPTPELRERL 484
Cdd:PHA02874   38 PLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSIL-----------PIPCIEKDM 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  485 tyefkghsllqaareadlakVKKTLALEI-INFKQPQShETALHCAVASlhpKRKQVTELLLRKGANVNEKNKDFMTPLH 563
Cdd:PHA02874  107 --------------------IKTILDCGIdVNIKDAEL-KTFLHYAIKK---GDLESIKMLFEYGADVNIEDDNGCYPIH 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  564 VAAERAHNDVMEVLHKHGAKMNALDTLGQTALHRAALAGHLQTCRLLLSYGSDPSIISLQGFtaaqmgneavqqilsesT 643
Cdd:PHA02874  163 IAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGF-----------------T 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  644 PIRTSDVDYRlleaskagdlETVKQLCSSQNVNCRDLEGrhSTPLHFAAGYN-RVSVVEYLLHHGADVHAKDKGGLVPLH 722
Cdd:PHA02874  226 PLHNAIIHNR----------SAIELLINNASINDQDIDG--STPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPID 293

                  ....*
gi 767950366  723 NACSY 727
Cdd:PHA02874  294 TAFKY 298
PHA02875 PHA02875
ankyrin repeat protein; Provisional
719-929 1.11e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 86.97  E-value: 1.11e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  719 VPLHNACSYGHYEVAELLVRHGASVNVADLWKFTPLHEAAAKGKYEICKLLLKHGADPTKKNRDGNTPL-DLVKEGDT-D 796
Cdd:PHA02875    4 VALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELhDAVEEGDVkA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  797 IQDLLRGDAALLDAAKKgclarvqklctpenincrdtqgRNSTPLHLAAGYNNLEVAEYLLEHGADVNAQDKGGLIPLHN 876
Cdd:PHA02875   84 VEELLDLGKFADDVFYK----------------------DGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHL 141
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767950366  877 AASYGHVDIAALLIKYNTCVNATDKWAFTPLHEAAQKGRTQLCALLLAHGADP 929
Cdd:PHA02875  142 AVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANI 194
PHA02878 PHA02878
ankyrin repeat protein; Provisional
429-772 2.47e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 86.86  E-value: 2.47e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  429 NAMDLWQFTPLHEAASKNRVEVCSLLLSHGAD----------PTLVNChgkSAVDMAPTPEL-----RERLTYEFKGHSL 493
Cdd:PHA02878   31 TSASLIPFIPLHQAVEARNLDVVKSLLTRGHNvnqpdhrdltPLHIIC---KEPNKLGMKEMirsinKCSVFYTLVAIKD 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  494 LQAAREADLAKVkktlaLEIINFKQPQSHETALHCAVASLHPKRKQVTELLLRKGANVNEKNKDFM-TPLHVAAERAHND 572
Cdd:PHA02878  108 AFNNRNVEIFKI-----ILTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDRHKGnTALHYATENKDQR 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  573 VMEVLHKHGAKMNALDTLGQTALHRAALAGHLQTCRLLLSYGSdpsiislqgftaaqmgneavqqilsestpirtsdvdy 652
Cdd:PHA02878  183 LTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA------------------------------------- 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  653 rlleaskagdletvkqlcssqNVNCRDLEGrhSTPLHFAAGY-NRVSVVEYLLHHGADVHAKDK-GGLVPLHnaCSYGHY 730
Cdd:PHA02878  226 ---------------------STDARDKCG--NTPLHISVGYcKDYDILKLLLEHGVDVNAKSYiLGLTALH--SSIKSE 280
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 767950366  731 EVAELLVRHGASVNVADLWKFTPLHEAAAK-GKYEICKLLLKH 772
Cdd:PHA02878  281 RKLKLLLEYGADINSLNSYKLTPLSSAVKQyLCINIGRILISN 323
PHA03100 PHA03100
ankyrin repeat protein; Provisional
379-755 3.72e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 85.49  E-value: 3.72e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  379 YNRVRIVQLLLQHGADVHA-----KDKGGLVPLHNACSYGHYEVTELLLKHGACVNAMDLWQFTPLH----EAASKNRV- 448
Cdd:PHA03100    7 LTKSRIIKVKNIKYIIMEDdlndySYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHylsnIKYNLTDVk 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  449 EVCSLLLSHGADPtlvnchgksavdmaptpelreRLTYEFKGHSLLQAAreadlakVKKTLALEIInfkqpqshetalhc 528
Cdd:PHA03100   87 EIVKLLLEYGANV---------------------NAPDNNGITPLLYAI-------SKKSNSYSIV-------------- 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  529 avaslhpkrkqvtELLLRKGANVNEKNKDFMTPLHVAAERAHND--VMEVLHKHGAKMNALDTLgqtalhraalaghlqt 606
Cdd:PHA03100  125 -------------EYLLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGVDINAKNRV---------------- 175
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  607 cRLLLSYGSDpsiislqgftaaqmgneavqqilsestpirtsdvdyrlleaskagdletvkqlcssqnVNCRDLEGrhST 686
Cdd:PHA03100  176 -NYLLSYGVP----------------------------------------------------------INIKDVYG--FT 194
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767950366  687 PLHFAAGYNRVSVVEYLLHHGADVHAKDKGGLVPLHNACSYGHYEVAELLVRHGASVNVAD----LWKFTPLH 755
Cdd:PHA03100  195 PLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIetllYFKDKDLN 267
PHA02875 PHA02875
ankyrin repeat protein; Provisional
592-787 4.01e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 85.43  E-value: 4.01e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  592 QTALHRAALAGHLQTCRLLLSYGSDPSIISLQGFTAAQMG-----NEAVQQILSEST--PIRTSDVDYRLLEASKAGDLE 664
Cdd:PHA02875    3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAmkfrdSEAIKLLMKHGAipDVKYPDIESELHDAVEEGDVK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  665 TVKQLCSSQNVNCRDLEGRHSTPLHFAAGYNRVSVVEYLLHHGADVHAKDKGGLVPLHNACSYGHYEVAELLVRHGASVN 744
Cdd:PHA02875   83 AVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLD 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 767950366  745 VADLWKFTPLHEAAAKGKYEICKLLLKHGADPTKKNRDGNTPL 787
Cdd:PHA02875  163 IEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAA 205
Ank_2 pfam12796
Ankyrin repeats (3 copies);
754-867 5.10e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.46  E-value: 5.10e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366   754 LHEAAAKGKYEICKLLLKHGADPTKKNRDGNTPLDLvkegdtdiqdllrgdaalldAAKKGCLARVQKLCTPENINCRDt 833
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHL--------------------AAKNGHLEIVKLLLEHADVNLKD- 59
                           90       100       110
                   ....*....|....*....|....*....|....
gi 767950366   834 qgRNSTPLHLAAGYNNLEVAEYLLEHGADVNAQD 867
Cdd:pfam12796   60 --NGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
410-813 1.21e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 84.24  E-value: 1.21e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  410 CSY-GHYEVTELLLKH-GACVNAMDLWQFTPLHEAASKNRVEVCSLLLSHGADPTLVNCHgksavdmAPTPelrerltye 487
Cdd:PHA02874    8 CIYsGDIEAIEKIIKNkGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTK-------IPHP--------- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  488 fkghsLLQAAReadlAKVKKTLALEIINfkqpqshetALHCAVASLHPKRKQVTELLLRKGANVNEKNKDFMTPLHVAAE 567
Cdd:PHA02874   72 -----LLTAIK----IGAHDIIKLLIDN---------GVDTSILPIPCIEKDMIKTILDCGIDVNIKDAELKTFLHYAIK 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  568 RAHNDVMEVLHKHGAKMNALDTLGQTALHRAALAGHLQTCRLLLSYGsdpsiislqgftaaqmgneavqqilsestpirt 647
Cdd:PHA02874  134 KGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKG--------------------------------- 180
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  648 sdvdyrlleaskagdletvkqlcSSQNVNCRDLEgrhsTPLHFAAGYNRVSVVEYLLHHGADVHAKDKGGLVPLHNACSY 727
Cdd:PHA02874  181 -----------------------AYANVKDNNGE----SPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIH 233
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  728 GHyEVAELLVrHGASVNVADLWKFTPLHEA-AAKGKYEICKLLLKHGADPTKKNRDGNTPLDLVKE---GDTDIQDLLrG 803
Cdd:PHA02874  234 NR-SAIELLI-NNASINDQDIDGSTPLHHAiNPPCDIDIIDILLYHKADISIKDNKGENPIDTAFKyinKDPVIKDII-A 310
                         410
                  ....*....|
gi 767950366  804 DAALLDAAKK 813
Cdd:PHA02874  311 NAVLIKEADK 320
PHA02878 PHA02878
ankyrin repeat protein; Provisional
526-790 1.45e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 84.16  E-value: 1.45e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  526 LHCAVASlhpKRKQVTELLLRKGANVNEKNKDFMTPLHVA-----------------------AERAHNDVMEVLHKHGA 582
Cdd:PHA02878   41 LHQAVEA---RNLDVVKSLLTRGHNVNQPDHRDLTPLHIIckepnklgmkemirsinkcsvfyTLVAIKDAFNNRNVEIF 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  583 KMNALD------TLGQTALHRAALAGHLQT--CRLLLSYGSDPSIISlqgftaAQMGNEAVQQIlsestpirTSDVDYRL 654
Cdd:PHA02878  118 KIILTNrykniqTIDLVYIDKKSKDDIIEAeiTKLLLSYGADINMKD------RHKGNTALHYA--------TENKDQRL 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  655 LEAskagdletvkQLCSSQNVNCRDLEgrHSTPLHFAAGYNRVSVVEYLLHHGADVHAKDKGGLVPLHNACSY-GHYEVA 733
Cdd:PHA02878  184 TEL----------LLSYGANVNIPDKT--NNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDIL 251
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767950366  734 ELLVRHGASVNV-ADLWKFTPLHEAAAKGkyEICKLLLKHGADPTKKNRDGNTPLDLV 790
Cdd:PHA02878  252 KLLLEHGVDVNAkSYILGLTALHSSIKSE--RKLKLLLEYGADINSLNSYKLTPLSSA 307
Ank_2 pfam12796
Ankyrin repeats (3 copies);
595-714 7.13e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 74.00  E-value: 7.13e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366   595 LHRAALAGHLQTCRLLLSYGSDPSIISLQGFTAaqmgneavqqilsestpirtsdvdyrLLEASKAGDLETVKQLCSSQN 674
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTA--------------------------LHLAAKNGHLEIVKLLLEHAD 54
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 767950366   675 VNCRDlegRHSTPLHFAAGYNRVSVVEYLLHHGADVHAKD 714
Cdd:pfam12796   55 VNLKD---NGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
191-400 8.68e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 81.25  E-value: 8.68e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  191 RNGDVsrVKRLVD-AANVNAKDMAGRKSSPLHFAAGFGRKDVVEH---LLQMGANVHARDDGGLIPLHNACS--FGHAEV 264
Cdd:PHA03100   46 RNIDV--VKILLDnGADINSSTKNNSTPLHYLSNIKYNLTDVKEIvklLLEYGANVNAPDNNGITPLLYAISkkSNSYSI 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  265 VSLLLCQGADPNARDNWNYTPLHEAAIKGKIDVCIV--LLQHGADPNIRNtdgksaldladpSAKAVLTGEYK---KDE- 338
Cdd:PHA03100  124 VEYLLDNGANVNIKNSDGENLLHLYLESNKIDLKILklLIDKGVDINAKN------------RVNYLLSYGVPiniKDVy 191
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767950366  339 ----LLEAARSGNEEKLMALL-TPLNVNCHASDGrkSTPLHLAAGYNRVRIVQLLLQHGADVHAKDK 400
Cdd:PHA03100  192 gftpLHYAVYNNNPEFVKYLLdLGANPNLVNKYG--DTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256
Ank_2 pfam12796
Ankyrin repeats (3 copies);
286-399 1.03e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.92  E-value: 1.03e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366   286 LHEAAIKGKIDVCIVLLQHGADPNIRNTDGKSALdladpsakavltgeykkdelLEAARSGNEEKLMALLTPLNVNChas 365
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTAL--------------------HLAAKNGHLEIVKLLLEHADVNL--- 57
                           90       100       110
                   ....*....|....*....|....*....|....
gi 767950366   366 DGRKSTPLHLAAGYNRVRIVQLLLQHGADVHAKD 399
Cdd:pfam12796   58 KDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA02875 PHA02875
ankyrin repeat protein; Provisional
185-464 1.13e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 77.72  E-value: 1.13e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  185 ELLEACRNGDVSRVKRLVDAA-NVNAKDMAGrkSSPLHFAAGFGRKDVVEHLLQMGANVHARDDGGLIPLHNACSFGHAE 263
Cdd:PHA02875    5 ALCDAILFGELDIARRLLDIGiNPNFEIYDG--ISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  264 VVSLLLCQGA---DPNARDnwNYTPLHEAAIKGKIDVCIVLLQHGADPNIRNTDgksaldladpsakavltgeykkdell 340
Cdd:PHA02875   83 AVEELLDLGKfadDVFYKD--GMTPLHLATILKKLDIMKLLIARGADPDIPNTD-------------------------- 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  341 eaarsgneeklmalltplnvnchasdgrKSTPLHLAAGYNRVRIVQLLLQHGADVHAKDKGGLVPLHNACSYGHYEVTEL 420
Cdd:PHA02875  135 ----------------------------KFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKM 186
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 767950366  421 LLKHGACVNAMDL-WQFTPLHEAASKNRVEVCSLLLSHGADPTLV 464
Cdd:PHA02875  187 LLDSGANIDYFGKnGCVAALCYAIENNKIDIVRLFIKRGADCNIM 231
Ank_2 pfam12796
Ankyrin repeats (3 copies);
186-279 1.53e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.14  E-value: 1.53e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366   186 LLEACRNGDVSRVKRLVDAaNVNAKDMAGRKSSPLHFAAGFGRKDVVEHLLQ-MGANVharDDGGLIPLHNACSFGHAEV 264
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLEN-GADANLQDKNGRTALHLAAKNGHLEIVKLLLEhADVNL---KDNGRTALHYAARSGHLEI 76
                           90
                   ....*....|....*
gi 767950366   265 VSLLLCQGADPNARD 279
Cdd:pfam12796   77 VKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
526-619 1.79e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.14  E-value: 1.79e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366   526 LHCAVASlhpKRKQVTELLLRKGANVNEKNKDFMTPLHVAAERAHNDVMEVLHKHGAKMNALDtlGQTALHRAALAGHLQ 605
Cdd:pfam12796    1 LHLAAKN---GNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN--GRTALHYAARSGHLE 75
                           90
                   ....*....|....
gi 767950366   606 TCRLLLSYGSDPSI 619
Cdd:pfam12796   76 IVKLLLEKGADINV 89
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
1031-1085 3.16e-14

SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of approximately 70 amino acids. This domain is found in the Fungi/Metazoa group and in a restricted number of bacteria. Proteins with SAM domains are represented by a wide variety of domain architectures and have different intracellular localization, including nucleus, cytoplasm and membranes. SAM domains have diverse functions. They can interact with proteins, RNAs and membrane lipids, contain site of phosphorylation and/or kinase docking site, and play a role in protein homo and hetero dimerization/oligomerization in processes ranging from signal transduction to regulation of transcription. Mutations in SAM domains have been linked to several diseases.


Pssm-ID: 188886 [Multi-domain]  Cd Length: 56  Bit Score: 68.03  E-value: 3.16e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767950366 1031 ISQFLKSLGLEHLRDIFETEQITLDVLADMGHEELKEIGINAYGHRHKLIKGVER 1085
Cdd:cd09487     2 VAEWLESLGLEQYADLFRKNEIDGDALLLLTDEDLKELGITSPGHRKKILRAIQR 56
PHA03100 PHA03100
ankyrin repeat protein; Provisional
836-954 4.40e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 76.24  E-value: 4.40e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  836 RNSTPLHLAAGYNNLEVAEYLLEHGADVNAQDKGGLIPLHNAASYGHV-----DIAALLIKYNTCVNATDKWAFTPLHEA 910
Cdd:PHA03100   34 KPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYA 113
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767950366  911 AQKGRTQ--LCALLLAHGADPTMKNQEGQTPLDLATAD-----DIRALLID 954
Cdd:PHA03100  114 ISKKSNSysIVEYLLDNGANVNIKNSDGENLLHLYLESnkidlKILKLLID 164
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
1030-1087 5.47e-14

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 67.68  E-value: 5.47e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 767950366  1030 NISQFLKSLGLEHLRDIFETEQIT-LDVLADMGHEELKEIGINAYGHRHKLIKGVERLL 1087
Cdd:pfam07647    8 SVADWLRSIGLEQYTDNFRDQGITgAELLLRLTLEDLKRLGITSVGHRRKILKKIQELK 66
PHA02878 PHA02878
ankyrin repeat protein; Provisional
205-362 1.27e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 74.92  E-value: 1.27e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  205 ANVNAKDmAGRKSSPLHFAAGFGRKDVVEHLLQMGANVHARDDGGLIPLHNACSFGHAEVVSLLLCQGADPNARDNWNYT 284
Cdd:PHA02878  158 ADINMKD-RHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNT 236
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  285 PLHEAAIKGK-IDVCIVLLQHGADPNIRNT-DGKSALDLADPSA-KAVLTGEYKKDelleaARSGNEEKL----MALLTP 357
Cdd:PHA02878  237 PLHISVGYCKdYDILKLLLEHGVDVNAKSYiLGLTALHSSIKSErKLKLLLEYGAD-----INSLNSYKLtplsSAVKQY 311

                  ....*
gi 767950366  358 LNVNC 362
Cdd:PHA02878  312 LCINI 316
PHA02875 PHA02875
ankyrin repeat protein; Provisional
686-891 3.82e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 73.10  E-value: 3.82e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  686 TPLHFAAGYNRVSVVEYLLHHGADVHAKDKGGLVPLHNACSYGHYEVAELLVRHGASVNVAdLWK--FTPLHEAAAKGKY 763
Cdd:PHA02875   37 SPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDV-FYKdgMTPLHLATILKKL 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  764 EICKLLLKHGADPTKKNRDGNTPLDL-VKEGDTDIQDLLrgdaalLDaakkgclarvQKLCTpeniNCRDTQGrnSTPLH 842
Cdd:PHA02875  116 DIMKLLIARGADPDIPNTDKFSPLHLaVMMGDIKGIELL------ID----------HKACL----DIEDCCG--CTPLI 173
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 767950366  843 LAAGYNNLEVAEYLLEHGADVNAQDKGGLIPLH-NAASYGHVDIAALLIK 891
Cdd:PHA02875  174 IAMAKGDIAICKMLLDSGANIDYFGKNGCVAALcYAIENNKIDIVRLFIK 223
Ank_4 pfam13637
Ankyrin repeats (many copies);
837-890 5.58e-13

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 64.60  E-value: 5.58e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 767950366   837 NSTPLHLAAGYNNLEVAEYLLEHGADVNAQDKGGLIPLHNAASYGHVDIAALLI 890
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
724-913 6.07e-13

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 73.75  E-value: 6.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  724 ACSYGHYEVAELLVRHGASVNVADLWKFTPLHEAAAKGkYEICKL-LLKHGADPTKKNRDGNTPL-DLVKEGDTDIQDLL 801
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKG-YEDCVLvLLKHACNVHIRDANGNTALwNAISAKHHKIFRIL 610
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  802 RGDAALLDAAKKGCLarvqkLCTpenincrdtqgrnstplhlAAGYNNLEVAEYLLEHGADVNAQDKGGLIPLHNAASYG 881
Cdd:PLN03192  611 YHFASISDPHAAGDL-----LCT-------------------AAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAED 666
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 767950366  882 HVDIAALLIKYN---TCVNATDKWAFTPLHEAAQK 913
Cdd:PLN03192  667 HVDMVRLLIMNGadvDKANTDDDFSPTELRELLQK 701
PHA02874 PHA02874
ankyrin repeat protein; Provisional
252-458 7.93e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 72.30  E-value: 7.93e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  252 PLHNACSFGHAEVVSLLLCQGADPNARDNWNYTPLHEAAIKGKIDVCIVLLQHGADPNIrntdgksaLDLADPSAKAVLT 331
Cdd:PHA02874   38 PLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSI--------LPIPCIEKDMIKT 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  332 geykkdeLLEAArsgneeklmalltplnVNCHASDGRKSTPLHLAAGYNRVRIVQLLLQHGADVHAKDKGGLVPLHNACS 411
Cdd:PHA02874  110 -------ILDCG----------------IDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIK 166
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 767950366  412 YGHYEVTELLLKHGACVNAMDLWQFTPLHEAASKNRVEVCSLLLSHG 458
Cdd:PHA02874  167 HNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHG 213
PHA03100 PHA03100
ankyrin repeat protein; Provisional
182-341 2.89e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 70.46  E-value: 2.89e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  182 ALRELLEACRNgDVSRVKRLVD-AANVNAKDmagrkssplhfaagfgrkdVVEHLLQMGANVHARDDGGLIPLHNACSFG 260
Cdd:PHA03100  144 LLHLYLESNKI-DLKILKLLIDkGVDINAKN-------------------RVNYLLSYGVPINIKDVYGFTPLHYAVYNN 203
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  261 HAEVVSLLLCQGADPNARDNWNYTPLHEAAIKGKIDVCIVLLQHGADPNI----------RNTDGKSALDLADPSAKAVL 330
Cdd:PHA03100  204 NPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTiietllyfkdKDLNTITKIKMLKKSIMYMF 283
                         170
                  ....*....|....
gi 767950366  331 T---GEYKKDELLE 341
Cdd:PHA03100  284 LldpGFYKNRKLIE 297
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
1030-1087 3.23e-12

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735  Cd Length: 68  Bit Score: 62.70  E-value: 3.23e-12
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 767950366   1030 NISQFLKSLGLEHLRDIFETEQIT-LDVLADMGHEELKEIGINAYGHRHKLIKGVERLL 1087
Cdd:smart00454    8 SVADWLESIGLEQYADNFRKNGIDgALLLLLTSEEDLKELGITKLGHRKKILKAIQKLK 66
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
542-754 3.88e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 71.05  E-value: 3.88e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  542 ELLLRKGANVNEKNKDFMTPLHVAAERAHNDVMEVLHKHGAKMNALDTLGQTALHRAALAGHLQTCRLLlsygsdpsiis 621
Cdd:PLN03192  542 EELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL----------- 610
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  622 lqgftaaqmgneavQQILSESTPIRTSDVdyrLLEASKAGDLETVKQLcssqnvncrdlegrhstplhfaagynrvsvve 701
Cdd:PLN03192  611 --------------YHFASISDPHAAGDL---LCTAAKRNDLTAMKEL-------------------------------- 641
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767950366  702 ylLHHGADVHAKDKGGLVPLHNACSYGHYEVAELLVRHGASVNVADLW-KFTPL 754
Cdd:PLN03192  642 --LKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDdDFSPT 693
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
232-439 5.37e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 70.67  E-value: 5.37e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  232 VEHLL--QMGANVHARDDGGLIplhNACSFGHAEVVSLLLCQGADPNARDNWNYTPLHEAAIKGKIDVCIVLLQHGADPN 309
Cdd:PLN03192  509 VGDLLgdNGGEHDDPNMASNLL---TVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVH 585
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  310 IRNTDGKSALdladpsAKAVLTGEYKKDELL-EAARSGNEeklmalltplnvncHASdgrkSTPLHLAAGYNRVRIVQLL 388
Cdd:PLN03192  586 IRDANGNTAL------WNAISAKHHKIFRILyHFASISDP--------------HAA----GDLLCTAAKRNDLTAMKEL 641
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 767950366  389 LQHGADVHAKDKGGLVPLHNACSYGHYEVTELLLKHGACVNAMDLWQ-FTPL 439
Cdd:PLN03192  642 LKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDDdFSPT 693
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
1031-1086 5.84e-12

SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.


Pssm-ID: 425739  Cd Length: 64  Bit Score: 61.90  E-value: 5.84e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 767950366  1031 ISQFLKSLGLEHLRDIFETEQITLDVLADMGHEELKEIGINAYGHRHKLIKGVERL 1086
Cdd:pfam00536    8 VGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRL 63
Ank_4 pfam13637
Ankyrin repeats (many copies);
684-737 9.30e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 61.14  E-value: 9.30e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 767950366   684 HSTPLHFAAGYNRVSVVEYLLHHGADVHAKDKGGLVPLHNACSYGHYEVAELLV 737
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
370-422 3.62e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 59.60  E-value: 3.62e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 767950366   370 STPLHLAAGYNRVRIVQLLLQHGADVHAKDKGGLVPLHNACSYGHYEVTELLL 422
Cdd:pfam13637    2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
752-946 4.14e-11

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: 67.35  E-value: 4.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  752 TPLHEAAAKGKYE-ICKLLLKHGADPTKKNRDGNTPLDLVKEGDTDiqdllrgDAA--LLDAAkkgclarvqklctPENI 828
Cdd:cd22192    19 SPLLLAAKENDVQaIKKLLKCPSCDLFQRGALGETALHVAALYDNL-------EAAvvLMEAA-------------PELV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  829 NCRDT----QGRnsTPLHLAAGYNNLEVAEYLLEHGADVNA---------QDKGGLI-----PLHNAASYGHVDIAALLI 890
Cdd:cd22192    79 NEPMTsdlyQGE--TALHIAVVNQNLNLVRELIARGADVVSpratgtffrPGPKNLIyygehPLSFAACVGNEEIVRLLI 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767950366  891 KYNTCVNATDKWAFTPLH----EAAQKGRTQLCALLLAhgADP--------TMKNQEGQTPLDLATAD 946
Cdd:cd22192   157 EHGADIRAQDSLGNTVLHilvlQPNKTFACQMYDLILS--YDKeddlqpldLVPNNQGLTPFKLAAKE 222
parp_like cd01437
Poly(ADP-ribose) polymerase (parp) catalytic domain catalyses the covalent attachment of ...
1063-1300 5.03e-11

Poly(ADP-ribose) polymerase (parp) catalytic domain catalyses the covalent attachment of ADP-ribose units from NAD+ to itself and to a limited number of other DNA binding proteins, which decreases their affinity for DNA. Poly(ADP-ribose) polymerase is a regulatory component induced by DNA damage. The carboxyl-terminal region is the most highly conserved region of the protein. Experiments have shown that a carboxyl 40 kDa fragment is still catalytically active. Poly(ADP-ribose)-like polymerases (PARPS 1-3, VPARP, tankyrase) catalyze the addition of up to 100 ADP_ribose units from NAD+. PARPs 1 and 2 are localized in the nucleaus, bind DNA, and are activated by DNA damage. VPARP is part of the vault ribonucleoprotein complex. Tankyrases regulates telomere length through interactions with telomere repeat binding factor 1.


Pssm-ID: 238717 [Multi-domain]  Cd Length: 347  Bit Score: 65.75  E-value: 5.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366 1063 EELKEIGInAYghrhKLIKGVERLLGgqqgtNP----YLTFHCvnqgtillDLAPEDK---EYQSVEEEMQSTirehrdg 1135
Cdd:cd01437   106 EALRDIEI-AS----KLLKDDEDDSD-----DPldanYEKLKC--------KIEPLDKdseEYKIIEKYLKNT------- 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366 1136 gnaGGIFNRYN--VIRIQKVVNKKLRERFchrqkevseENHNH-HNERMLFHGSPFIN--AIIHKGF--DERHAYIGG-M 1207
Cdd:cd01437   161 ---HAPTTEYTveVQEIFRVEREGETDRF---------KPFKKlGNRKLLWHGSRLTNfvGILSQGLriAPPEAPVTGyM 228
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366 1208 FGAGIYFAENSSKSNQYVYgigGGTGCPThkdrscyichRQMLFCRVTLGKSF-LQFSTMKMAHAPPGHHSVIGR----- 1281
Cdd:cd01437   229 FGKGIYFADMFSKSANYCH---ASASDPT----------GLLLLCEVALGKMNeLKKADYMAKELPKGKHSVKGLgktap 295
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 767950366 1282 -PSVN-----------------------GLAYAEYVIYRGEQV 1300
Cdd:cd01437   296 dPSEFeidldgvvvplgkpvpsghktdtSLLYNEYIVYDVAQV 338
PHA02875 PHA02875
ankyrin repeat protein; Provisional
404-628 8.61e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 65.78  E-value: 8.61e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  404 VPLHNACSYGHYEVTELLLKHGACVNAMDLWQFTPLHEAASKNRVEVCSLLLSHGADPTLvnchgksavdmaPTPELRER 483
Cdd:PHA02875    4 VALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDV------------KYPDIESE 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  484 LtyefkgHsllQAAREADLAKVKKTLAL-EIINFKQPQSHETALHCAVASlhpKRKQVTELLLRKGANVNEKNKDFMTPL 562
Cdd:PHA02875   72 L------H---DAVEEGDVKAVEELLDLgKFADDVFYKDGMTPLHLATIL---KKLDIMKLLIARGADPDIPNTDKFSPL 139
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767950366  563 HVAAERAHNDVMEVLHKHGAKMNALDTLGQTALHRAALAGHLQTCRLLLSYGSDPSIISLQGFTAA 628
Cdd:PHA02875  140 HLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAA 205
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
339-493 8.75e-11

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 66.43  E-value: 8.75e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  339 LLEAARSGN----EEKLMALLTPlnvncHASDGRKSTPLHLAAGYNRVRIVQLLLQHGADVHAKDKGGLVPLHNACSYGH 414
Cdd:PLN03192  529 LLTVASTGNaallEELLKAKLDP-----DIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKH 603
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  415 YEVTEL-------------------------------LLKHGACVNAMDLWQFTPLHEAASKNRVEVCSLLLSHGADPTL 463
Cdd:PLN03192  604 HKIFRIlyhfasisdphaagdllctaakrndltamkeLLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDK 683
                         170       180       190
                  ....*....|....*....|....*....|
gi 767950366  464 VNCHGksavDMAPTpELRERLTYEFKGHSL 493
Cdd:PLN03192  684 ANTDD----DFSPT-ELRELLQKRELGHSI 708
TCCD_inducible_PARP_like cd01439
Poly(ADP-ribose) polymerases catalyse the covalent attachment of ADP-ribose units from NAD+ to ...
1181-1300 2.19e-10

Poly(ADP-ribose) polymerases catalyse the covalent attachment of ADP-ribose units from NAD+ to itself and to a limited number of other DNA binding proteins, which decreases their affinity for DNA. Poly(ADP-ribose) polymerase is a regulatory component induced by DNA damage. The carboxyl-terminal region is the most highly conserved region of the protein. 2,3,7,8-Tetrachlorodibenzo-p-dioxin (TCDD) causes pleotropic effects in mammalian species through modulating gene expression. TCCD indicible PARP (TiPARP) is a target of TCDD that may contribute to multiple responses to TCDD by modulating protein function through poly ADP-ribosylation


Pssm-ID: 238719 [Multi-domain]  Cd Length: 121  Bit Score: 59.26  E-value: 2.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366 1181 MLFHG--SPFINAIIHKGFDER-HAYIGGMFGAGIYFAENSSKSNQYVYGIGGGTGcpthkdrscyicHRQMLFCRVTLG 1257
Cdd:cd01439     1 LLFHGtsADAVEAICRHGFDRRfCGKHGTMYGKGSYFAKNASYSHQYSKKSPKADG------------LKEMFLARVLTG 68
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 767950366 1258 KSFLQFSTMKMAHAPPGHHSVIGRPS-VNGLAYAE-YVIYRGEQV 1300
Cdd:cd01439    69 DYTQGHPGYRRPPLKPSGVELDRYDScVDNVSNPSiFVIFSDVQA 113
Ank_4 pfam13637
Ankyrin repeats (many copies);
559-611 2.74e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 56.90  E-value: 2.74e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 767950366   559 MTPLHVAAERAHNDVMEVLHKHGAKMNALDTLGQTALHRAALAGHLQTCRLLL 611
Cdd:pfam13637    2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
217-269 4.38e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 56.51  E-value: 4.38e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 767950366   217 SSPLHFAAGFGRKDVVEHLLQMGANVHARDDGGLIPLHNACSFGHAEVVSLLL 269
Cdd:pfam13637    2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02946 PHA02946
ankyin-like protein; Provisional
232-406 5.12e-10

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 63.53  E-value: 5.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  232 VEHLLQMGANVHARDDGGLIPLHNACSFGHAEVVSLLLCQGADPNARDNWNYTPLHeaAIKGKIDVCI----VLLQHGAD 307
Cdd:PHA02946   55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLY--YLSGTDDEVIerinLLVQYGAK 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  308 PN--IRNTDGKSALDLADPSAK-----------AVLTGEYKKDELLEAARSGN-EEKLMALLTPLNVNCHASDGRKSTPL 373
Cdd:PHA02946  133 INnsVDEEGCGPLLACTDPSERvfkkimsigfeARIVDKFGKNHIHRHLMSDNpKASTISWMMKLGISPSKPDHDGNTPL 212
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 767950366  374 HLAAG--YNRVRIVQLLLQhGADVHAKDKGGLVPL 406
Cdd:PHA02946  213 HIVCSktVKNVDIINLLLP-STDVNKQNKFGDSPL 246
PHA02876 PHA02876
ankyrin repeat protein; Provisional
191-426 5.13e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 63.93  E-value: 5.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  191 RNG-DVSRVKRLVD-AANVNAKDMAgrKSSPLHFAAGFGR-KDVVEHLLQMGANVharddggliplhnacsfghaevvsl 267
Cdd:PHA02876  316 KNGyDTENIRTLIMlGADVNAADRL--YITPLHQASTLDRnKDIVITLLELGANV------------------------- 368
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  268 llcqgadpNARDNWNYTPLHEAAIKGKIDVCIVLLQHGADPNIRNTDGKSALDLAdpsakavLTGEykkdelleaarsgN 347
Cdd:PHA02876  369 --------NARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFA-------LCGT-------------N 420
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  348 EEKLMALLTPLNVNCHASDGRKSTPLHLAAGYN-RVRIVQLLLQHGADVHAKDKGGLVPLHNACSYghYEVTELLLKHGA 426
Cdd:PHA02876  421 PYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIALEY--HGIVNILLHYGA 498
Ank_5 pfam13857
Ankyrin repeats (many copies);
267-322 5.23e-10

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 56.20  E-value: 5.23e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 767950366   267 LLLCQGADPNARDNWNYTPLHEAAIKGKIDVCIVLLQHGADPNIRNTDGKSALDLA 322
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
180-322 7.78e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 63.35  E-value: 7.78e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  180 SGALRELLEACRNGDVSrvkrlvdaanvnakDMAGRksSPLHFAAGFGRKDVVEHLLQMGANVHARDDGGLIPLHNACSF 259
Cdd:PLN03192  538 AALLEELLKAKLDPDIG--------------DSKGR--TPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISA 601
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767950366  260 GHAEVVSLL--LCQGADPNARDNWnytpLHEAAIKGKIDVCIVLLQHGADPNIRNTDGKSALDLA 322
Cdd:PLN03192  602 KHHKIFRILyhFASISDPHAAGDL----LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVA 662
Ank_4 pfam13637
Ankyrin repeats (many copies);
405-455 9.86e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.36  E-value: 9.86e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 767950366   405 PLHNACSYGHYEVTELLLKHGACVNAMDLWQFTPLHEAASKNRVEVCSLLL 455
Cdd:pfam13637    4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
654-739 1.38e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 62.61  E-value: 1.38e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  654 LLEASKAGDLETVKQLCSS-QNVNCRDLEGRhsTPLHFAAGYNRVSVVEYLLHHGADVHAKDKGGLVPLHNACSYGHYEV 732
Cdd:PTZ00322   86 LCQLAASGDAVGARILLTGgADPNCRDYDGR--TPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREV 163

                  ....*..
gi 767950366  733 AELLVRH 739
Cdd:PTZ00322  164 VQLLSRH 170
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
320-427 2.22e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 61.84  E-value: 2.22e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  320 DLADPSAKAVLTGEykkdeLLEAARSGNEEKLMALLTP-LNVNCHASDGRksTPLHLAAGYNRVRIVQLLLQHGADVHAK 398
Cdd:PTZ00322   72 EVIDPVVAHMLTVE-----LCQLAASGDAVGARILLTGgADPNCRDYDGR--TPLHIACANGHVQVVRVLLEFGADPTLL 144
                          90       100
                  ....*....|....*....|....*....
gi 767950366  399 DKGGLVPLHNACSYGHYEVTELLLKHGAC 427
Cdd:PTZ00322  145 DKDGKTPLELAEENGFREVVQLLSRHSQC 173
Ank_5 pfam13857
Ankyrin repeats (many copies);
827-875 2.76e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 54.27  E-value: 2.76e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 767950366   827 NINCRDTQGRNSTPLHLAAGYNNLEVAEYLLEHGADVNAQDKGGLIPLH 875
Cdd:pfam13857    6 PIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
374-457 3.05e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 61.45  E-value: 3.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  374 HLAAGYNRVRIvQLLLQHGADVHAKDKGGLVPLHNACSYGHYEVTELLLKHGACVNAMDLWQFTPLHEAASKNRVEVCSL 453
Cdd:PTZ00322   88 QLAASGDAVGA-RILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166

                  ....
gi 767950366  454 LLSH 457
Cdd:PTZ00322  167 LSRH 170
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
260-325 3.61e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 61.07  E-value: 3.61e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767950366  260 GHAEVVSLLLCQGADPNARDNWNYTPLHEAAIKGKIDVCIVLLQHGADPNIRNTDGKSALDLADPS 325
Cdd:PTZ00322   93 GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEEN 158
PHA02874 PHA02874
ankyrin repeat protein; Provisional
284-598 4.60e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 60.36  E-value: 4.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  284 TPLHEAAIKGKIDVCIVLLQHGADPNIRNTDgksaldLADPSAKAVLTGEYKKDELLeaARSGNEEKLmalltpLNVNCH 363
Cdd:PHA02874   37 TPLIDAIRSGDAKIVELFIKHGADINHINTK------IPHPLLTAIKIGAHDIIKLL--IDNGVDTSI------LPIPCI 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  364 ASDgrkstplhlaagynrvrIVQLLLQHGADVHAKDKGGLVPLHNACSYGHYEVTELLLKHGACVNAMDLWQFTPLHEAA 443
Cdd:PHA02874  103 EKD-----------------MIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAI 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  444 SKNRVEVCSLLLSHGADPTLVNCHGKSavdmaptpelrerltyefkghSLLQAAREADLAKVKKTLALEIINFKQPQSHE 523
Cdd:PHA02874  166 KHNFFDIIKLLLEKGAYANVKDNNGES---------------------PLHNAAEYGDYACIKLLIDHGNHIMNKCKNGF 224
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767950366  524 TALHCAVasLHpkRKQVTELLLrKGANVNEKNKDFMTPLHVAAER-AHNDVMEVLHKHGAKMNALDTLGQTALHRA 598
Cdd:PHA02874  225 TPLHNAI--IH--NRSAIELLI-NNASINDQDIDGSTPLHHAINPpCDIDIIDILLYHKADISIKDNKGENPIDTA 295
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
654-857 6.49e-09

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: 60.41  E-value: 6.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  654 LLEASKAGDLETVKQL--CSSQNVNCRDLEGRhsTPLHFAAGYNRVSVVEYLLHHG---------ADVHAkdkgGLVPLH 722
Cdd:cd22192    21 LLLAAKENDVQAIKKLlkCPSCDLFQRGALGE--TALHVAALYDNLEAAVVLMEAApelvnepmtSDLYQ----GETALH 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  723 NACSYGHYEVAELLVRHGASVNVA------------DLWKFT--PLHEAAAKGKYEICKLLLKHGADPTKKNRDGNTPLD 788
Cdd:cd22192    95 IAVVNQNLNLVRELIARGADVVSPratgtffrpgpkNLIYYGehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767950366  789 -LV----KEGDTDIQDLlrgdaaLLDAAKKGCLARVQKLctpenincrdTQGRNSTPLHLAAGYNNLEVAEYLL 857
Cdd:cd22192   175 iLVlqpnKTFACQMYDL------ILSYDKEDDLQPLDLV----------PNNQGLTPFKLAAKEGNIVMFQHLV 232
SAM_Ste50-like_fungal cd09533
SAM domain of Ste50_like (ubc2) subfamily; SAM (sterile alpha motif) domain of Ste50-like (or ...
1033-1086 8.31e-09

SAM domain of Ste50_like (ubc2) subfamily; SAM (sterile alpha motif) domain of Ste50-like (or Ubc2 for Ustilago bypass of cyclase) subfamily is a putative protein-protein interaction domain. This group includes only fungal proteins. Basidiomycetes have an N-terminal SAM domain, central UBQ domain, and C-terminal SH3 domain, while Ascomycetes lack the SH3 domain. Ubc2 of Ustilago maydis is a major virulence and maize pathogenicity factor. It is required for filamentous growth (the budding haploid form of Ustilago maydis is a saprophyte, while filamentous dikaryotic form is a pathogen). Also the Ubc2 protein is involved in the pheromone-responsive morphogenesis via the MAP kinase cascade. The SAM domain is necessary for ubc2 function; deletion of SAM eliminates this function. A Lys-to-Glu mutation in the SAM domain of ubc2 gene induces temperature sensitivity.


Pssm-ID: 188932  Cd Length: 58  Bit Score: 52.70  E-value: 8.31e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767950366 1033 QFLKSLGLEHLRDIFETEQITLDVLADMGHEELKEIGINAYGHRHKLIKGVERL 1086
Cdd:cd09533     4 DWLSSLGLPQYEDQFIENGITGDVLVALDHEDLKEMGITSVGHRLTILKAVYEL 57
Ank_4 pfam13637
Ankyrin repeats (many copies);
720-770 9.01e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.66  E-value: 9.01e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 767950366   720 PLHNACSYGHYEVAELLVRHGASVNVADLWKFTPLHEAAAKGKYEICKLLL 770
Cdd:pfam13637    4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
733-803 9.08e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 59.91  E-value: 9.08e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767950366  733 AELLVRHGASVNVADLWKFTPLHEAAAKGKYEICKLLLKHGADPTKKNRDGNTPLDLVKEGDT-DIQDLLRG 803
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFrEVVQLLSR 169
Ank_4 pfam13637
Ankyrin repeats (many copies);
252-302 1.31e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.28  E-value: 1.31e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 767950366   252 PLHNACSFGHAEVVSLLLCQGADPNARDNWNYTPLHEAAIKGKIDVCIVLL 302
Cdd:pfam13637    4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02798 PHA02798
ankyrin-like protein; Provisional
382-626 1.40e-08

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 59.08  E-value: 1.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  382 VRIVQLLLQHGADVHAKDKGGLVPL----HNACSYGH-YEVTELLLKHGACVNAMDLWQFTPLHEAASK---NRVEVCSL 453
Cdd:PHA02798   51 TDIVKLFINLGANVNGLDNEYSTPLctilSNIKDYKHmLDIVKILIENGADINKKNSDGETPLYCLLSNgyiNNLEILLF 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  454 LLSHGADPTLVNCHGKSAVDMaptpelrerltyefkghsLLQAAREADLAKVKKTLALEI-INFKQPQSHETALHCAVAS 532
Cdd:PHA02798  131 MIENGADTTLLDKDGFTMLQV------------------YLQSNHHIDIEIIKLLLEKGVdINTHNNKEKYDTLHCYFKY 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  533 LHPK-RKQVTELLLRKGANVNEKNK-------DFMTPLHVAAERAHNDVMEVLHKHgAKMNALDTLGQTALHRAALAGHL 604
Cdd:PHA02798  193 NIDRiDADILKLFVDNGFIINKENKshkkkfmEYLNSLLYDNKRFKKNILDFIFSY-IDINQVDELGFNPLYYSVSHNNR 271
                         250       260
                  ....*....|....*....|..
gi 767950366  605 QTCRLLLSYGSDPSIISLQGFT 626
Cdd:PHA02798  272 KIFEYLLQLGGDINIITELGNT 293
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
729-944 1.90e-08

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: 58.94  E-value: 1.90e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366   729 HYEVAELLVRHGASVNVADlwkfTPLHeAAAKGKYEICKLLLKHgadpTKKNRDGNTPLDLVKEGDTDiqDLLRGdaall 808
Cdd:TIGR00870   65 NLELTELLLNLSCRGAVGD----TLLH-AISLEYVDAVEAILLH----LLAAFRKSGPLELANDQYTS--EFTPG----- 128
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366   809 daakkgclarvqklctpenincrdtqgrnSTPLHLAAGYNNLEVAEYLLEHGADVNAQDKG--------------GLIPL 874
Cdd:TIGR00870  129 -----------------------------ITALHLAAHRQNYEIVKLLLERGASVPARACGdffvksqgvdsfyhGESPL 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366   875 HNAASYGHVDIAALLIKYNTCVNATDKWAFTPLHEAA---------QKGRTQLCALLLAHGA--DPTMK-----NQEGQT 938
Cdd:TIGR00870  180 NAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVmenefkaeyEELSCQMYNFALSLLDklRDSKElevilNHQGLT 259

                   ....*.
gi 767950366   939 PLDLAT 944
Cdd:TIGR00870  260 PLKLAA 265
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
284-440 3.78e-08

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 57.72  E-value: 3.78e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  284 TPLHEAAIKGKID-VCIVLLQHGADPNIRNTDGKSALDLAdpsakaVLtgeYKKDE----LLEAARsgneeklmallTPL 358
Cdd:cd22192    19 SPLLLAAKENDVQaIKKLLKCPSCDLFQRGALGETALHVA------AL---YDNLEaavvLMEAAP-----------ELV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  359 NVNCHASDGRKSTPLHLAAGYNRVRIVQLLLQHGADVHA---------KDKGGLV-----PLHNACSYGHYEVTELLLKH 424
Cdd:cd22192    79 NEPMTSDLYQGETALHIAVVNQNLNLVRELIARGADVVSpratgtffrPGPKNLIyygehPLSFAACVGNEEIVRLLIEH 158
                         170
                  ....*....|....*.
gi 767950366  425 GACVNAMDLWQFTPLH 440
Cdd:cd22192   159 GADIRAQDSLGNTVLH 174
Ank_5 pfam13857
Ankyrin repeats (many copies);
354-407 4.08e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 50.81  E-value: 4.08e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 767950366   354 LLTPLNVNCHASDGRKSTPLHLAAGYNRVRIVQLLLQHGADVHAKDKGGLVPLH 407
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
735-790 4.59e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 50.81  E-value: 4.59e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 767950366   735 LLVRHGASVNVADLWKFTPLHEAAAKGKYEICKLLLKHGADPTKKNRDGNTPLDLV 790
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
829-895 6.69e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 57.22  E-value: 6.69e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767950366  829 NCRDTQGRnsTPLHLAAGYNNLEVAEYLLEHGADVNAQDKGGLIPLHNAASYGHVDIAALLIKYNTC 895
Cdd:PTZ00322  109 NCRDYDGR--TPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQC 173
Ank_5 pfam13857
Ankyrin repeats (many copies);
896-943 1.09e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 49.65  E-value: 1.09e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 767950366   896 VNATDKWAFTPLHEAAQKGRTQLCALLLAHGADPTMKNQEGQTPLDLA 943
Cdd:pfam13857    9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
437-705 1.40e-07

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: 55.79  E-value: 1.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  437 TPLHEAASKNRVE-VCSLLLSHGADPTLVNCHGKSAVDMAPTPELRERLTYefkghsLLQAAREadLAKVKKTLALeiin 515
Cdd:cd22192    19 SPLLLAAKENDVQaIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVV------LMEAAPE--LVNEPMTSDL---- 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  516 fkqpQSHETALHCAVASlhpKRKQVTELLLRKGANV------------NEKNKDFMT--PLHVAAERAHNDVMEVLHKHG 581
Cdd:cd22192    87 ----YQGETALHIAVVN---QNLNLVRELIARGADVvspratgtffrpGPKNLIYYGehPLSFAACVGNEEIVRLLIEHG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  582 AKMNALDTLGQTALHRAAL-AGHLQTCR---LLLSYGSDPSIISL------QGFT----AAQMGN-EAVQQILS------ 640
Cdd:cd22192   160 ADIRAQDSLGNTVLHILVLqPNKTFACQmydLILSYDKEDDLQPLdlvpnnQGLTpfklAAKEGNiVMFQHLVQkrrhiq 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  641 -----------ESTPIRTSDVDYRLLE---------ASKAGDLETVKQLCSSQnvncRDLEGRHstplhfaagYNRVSVV 700
Cdd:cd22192   240 wtygpltstlyDLTEIDSWGDEQSVLElivsskkreARKILDVTPVKELVSLK----WKRYGRP---------YFRILAL 306

                  ....*
gi 767950366  701 EYLLH 705
Cdd:cd22192   307 LYLLY 311
Ank_2 pfam12796
Ankyrin repeats (3 copies);
493-588 1.44e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 50.50  E-value: 1.44e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366   493 LLQAAREADLAKVKKTLALEIINFKQPQSHETALHCAVASLHpkrKQVTELLLRKgANVNEKNKDfMTPLHVAAERAHND 572
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGH---LEIVKLLLEH-ADVNLKDNG-RTALHYAARSGHLE 75
                           90
                   ....*....|....*.
gi 767950366   573 VMEVLHKHGAKMNALD 588
Cdd:pfam12796   76 IVKLLLEKGADINVKD 91
Ank_5 pfam13857
Ankyrin repeats (many copies);
674-722 1.77e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.88  E-value: 1.77e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 767950366   674 NVNCRDLEGRHSTPLHFAAGYNRVSVVEYLLHHGADVHAKDKGGLVPLH 722
Cdd:pfam13857    6 PIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
235-304 1.83e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 55.67  E-value: 1.83e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  235 LLQMGANVHARDDGGLIPLHNACSFGHAEVVSLLLCQGADPNARDNWNYTPLHEAAIKGKIDVCIVLLQH 304
Cdd:PTZ00322  101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PHA02798 PHA02798
ankyrin-like protein; Provisional
649-940 1.94e-07

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 55.23  E-value: 1.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  649 DVD--YRLLEASKAGDLETVKQLCSSQNVNcrDLEGRHSTplhFAAGYNR----VSVVEYLLHHGADVHAKDKGGLVPL- 721
Cdd:PHA02798    2 DIDnlYNYITFSDNVKLSTVKLLIKSCNPN--EIVNEYSI---FQKYLQRdspsTDIVKLFINLGANVNGLDNEYSTPLc 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  722 ---HNACSYGH-YEVAELLVRHGASVNVADLWKFTPLHEAAAKG---KYEICKLLLKHGADPTKKNRDGNTPLDLVKEGD 794
Cdd:PHA02798   77 tilSNIKDYKHmLDIVKILIENGADINKKNSDGETPLYCLLSNGyinNLEILLFMIENGADTTLLDKDGFTMLQVYLQSN 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  795 TDIQ-DLLRgdaALLDaakKGClarvqklctpeNINCRDTQGRNSTpLHLAAGYN----NLEVAEYLLEHGADVNAQDKG 869
Cdd:PHA02798  157 HHIDiEIIK---LLLE---KGV-----------DINTHNNKEKYDT-LHCYFKYNidriDADILKLFVDNGFIINKENKS 218
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767950366  870 G-------LIPLHNAASYGHVDIAALLIKYNTcVNATDKWAFTPLHEAAQKGRTQLCALLLAHGADPTMKNQEGQTPL 940
Cdd:PHA02798  219 HkkkfmeyLNSLLYDNKRFKKNILDFIFSYID-INQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCL 295
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
263-468 2.56e-07

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 55.30  E-value: 2.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  263 EVVSLLLCQGADPNARDNWNYTPLHEAAIKGKIDVCIV--LLQHGADPNIRNTDGKSaldladpsakAVLTGEYKKDELl 340
Cdd:PHA02716  193 DILEWLCNNGVNVNLQNNHLITPLHTYLITGNVCASVIkkIIELGGDMDMKCVNGMS----------PIMTYIINIDNI- 261
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  341 eaarsgNEEklmalLTPLNVNCHASDGRKSTP--LHL---AAGYNRVRIVQLLLQHGADVHAKDKGGLVPLHNAC--SYG 413
Cdd:PHA02716  262 ------NPE-----ITNIYIESLDGNKVKNIPmiLHSyitLARNIDISVVYSFLQPGVKLHYKDSAGRTCLHQYIlrHNI 330
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767950366  414 HYEVTELLLKHGACVNAMDLWQFTPLH--------------EAASKNRVEVCSLLLSHGADPTLVNCHG 468
Cdd:PHA02716  331 STDIIKLLHEYGNDLNEPDNIGNTVLHtylsmlsvvnildpETDNDIRLDVIQCLISLGADITAVNCLG 399
SAM_BOI-like_fungal cd09535
SAM domain of BOI-like fungal subfamily; SAM (sterile alpha motif) domain of BOI-like fungal ...
1029-1086 2.64e-07

SAM domain of BOI-like fungal subfamily; SAM (sterile alpha motif) domain of BOI-like fungal subfamily is a potential protein-protein interaction domain. Proteins of this subfamily are apparently scaffold proteins, since most contain SH3 and PH domains, which are also protein-protein interaction domains, in addition to SAM domain. BOI-like proteins participate in cell cycle regulation. In particular BOI1 and BOI2 proteins of budding yeast S.cerevisiae are involved in bud formation, and POB1 protein of fission yeast S.pombe plays a role in cell elongation and separation. Among binding partners of BOI-like fungal subfamily members are such proteins as Bem1 and Cdc42 (they are known to be involved in cell polarization and bud formation).


Pssm-ID: 188934  Cd Length: 65  Bit Score: 48.71  E-value: 2.64e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767950366 1029 MNISQFLKSLGLE-HLRDIFETEQITLDVLADMGHEELKEIGINAYGHRHKLIKGVERL 1086
Cdd:cd09535     6 EQVAEWLLSAGFDdSVCEKFRENEITGDILLELDLEDLKELDIGSFGKRFKLWNEIKSL 64
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
842-925 3.08e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.90  E-value: 3.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  842 HLAAGYNNLEvAEYLLEHGADVNAQDKGGLIPLHNAASYGHVDIAALLIKYNTCVNATDKWAFTPLHEAAQKGRTQLCAL 921
Cdd:PTZ00322   88 QLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166

                  ....
gi 767950366  922 LLAH 925
Cdd:PTZ00322  167 LSRH 170
PHA02798 PHA02798
ankyrin-like protein; Provisional
230-470 3.12e-07

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 54.46  E-value: 3.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  230 DVVEHLLQMGANVHARDDGGLIP----LHNACSFGHA-EVVSLLLCQGADPNARDNWNYTP----LHEAAIKGKiDVCIV 300
Cdd:PHA02798   52 DIVKLFINLGANVNGLDNEYSTPlctiLSNIKDYKHMlDIVKILIENGADINKKNSDGETPlyclLSNGYINNL-EILLF 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  301 LLQHGADPNIRNTDGKSALDLadpsakAVLTGEYKKDELLEaarsgneeklMALLTPLNVNCHaSDGRKSTPLHLAAGYN 380
Cdd:PHA02798  131 MIENGADTTLLDKDGFTMLQV------YLQSNHHIDIEIIK----------LLLEKGVDINTH-NNKEKYDTLHCYFKYN 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  381 ----RVRIVQLLLQHGADVHAKDKGG-------LVPLHNACSYGHYEVTELLLKHgACVNAMDLWQFTPLHEAASKNRVE 449
Cdd:PHA02798  194 idriDADILKLFVDNGFIINKENKSHkkkfmeyLNSLLYDNKRFKKNILDFIFSY-IDINQVDELGFNPLYYSVSHNNRK 272
                         250       260
                  ....*....|....*....|.
gi 767950366  450 VCSLLLSHGADPTLVNCHGKS 470
Cdd:PHA02798  273 IFEYLLQLGGDINIITELGNT 293
Ank_4 pfam13637
Ankyrin repeats (many copies);
873-923 3.38e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.04  E-value: 3.38e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 767950366   873 PLHNAASYGHVDIAALLIKYNTCVNATDKWAFTPLHEAAQKGRTQLCALLL 923
Cdd:pfam13637    4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
839-868 4.81e-07

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: 47.28  E-value: 4.81e-07
                           10        20        30
                   ....*....|....*....|....*....|.
gi 767950366   839 TPLHLAAG-YNNLEVAEYLLEHGADVNAQDK 868
Cdd:pfam00023    4 TPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
790-947 7.22e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 53.72  E-value: 7.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  790 VKEGDTDIQDLL----------RGDAALLDAAKKGCLARVQKLCTPE-NINCRDTQGRnsTPLHLAAGYNNLEVAEYLLE 858
Cdd:PLN03192  502 KELHDLNVGDLLgdnggehddpNMASNLLTVASTGNAALLEELLKAKlDPDIGDSKGR--TPLHIAASKGYEDCVLVLLK 579
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  859 HGADVNAQDKGGLIPLHNAASYGHVDIAALLIKyntCVNATDKWAFTP-LHEAAQKGRTQLCALLLAHGADPTMKNQEGQ 937
Cdd:PLN03192  580 HACNVHIRDANGNTALWNAISAKHHKIFRILYH---FASISDPHAAGDlLCTAAKRNDLTAMKELLKQGLNVDSEDHQGA 656
                         170
                  ....*....|
gi 767950366  938 TPLDLATADD 947
Cdd:PLN03192  657 TALQVAMAED 666
Ank_2 pfam12796
Ankyrin repeats (3 copies);
439-555 8.54e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 48.19  E-value: 8.54e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366   439 LHEAASKNRVEVCSLLLSHGADPTLVNCHGKSAvdmaptpelrerltyefkghsLLQAAREADLAKVKktLALEIINFKQ 518
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTA---------------------LHLAAKNGHLEIVK--LLLEHADVNL 57
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 767950366   519 PQSHETALHCAVASLHPKrkqVTELLLRKGANVNEKN 555
Cdd:pfam12796   58 KDNGRTALHYAARSGHLE---IVKLLLEKGADINVKD 91
Ank_4 pfam13637
Ankyrin repeats (many copies);
752-801 9.56e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.88  E-value: 9.56e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 767950366   752 TPLHEAAAKGKYEICKLLLKHGADPTKKNRDGNTPLDL-VKEGDTDIQDLL 801
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFaASNGNVEVLKLL 53
PHA02859 PHA02859
ankyrin repeat protein; Provisional
661-801 1.12e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 50.97  E-value: 1.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  661 GDLETVKQLCSSQNvNCRDLegrHSTPLH--FAAGYNRVSVVEYLLHHGADVHAKDKG-GLVPLHNACSYG---HYEVAE 734
Cdd:PHA02859   32 DDIEGVKKWIKFVN-DCNDL---YETPIFscLEKDKVNVEILKFLIENGADVNFKTRDnNLSALHHYLSFNknvEPEILK 107
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767950366  735 LLVRHGASVNVADLWKFTPLHE--AAAKGKYEICKLLLKHGADPTKKNRDGNTPLD--LVKEGDTDIQDLL 801
Cdd:PHA02859  108 ILIDSGSSITEEDEDGKNLLHMymCNFNVRINVIKLLIDSGVSFLNKDFDNNNILYsyILFHSDKKIFDFL 178
Ank_5 pfam13857
Ankyrin repeats (many copies);
240-289 1.26e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.57  E-value: 1.26e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 767950366   240 ANVHARDDGGLIPLHNACSFGHAEVVSLLLCQGADPNARDNWNYTPLHEA 289
Cdd:pfam13857    7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PLN03123 PLN03123
poly [ADP-ribose] polymerase; Provisional
1177-1306 1.30e-06

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215590 [Multi-domain]  Cd Length: 981  Bit Score: 52.87  E-value: 1.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366 1177 HNERMLFHGSPFIN--AIIHKGFdeRHA-----YIGGMFGAGIYFAENSSKSNQYvygigggtgcpthkdrsCYICHRQ- 1248
Cdd:PLN03123  824 KNRMLLWHGSRLTNfvGILSQGL--RIAppeapATGYMFGKGVYFADLVSKSAQY-----------------CYTDRKNp 884
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366 1249 ---MLFCRVTLGKSFLQFSTMKMAHAPPGHHS--------------------VI---GRPSVNG-----LAYAEYVIYRG 1297
Cdd:PLN03123  885 vglMLLSEVALGEIYELKKAKYMDKPPRGKHStkglgktvpqesefvkwrddVVvpcGKPVPSKvkaseLMYNEYIVYNT 964
                         170
                  ....*....|..
gi 767950366 1298 EQVDT---LKAR 1306
Cdd:PLN03123  965 AQVKLqflLKVR 976
PHA02876 PHA02876
ankyrin repeat protein; Provisional
848-952 1.31e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 52.76  E-value: 1.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  848 NNLEVAEYLLEHGADVNAQDKGGLIPLHNAASYGHVDIAALLIKYNT--------------------------------- 894
Cdd:PHA02876  156 DELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGAdvniialddlsvlecavdsknidtikaiidnrs 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  895 -----------------------------CVNATDKWAFTPLHEAAQK-GRTQLCALLLAHGADPTMKNQEGQTPLDLAT 944
Cdd:PHA02876  236 ninkndlsllkairnedletslllydagfSVNSIDDCKNTPLHHASQApSLSRLVPKLLERGADVNAKNIKGETPLYLMA 315
                         170
                  ....*....|...
gi 767950366  945 -----ADDIRALL 952
Cdd:PHA02876  316 kngydTENIRTLI 328
SAM_BICC1 cd09520
SAM domain of BICC1 (bicaudal) subfamily; SAM (sterile alpha motif) domain of BICC1 (bicaudal) ...
1035-1080 1.62e-06

SAM domain of BICC1 (bicaudal) subfamily; SAM (sterile alpha motif) domain of BICC1 (bicaudal) subfamily is a protein-protein interaction domain. Proteins of this group have N-terminal K homology RNA-binding vigilin-like repeats and a C-terminal SAM domain. BICC1 is involved in the regulation of embryonic differentiation. It plays a role in the regulation of Dvl (Dishevelled) signaling, particularly in the correct cilia orientation and nodal flow generation. In Drosophila, disruption of BICC1 can disturb the normal migration direction of the anterior follicle cell of oocytes; the specific function of SAM is to recruit whole protein to the periphery of P-bodies. In mammals, mutations in this gene are associated with polycystic kidney disease and it was suggested that the BICC1 protein can indirectly interact with ANKS6 protein (ANKS6 is also associated with polycystic kidney disease) through some protein and RNA intermediates.


Pssm-ID: 188919  Cd Length: 65  Bit Score: 46.52  E-value: 1.62e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 767950366 1035 LKSLGLEHLRDIFETEQITLDVLADMGHEELKEIGINAYGHRHKLI 1080
Cdd:cd09520    11 LAKLGLEKYIDLFAQQEIDLQTFLTLTDQDLKELGITAFGARRKML 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
856-910 1.69e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.19  E-value: 1.69e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 767950366   856 LLEHG-ADVNAQDKGGLIPLHNAASYGHVDIAALLIKYNTCVNATDKWAFTPLHEA 910
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA03095 PHA03095
ankyrin-like protein; Provisional
198-300 1.89e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 51.95  E-value: 1.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  198 VKRLVDAA-NVNAKDMAGRksSPLHFAAGFG--RKDVVEHLLQMGANVHARDDGGLIPLHNACSFGHAEVVSLLLCQGAD 274
Cdd:PHA03095  205 VRELIRAGcDPAATDMLGN--TPLHSMATGSscKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGAD 282
                          90       100
                  ....*....|....*....|....*.
gi 767950366  275 PNARDNWNYTPLHEAAIKGkiDVCIV 300
Cdd:PHA03095  283 INAVSSDGNTPLSLMVRNN--NGRAV 306
SAM_Ste11_fungal cd09534
SAM domain of Ste11_fungal subfamily; SAM (sterile alpha motif) domain of Ste11 subfamily is a ...
1030-1086 2.15e-06

SAM domain of Ste11_fungal subfamily; SAM (sterile alpha motif) domain of Ste11 subfamily is a protein-protein interaction domain. Proteins of this subfamily have SAM domain at the N-terminus and protein kinase domain at the C-terminus. They participate in regulation of mating pheromone response, invasive growth and high osmolarity growth response. MAP triple kinase Ste11 from S.cerevisia is known to interact with Ste20 kinase and Ste50 regulator. These kinases are able to form homodimers interacting through their SAM domains as well as heterodimers or heterogenous complexes when either SAM domain of monomeric or homodimeric form of Ste11 interacts with Ste50 regulator.


Pssm-ID: 188933  Cd Length: 62  Bit Score: 46.05  E-value: 2.15e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767950366 1030 NISQFLKSLGLEHLRDIFETEQITLDVLADMGHEELKEIGINAYGHRHKLIKGVERL 1086
Cdd:cd09534     5 FVEEWLNELNCGQYLDIFEKNLITGDLLLELDKEALKELGITKVGDRIRLLRAIKSL 61
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
371-400 2.24e-06

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 45.36  E-value: 2.24e-06
                           10        20        30
                   ....*....|....*....|....*....|.
gi 767950366   371 TPLHLAAG-YNRVRIVQLLLQHGADVHAKDK 400
Cdd:pfam00023    4 TPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
875-981 2.32e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.21  E-value: 2.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  875 HNAASYGHVDIAALLIKYNTCvNATDKWAFTPLHEAAQKGRTQLCALLLAHGADPTMKNQEGQTPLDLATADDIR----A 950
Cdd:PTZ00322   88 QLAASGDAVGARILLTGGADP-NCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFRevvqL 166
                          90       100       110
                  ....*....|....*....|....*....|...
gi 767950366  951 LLIDAMPPEALPTCFKPQA--TVVSASLISPAS 981
Cdd:PTZ00322  167 LSRHSQCHFELGANAKPDSftGKPPSLEDSPIS 199
PHA02798 PHA02798
ankyrin-like protein; Provisional
350-598 2.62e-06

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 51.76  E-value: 2.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  350 KLMALLTPLNVNCHASDGRKSTPL-----HLAAGYNRVRIVQLLLQHGADVHAKDKGGLVPLHNACSYGHYEVTELLL-- 422
Cdd:PHA02798   52 DIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLfm 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  423 -KHGACVNAMDLWQFTPLHEAASKN---RVEVCSLLLSHGADPTLVN---------CHGKSAVDmaptpelreRLtyefk 489
Cdd:PHA02798  132 iENGADTTLLDKDGFTMLQVYLQSNhhiDIEIIKLLLEKGVDINTHNnkekydtlhCYFKYNID---------RI----- 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  490 ghsllqaarEADLAKVKKTLALeIINfKQPQSHETALHCAVASLHPKRKQVTELLLR---KGANVNEKNKDFMTPLHVAA 566
Cdd:PHA02798  198 ---------DADILKLFVDNGF-IIN-KENKSHKKKFMEYLNSLLYDNKRFKKNILDfifSYIDINQVDELGFNPLYYSV 266
                         250       260       270
                  ....*....|....*....|....*....|..
gi 767950366  567 ERAHNDVMEVLHKHGAKMNALDTLGQTALHRA 598
Cdd:PHA02798  267 SHNNRKIFEYLLQLGGDINIITELGNTCLFTA 298
Ank_5 pfam13857
Ankyrin repeats (many copies);
543-598 2.79e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.80  E-value: 2.79e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 767950366   543 LLLRKGANVNEKNKDFMTPLHVAAERAHNDVMEVLHKHGAKMNALDTLGQTALHRA 598
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
SAM_ASZ1 cd09521
SAM domain of ASZ1 subfamily; SAM (sterile alpha motif) domain of ASZ1 (Ankyrin, SAM, leucine ...
1034-1086 3.99e-06

SAM domain of ASZ1 subfamily; SAM (sterile alpha motif) domain of ASZ1 (Ankyrin, SAM, leucine Zipper) also known as GASZ (Germ cell-specific Ankyrin, SAM, leucine Zipper) subfamily is a potential protein-protein interaction domain. Proteins of this group are involved in the repression of transposable elements during spermatogenesis, oogenesis, and preimplantation embryogenesis. They support synthesis of PIWI-interacting RNA via association with some PIWI proteins, such as MILI and MIWI. This association is required for initiation and maintenance of retrotransposon repression during the meiosis. In mice lacking ASZ1, DNA damage and delayed germ cell maturation was observed due to retrotransposons releasing from their repressed state.


Pssm-ID: 188920  Cd Length: 64  Bit Score: 45.36  E-value: 3.99e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767950366 1034 FLKSLGLEHLRDIFETEQITLDVLADMGHEELKEIGINAYGHRHKLIKGVERL 1086
Cdd:cd09521    11 FLHGLELGHLTPLFKEHDVTFSQLLKMTEEDLEKIGITQPGDQKKILDAIKEV 63
Ank_5 pfam13857
Ankyrin repeats (many copies);
421-475 4.13e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.03  E-value: 4.13e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 767950366   421 LLKHGAC-VNAMDLWQFTPLHEAASKNRVEVCSLLLSHGADPTLVNCHGKSAVDMA 475
Cdd:pfam13857    1 LLEHGPIdLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
703-757 4.38e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.03  E-value: 4.38e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 767950366   703 LLHHG-ADVHAKDKGGLVPLHNACSYGHYEVAELLVRHGASVNVADLWKFTPLHEA 757
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
218-287 5.02e-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: 50.78  E-value: 5.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  218 SPLHFAAGFGRKDVVEHLLQMGANV-HARDDG--------GLI-----PLHNACSFGHAEVVSLLLCQGADPNARDNWNY 283
Cdd:cd22192    91 TALHIAVVNQNLNLVRELIARGADVvSPRATGtffrpgpkNLIyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGN 170

                  ....
gi 767950366  284 TPLH 287
Cdd:cd22192   171 TVLH 174
SAM_TAL cd09523
SAM domain of TAL subfamily; SAM (sterile alpha motif) domain of TAL (Tsg101-associated ligase) ...
1025-1087 5.55e-06

SAM domain of TAL subfamily; SAM (sterile alpha motif) domain of TAL (Tsg101-associated ligase) proteins, also known as LRSAM1 (Leucine-rich repeat and sterile alpha motif-containing) proteins, is a putative protein-protein interaction domain. Proteins of this subfamily participate in the regulation of retrovirus budding and receptor endocytosis. They show E3 ubiquitin ligase activity. Human TAL protein interacts with Tsg101 and TAL's C-terminal ring finger domain is essential for the multiple monoubiquitylation of Tsg101.


Pssm-ID: 188922  Cd Length: 65  Bit Score: 44.97  E-value: 5.55e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767950366 1025 AGLDMNISQFLKSLGLEHLRDIFETEQITLDVLADMGHEELKEIGINAYGHRHKLIKGVERLL 1087
Cdd:cd09523     2 AGVDPQLVNLLNELSAEHYLPVFARHRITMETLSTMTDEDLKKIGIHEIGLRKEILRAAQELL 64
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
585-797 6.62e-06

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: 50.46  E-value: 6.62e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366   585 NALDTLGQTALHRAALAG-HLQTCRLLLSYGSDPSIislqGFTAAQMGNEAVQQILSESTpirtsdvdyRLLEAS--KAG 661
Cdd:TIGR00870   46 NCPDRLGRSALFVAAIENeNLELTELLLNLSCRGAV----GDTLLHAISLEYVDAVEAIL---------LHLLAAfrKSG 112
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366   662 DLETVKQLCSSQnvncrdlEGRHSTPLHFAAGYNRVSVVEYLLHHGADVHAKDKGGLV---PLHNACSYGHY-------- 730
Cdd:TIGR00870  113 PLELANDQYTSE-------FTPGITALHLAAHRQNYEIVKLLLERGASVPARACGDFFvksQGVDSFYHGESplnaaacl 185
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366   731 ---EVAELLVRHGASVNVADLWKFTPLH----EAAAKGKYEI----CK-LLLKHGA--DPTKK-----NRDGNTPLDL-V 790
Cdd:TIGR00870  186 gspSIVALLSEDPADILTADSLGNTLLHllvmENEFKAEYEElscqMYnFALSLLDklRDSKElevilNHQGLTPLKLaA 265

                   ....*..
gi 767950366   791 KEGDTDI 797
Cdd:TIGR00870  266 KEGRIVL 272
PHA02743 PHA02743
Viral ankyrin protein; Provisional
328-459 1.03e-05

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 47.12  E-value: 1.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  328 AVLTGEYKKDELLEAARSGNEEKLMALLTPLNVNCHA-----SDGRKSTplHLAAGYNR---VRIVQLLLQHGADVHAKD 399
Cdd:PHA02743   13 AVEIDEDEQNTFLRICRTGNIYELMEVAPFISGDGHLlhrydHHGRQCT--HMVAWYDRanaVMKIELLVNMGADINARE 90
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767950366  400 KG-GLVPLHNACSYGHYEVTELLLKH-GACVNAMDLWQFTPLHEAASKNRVEVCSLLLSHGA 459
Cdd:PHA02743   91 LGtGNTLLHIAASTKNYELAEWLCRQlGVNLGAINYQHETAYHIAYKMRDRRMMEILRANGA 152
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
839-865 1.06e-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.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 43.40  E-value: 1.06e-05
                           10        20
                   ....*....|....*....|....*..
gi 767950366   839 TPLHLAAGYNNLEVAEYLLEHGADVNA 865
Cdd:pfam13606    4 TPLHLAARNGRLEIVKLLLENGADINA 30
PLN03124 PLN03124
poly [ADP-ribose] polymerase; Provisional
1059-1300 1.34e-05

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215591 [Multi-domain]  Cd Length: 643  Bit Score: 49.45  E-value: 1.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366 1059 DMGHEELKEIGINA-YGHRHKL--------IKGVERLLGGQQGT--NP-YLTFHCVNQGTILLDLAPEdkEYQSVEEEMQ 1126
Cdd:PLN03124  371 DFGFKKMRQFTIDTpQKLKHKLemvealgeIEIATKLLKDDIGEqdDPlYAHYKRLNCELEPLDTDSE--EFSMIAKYLE 448
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366 1127 STIREHRDGgnaggifnrYNVIRIQ--KVVNKKLRERFchrQKevSEENHNhhneRML-FHGSPFIN--AIIHKGFdeRH 1201
Cdd:PLN03124  449 NTHGQTHSG---------YTLEIVQifKVSREGEDERF---QK--FSSTKN----RMLlWHGSRLTNwtGILSQGL--RI 508
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366 1202 A-----YIGGMFGAGIYFAENSSKSNQYVYgigGGTGCPTHkdrscyichrQMLFCRVTLGK--SFLQFStmkmAHA--- 1271
Cdd:PLN03124  509 AppeapSTGYMFGKGVYFADMFSKSANYCY---ASAANPDG----------VLLLCEVALGDmnELLQAD----YNAnkl 571
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767950366 1272 PPGHHSV-----------------------IGRP-----SVNGLAYAEYVIYRGEQV 1300
Cdd:PLN03124  572 PPGKLSTkgvgrtvpdpseaktledgvvvpLGKPvespySKGSLEYNEYIVYNVDQI 628
PHA02859 PHA02859
ankyrin repeat protein; Provisional
837-908 1.72e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 47.51  E-value: 1.72e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767950366  837 NSTPLH--LAAGYNNLEVAEYLLEHGADVNAQDKG-GLIPLHNAASYG---HVDIAALLIKYNTCVNATDKWAFTPLH 908
Cdd:PHA02859   51 YETPIFscLEKDKVNVEILKFLIENGADVNFKTRDnNLSALHHYLSFNknvEPEILKILIDSGSSITEEDEDGKNLLH 128
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
839-865 1.86e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.57  E-value: 1.86e-05
                            10        20
                    ....*....|....*....|....*..
gi 767950366    839 TPLHLAAGYNNLEVAEYLLEHGADVNA 865
Cdd:smart00248    4 TPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
686-715 1.94e-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: 42.66  E-value: 1.94e-05
                           10        20        30
                   ....*....|....*....|....*....|.
gi 767950366   686 TPLHFAAG-YNRVSVVEYLLHHGADVHAKDK 715
Cdd:pfam00023    4 TPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
388-442 2.09e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.10  E-value: 2.09e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 767950366   388 LLQHG-ADVHAKDKGGLVPLHNACSYGHYEVTELLLKHGACVNAMDLWQFTPLHEA 442
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
576-640 2.66e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.74  E-value: 2.66e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767950366  576 VLHKHGAKMNALDTLGQTALHRAALAGHLQTCRLLLSYGSDPSIISLQGFT----AAQMGNEAVQQILS 640
Cdd:PTZ00322  100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTplelAEENGFREVVQLLS 168
PHA02946 PHA02946
ankyin-like protein; Provisional
700-907 2.98e-05

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 48.13  E-value: 2.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  700 VEYLLHHGADVHAKDKGGLVPLHNACSYGHYEVAELLVRHGASVNVADLWKFTPLHEAAAKGK--YEICKLLLKHGADPT 777
Cdd:PHA02946   55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYGAKIN 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  778 KK-NRDGNTPLdlvkegdtdiqdllrgdAALLDAAKkgclaRVQKLCTPENINCR--DTQGRNSTPLHLAAGYNNLEVAE 854
Cdd:PHA02946  135 NSvDEEGCGPL-----------------LACTDPSE-----RVFKKIMSIGFEARivDKFGKNHIHRHLMSDNPKASTIS 192
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767950366  855 YLLEHGADVNAQDKGGLIPLHNAAS--YGHVDIAALLIKyNTCVNATDKWAFTPL 907
Cdd:PHA02946  193 WMMKLGISPSKPDHDGNTPLHIVCSktVKNVDIINLLLP-STDVNKQNKFGDSPL 246
Ank_4 pfam13637
Ankyrin repeats (many copies);
282-322 3.06e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.65  E-value: 3.06e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 767950366   282 NYTPLHEAAIKGKIDVCIVLLQHGADPNIRNTDGKSALDLA 322
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFA 41
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
420-482 5.08e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.59  E-value: 5.08e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767950366  420 LLLKHGACVNAMDLWQFTPLHEAASKNRVEVCSLLLSHGADPTLVNCHGKSAVDMAPTPELRE 482
Cdd:PTZ00322  100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFRE 162
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
371-459 5.09e-05

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 47.77  E-value: 5.09e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366   371 TPLHLAAGYNRVRIVQLLLQHGADVHAKDKGGLV---PLHNACSYGHY-----------EVTELLLKHGACVNAMDLWQF 436
Cdd:TIGR00870  130 TALHLAAHRQNYEIVKLLLERGASVPARACGDFFvksQGVDSFYHGESplnaaaclgspSIVALLSEDPADILTADSLGN 209
                           90       100       110
                   ....*....|....*....|....*....|..
gi 767950366   437 TPLH------EAASKNRVEVCS---LLLSHGA 459
Cdd:TIGR00870  210 TLLHllvmenEFKAEYEELSCQmynFALSLLD 241
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
177-269 5.35e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.59  E-value: 5.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  177 PAVSGALR-ELLEACRNGDVSRVKRLVDA-ANVNAKDMAGRksSPLHFAAGFGRKDVVEHLLQMGANVHARDDGGLIPLH 254
Cdd:PTZ00322   76 PVVAHMLTvELCQLAASGDAVGARILLTGgADPNCRDYDGR--TPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLE 153
                          90
                  ....*....|....*
gi 767950366  255 NACSFGHAEVVSLLL 269
Cdd:PTZ00322  154 LAEENGFREVVQLLS 168
Ank_4 pfam13637
Ankyrin repeats (many copies);
522-578 5.68e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.88  E-value: 5.68e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 767950366   522 HETALHCAVASlhpKRKQVTELLLRKGANVNEKNKDFMTPLHVAAERAHNDVMEVLH 578
Cdd:pfam13637    1 ELTALHAAAAS---GHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
806-857 5.97e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.88  E-value: 5.97e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 767950366   806 ALLDAAKKGCLARVQKL-CTPENINCRDTQGRnsTPLHLAAGYNNLEVAEYLL 857
Cdd:pfam13637    4 ALHAAAASGHLELLRLLlEKGADINAVDGNGE--TALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
190-269 6.45e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.94  E-value: 6.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  190 CRNGDVSRVkrLVDAANVNAKDMAGRksSPLHFAAGFGRKDVVEHLLQMGANVHARDDGGLIPLHNACSFGHAEVVSLLL 269
Cdd:PHA03095  235 CKRSLVLPL--LIAGISINARNRYGQ--TPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAAL 310
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
810-943 7.29e-05

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 47.06  E-value: 7.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  810 AAKKGCLARVqklctpenINCRDTQG--RNSTPLHLAAGYNNLEVAEYLLEHGADVNAQDKG--------------GLIP 873
Cdd:cd22194   120 AEENGILDRF--------INAEYTEEayEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGvffnpkykhegfyfGETP 191
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  874 LHNAASYGHVDIAALLI-KYNTCVNATDKWAFTPLH---EAAQKGRTQLC-------ALLLAHGAD--PTMKNQEGQTPL 940
Cdd:cd22194   192 LALAACTNQPEIVQLLMeKESTDITSQDSRGNTVLHalvTVAEDSKTQNDfvkrmydMILLKSENKnlETIRNNEGLTPL 271

                  ...
gi 767950366  941 DLA 943
Cdd:cd22194   272 QLA 274
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
827-943 8.26e-05

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong 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: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 47.10  E-value: 8.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  827 NINCRDTQGRNSTPLHLAAGYNNLEVAEYLLEHGADVNAQDKG--------------GLIPLHNAASYGHVDIAALLIK- 891
Cdd:cd22193    66 NAEYTDEYYEGQTALHIAIERRQGDIVALLVENGADVHAHAKGrffqpkyqgegfyfGELPLSLAACTNQPDIVQYLLEn 145
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  892 --YNTCVNATDKWAFTPLH---EAAQKGRTQ-------------LCALLLAHGADPTMKNQEGQTPLDLA 943
Cdd:cd22193   146 ehQPADIEAQDSRGNTVLHalvTVADNTKENtkfvtrmydmiliRGAKLCPTVELEEIRNNDGLTPLQLA 215
Ank_4 pfam13637
Ankyrin repeats (many copies);
905-943 8.33e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.49  E-value: 8.33e-05
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 767950366   905 TPLHEAAQKGRTQLCALLLAHGADPTMKNQEGQTPLDLA 943
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFA 41
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
371-397 8.43e-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.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 40.70  E-value: 8.43e-05
                           10        20
                   ....*....|....*....|....*..
gi 767950366   371 TPLHLAAGYNRVRIVQLLLQHGADVHA 397
Cdd:pfam13606    4 TPLHLAARNGRLEIVKLLLENGADINA 30
SAM_sec23ip-like cd09516
SAM domain of sec23ip-like subfamily; SAM (sterile alpha motif) domain of Sec23ip-like (Sec23 ...
1017-1080 8.56e-05

SAM domain of sec23ip-like subfamily; SAM (sterile alpha motif) domain of Sec23ip-like (Sec23 interacting protein) subfamily is a potential protein-protein interaction domain. This group of proteins includes Sec23ip and DDHD2 proteins. All of them contain at least two domains: a SAM domain and a predicted metal-binding domain. For mammalian DDHD2 members of this group, phospholipase activity has been demonstrated. Sec23ip proteins of this group interact with Sec23 proteins via an N-terminal proline-rich region. Members of this subfamily are involved in organization of ER/Golgi intermediate compartment.


Pssm-ID: 188915  Cd Length: 69  Bit Score: 42.01  E-value: 8.56e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767950366 1017 TERKEGEVAGLDmnisQFLKSLGLEHLRDIFETEQITLDVLADMGHEELKEIGInAYGHRHKLI 1080
Cdd:cd09516     2 SVEEQEEPLTLE----EDLEKLGLSEYFDTFEKEKIDMESLLLCSESDLKEMGI-PMGPRKKLL 60
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
805-943 8.97e-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: 46.80  E-value: 8.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  805 AALLDAAKKGclarvQKLCTPENINCRDTQGRNSTPLHLAAGYNNLEVAEYLLEHGADVNAQDKG-------------GL 871
Cdd:cd21882    46 MLLLEAAPDS-----GNPKELVNAPCTDEFYQGQTALHIAIENRNLNLVRLLVENGADVSARATGrffrkspgnlfyfGE 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  872 IPLHNAASYGHVDIAALLIKYN---TCVNATDKWAFTPLH---EAAQKGR------TQLCALLLAHGA--DPTMK----- 932
Cdd:cd21882   121 LPLSLAACTNQEEIVRLLLENGaqpAALEAQDSLGNTVLHalvLQADNTPensafvCQMYNLLLSYGAhlDPTQQleeip 200
                         170
                  ....*....|.
gi 767950366  933 NQEGQTPLDLA 943
Cdd:cd21882   201 NHQGLTPLKLA 211
SAM_WDSUB1 cd09505
SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins ...
1031-1086 1.06e-04

SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins is a putative protein-protein interaction domain. Proteins of this group contain multiple domains: SAM, one or more WD40 repeats and U-box (derived version of the RING-finger domain). Apparently the WDSUB1 subfamily proteins participate in protein degradation through ubiquitination, since U-box domain are known as a member of E3 ubiquitin ligase family, while SAM and WD40 domains most probably are responsible for an E2 ubiquitin-conjugating enzyme binding and a target protein binding.


Pssm-ID: 188904  Cd Length: 72  Bit Score: 41.92  E-value: 1.06e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767950366 1031 ISQFLKSLGLEHLRDIFETEQITLDVLADMGHEEL-KEIGINAYGHRHKLIKGVERL 1086
Cdd:cd09505    10 VCTWLRSIGLEQYVEVFRANNIDGKELLNLTKESLsKDLKIESLGHRNKILRKIEEL 66
SAM_ANKS3 cd09519
SAM domain of ANKS3 subfamily; SAM (sterile alpha motif) domain of ANKS3 subfamily is a ...
1030-1086 1.23e-04

SAM domain of ANKS3 subfamily; SAM (sterile alpha motif) domain of ANKS3 subfamily is a potential protein-protein interaction domain. Proteins of this subfamily have N-terminal ankyrin repeats and a C-terminal SAM domain. SAM is a widespread domain in signaling proteins. In many cases it mediates homo-dimerization/oligomerization.


Pssm-ID: 188918  Cd Length: 64  Bit Score: 41.33  E-value: 1.23e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767950366 1030 NISQFLKSLGLEHLRDIFETEQITLDVLADMGHEELKEIGINAYGHRHKLIKGVERL 1086
Cdd:cd09519     6 DLSELLEQIGCSKYLPIFEEQDIDLRIFLTLTESDLKEIGITLFGPKRKMTSAIARW 62
SAM_EPH-A4 cd09545
SAM domain of EPH-A4 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
1030-1091 1.41e-04

SAM domain of EPH-A4 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A4 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A4 receptors and appears to mediate cell-cell initiated signal transduction. SAM domains of EPH-A4 receptors can form homodimers. EPH-A4 receptors bind ligands such as erphirin A1, A4, A5. They are known to interact with a number of different proteins, including meltrin beta metalloprotease, Cdk5, and EFS2alpha, however SAM domain doesn't participate in these interactions. EPH-A4 receptors are involved in regulation of corticospinal tract formation, in pathway controlling voluntary movements, in formation of motor neurons, and in axon guidance (SAM domain is not required for axon guidance or for EPH-A4 kinase signaling). In Xenopus embryos EPH-A4 induces loss of cell adhesion, ventro-lateral protrusions, and severely expanded posterior structures. Mutations in SAM domain conserved tyrosine (Y928F) enhance the ability of EPH-A4 to induce these phenotypes, thus supporting the idea that the SAM domain may negatively regulate some aspects of EPH-A4 activity. EphA4 gene was found overexpressed in a number of different cancers including human gastric cancer, colorectal cancer, and pancreatic ductal adenocarcinoma. It is likely to be a promising molecular target for the cancer therapy.


Pssm-ID: 188944  Cd Length: 71  Bit Score: 41.48  E-value: 1.41e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767950366 1030 NISQFLKSLGLEHLRDIFETEQIT-LDVLADMGHEELKEIGINAYGHRHKLIKGVERLLGGQQ 1091
Cdd:cd09545     5 SVDDWLQAIKMERYKDNFTAAGYTtLEAVVHMNQDDLARIGISAIAHQNKILSSVQGMRSQMQ 67
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
751-781 1.48e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 40.35  E-value: 1.48e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 767950366   751 FTPLHEAAAK-GKYEICKLLLKHGADPTKKNR 781
Cdd:pfam00023    3 NTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
315-436 1.58e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. 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.


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 45.95  E-value: 1.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  315 GKSALdladpsAKAVLTGEYKKDE----LLEAARSGNEEKLMalltplnVNCHASDG--RKSTPLHLAAGYNRVRIVQLL 388
Cdd:cd22196    47 GKTCL------LKAMLNLHNGQNDtislLLDIAEKTGNLKEF-------VNAAYTDSyyKGQTALHIAIERRNMHLVELL 113
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 767950366  389 LQHGADVHAKDKGGLVPLhNACSYGHYeVTELLLKHGACVNAMDLWQF 436
Cdd:cd22196   114 VQNGADVHARASGEFFKK-KKGGPGFY-FGELPLSLAACTNQLDIVKF 159
Ank_4 pfam13637
Ankyrin repeats (many copies);
654-704 1.90e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 40.34  E-value: 1.90e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 767950366   654 LLEASKAGDLETVKQL-CSSQNVNCRDLEGRhsTPLHFAAGYNRVSVVEYLL 704
Cdd:pfam13637    5 LHAAAASGHLELLRLLlEKGADINAVDGNGE--TALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
543-663 1.95e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 45.66  E-value: 1.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  543 LLLRKGANVNEKNKDFMTPLHVAAERAHNDVMEVLHKHGAKMNALDTLGQTALHRAALAGHLQTCRLLLSYGSDPSIISL 622
Cdd:PTZ00322  100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGA 179
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 767950366  623 QGFTAAQMGNEAVQqilsESTPIRTSDVDYRLLEASKAGDL 663
Cdd:PTZ00322  180 NAKPDSFTGKPPSL----EDSPISSHHPDFSAVPQPMMGSL 216
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
686-712 2.32e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 39.55  E-value: 2.32e-04
                           10        20
                   ....*....|....*....|....*..
gi 767950366   686 TPLHFAAGYNRVSVVEYLLHHGADVHA 712
Cdd:pfam13606    4 TPLHLAARNGRLEIVKLLLENGADINA 30
PHA02946 PHA02946
ankyin-like protein; Provisional
687-801 2.32e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 45.43  E-value: 2.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  687 PLHFAAGYNRVSVVEYLLHHGADVHAKDKGGLVPLHnACSYGHYEVAE---LLVRHGASVN------------------- 744
Cdd:PHA02946   75 PLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLY-YLSGTDDEVIErinLLVQYGAKINnsvdeegcgpllactdpse 153
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767950366  745 --------------VADLWKFTPLHE--AAAKGKYEICKLLLKHGADPTKKNRDGNTPLDLV---KEGDTDIQDLL 801
Cdd:PHA02946  154 rvfkkimsigfearIVDKFGKNHIHRhlMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIVcskTVKNVDIINLL 229
SAM_caskin1,2_repeat2 cd09498
SAM domain of caskin protein repeat 2; SAM (sterile alpha motif) domain repeat 2 of caskin1,2 ...
1030-1086 2.46e-04

SAM domain of caskin protein repeat 2; SAM (sterile alpha motif) domain repeat 2 of caskin1,2 proteins is a protein-protein interaction domain. Caskin has two tandem SAM domains. Caskin protein is known to interact with membrane-associated guanylate kinase CASK, and may play a role in neural development, synaptic protein targeting, and regulation of gene expression.


Pssm-ID: 188897  Cd Length: 71  Bit Score: 40.74  E-value: 2.46e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767950366 1030 NISQFLKSLGLEHLRDIFETEQI-TLDVLADMGHEELKEIGINAYGHRHKLIKGVERL 1086
Cdd:cd09498     9 DLLEWLSLLGLPQYHKVLVENGYdSIDFVTDLTWEDLQDIGITKLGHQKKLMLAIKKL 66
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
283-312 2.75e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.58  E-value: 2.75e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 767950366   283 YTPLHEAAIK-GKIDVCIVLLQHGADPNIRN 312
Cdd:pfam00023    3 NTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
807-943 2.75e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. 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.


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 45.18  E-value: 2.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  807 LLDAAKKGCLARvqklctpENINC--RDTQGRNSTPLHLAAGYNNLEVAEYLLEHGADVNAQDKG--------------G 870
Cdd:cd22196    69 LLDIAEKTGNLK-------EFVNAayTDSYYKGQTALHIAIERRNMHLVELLVQNGADVHARASGeffkkkkggpgfyfG 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  871 LIPLHNAASYGHVDIAALLIK--YNTC-VNATDKWAFTPLH---EAAQ------KGRTQLCALLLAHGAD--PTMK---- 932
Cdd:cd22196   142 ELPLSLAACTNQLDIVKFLLEnpHSPAdISARDSMGNTVLHalvEVADntpentKFVTKMYNEILILGAKirPLLKleei 221
                         170
                  ....*....|..
gi 767950366  933 -NQEGQTPLDLA 943
Cdd:cd22196   222 tNKKGLTPLKLA 233
PHA02946 PHA02946
ankyin-like protein; Provisional
346-472 3.24e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 44.66  E-value: 3.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  346 GNEEKLMALLTPLNVNCHASDGRKSTPLHLAAGYNRVRIVQLLLQHGADVHAKDKGGLVPLHnACSYGHYEVTE---LLL 422
Cdd:PHA02946   49 GLDERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLY-YLSGTDDEVIErinLLV 127
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767950366  423 KHGACV-NAMDLWQFTPLHeAASKNRVEVCSLLLSHGADPTLVNCHGKSAV 472
Cdd:PHA02946  128 QYGAKInNSVDEEGCGPLL-ACTDPSERVFKKIMSIGFEARIVDKFGKNHI 177
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
751-778 3.36e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.11  E-value: 3.36e-04
                            10        20
                    ....*....|....*....|....*...
gi 767950366    751 FTPLHEAAAKGKYEICKLLLKHGADPTK 778
Cdd:smart00248    3 RTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
249-280 3.44e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.19  E-value: 3.44e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 767950366   249 GLIPLHNAC-SFGHAEVVSLLLCQGADPNARDN 280
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
282-310 3.46e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.11  E-value: 3.46e-04
                            10        20
                    ....*....|....*....|....*....
gi 767950366    282 NYTPLHEAAIKGKIDVCIVLLQHGADPNI 310
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
218-330 3.59e-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: 3.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366   218 SPLHFAAGFGRKDVVEHLLQMGANVHARDDG--------------GLIPLHNACSFGHAEVVSLLLCQGADPNARDNWNY 283
Cdd:TIGR00870  130 TALHLAAHRQNYEIVKLLLERGASVPARACGdffvksqgvdsfyhGESPLNAAACLGSPSIVALLSEDPADILTADSLGN 209
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767950366   284 TPLHEAAIKGKID------VCIV---LLQHGADPN-------IRNTDGKSALDLADPSAKAVL 330
Cdd:TIGR00870  210 TLLHLLVMENEFKaeyeelSCQMynfALSLLDKLRdskelevILNHQGLTPLKLAAKEGRIVL 272
PHA02798 PHA02798
ankyrin-like protein; Provisional
540-711 4.49e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 44.44  E-value: 4.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  540 VTELLLRKGANVNEKNKDFMTPLHVAAERAHNDVMEVLH---KHGAKMNALDTLGQTALHRAALAGH---LQTCRLLLSY 613
Cdd:PHA02798   91 IVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLfmiENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEK 170
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  614 GSDPSIIS-LQGFTAAQ------------------MGNEAVQQILSESTPIRTSDVDYRLLEASKAGDLETVKQLCSSQN 674
Cdd:PHA02798  171 GVDINTHNnKEKYDTLHcyfkynidridadilklfVDNGFIINKENKSHKKKFMEYLNSLLYDNKRFKKNILDFIFSYID 250
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 767950366  675 VNCRDLEGrhSTPLHFAAGYNRVSVVEYLLHHGADVH 711
Cdd:PHA02798  251 INQVDELG--FNPLYYSVSHNNRKIFEYLLQLGGDIN 285
Ank_4 pfam13637
Ankyrin repeats (many copies);
593-639 4.99e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.18  E-value: 4.99e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 767950366   593 TALHRAALAGHLQTCRLLLSYGSDPSIISLQGFT----AAQMGNEAVQQIL 639
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETalhfAASNGNVEVLKLL 53
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
371-397 5.12e-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: 5.12e-04
                            10        20
                    ....*....|....*....|....*..
gi 767950366    371 TPLHLAAGYNRVRIVQLLLQHGADVHA 397
Cdd:smart00248    4 TPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02946 PHA02946
ankyin-like protein; Provisional
518-726 5.34e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 44.27  E-value: 5.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  518 QPQSHETALH--CAVASLHpkrKQVTELLLRKGANVNEKNKDFMTPLHVAAERAHNDVMEVLHKHGAKMNALDTLGQTAL 595
Cdd:PHA02946   33 EPSGNYHILHayCGIKGLD---ERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPL 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  596 HRaaLAGH----LQTCRLLLSYGSDPSiislqgftaAQMGNEAVQQILSESTPIrtsdvdyrlleaskagdlETVKQLCS 671
Cdd:PHA02946  110 YY--LSGTddevIERINLLVQYGAKIN---------NSVDEEGCGPLLACTDPS------------------ERVFKKIM 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767950366  672 SQNVNCR--DLEGRHSTPLHFAAGYNRVSVVEYLLHHGADVHAKDKGGLVPLHNACS 726
Cdd:PHA02946  161 SIGFEARivDKFGKNHIHRHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIVCS 217
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
282-310 5.44e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 38.39  E-value: 5.44e-04
                           10        20
                   ....*....|....*....|....*....
gi 767950366   282 NYTPLHEAAIKGKIDVCIVLLQHGADPNI 310
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
311-463 5.91e-04

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 44.10  E-value: 5.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  311 RNTDGKSALdladpsAKAVLTGEYKKDE----LLEAARSGNEEKLMAlltplNVNCHASDGRKSTPLHLAAGYNRVRIVQ 386
Cdd:cd21882    22 RGATGKTCL------HKAALNLNDGVNEaimlLLEAAPDSGNPKELV-----NAPCTDEFYQGQTALHIAIENRNLNLVR 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  387 LLLQHGADVHAKDKG-------------GLVPLHNACSYGHYEVTELLLKHG---ACVNAMDLWQFTPLH---EAASK-- 445
Cdd:cd21882    91 LLVENGADVSARATGrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGaqpAALEAQDSLGNTVLHalvLQADNtp 170
                         170       180
                  ....*....|....*....|....
gi 767950366  446 -NRVEVCS---LLLSHGA--DPTL 463
Cdd:cd21882   171 eNSAFVCQmynLLLSYGAhlDPTQ 194
SAM_ANKS6 cd09518
SAM domain of ANKS6 (or SamCystin) subfamily; SAM (sterile alpha motif) domain of ANKS6 (or ...
1031-1086 6.20e-04

SAM domain of ANKS6 (or SamCystin) subfamily; SAM (sterile alpha motif) domain of ANKS6 (or SamCystin) subfamily is a potential protein-protein interaction domain. Proteins of this subfamily have N-terminal ankyrin repeats and a C-terminal SAM domain. They are able to form self-associated complexes and both (SAM and ANK) domains play a role in such interactions. Mutations in Anks6 gene are associated with polycystic kidney disease. They cause formation of renal cysts in rodent models. It was suggested that the ANKS6 protein can interact indirectly (through RNA and protein intermediates) with BICC1, another polycystic kidney disease-associated protein.


Pssm-ID: 188917  Cd Length: 65  Bit Score: 39.47  E-value: 6.20e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767950366 1031 ISQFLKSLGLEHLRDIFETEQITLDVLADMGHEELKEIGINAYGHRHKLIKGVERL 1086
Cdd:cd09518     8 LSGILRKLSLEKYQPIFEEQEVDMEAFLTLTDGDLKELGIKTDGPRQQILAAISEL 63
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
334-461 7.03e-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: 43.92  E-value: 7.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366   334 YKKDELLEAARSGNEEKLMALLtpLNVNCHASDGRksTPLHLAAgYNRVRIVQLLLQHGADVHAKDKG------------ 401
Cdd:TIGR00870   51 LGRSALFVAAIENENLELTELL--LNLSCRGAVGD--TLLHAIS-LEYVDAVEAILLHLLAAFRKSGPlelandqytsef 125
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767950366   402 --GLVPLHNACSYGHYEVTELLLKHGACVNA------------MDLWQFT--PLHEAASKNRVEVCSLLLSHGADP 461
Cdd:TIGR00870  126 tpGITALHLAAHRQNYEIVKLLLERGASVPAracgdffvksqgVDSFYHGesPLNAAACLGSPSIVALLSEDPADI 201
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
720-745 7.10e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 38.01  E-value: 7.10e-04
                           10        20
                   ....*....|....*....|....*.
gi 767950366   720 PLHNACSYGHYEVAELLVRHGASVNV 745
Cdd:pfam13606    5 PLHLAARNGRLEIVKLLLENGADINA 30
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
654-858 8.24e-04

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 43.72  E-value: 8.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  654 LLEASKagDLETVKQLCSSQnVNCRDLEGRhsTPLHFAAGYNRVSVVEYLLHHGADVHAKDKGGLVPLH--NACSYGHYe 731
Cdd:cd21882    48 LLEAAP--DSGNPKELVNAP-CTDEFYQGQ--TALHIAIENRNLNLVRLLVENGADVSARATGRFFRKSpgNLFYFGEL- 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  732 vaellvrhgasvnvadlwkftPLHEAAAKGKYEICKLLLKHGADP-TKKNRD--GNTPLDLVKEgdtdIQDLLRGDAALL 808
Cdd:cd21882   122 ---------------------PLSLAACTNQEEIVRLLLENGAQPaALEAQDslGNTVLHALVL----QADNTPENSAFV 176
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767950366  809 DAAKKGCLARVQKLCTPENIN-CRDTQGRnsTPLHLAAGYNNLEVAEYLLE 858
Cdd:cd21882   177 CQMYNLLLSYGAHLDPTQQLEeIPNHQGL--TPLKLAAVEGKIVMFQHILQ 225
SAM_DDHD2 cd09585
SAM domain of DDHD2; SAM (sterile alpha motif) domain of DDHD2 group is a potential ...
1031-1085 8.83e-04

SAM domain of DDHD2; SAM (sterile alpha motif) domain of DDHD2 group is a potential protein-protein interaction domain. DDHD2 proteins contain at least two domains:a SAM domain and a predicted metal-binding domain. Phospholipase A1 activity was demonstrated for the mammalian DDHD2 protein. Mutation of the putative catalytic serine resulted in elimination of activity. Unlike SEC23IP, DDHD2 proteins do not have an N-terminal proline-rich region and correspondingly they are not able to interact with Sec23p/Sec24p complex. Overexpression of DDHD2 is the cause of dispersion of ER/Golgi intermediate compartment and dispersion of tethering proteins located in the Golgi region, leading to aggregation in the endoplasmic reticulum.


Pssm-ID: 188984  Cd Length: 69  Bit Score: 38.97  E-value: 8.83e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767950366 1031 ISQFLKSLGLEHLRDIFETEQITLDVLADMGHEELKEIGInAYGHRHKLIKGVER 1085
Cdd:cd09585    12 LEETLKKLGLSEYCDVFEKEKIDLEALALCQERDLKDLGI-PLGPRKKILNYIRR 65
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
218-247 9.20e-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: 38.04  E-value: 9.20e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 767950366   218 SPLHFAAG-FGRKDVVEHLLQMGANVHARDD 247
Cdd:pfam00023    4 TPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
339-433 9.35e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely related to TRPV1, sharing high sequence identity (>50%), but TRPV2 shows a higher temperature threshold and sensitivity for activation than TRPV1. TRPV2 can be stimulated by ligands or lipids, and is involved in osmosensation and mechanosensation. TRPV2 is expressed in both neuronal and non-neuronal tissues, and it has been implicated in diverse physiological and pathophysiological processes, including cardiac-structure maintenance, innate immunity, and cancer. TRPV2 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 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.


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 43.69  E-value: 9.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  339 LLEAARSGNEEKLmalltpLNVNCHASDGRKSTPLHLAAGYNRVRIVQLLLQHGADVHAKDKGGLVPLHNA-CSYghyeV 417
Cdd:cd22197    70 LEIDKDSGNPKPL------VNAQCTDEYYRGHSALHIAIEKRSLQCVKLLVENGADVHARACGRFFQKKQGtCFY----F 139
                          90
                  ....*....|....*.
gi 767950366  418 TELLLKHGACVNAMDL 433
Cdd:cd22197   140 GELPLSLAACTKQWDV 155
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
502-714 9.55e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. 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.


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 43.64  E-value: 9.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  502 LAKVKKTLALEiiNFKQPQSHETALHCAVASLHPKRKQVTELLL---RKGANVneknKDFM------------TPLHVAA 566
Cdd:cd22196    29 LMRTKKRLTDS--EFKDPETGKTCLLKAMLNLHNGQNDTISLLLdiaEKTGNL----KEFVnaaytdsyykgqTALHIAI 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  567 ERAHNDVMEVLHKHGAKMNALDT--------------LGQTALHRAALAGHLQTCRLLLSYGSDPSIISLQGftaaQMGN 632
Cdd:cd22196   103 ERRNMHLVELLVQNGADVHARASgeffkkkkggpgfyFGELPLSLAACTNQLDIVKFLLENPHSPADISARD----SMGN 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  633 EAVQQILS------ESTPIRTSDVDYRLLEASKAGDLETVKQLcssqnVNCRDLegrhsTPLHFAAGYNRVSVVEYLLhh 706
Cdd:cd22196   179 TVLHALVEvadntpENTKFVTKMYNEILILGAKIRPLLKLEEI-----TNKKGL-----TPLKLAAKTGKIGIFAYIL-- 246

                  ....*...
gi 767950366  707 GADVHAKD 714
Cdd:cd22196   247 GREIKEPE 254
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
720-745 9.80e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.57  E-value: 9.80e-04
                            10        20
                    ....*....|....*....|....*.
gi 767950366    720 PLHNACSYGHYEVAELLVRHGASVNV 745
Cdd:smart00248    5 PLHLAAENGNLEVVKLLLDKGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
203-254 1.02e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.48  E-value: 1.02e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 767950366   203 DAANVNAKDmaGRKSSPLHFAAGFGRKDVVEHLLQMGANVHARDDGGLIPLH 254
Cdd:pfam13857    5 GPIDLNRLD--GEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
485-787 1.18e-03

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 43.36  E-value: 1.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  485 TYeFKGHSLlqaaREADLAKVKKTLALEI--INFKQPQSHETALHCAVASLHPKrKQVTELLLRKGANVNEKNKDFMTPL 562
Cdd:PHA02716  143 TY-FNSPNT----RGIDLDLIKYMVDVGIvnLNYVCKKTGYGILHAYLGNMYVD-IDILEWLCNNGVNVNLQNNHLITPL 216
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  563 HVAAERAH--NDVMEVLHKHGAKMNALDTLGQTALhraalaghlqtcrllLSYgsdpsiislqgFTAAQMGNEAVQQILS 640
Cdd:PHA02716  217 HTYLITGNvcASVIKKIIELGGDMDMKCVNGMSPI---------------MTY-----------IINIDNINPEITNIYI 270
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  641 EStpirtsdvdyrlLEASKAGDLETVKQL--CSSQNVNcrdlegrhstplhfaagynrVSVVEYLLHHGADVHAKDKGGL 718
Cdd:PHA02716  271 ES------------LDGNKVKNIPMILHSyiTLARNID--------------------ISVVYSFLQPGVKLHYKDSAGR 318
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  719 VPLHNAC--SYGHYEVAELLVRHGASVNVADLWKFTPLH--------------EAAAKGKYEICKLLLKHGADPTKKNRD 782
Cdd:PHA02716  319 TCLHQYIlrHNISTDIIKLLHEYGNDLNEPDNIGNTVLHtylsmlsvvnildpETDNDIRLDVIQCLISLGADITAVNCL 398

                  ....*
gi 767950366  783 GNTPL 787
Cdd:PHA02716  399 GYTPL 403
PHA02743 PHA02743
Viral ankyrin protein; Provisional
679-774 1.19e-03

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 40.95  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  679 DLEGRHSTplHFAAGYNRVSVV---EYLLHHGADVHAKDKG-GLVPLHNACSYGHYEVAELLVRH-GASVNVADLWKFTP 753
Cdd:PHA02743   54 DHHGRQCT--HMVAWYDRANAVmkiELLVNMGADINARELGtGNTLLHIAASTKNYELAEWLCRQlGVNLGAINYQHETA 131
                          90       100
                  ....*....|....*....|.
gi 767950366  754 LHEAAAKGKYEICKLLLKHGA 774
Cdd:PHA02743  132 YHIAYKMRDRRMMEILRANGA 152
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
686-712 1.87e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.80  E-value: 1.87e-03
                            10        20
                    ....*....|....*....|....*..
gi 767950366    686 TPLHFAAGYNRVSVVEYLLHHGADVHA 712
Cdd:smart00248    4 TPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
436-463 1.91e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.80  E-value: 1.91e-03
                            10        20
                    ....*....|....*....|....*...
gi 767950366    436 FTPLHEAASKNRVEVCSLLLSHGADPTL 463
Cdd:smart00248    3 RTPLHLAAENGNLEVVKLLLDKGADINA 30
SAM_Shank1,2,3 cd09506
SAM domain of Shank1,2,3 family proteins; SAM (sterile alpha motif) domain of Shank1,2,3 ...
1031-1087 1.96e-03

SAM domain of Shank1,2,3 family proteins; SAM (sterile alpha motif) domain of Shank1,2,3 family proteins is a protein-protein interaction domain. Shank1,2,3 proteins are scaffold proteins that are known to interact with a variety of cytoplasmic and membrane proteins. SAM domains of the Shank1,2,3 family are prone to homooligomerization. They are highly enriched in the postsynaptic density, acting as scaffolds to organize assembly of postsynaptic proteins. SAM domains of Shank3 proteins can form large sheets of helical fibers. Shank genes show distinct patterns of expression, in rat Shank1 mRNA is found almost exclusively in brain, Shank2 in brain, kidney and liver, and Shank3 in heart, brain and spleen.


Pssm-ID: 188905  Cd Length: 66  Bit Score: 38.07  E-value: 1.96e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767950366 1031 ISQFLKSLGLEHLRDIFETEQITLDVLADMGHEELKEIGINAYGHRHKLIKGVERLL 1087
Cdd:cd09506    10 VGDWLESLNLGEHRERFMDNEIDGSHLPNLDKEDLTELGVTRVGHRMNIERALKKLL 66
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
436-465 1.98e-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: 36.88  E-value: 1.98e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 767950366   436 FTPLHEAASK-NRVEVCSLLLSHGADPTLVN 465
Cdd:pfam00023    3 NTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
402-432 2.02e-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: 36.88  E-value: 2.02e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 767950366   402 GLVPLHNAC-SYGHYEVTELLLKHGACVNAMD 432
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
717-747 2.06e-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: 36.88  E-value: 2.06e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 767950366   717 GLVPLHNAC-SYGHYEVAELLVRHGASVNVAD 747
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
Ank_2 pfam12796
Ankyrin repeats (3 copies);
907-952 2.15e-03

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 38.56  E-value: 2.15e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 767950366   907 LHEAAQKGRTQLCALLLAHGADPTMKNQEGQTPLDLATADD----IRALL 952
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGhleiVKLLL 50
SAM_Arap1,2,3 cd09490
SAM domain of Arap1,2,3 (angiotensin receptor-associated protein); SAM (sterile alpha motif) ...
1028-1085 2.32e-03

SAM domain of Arap1,2,3 (angiotensin receptor-associated protein); SAM (sterile alpha motif) domain of Arap1,2,3 subfamily proteins (angiotensin receptor-associated) is a protein-protein interaction domain. Arap1,2,3 proteins are phosphatidylinositol-3,4,5-trisphosphate-dependent GTPase-activating proteins. They are involved in phosphatidylinositol-3 kinase (PI3K) signaling pathways. In addition to SAM domain, Arap1,2,3 proteins contain ArfGap, PH-like, RhoGAP and UBQ domains. SAM domain of Arap3 protein was shown to interact with SAM domain of Ship2 phosphatidylinositol-trisphosphate phosphatase proteins. Such interaction apparently plays a role in inhibition of PI3K regulated pathways since Ship2 converts PI(3,4,5)P3 into PI(3,4)P2. Proteins of this subfamily participate in regulation of signaling and trafficking associated with a number of different receptors (including EGFR, TRAIL-R1/DR4, TRAIL-R2/DR5) in normal and cancer cells; they are involved in regulation of actin cytoskeleton remodeling, cell spreading and formation of lamellipodia.


Pssm-ID: 188889  Cd Length: 63  Bit Score: 37.66  E-value: 2.32e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767950366 1028 DMNISQFLKSLGLEHLRDIFETEQ-ITLDVLADMGHEELKEIGINAYGHRHKLIKGVER 1085
Cdd:cd09490     3 DLDIAEWLASIHLEQYLDLFREHGyVTATDCQGINDSRLKQIGISPTGHRRRILKQLPI 61
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
752-776 2.42e-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: 2.42e-03
                           10        20
                   ....*....|....*....|....*
gi 767950366   752 TPLHEAAAKGKYEICKLLLKHGADP 776
Cdd:pfam13606    4 TPLHLAARNGRLEIVKLLLENGADI 28
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
557-586 2.86e-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: 36.41  E-value: 2.86e-03
                            10        20        30
                    ....*....|....*....|....*....|
gi 767950366    557 DFMTPLHVAAERAHNDVMEVLHKHGAKMNA 586
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
437-475 2.88e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.25  E-value: 2.88e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 767950366   437 TPLHEAASKNRVEVCSLLLSHGADPTLVNCHGKSAVDMA 475
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFA 41
Ank_4 pfam13637
Ankyrin repeats (many copies);
339-389 3.27e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.87  E-value: 3.27e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 767950366   339 LLEAARSGNEEKLMALLtPLNVNCHASDGRKSTPLHLAAGYNRVRIVQLLL 389
Cdd:pfam13637    5 LHAAAASGHLELLRLLL-EKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
516-756 3.63e-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: 41.79  E-value: 3.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  516 FKQPQSHETALHCAVASLHPKRKQVTELLL---RKGAN----VNEKNKDFM----TPLHVAAERAHNDVMEVLHKHGAKM 584
Cdd:cd21882    20 YQRGATGKTCLHKAALNLNDGVNEAIMLLLeaaPDSGNpkelVNAPCTDEFyqgqTALHIAIENRNLNLVRLLVENGADV 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  585 NALDT-------------LGQTALHRAALAGHLQTCRLLLSYGSDPSIISLQGftaaQMGNeAVQQIL---SESTPIRTS 648
Cdd:cd21882   100 SARATgrffrkspgnlfyFGELPLSLAACTNQEEIVRLLLENGAQPAALEAQD----SLGN-TVLHALvlqADNTPENSA 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  649 DVD--YRLLeaskagdLETVKQLCSSQNVncrDLEGRHS--TPLHFAAGYNRVSVVEYLLH---HGADVHAKDK------ 715
Cdd:cd21882   175 FVCqmYNLL-------LSYGAHLDPTQQL---EEIPNHQglTPLKLAAVEGKIVMFQHILQrefSGPYQPLSRKftewty 244
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 767950366  716 ----GGLVPLHNACSYGHYEVAELLVRHGASVNVADLWKFTPLHE 756
Cdd:cd21882   245 gpvtSSLYDLSEIDSWEKNSVLELIAFSKKREARHQMLVQEPLNE 289
PHA02946 PHA02946
ankyin-like protein; Provisional
832-958 4.31e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 41.19  E-value: 4.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  832 DTQGRNSTPLHLAAGYNNLEVAEYLLEHGADVNAQDKGGLIPLHNAASYGH--VDIAALLIKYNTCV-NATDKWAFTPL- 907
Cdd:PHA02946   67 ETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYGAKInNSVDEEGCGPLl 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  908 ---------------------------------HEAAQKGRTQLCALLLAHGADPTMKNQEGQTPLDLATADDIRAL-LI 953
Cdd:PHA02946  147 actdpservfkkimsigfearivdkfgknhihrHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIVCSKTVKNVdII 226

                  ....*
gi 767950366  954 DAMPP 958
Cdd:PHA02946  227 NLLLP 231
PHA02736 PHA02736
Viral ankyrin protein; Provisional
374-459 4.50e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 39.09  E-value: 4.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  374 HLAAGYNR-----VRIV------------QLLLQHGADVHAKD-KGGLVPLHNACSYGHYEVTELLLKH-GACVNAMDLW 434
Cdd:PHA02736   46 YLVLEYNRhgkqcVHIVsnpdkadpqeklKLLMEWGADINGKErVFGNTPLHIAVYTQNYELATWLCNQpGVNMEILNYA 125
                          90       100
                  ....*....|....*....|....*
gi 767950366  435 QFTPLHEAASKNRVEVCSLLLSHGA 459
Cdd:PHA02736  126 FKTPYYVACERHDAKMMNILRAKGA 150
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
218-244 5.07e-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: 5.07e-03
                           10        20
                   ....*....|....*....|....*..
gi 767950366   218 SPLHFAAGFGRKDVVEHLLQMGANVHA 244
Cdd:pfam13606    4 TPLHLAARNGRLEIVKLLLENGADINA 30
PHA02798 PHA02798
ankyrin-like protein; Provisional
850-941 5.07e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 40.97  E-value: 5.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  850 LEVAEYLLEHGADVNAQDKGGLIPLHNAASYGHV---DIAALLIKYNTCVNATDKWAFTPLHEAAQKGRT---QLCALLL 923
Cdd:PHA02798   89 LDIVKILIENGADINKKNSDGETPLYCLLSNGYInnlEILLFMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLL 168
                          90
                  ....*....|....*....
gi 767950366  924 AHGAD-PTMKNQEGQTPLD 941
Cdd:PHA02798  169 EKGVDiNTHNNKEKYDTLH 187
PHA02884 PHA02884
ankyrin repeat protein; Provisional
699-789 5.83e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 40.35  E-value: 5.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  699 VVEYLLHHGADVHAKDKGGLV----PLHNACSYGHYEVAELLVRHGASVNV-ADLWKFTPLHEAAAKGKYEICKLLLKHG 773
Cdd:PHA02884   48 IIDAILKLGADPEAPFPLSENsktnPLIYAIDCDNDDAAKLLIRYGADVNRyAEEAKITPLYISVLHGCLKCLEILLSYG 127
                          90
                  ....*....|....*.
gi 767950366  774 ADPTKKNRDGNTPLDL 789
Cdd:PHA02884  128 ADINIQTNDMVTPIEL 143
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
523-556 6.52e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 35.73  E-value: 6.52e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 767950366   523 ETALHCAVAslHPKRKQVTELLLRKGANVNEKNK 556
Cdd:pfam00023    3 NTPLHLAAG--RRGNLEIVKLLLSKGADVNARDK 34
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
186-287 7.00e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. 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.


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 40.56  E-value: 7.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  186 LLEACRNGDvsRVKRLVDAAnvnAKDMAGRKSSPLHFAAGFGRKDVVEHLLQMGANVHARDDG--------------GLI 251
Cdd:cd22196    69 LLDIAEKTG--NLKEFVNAA---YTDSYYKGQTALHIAIERRNMHLVELLVQNGADVHARASGeffkkkkggpgfyfGEL 143
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 767950366  252 PLHNACSFGHAEVVSLLL---CQGADPNARDNWNYTPLH 287
Cdd:cd22196   144 PLSLAACTNQLDIVKFLLenpHSPADISARDSMGNTVLH 182
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
591-619 7.19e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 35.34  E-value: 7.19e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 767950366   591 GQTALHRAAL-AGHLQTCRLLLSYGSDPSI 619
Cdd:pfam00023    2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNA 31
SAM_EPH-R cd09488
SAM domain of EPH family of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH ...
1031-1086 7.22e-03

SAM domain of EPH family of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH (erythropoietin-producing hepatocyte) family of receptor tyrosine kinases is a C-terminal signal transduction module located in the cytoplasmic region of these receptors. SAM appears to mediate cell-cell initiated signal transduction via binding proteins to a conserved tyrosine that is phosphorylated. In some cases the SAM domain mediates homodimerization/oligomerization and plays a role in the clustering process necessary for signaling. EPH kinases are the largest family of receptor tyrosine kinases. They are classified into two groups based on their abilities to bind ephrin-A and ephrin-B ligands. The EPH receptors are involved in regulation of cell movement, shape, and attachment during embryonic development; they control cell-cell interactions in the vascular, nervous, epithelial, and immune systems, and in many tumors. They are potential molecular markers for cancer diagnostics and potential targets for cancer therapy.


Pssm-ID: 188887  Cd Length: 61  Bit Score: 36.05  E-value: 7.22e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767950366 1031 ISQFLKSLGLEHLRDIFET-EQITLDVLADMGHEELKEIGINAYGHRHKLIKGVERL 1086
Cdd:cd09488     5 VGEWLESIKMGRYKENFTAaGYTSLDAVAQMTAEDLTRLGVTLVGHQKKILNSIQAL 61
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
249-277 7.36e-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: 35.26  E-value: 7.36e-03
                            10        20
                    ....*....|....*....|....*....
gi 767950366    249 GLIPLHNACSFGHAEVVSLLLCQGADPNA 277
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
823-928 7.44e-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: 40.77  E-value: 7.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  823 CTPENINCRDTQGRNSTPLHLAAGYNNLEVAEYLLE-HGADVNAQDKGGLIPLHNAASYGHVDIAALLIKYN-TCVNATD 900
Cdd:cd22192     3 QMLDELHLLQQKRISESPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAApELVNEPM 82
                          90       100       110
                  ....*....|....*....|....*....|..
gi 767950366  901 KWAF----TPLHEAAQKGRTQLCALLLAHGAD 928
Cdd:cd22192    83 TSDLyqgeTALHIAVVNQNLNLVRELIARGAD 114
PHA02798 PHA02798
ankyrin-like protein; Provisional
205-396 7.79e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 40.59  E-value: 7.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  205 ANVNAKDMAGRksSPLHFAAGFG---RKDVVEHLLQMGANVHARDDGGLIPLHNACSFGHA---EVVSLLLCQGADPNAR 278
Cdd:PHA02798  100 ADINKKNSDGE--TPLYCLLSNGyinNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKGVDINTH 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950366  279 DNW-NYTPLHeAAIKGKIDvCIvllqhgaDPNIRN--TDGKSALDLADPSAKAVLTgEYKKDeLLEAARSGNEEKLMALL 355
Cdd:PHA02798  178 NNKeKYDTLH-CYFKYNID-RI-------DADILKlfVDNGFIINKENKSHKKKFM-EYLNS-LLYDNKRFKKNILDFIF 246
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 767950366  356 TPLNVNchASDGRKSTPLHLAAGYNRVRIVQLLLQHGADVH 396
Cdd:PHA02798  247 SYIDIN--QVDELGFNPLYYSVSHNNRKIFEYLLQLGGDIN 285
SAM_EPH-B6 cd09555
SAM domain of EPH-B6 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
1030-1086 7.89e-03

SAM domain of EPH-B6 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-B6 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-B6 receptors and appears to mediate cell-cell initiated signal transduction. Receptors of this type are highly expressed in embryo and adult nervous system, in thymus and also in T-cells. They are involved in regulation of cell adhesion and migration. (EPH-B6 receptor is unusual; it fails to show catalytic activity due to alteration in kinase domain). EPH-B6 may be considered as a biomarker in some types of tumors; EPH-B6 activates MAP kinase signaling in lung adenocarcinoma, suppresses metastasis formation in non-small cell lung cancer, and slows invasiveness in some breast cancer cell lines.


Pssm-ID: 188954  Cd Length: 69  Bit Score: 36.45  E-value: 7.89e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767950366 1030 NISQFLKSLGLEHLRDIFETEQ-ITLDVLADMGHEELKEIGINAYGHRHKLIKGVERL 1086
Cdd:cd09555     8 SPQAWLSAIGLECYQDNFSKFGlCTFSDVAQLSLEDLPALGITLAGHQKKLLHHIQLL 65
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
405-430 8.28e-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: 35.26  E-value: 8.28e-03
                            10        20
                    ....*....|....*....|....*.
gi 767950366    405 PLHNACSYGHYEVTELLLKHGACVNA 430
Cdd:smart00248    5 PLHLAAENGNLEVVKLLLDKGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
252-277 8.62e-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: 34.93  E-value: 8.62e-03
                           10        20
                   ....*....|....*....|....*.
gi 767950366   252 PLHNACSFGHAEVVSLLLCQGADPNA 277
Cdd:pfam13606    5 PLHLAARNGRLEIVKLLLENGADINA 30
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH