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Conserved domains on  [gi|13376842|ref|NP_079511|]
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poly [ADP-ribose] polymerase tankyrase-2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
tankyrase_like cd01438
Tankyrases interact with the telomere reverse transcriptase complex (TERT). Tankyrase 1 ...
938-1160 8.95e-152

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: 452.82  E-value: 8.95e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842  938 QGLNPYLTLNTSGSGTILIDLSPDDKEFQSVEEEMQSTVREHRDGGHAGGIFNRYNILKIQKVCNKKLWERYTHRRKEVS 1017
Cdd:cd01438    1 QGRNPYLTFHCVNQGTILLDLAPDDKEYQSVEEEMQSTIREHRDGGNAGGIFNRYNIIRIQKVVNKKLRERYCHRQKEIA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842 1018 EENHNHANERMLFHGSPFVNAIIHKGFDERHAYIGGMFGAGIYFAENSSKSNQYVYGIGGGTGCPVHKDRSCYICHRQLL 1097
Cdd:cd01438   81 EENHNHHNERMLFHGSPFINAIIHKGFDERHAYIGGMFGAGIYFAENSSKSNQYVYGIGGGTGCPTHKDRSCYVCHRQML 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13376842 1098 FCRVTLGKSFLQFSAMKMAHSPPGHHSVTGRPSVNGLALAEYVIYRGEQAYPEYLITYQIMRP 1160
Cdd:cd01438  161 FCRVTLGKSFLQFSAMKMAHAPPGHHSVIGRPSVNGLAYAEYVIYRGEQAYPEYLITYQIVKP 223
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
485-789 3.02e-48

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 173.99  E-value: 3.02e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842  485 ISLGNSEADRQLLEAAKAGDVETVKKLCTVQSVNCRDIEGRQSTPLHFAAGYNRVSVVEYLLQHGADVHAKDKGGLVPLH 564
Cdd:COG0666   13 AALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLH 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842  565 NACSYGHYEVAELLVKHGAVVNVADLWKFTPLHEAAAKGKYEICKLLLQHGADPTKKNRDGNTPLdlvkdgdtdiqdllr 644
Cdd:COG0666   93 AAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPL--------------- 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842  645 gdaalldaakkgclarvkklsspdnvncrdtqgrhstplHLAAGYNNLEVAEYLLQHGADVNAQDKGGLIPLHNAASYGH 724
Cdd:COG0666  158 ---------------------------------------HLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGH 198
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13376842  725 VDVAALLIKYNACVNATDKWAFTPLHEAAQKGRTQLCALLLAHGADPTLKNQEGQTPLDLVSADD 789
Cdd:COG0666  199 LEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAG 263
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
60-343 4.91e-45

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 164.74  E-value: 4.91e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   60 TPLHFAAGFGRKDVVEYLLQNGANVQARDDGGLIPLHNACSFGHAEVVNLLLRHGADPNARDNWNYTPLHEAAIKGKIDV 139
Cdd:COG0666   56 LLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEI 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842  140 CIVLLQHGAEPTIRNTDGRtaldladpsakavltgeykkdellesarsgneekmmalltplnvnchasdgrksTPLHLAA 219
Cdd:COG0666  136 VKLLLEAGADVNAQDNDGN------------------------------------------------------TPLHLAA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842  220 GYNRVKIVQLLLQHGADVHAKDKGDLVPLHNACSYGHYEVTELLVKHGACVNAMDLWQFTPLHEAASKNRVEVCSLLLSY 299
Cdd:COG0666  162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 13376842  300 GADPTLLNCHNKSAIDLAPTPQLKERLAYEFKGHSLLQAAREAD 343
Cdd:COG0666  242 GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDL 285
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
160-470 7.52e-39

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 146.64  E-value: 7.52e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842  160 ALDLADPSAKAVLTGEYKKDELLESARSGNEEKMMALLTPLNVNCHASDGRKSTPLHLAAGYNRVKIVQLLLQHGADVHA 239
Cdd:COG0666   36 LLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNA 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842  240 KDKGDLVPLHNACSYGHYEVTELLVKHGACVNAMDLWQFTPLHEAASKNRVEVCSLLLSYGADPTLLNCHNksaidlapt 319
Cdd:COG0666  116 RDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDG--------- 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842  320 pqlkerlayefkghsllqaareadvtrikkhlslemvnfkhpqthETALHCAAASpypKRKQICELLLRKGANINEKTKE 399
Cdd:COG0666  187 ---------------------------------------------ETPLHLAAEN---GHLEIVKLLLEAGADVNAKDND 218
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13376842  400 FLTPLHVASEKAHNDVVEVVVKHEAKVNALDNLGQTSLHRAAYCGHLQTCRLLLSYGCDPNIISLQGFTAL 470
Cdd:COG0666  219 GKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
SAM_tankyrase1,2 cd09524
SAM domain of tankyrase1,2 subfamily; SAM (sterile alpha motif) domain of Tankyrase1,2 ...
871-936 6.77e-38

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: 135.92  E-value: 6.77e-38
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13376842  871 VPGVDFSITQFVRNLGLEHLMDIFEREQITLDVLVEMGHKELKEIGINAYGHRHKLIKGVERLISG 936
Cdd:cd09524    1 VNGTDFSISQFLSSLGLEHLREIFEREQITLDVLAEMGHEELKEIGINAYGHRHKLIKGVERLISG 66
Ank_4 pfam13637
Ankyrin repeats (many copies);
648-699 1.59e-04

Ankyrin repeats (many copies);


:

Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 40.34  E-value: 1.59e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 13376842    648 ALLDAAKKGCLARVKKL-SSPDNVNCRDTQGRhsTPLHLAAGYNNLEVAEYLL 699
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 ...
938-1160 8.95e-152

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: 452.82  E-value: 8.95e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842  938 QGLNPYLTLNTSGSGTILIDLSPDDKEFQSVEEEMQSTVREHRDGGHAGGIFNRYNILKIQKVCNKKLWERYTHRRKEVS 1017
Cdd:cd01438    1 QGRNPYLTFHCVNQGTILLDLAPDDKEYQSVEEEMQSTIREHRDGGNAGGIFNRYNIIRIQKVVNKKLRERYCHRQKEIA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842 1018 EENHNHANERMLFHGSPFVNAIIHKGFDERHAYIGGMFGAGIYFAENSSKSNQYVYGIGGGTGCPVHKDRSCYICHRQLL 1097
Cdd:cd01438   81 EENHNHHNERMLFHGSPFINAIIHKGFDERHAYIGGMFGAGIYFAENSSKSNQYVYGIGGGTGCPTHKDRSCYVCHRQML 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13376842 1098 FCRVTLGKSFLQFSAMKMAHSPPGHHSVTGRPSVNGLALAEYVIYRGEQAYPEYLITYQIMRP 1160
Cdd:cd01438  161 FCRVTLGKSFLQFSAMKMAHAPPGHHSVIGRPSVNGLAYAEYVIYRGEQAYPEYLITYQIVKP 223
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
485-789 3.02e-48

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 173.99  E-value: 3.02e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842  485 ISLGNSEADRQLLEAAKAGDVETVKKLCTVQSVNCRDIEGRQSTPLHFAAGYNRVSVVEYLLQHGADVHAKDKGGLVPLH 564
Cdd:COG0666   13 AALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLH 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842  565 NACSYGHYEVAELLVKHGAVVNVADLWKFTPLHEAAAKGKYEICKLLLQHGADPTKKNRDGNTPLdlvkdgdtdiqdllr 644
Cdd:COG0666   93 AAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPL--------------- 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842  645 gdaalldaakkgclarvkklsspdnvncrdtqgrhstplHLAAGYNNLEVAEYLLQHGADVNAQDKGGLIPLHNAASYGH 724
Cdd:COG0666  158 ---------------------------------------HLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGH 198
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13376842  725 VDVAALLIKYNACVNATDKWAFTPLHEAAQKGRTQLCALLLAHGADPTLKNQEGQTPLDLVSADD 789
Cdd:COG0666  199 LEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAG 263
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
60-343 4.91e-45

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 164.74  E-value: 4.91e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   60 TPLHFAAGFGRKDVVEYLLQNGANVQARDDGGLIPLHNACSFGHAEVVNLLLRHGADPNARDNWNYTPLHEAAIKGKIDV 139
Cdd:COG0666   56 LLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEI 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842  140 CIVLLQHGAEPTIRNTDGRtaldladpsakavltgeykkdellesarsgneekmmalltplnvnchasdgrksTPLHLAA 219
Cdd:COG0666  136 VKLLLEAGADVNAQDNDGN------------------------------------------------------TPLHLAA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842  220 GYNRVKIVQLLLQHGADVHAKDKGDLVPLHNACSYGHYEVTELLVKHGACVNAMDLWQFTPLHEAASKNRVEVCSLLLSY 299
Cdd:COG0666  162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 13376842  300 GADPTLLNCHNKSAIDLAPTPQLKERLAYEFKGHSLLQAAREAD 343
Cdd:COG0666  242 GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDL 285
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
160-470 7.52e-39

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 146.64  E-value: 7.52e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842  160 ALDLADPSAKAVLTGEYKKDELLESARSGNEEKMMALLTPLNVNCHASDGRKSTPLHLAAGYNRVKIVQLLLQHGADVHA 239
Cdd:COG0666   36 LLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNA 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842  240 KDKGDLVPLHNACSYGHYEVTELLVKHGACVNAMDLWQFTPLHEAASKNRVEVCSLLLSYGADPTLLNCHNksaidlapt 319
Cdd:COG0666  116 RDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDG--------- 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842  320 pqlkerlayefkghsllqaareadvtrikkhlslemvnfkhpqthETALHCAAASpypKRKQICELLLRKGANINEKTKE 399
Cdd:COG0666  187 ---------------------------------------------ETPLHLAAEN---GHLEIVKLLLEAGADVNAKDND 218
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13376842  400 FLTPLHVASEKAHNDVVEVVVKHEAKVNALDNLGQTSLHRAAYCGHLQTCRLLLSYGCDPNIISLQGFTAL 470
Cdd:COG0666  219 GKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
SAM_tankyrase1,2 cd09524
SAM domain of tankyrase1,2 subfamily; SAM (sterile alpha motif) domain of Tankyrase1,2 ...
871-936 6.77e-38

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: 135.92  E-value: 6.77e-38
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13376842  871 VPGVDFSITQFVRNLGLEHLMDIFEREQITLDVLVEMGHKELKEIGINAYGHRHKLIKGVERLISG 936
Cdd:cd09524    1 VNGTDFSISQFLSSLGLEHLREIFEREQITLDVLAEMGHEELKEIGINAYGHRHKLIKGVERLISG 66
PHA03095 PHA03095
ankyrin-like protein; Provisional
494-802 9.64e-33

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 133.61  E-value: 9.64e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   494 RQLLEAAKAgDVETVKKLC-TVQSVNCRDIEGRqsTPLHFAAGYN---RVSVVEYLLQHGADVHAKDKGGLVPLH----N 565
Cdd:PHA03095   17 DYLLNASNV-TVEEVRRLLaAGADVNFRGEYGK--TPLHLYLHYSsekVKDIVRLLLEAGADVNAPERCGFTPLHlylyN 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   566 ACSYghyEVAELLVKHGAVVNVADLWKFTPLHeAAAKGK---YEICKLLLQHGADPTKKNRDGNTPLD-LVKDGDTDIqD 641
Cdd:PHA03095   94 ATTL---DVIKLLIKAGADVNAKDKVGRTPLH-VYLSGFninPKVIRLLLRKGADVNALDLYGMTPLAvLLKSRNANV-E 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   642 LLRgdaALLDAakkGCLARVKKLsspdnvncrdtqgRHSTPLHLAAGY--NNLEVAEYLLQHGADVNAQDKGGLIPLHNA 719
Cdd:PHA03095  169 LLR---LLIDA---GADVYAVDD-------------RFRSLLHHHLQSfkPRARIVRELIRAGCDPAATDMLGNTPLHSM 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   720 ASYG---HVDVAALLIKyNACVNATDKWAFTPLHEAAQKGRTQLCALLLAHGADPTLKNQEGQTPLDLVSADDVSALLTA 796
Cdd:PHA03095  230 ATGSsckRSLVLPLLIA-GISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRA 308

                  ....*...
gi 13376842   797 AMP--PSA 802
Cdd:PHA03095  309 ALAknPSA 316
PHA02876 PHA02876
ankyrin repeat protein; Provisional
73-458 8.01e-30

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 127.10  E-value: 8.01e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842    73 VVEYLLQNGANVQARDDGGLIPLHNACSFGHAEVVNLLLRHGADPNARDNWNYTPLHEAAIKGKIDVCIVLLQHGAE--- 149
Cdd:PHA02876  160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNink 239
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   150 ------PTIRNTDGRTALDLADPSAKAVLTGEYKKDELLESARSGNEEKMMALLTPLNVNCHASDGRKSTPLHLAA--GY 221
Cdd:PHA02876  240 ndlsllKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAknGY 319
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   222 NRVKIvQLLLQHGADVHAKDKGDLVPLHNACSYGHYEVTEL-LVKHGACVNAMDLWQFTPLHEAASKNRVEVCSLLLSYG 300
Cdd:PHA02876  320 DTENI-RTLIMLGADVNAADRLYITPLHQASTLDRNKDIVItLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYG 398
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   301 ADPTLLNchnksaidlaptpqlkerlayefkghsllqaareadvtrikkhlslemvnfkhpQTHETALHCA--AASPYPK 378
Cdd:PHA02876  399 ADIEALS------------------------------------------------------QKIGTALHFAlcGTNPYMS 424
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   379 RKQicelLLRKGANINEKTKEFLTPLHVASEK-AHNDVVEVVVKHEAKVNALDNLGQTSLHRAayCGHLQTCRLLLSYGC 457
Cdd:PHA02876  425 VKT----LIDRGANVNSKNKDLSTPLHYACKKnCKLDVIEMLLDNGADVNAINIQNQYPLLIA--LEYHGIVNILLHYGA 498

                  .
gi 13376842   458 D 458
Cdd:PHA02876  499 E 499
PHA03100 PHA03100
ankyrin repeat protein; Provisional
207-472 2.22e-27

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 116.30  E-value: 2.22e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   207 SDGRKSTPLHLAAGYNRVKIVQLLLQHGADVHAKDKGDLVPLHNACSYGHY-----EVTELLVKHGACVNAMDLWQFTPL 281
Cdd:PHA03100   31 SYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPL 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   282 HEAASK--NRVEVCSLLLSYGADPTLLNCHNksaidlaptpqlkerlayefkghsllqaareadvtrikkhlslemvnfk 359
Cdd:PHA03100  111 LYAISKksNSYSIVEYLLDNGANVNIKNSDG------------------------------------------------- 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   360 hpqthETALHCAAASPYPKRKqICELLLRKGANINEKTKefltplhvasekahndvVEVVVKHEAKVNALDNLGQTSLHR 439
Cdd:PHA03100  142 -----ENLLHLYLESNKIDLK-ILKLLIDKGVDINAKNR-----------------VNYLLSYGVPINIKDVYGFTPLHY 198
                         250       260       270
                  ....*....|....*....|....*....|...
gi 13376842   440 AAYCGHLQTCRLLLSYGCDPNIISLQGFTALQM 472
Cdd:PHA03100  199 AVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHI 231
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
963-1155 3.88e-25

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: 103.95  E-value: 3.88e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842    963 KEFQSVEEEMQSTvrehRDGGHAGGIFnrynILKIQKVCNKKLWERYTHRRKevseenhnHANERMLFHGSP--FVNAII 1040
Cdd:pfam00644    2 EEYQIIEKYFLST----HDPTHGYPLF----ILEIFRVQRDGEWERFQPKKK--------LRNRRLLWHGSRltNFLGIL 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   1041 HKGF--DERHAYIGG-MFGAGIYFAENSSKSNQYvygigggtgCPVHKDRScyicHRQLLFCRVTLGKSFLQFSAMKMAH 1117
Cdd:pfam00644   66 SQGLriAPPEAPVTGyMFGKGIYFADDASKSANY---------CPPSEAHG----NGLMLLSEVALGDMNELKKADYAEK 132
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13376842   1118 SPPGHHSV------------------TGRPSVNGLALA-----EYVIYRGEQAYPEYLITY 1155
Cdd:pfam00644  133 LPPGKHSVkglgktapesfvdldgvpLGKLVATGYDSSvllynEYVVYNVNQVRPKYLLEV 193
PHA02876 PHA02876
ankyrin repeat protein; Provisional
259-652 2.47e-23

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 106.69  E-value: 2.47e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   259 VTELLVKHGACVNAMDLWQFTPLHEAASKNRVEVCSLLLSYGADPTLLNCHNKSAIDLAPTPQ--------LKERLAYEF 330
Cdd:PHA02876  160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKnidtikaiIDNRSNINK 239
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   331 KGHSLLQAAREADV-TRIKKHLSLEMVNfKHPQTHETALHCAAASPYPKRkqICELLLRKGANINEKTKEFLTPLHVASE 409
Cdd:PHA02876  240 NDLSLLKAIRNEDLeTSLLLYDAGFSVN-SIDDCKNTPLHHASQAPSLSR--LVPKLLERGADVNAKNIKGETPLYLMAK 316
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   410 KAHN-DVVEVVVKHEAKVNALDNLGQTSLHRAaycghlqtcrlllsygcdpniislqgfTALQMGNENVQQLLQEGislg 488
Cdd:PHA02876  317 NGYDtENIRTLIMLGADVNAADRLYITPLHQA---------------------------STLDRNKDIVITLLELG---- 365
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   489 nseadrqlleaakagdvetvkklctvQSVNCRDIegRQSTPLHFAAGYNRVSVVEYLLQHGADVHAKDKGGLVPLHNA-C 567
Cdd:PHA02876  366 --------------------------ANVNARDY--CDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlC 417
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   568 SYGHYEVAELLVKHGAVVNVADLWKFTPLHEAAAKG-KYEICKLLLQHGADPTKKNRDGNTPLDLVKDGDTDIQDLLRGD 646
Cdd:PHA02876  418 GTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIALEYHGIVNILLHYG 497

                  ....*.
gi 13376842   647 AALLDA 652
Cdd:PHA02876  498 AELRDS 503
Ank_2 pfam12796
Ankyrin repeats (3 copies);
530-622 3.06e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.10  E-value: 3.06e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842    530 LHFAAGYNRVSVVEYLLQHGADVHAKDKGGLVPLHNACSYGHYEVAELLVKHGAVVNVADLWkfTPLHEAAAKGKYEICK 609
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGR--TALHYAARSGHLEIVK 78
                           90
                   ....*....|...
gi 13376842    610 LLLQHGADPTKKN 622
Cdd:pfam12796   79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
62-154 7.14e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 88.25  E-value: 7.14e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842     62 LHFAAGFGRKDVVEYLLQNGANVQARDDGGLIPLHNACSFGHAEVVNLLLRHgADPNARDNwNYTPLHEAAIKGKIDVCI 141
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78
                           90
                   ....*....|...
gi 13376842    142 VLLQHGAEPTIRN 154
Cdd:pfam12796   79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
368-461 4.39e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 74.38  E-value: 4.39e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842    368 LHCAAASPYPkrkQICELLLRKGANINEKTKEFLTPLHVASEKAHNDVVEVVVKHeAKVNALDNlGQTSLHRAAYCGHLQ 447
Cdd:pfam12796    1 LHLAAKNGNL---ELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLE 75
                           90
                   ....*....|....
gi 13376842    448 TCRLLLSYGCDPNI 461
Cdd:pfam12796   76 IVKLLLEKGADINV 89
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
877-934 6.36e-13

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 64.60  E-value: 6.36e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 13376842    877 SITQFVRNLGLEHLMDIFEREQIT-LDVLVEMGHKELKEIGINAYGHRHKLIKGVERLI 934
Cdd:pfam07647    8 SVADWLRSIGLEQYTDNFRDQGITgAELLLRLTLEDLKRLGITSVGHRRKILKKIQELK 66
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
496-700 1.00e-10

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: 65.80  E-value: 1.00e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842  496 LLEAAKAGDVETVKKLCTVQSVncrDIEGRQS---TPLHFAAGYNRVSVVEYLLQHG---------ADVHAkdkgGLVPL 563
Cdd:cd22192   21 LLLAAKENDVQAIKKLLKCPSC---DLFQRGAlgeTALHVAALYDNLEAAVVLMEAApelvnepmtSDLYQ----GETAL 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842  564 HNACSYGHYEVAELLVKHGAVVNVA------------DLWKFT--PLHEAAAKGKYEICKLLLQHGADPTKKNRDGNTPL 629
Cdd:cd22192   94 HIAVVNQNLNLVRELIARGADVVSPratgtffrpgpkNLIYYGehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13376842  630 D-LV----KDGDTDIQDLLrgdaalldaakkgcLARVKklssPDNVNCRDTQGRHS--TPLHLAAGYNNLEVAEYLLQ 700
Cdd:cd22192  174 HiLVlqpnKTFACQMYDLI--------------LSYDK----EDDLQPLDLVPNNQglTPFKLAAKEGNIVMFQHLVQ 233
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
877-933 1.09e-09

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: 55.38  E-value: 1.09e-09
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 13376842     877 SITQFVRNLGLEHLMDIFEREQITLDVLVEMGHKE-LKEIGINAYGHRHKLIKGVERL 933
Cdd:smart00454    8 SVADWLESIGLEQYADNFRKNGIDGALLLLLTSEEdLKELGITKLGHRKKILKAIQKL 65
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
28-164 4.87e-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: 4.87e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   28 LFEACRNGDVERVKRLVT------------------------------------PEKVNSRDT----AGRksTPLHFAAG 67
Cdd:cd22192   21 LLLAAKENDVQAIKKLLKcpscdlfqrgalgetalhvaalydnleaavvlmeaaPELVNEPMTsdlyQGE--TALHIAVV 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   68 FGRKDVVEYLLQNGANVQ-ARDDG--------GLI-----PLHNACSFGHAEVVNLLLRHGADPNARDNWNYTPLHE-AA 132
Cdd:cd22192   99 NQNLNLVRELIARGADVVsPRATGtffrpgpkNLIyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHIlVL 178
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 13376842  133 IKGKIDVCIV---LLQHGAE------PTIRNTDGRTALDLA 164
Cdd:cd22192  179 QPNKTFACQMydlILSYDKEddlqplDLVPNNQGLTPFKLA 219
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
571-784 9.31e-09

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: 59.71  E-value: 9.31e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842    571 HYEVAELLVKHGAVVNVADlwkfTPLHeAAAKGKYEICKLLLQHgadpTKKNRDGNTPLDLVKDGDTDiqDLLRGdaall 650
Cdd:TIGR00870   65 NLELTELLLNLSCRGAVGD----TLLH-AISLEYVDAVEAILLH----LLAAFRKSGPLELANDQYTS--EFTPG----- 128
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842    651 daakkgclarvkklsspdnvncrdtqgrhSTPLHLAAGYNNLEVAEYLLQHGADVNAQDKG--------------GLIPL 716
Cdd:TIGR00870  129 -----------------------------ITALHLAAHRQNYEIVKLLLERGASVPARACGdffvksqgvdsfyhGESPL 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842    717 HNAASYGHVDVAALLIKYNACVNATDKWAFTPLHEAA---------QKGRTQLCALLLAHGA--DPTLK-----NQEGQT 780
Cdd:TIGR00870  180 NAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVmenefkaeyEELSCQMYNFALSLLDklRDSKElevilNHQGLT 259

                   ....
gi 13376842    781 PLDL 784
Cdd:TIGR00870  260 PLKL 263
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
60-172 1.75e-07

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: 55.47  E-value: 1.75e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842     60 TPLHFAAGFGRKDVVEYLLQNGANVQARDDG--------------GLIPLHNACSFGHAEVVNLLLRHGADPNARDNWNY 125
Cdd:TIGR00870  130 TALHLAAHRQNYEIVKLLLERGASVPARACGdffvksqgvdsfyhGESPLNAAACLGSPSIVALLSEDPADILTADSLGN 209
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13376842    126 TPLHEAAIKGKID------VCIV---LLQHGAEP-------TIRNTDGRTALDLADPSAKAVL 172
Cdd:TIGR00870  210 TLLHLLVMENEFKaeyeelSCQMynfALSLLDKLrdskeleVILNHQGLTPLKLAAKEGRIVL 272
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
681-707 1.57e-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: 1.57e-05
                            10        20
                    ....*....|....*....|....*..
gi 13376842     681 TPLHLAAGYNNLEVAEYLLQHGADVNA 707
Cdd:smart00248    4 TPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
91-119 9.45e-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: 40.65  E-value: 9.45e-05
                            10        20
                    ....*....|....*....|....*....
gi 13376842      91 GLIPLHNACSFGHAEVVNLLLRHGADPNA 119
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
648-699 1.59e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 40.34  E-value: 1.59e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 13376842    648 ALLDAAKKGCLARVKKL-SSPDNVNCRDTQGRhsTPLHLAAGYNNLEVAEYLL 699
Cdd:pfam13637    4 ALHAAAASGHLELLRLLlEKGADINAVDGNGE--TALHFAASNGNVEVLKLLL 54
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
346-428 6.88e-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: 6.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842  346 RIKKHLSLEmvNFKHPQTHETALHCAAASPYPKRKQICELLLrkgaNINEKT---KEFL------------TPLHVASEK 410
Cdd:cd22196   31 RTKKRLTDS--EFKDPETGKTCLLKAMLNLHNGQNDTISLLL----DIAEKTgnlKEFVnaaytdsyykgqTALHIAIER 104
                         90
                 ....*....|....*...
gi 13376842  411 AHNDVVEVVVKHEAKVNA 428
Cdd:cd22196  105 RNMHLVELLVQNGADVHA 122
 
Name Accession Description Interval E-value
tankyrase_like cd01438
Tankyrases interact with the telomere reverse transcriptase complex (TERT). Tankyrase 1 ...
938-1160 8.95e-152

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: 452.82  E-value: 8.95e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842  938 QGLNPYLTLNTSGSGTILIDLSPDDKEFQSVEEEMQSTVREHRDGGHAGGIFNRYNILKIQKVCNKKLWERYTHRRKEVS 1017
Cdd:cd01438    1 QGRNPYLTFHCVNQGTILLDLAPDDKEYQSVEEEMQSTIREHRDGGNAGGIFNRYNIIRIQKVVNKKLRERYCHRQKEIA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842 1018 EENHNHANERMLFHGSPFVNAIIHKGFDERHAYIGGMFGAGIYFAENSSKSNQYVYGIGGGTGCPVHKDRSCYICHRQLL 1097
Cdd:cd01438   81 EENHNHHNERMLFHGSPFINAIIHKGFDERHAYIGGMFGAGIYFAENSSKSNQYVYGIGGGTGCPTHKDRSCYVCHRQML 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13376842 1098 FCRVTLGKSFLQFSAMKMAHSPPGHHSVTGRPSVNGLALAEYVIYRGEQAYPEYLITYQIMRP 1160
Cdd:cd01438  161 FCRVTLGKSFLQFSAMKMAHAPPGHHSVIGRPSVNGLAYAEYVIYRGEQAYPEYLITYQIVKP 223
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
485-789 3.02e-48

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 173.99  E-value: 3.02e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842  485 ISLGNSEADRQLLEAAKAGDVETVKKLCTVQSVNCRDIEGRQSTPLHFAAGYNRVSVVEYLLQHGADVHAKDKGGLVPLH 564
Cdd:COG0666   13 AALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLH 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842  565 NACSYGHYEVAELLVKHGAVVNVADLWKFTPLHEAAAKGKYEICKLLLQHGADPTKKNRDGNTPLdlvkdgdtdiqdllr 644
Cdd:COG0666   93 AAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPL--------------- 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842  645 gdaalldaakkgclarvkklsspdnvncrdtqgrhstplHLAAGYNNLEVAEYLLQHGADVNAQDKGGLIPLHNAASYGH 724
Cdd:COG0666  158 ---------------------------------------HLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGH 198
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13376842  725 VDVAALLIKYNACVNATDKWAFTPLHEAAQKGRTQLCALLLAHGADPTLKNQEGQTPLDLVSADD 789
Cdd:COG0666  199 LEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAG 263
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
60-343 4.91e-45

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 164.74  E-value: 4.91e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   60 TPLHFAAGFGRKDVVEYLLQNGANVQARDDGGLIPLHNACSFGHAEVVNLLLRHGADPNARDNWNYTPLHEAAIKGKIDV 139
Cdd:COG0666   56 LLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEI 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842  140 CIVLLQHGAEPTIRNTDGRtaldladpsakavltgeykkdellesarsgneekmmalltplnvnchasdgrksTPLHLAA 219
Cdd:COG0666  136 VKLLLEAGADVNAQDNDGN------------------------------------------------------TPLHLAA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842  220 GYNRVKIVQLLLQHGADVHAKDKGDLVPLHNACSYGHYEVTELLVKHGACVNAMDLWQFTPLHEAASKNRVEVCSLLLSY 299
Cdd:COG0666  162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 13376842  300 GADPTLLNCHNKSAIDLAPTPQLKERLAYEFKGHSLLQAAREAD 343
Cdd:COG0666  242 GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDL 285
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
28-307 9.16e-44

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 160.89  E-value: 9.16e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   28 LFEACRNGDVERVKRLVTPEKVNSRDTAGRKSTPLHFAAGFGRKDVVEYLLQNGANVQARDDGGLIPLHNACSFGHAEVV 107
Cdd:COG0666   57 LLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIV 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842  108 NLLLRHGADPNARDNWNYTPLHEAAIKGKIDVCIVLLQHGAEPTIRNTDGRtaldladpsakavltgeykkdellesars 187
Cdd:COG0666  137 KLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGE----------------------------- 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842  188 gneekmmalltplnvnchasdgrksTPLHLAAGYNRVKIVQLLLQHGADVHAKDKGDLVPLHNACSYGHYEVTELLVKHG 267
Cdd:COG0666  188 -------------------------TPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAG 242
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 13376842  268 ACVNAMDLWQFTPLHEAASKNRVEVCSLLLSYGADPTLLN 307
Cdd:COG0666  243 ADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
347-716 1.09e-40

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 152.03  E-value: 1.09e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842  347 IKKHLSLEMVNFKHPQTHETALHCAAASPYPKRKQICELLLRKGANINEKTKEFLTPLHVASEKAHNDVVEVVVKHEAKV 426
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842  427 NALDNLGQTSLHRAAYCGHLQTCRLLLSYGCDPNIISLQGFTalqmgnenvqqllqegislgnseadrqlleaakagdve 506
Cdd:COG0666   81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGET-------------------------------------- 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842  507 tvkklctvqsvncrdiegrqstPLHFAAGYNRVSVVEYLLQHGADVHAKDKGGLVPLHNACSYGHYEVAELLVKHGAVVN 586
Cdd:COG0666  123 ----------------------PLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVN 180
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842  587 VADLWKFTPLHEAAAKGKYEICKLLLQHGADPTKKNRDGNTPLDL-VKDGDTDIQDLLRGDAALLDAAKKgclarvkkls 665
Cdd:COG0666  181 ARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLaAENGNLEIVKLLLEAGADLNAKDK---------- 250
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 13376842  666 spdnvncrdtqgRHSTPLHLAAGYNNLEVAEYLLQHGADVNAQDKGGLIPL 716
Cdd:COG0666  251 ------------DGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
28-245 2.66e-40

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 150.87  E-value: 2.66e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   28 LFEACRNGDVERVKRLVT-PEKVNSRDTAGRksTPLHFAAGFGRKDVVEYLLQNGANVQARDDGGLIPLHNACSFGHAEV 106
Cdd:COG0666   91 LHAAARNGDLEIVKLLLEaGADVNARDKDGE--TPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEI 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842  107 VNLLLRHGADPNARDNWNYTPLHEAAIKGKIDVCIVLLQHGAEPTIRNTDGRTALDLAdpsakavltgeykkdellesAR 186
Cdd:COG0666  169 VKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLA--------------------AE 228
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 13376842  187 SGNEEkMMALLTPLNVNCHASDGRKSTPLHLAAGYNRVKIVQLLLQHGADVHAKDKGDL 245
Cdd:COG0666  229 NGNLE-IVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLL 286
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
160-470 7.52e-39

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 146.64  E-value: 7.52e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842  160 ALDLADPSAKAVLTGEYKKDELLESARSGNEEKMMALLTPLNVNCHASDGRKSTPLHLAAGYNRVKIVQLLLQHGADVHA 239
Cdd:COG0666   36 LLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNA 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842  240 KDKGDLVPLHNACSYGHYEVTELLVKHGACVNAMDLWQFTPLHEAASKNRVEVCSLLLSYGADPTLLNCHNksaidlapt 319
Cdd:COG0666  116 RDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDG--------- 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842  320 pqlkerlayefkghsllqaareadvtrikkhlslemvnfkhpqthETALHCAAASpypKRKQICELLLRKGANINEKTKE 399
Cdd:COG0666  187 ---------------------------------------------ETPLHLAAEN---GHLEIVKLLLEAGADVNAKDND 218
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13376842  400 FLTPLHVASEKAHNDVVEVVVKHEAKVNALDNLGQTSLHRAAYCGHLQTCRLLLSYGCDPNIISLQGFTAL 470
Cdd:COG0666  219 GKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
53-317 3.75e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 144.71  E-value: 3.75e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   53 DTAGRKSTPLHFAAGFGRKDVVEYLLQNGANVQARDDGGLIPLHNACSFGHAEVVNLLLRHGADPNARDNWNYTPLHEAA 132
Cdd:COG0666   16 LLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAA 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842  133 IKGKIDVCIVLLQHGAEPTIRNTDGRTaldladpsakavltgeykkdellesarsgneekmmalltplnvnchasdgrks 212
Cdd:COG0666   96 RNGDLEIVKLLLEAGADVNARDKDGET----------------------------------------------------- 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842  213 tPLHLAAGYNRVKIVQLLLQHGADVHAKDKGDLVPLHNACSYGHYEVTELLVKHGACVNAMDLWQFTPLHEAASKNRVEV 292
Cdd:COG0666  123 -PLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEI 201
                        250       260
                 ....*....|....*....|....*
gi 13376842  293 CSLLLSYGADPTLLNCHNKSAIDLA 317
Cdd:COG0666  202 VKLLLEAGADVNAKDNDGKTALDLA 226
SAM_tankyrase1,2 cd09524
SAM domain of tankyrase1,2 subfamily; SAM (sterile alpha motif) domain of Tankyrase1,2 ...
871-936 6.77e-38

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: 135.92  E-value: 6.77e-38
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13376842  871 VPGVDFSITQFVRNLGLEHLMDIFEREQITLDVLVEMGHKELKEIGINAYGHRHKLIKGVERLISG 936
Cdd:cd09524    1 VNGTDFSISQFLSSLGLEHLREIFEREQITLDVLAEMGHEELKEIGINAYGHRHKLIKGVERLISG 66
PHA03095 PHA03095
ankyrin-like protein; Provisional
494-802 9.64e-33

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 133.61  E-value: 9.64e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   494 RQLLEAAKAgDVETVKKLC-TVQSVNCRDIEGRqsTPLHFAAGYN---RVSVVEYLLQHGADVHAKDKGGLVPLH----N 565
Cdd:PHA03095   17 DYLLNASNV-TVEEVRRLLaAGADVNFRGEYGK--TPLHLYLHYSsekVKDIVRLLLEAGADVNAPERCGFTPLHlylyN 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   566 ACSYghyEVAELLVKHGAVVNVADLWKFTPLHeAAAKGK---YEICKLLLQHGADPTKKNRDGNTPLD-LVKDGDTDIqD 641
Cdd:PHA03095   94 ATTL---DVIKLLIKAGADVNAKDKVGRTPLH-VYLSGFninPKVIRLLLRKGADVNALDLYGMTPLAvLLKSRNANV-E 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   642 LLRgdaALLDAakkGCLARVKKLsspdnvncrdtqgRHSTPLHLAAGY--NNLEVAEYLLQHGADVNAQDKGGLIPLHNA 719
Cdd:PHA03095  169 LLR---LLIDA---GADVYAVDD-------------RFRSLLHHHLQSfkPRARIVRELIRAGCDPAATDMLGNTPLHSM 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   720 ASYG---HVDVAALLIKyNACVNATDKWAFTPLHEAAQKGRTQLCALLLAHGADPTLKNQEGQTPLDLVSADDVSALLTA 796
Cdd:PHA03095  230 ATGSsckRSLVLPLLIA-GISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRA 308

                  ....*...
gi 13376842   797 AMP--PSA 802
Cdd:PHA03095  309 ALAknPSA 316
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
191-629 1.75e-31

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 125.45  E-value: 1.75e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842  191 EKMMALLTPLNVNCHASDGRKSTPLHLAAGYNRVKIVQLLLQHGADVHAKDKGDLVPLHNACSYGHYEVTELLVKHGACV 270
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842  271 NAMDLWQFTPLHEAASKNRVEVCSLLLSYGADptllnchnksaidlaptpqlkerlayefkghsllqaareadvtrikkh 350
Cdd:COG0666   81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGAD------------------------------------------------ 112
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842  351 lslemvnfkhpqthetalhcaaaspypkrkqicelllrkganINEKTKEFLTPLHVASEKAHNDVVEVVVKHEAKVNALD 430
Cdd:COG0666  113 ------------------------------------------VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQD 150
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842  431 NLGQTSLHRAAYCGHLQTCRLLLSYGCDPNIislqgftalqmgnenvqqllqegislgnseadrqlleaakagdvetvkk 510
Cdd:COG0666  151 NDGNTPLHLAAANGNLEIVKLLLEAGADVNA------------------------------------------------- 181
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842  511 lctvqsvncRDIEGRqsTPLHFAAGYNRVSVVEYLLQHGADVHAKDKGGLVPLHNACSYGHYEVAELLVKHGAVVNVADL 590
Cdd:COG0666  182 ---------RDNDGE--TPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250
                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 13376842  591 WKFTPLHEAAAKGKYEICKLLLQHGADPTKKNRDGNTPL 629
Cdd:COG0666  251 DGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA02876 PHA02876
ankyrin repeat protein; Provisional
73-458 8.01e-30

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 127.10  E-value: 8.01e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842    73 VVEYLLQNGANVQARDDGGLIPLHNACSFGHAEVVNLLLRHGADPNARDNWNYTPLHEAAIKGKIDVCIVLLQHGAE--- 149
Cdd:PHA02876  160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNink 239
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   150 ------PTIRNTDGRTALDLADPSAKAVLTGEYKKDELLESARSGNEEKMMALLTPLNVNCHASDGRKSTPLHLAA--GY 221
Cdd:PHA02876  240 ndlsllKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAknGY 319
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   222 NRVKIvQLLLQHGADVHAKDKGDLVPLHNACSYGHYEVTEL-LVKHGACVNAMDLWQFTPLHEAASKNRVEVCSLLLSYG 300
Cdd:PHA02876  320 DTENI-RTLIMLGADVNAADRLYITPLHQASTLDRNKDIVItLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYG 398
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   301 ADPTLLNchnksaidlaptpqlkerlayefkghsllqaareadvtrikkhlslemvnfkhpQTHETALHCA--AASPYPK 378
Cdd:PHA02876  399 ADIEALS------------------------------------------------------QKIGTALHFAlcGTNPYMS 424
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   379 RKQicelLLRKGANINEKTKEFLTPLHVASEK-AHNDVVEVVVKHEAKVNALDNLGQTSLHRAayCGHLQTCRLLLSYGC 457
Cdd:PHA02876  425 VKT----LIDRGANVNSKNKDLSTPLHYACKKnCKLDVIEMLLDNGADVNAINIQNQYPLLIA--LEYHGIVNILLHYGA 498

                  .
gi 13376842   458 D 458
Cdd:PHA02876  499 E 499
PHA03100 PHA03100
ankyrin repeat protein; Provisional
525-743 2.49e-29

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 122.47  E-value: 2.49e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   525 RQSTPLHFAAGYNRVSVVEYLLQHGADVHAKDKGGLVPLHNACSYGHY-----EVAELLVKHGAVVNVADLWKFTPLHEA 599
Cdd:PHA03100   34 KPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYA 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   600 AAK--GKYEICKLLLQHGADPTKKNRDGNTPLDLVKDG---DTDIQDLLRGDAALLDAAKkgclaRVKKL-SSPDNVNCR 673
Cdd:PHA03100  114 ISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESnkiDLKILKLLIDKGVDINAKN-----RVNYLlSYGVPINIK 188
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   674 DTQGrhSTPLHLAAGYNNLEVAEYLLQHGADVNAQDKGGLIPLHNAASYGHVDVAALLIKYNACVNATDK 743
Cdd:PHA03100  189 DVYG--FTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256
PHA02876 PHA02876
ankyrin repeat protein; Provisional
378-782 9.22e-29

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 124.02  E-value: 9.22e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   378 KRKQICELLLRKGANINE----KTKEFLTPLHVASEKAHND---VVEVVVKHEAKVNALDNLGQTSLHRAAYCGHLQTCR 450
Cdd:PHA02876  116 KLDEACIHILKEAISGNDihydKINESIEYMKLIKERIQQDellIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVN 195
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   451 LLLSYGCDPNIISLQGFTALQ--MGNENVQQLLQEGISLGN-SEADRQLLEAAKAGDVETVKKLCTVQ-SVNcrDIEGRQ 526
Cdd:PHA02876  196 LLLSYGADVNIIALDDLSVLEcaVDSKNIDTIKAIIDNRSNiNKNDLSLLKAIRNEDLETSLLLYDAGfSVN--SIDDCK 273
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   527 STPLHFAAGYNRVS-VVEYLLQHGADVHAKDKGGLVPLHNACSYGH-YEVAELLVKHGAVVNVADLWKFTPLHEAAAKGK 604
Cdd:PHA02876  274 NTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDR 353
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   605 Y-EICKLLLQHGAdptkknrdgntpldlvkdgdtdiqdllrgdaalldaakkgclarvkklsspdNVNCRDTQGRhsTPL 683
Cdd:PHA02876  354 NkDIVITLLELGA----------------------------------------------------NVNARDYCDK--TPI 379
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   684 HLAAGYNNLEVAEYLLQHGADVNAQDKGGLIPLHNAAsYGHVDVAAL--LIKYNACVNATDKWAFTPLHEAAQKG-RTQL 760
Cdd:PHA02876  380 HYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAL-CGTNPYMSVktLIDRGANVNSKNKDLSTPLHYACKKNcKLDV 458
                         410       420
                  ....*....|....*....|..
gi 13376842   761 CALLLAHGADPTLKNQEGQTPL 782
Cdd:PHA02876  459 IEMLLDNGADVNAINIQNQYPL 480
PHA03100 PHA03100
ankyrin repeat protein; Provisional
207-472 2.22e-27

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 116.30  E-value: 2.22e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   207 SDGRKSTPLHLAAGYNRVKIVQLLLQHGADVHAKDKGDLVPLHNACSYGHY-----EVTELLVKHGACVNAMDLWQFTPL 281
Cdd:PHA03100   31 SYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPL 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   282 HEAASK--NRVEVCSLLLSYGADPTLLNCHNksaidlaptpqlkerlayefkghsllqaareadvtrikkhlslemvnfk 359
Cdd:PHA03100  111 LYAISKksNSYSIVEYLLDNGANVNIKNSDG------------------------------------------------- 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   360 hpqthETALHCAAASPYPKRKqICELLLRKGANINEKTKefltplhvasekahndvVEVVVKHEAKVNALDNLGQTSLHR 439
Cdd:PHA03100  142 -----ENLLHLYLESNKIDLK-ILKLLIDKGVDINAKNR-----------------VNYLLSYGVPINIKDVYGFTPLHY 198
                         250       260       270
                  ....*....|....*....|....*....|...
gi 13376842   440 AAYCGHLQTCRLLLSYGCDPNIISLQGFTALQM 472
Cdd:PHA03100  199 AVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHI 231
PHA02874 PHA02874
ankyrin repeat protein; Provisional
382-722 1.07e-26

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 114.68  E-value: 1.07e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   382 ICELLLRKGANINEKTKEFLTPLHVASEKAHNDVVEVVVKHEAKVNALDNLGQTSLHRAAYCGHLQTCRLLLSYGCDPNI 461
Cdd:PHA02874   17 IEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSI 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   462 ISLQgftalQMGNENVQQLLQEGIslgnseadrqlleaakagdvetvkklctvqSVNCRDIEGRqsTPLHFAAGYNRVSV 541
Cdd:PHA02874   97 LPIP-----CIEKDMIKTILDCGI------------------------------DVNIKDAELK--TFLHYAIKKGDLES 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   542 VEYLLQHGADVHAKDKGGLVPLHNACSYGHYEVAELLVKHGAVVNVADLWKFTPLHEAAAKGKYEICKLLLQHGADPTKK 621
Cdd:PHA02874  140 IKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNK 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   622 NRDGNTPLDLVKDGDTDIQDLLRGDAAlldaakkgclarvkklsspdnVNCRDTQGrhSTPLHLAAGYN-NLEVAEYLLQ 700
Cdd:PHA02874  220 CKNGFTPLHNAIIHNRSAIELLINNAS---------------------INDQDIDG--STPLHHAINPPcDIDIIDILLY 276
                         330       340
                  ....*....|....*....|..
gi 13376842   701 HGADVNAQDKGGLIPLHNAASY 722
Cdd:PHA02874  277 HKADISIKDNKGENPIDTAFKY 298
PHA03095 PHA03095
ankyrin-like protein; Provisional
29-317 8.29e-26

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 112.43  E-value: 8.29e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842    29 FEACRNGDVERVKRLV-TPEKVNSRDTAGRksTPLHFAAGFG---RKDVVEYLLQNGANVQARDDGGLIPLH----NACS 100
Cdd:PHA03095   19 LLNASNVTVEEVRRLLaAGADVNFRGEYGK--TPLHLYLHYSsekVKDIVRLLLEAGADVNAPERCGFTPLHlylyNATT 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   101 fghAEVVNLLLRHGADPNARDNWNYTPLHeAAIKGK-IDVCIV--LLQHGAEPTIRNTDGRTALDLadpsakavltgeyk 177
Cdd:PHA03095   97 ---LDVIKLLIKAGADVNAKDKVGRTPLH-VYLSGFnINPKVIrlLLRKGADVNALDLYGMTPLAV-------------- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   178 kdeLLESARSgnEEKMMALLTPLNVNCHASDGRKSTPLHLAAGY--NRVKIVQLLLQHGADVHAKDKGDLVPLHNACSYG 255
Cdd:PHA03095  159 ---LLKSRNA--NVELLRLLIDAGADVYAVDDRFRSLLHHHLQSfkPRARIVRELIRAGCDPAATDMLGNTPLHSMATGS 233
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13376842   256 HYEVTEL--LVKHGACVNAMDLWQFTPLHEAASKNRVEVCSLLLSYGADPTLLNCHNKSAIDLA 317
Cdd:PHA03095  234 SCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLM 297
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
963-1155 3.88e-25

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: 103.95  E-value: 3.88e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842    963 KEFQSVEEEMQSTvrehRDGGHAGGIFnrynILKIQKVCNKKLWERYTHRRKevseenhnHANERMLFHGSP--FVNAII 1040
Cdd:pfam00644    2 EEYQIIEKYFLST----HDPTHGYPLF----ILEIFRVQRDGEWERFQPKKK--------LRNRRLLWHGSRltNFLGIL 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   1041 HKGF--DERHAYIGG-MFGAGIYFAENSSKSNQYvygigggtgCPVHKDRScyicHRQLLFCRVTLGKSFLQFSAMKMAH 1117
Cdd:pfam00644   66 SQGLriAPPEAPVTGyMFGKGIYFADDASKSANY---------CPPSEAHG----NGLMLLSEVALGDMNELKKADYAEK 132
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13376842   1118 SPPGHHSV------------------TGRPSVNGLALA-----EYVIYRGEQAYPEYLITY 1155
Cdd:pfam00644  133 LPPGKHSVkglgktapesfvdldgvpLGKLVATGYDSSvllynEYVVYNVNQVRPKYLLEV 193
PHA03100 PHA03100
ankyrin repeat protein; Provisional
57-358 6.52e-25

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 108.98  E-value: 6.52e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842    57 RKSTPLHFAAGFGRKDVVEYLLQNGANVQARDDGGLIPLHNACSFGHA-----EVVNLLLRHGADPNARDNWNYTPLHEA 131
Cdd:PHA03100   34 KPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYA 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   132 AIKGKIDVCIV--LLQHGAeptirntdgrtaldladpsakavltgeykkdellesarsgneekmmalltplNVNCHASDG 209
Cdd:PHA03100  114 ISKKSNSYSIVeyLLDNGA----------------------------------------------------NVNIKNSDG 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   210 RksTPLHLAAGYNRV--KIVQLLLQHGADVHAKDKgdlvplhnacsyghyevTELLVKHGACVNAMDLWQFTPLHEAASK 287
Cdd:PHA03100  142 E--NLLHLYLESNKIdlKILKLLIDKGVDINAKNR-----------------VNYLLSYGVPINIKDVYGFTPLHYAVYN 202
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13376842   288 NRVEVCSLLLSYGADPTLLNCHNKSAIDLAPTPQLKERLAyefkghSLLQAAreADVTRIKKHLSLEMVNF 358
Cdd:PHA03100  203 NNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFK------LLLNNG--PSIKTIIETLLYFKDKD 265
PHA03095 PHA03095
ankyrin-like protein; Provisional
179-470 1.25e-24

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 108.96  E-value: 1.25e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   179 DELLESARSGNEEKMMALLTPLNVNChaSDGRKSTPLHLAAGYN---RVKIVQLLLQHGADVHAKDKGDLVPLH----NA 251
Cdd:PHA03095   17 DYLLNASNVTVEEVRRLLAAGADVNF--RGEYGKTPLHLYLHYSsekVKDIVRLLLEAGADVNAPERCGFTPLHlylyNA 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   252 CSYghyEVTELLVKHGACVNAMDLWQFTPLHE-AASKN-RVEVCSLLLSYGADPTLLNCHNKSAIdlaptpqlkerlaye 329
Cdd:PHA03095   95 TTL---DVIKLLIKAGADVNAKDKVGRTPLHVyLSGFNiNPKVIRLLLRKGADVNALDLYGMTPL--------------- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   330 fkgHSLLqaaREADVTrikkhlsLEMVNF-----KHPQT----HETALHCAAASPYPkRKQICELLLRKGANINEKTKEF 400
Cdd:PHA03095  157 ---AVLL---KSRNAN-------VELLRLlidagADVYAvddrFRSLLHHHLQSFKP-RARIVRELIRAGCDPAATDMLG 222
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13376842   401 LTPLHVAS--EKAHNDVVEVVVKHEAKVNALDNLGQTSLHRAAYCGHLQTCRLLLSYGCDPNIISLQGFTAL 470
Cdd:PHA03095  223 NTPLHSMAtgSSCKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPL 294
PHA02874 PHA02874
ankyrin repeat protein; Provisional
502-783 8.91e-24

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 105.82  E-value: 8.91e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   502 AGDVETVKKLCTVQSvNCRDIEGRQS-TPLHFAAGYNRVSVVEYLLQHGADVHAKDKGGLVPLHNACSYGHYEVAELLVK 580
Cdd:PHA02874   11 SGDIEAIEKIIKNKG-NCINISVDETtTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLID 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   581 HGA-----------------------VVNVADLWKFTPLHEAAAKGKYEICKLLLQHGADPTKKNRDGNTPLDL-VKDGD 636
Cdd:PHA02874   90 NGVdtsilpipciekdmiktildcgiDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIaIKHNF 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   637 TDIQDLLrgdaalldaAKKGCLARVKKlsspDNVNcrdtqgrhsTPLHLAAGYNNLEVAEYLLQHGADVNAQDKGGLIPL 716
Cdd:PHA02874  170 FDIIKLL---------LEKGAYANVKD----NNGE---------SPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPL 227
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13376842   717 HNAASYGHvDVAALLIKyNACVNATDKWAFTPLHEAAQKG-RTQLCALLLAHGADPTLKNQEGQTPLD 783
Cdd:PHA02874  228 HNAIIHNR-SAIELLIN-NASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPID 293
PHA03100 PHA03100
ankyrin repeat protein; Provisional
378-629 1.69e-23

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 104.75  E-value: 1.69e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   378 KRKQICELLLRKGANINEKTKEFLTPLHVASEKAHN-----DVVEVVVKHEAKVNALDNLGQTSLHRAAYC--GHLQTCR 450
Cdd:PHA03100   46 RNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVE 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   451 LLLSYGCDPNIISLQGFTALQMgnenvqqllqegislgnseadrqlleaakagdvetvkklctVQSVNCRDIEgrqstpl 530
Cdd:PHA03100  126 YLLDNGANVNIKNSDGENLLHL-----------------------------------------YLESNKIDLK------- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   531 hfaagynrvsVVEYLLQHGADVHAKDKgglvplhnacsyghyevAELLVKHGAVVNVADLWKFTPLHEAAAKGKYEICKL 610
Cdd:PHA03100  158 ----------ILKLLIDKGVDINAKNR-----------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKY 210
                         250
                  ....*....|....*....
gi 13376842   611 LLQHGADPTKKNRDGNTPL 629
Cdd:PHA03100  211 LLDLGANPNLVNKYGDTPL 229
PHA02876 PHA02876
ankyrin repeat protein; Provisional
259-652 2.47e-23

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 106.69  E-value: 2.47e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   259 VTELLVKHGACVNAMDLWQFTPLHEAASKNRVEVCSLLLSYGADPTLLNCHNKSAIDLAPTPQ--------LKERLAYEF 330
Cdd:PHA02876  160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKnidtikaiIDNRSNINK 239
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   331 KGHSLLQAAREADV-TRIKKHLSLEMVNfKHPQTHETALHCAAASPYPKRkqICELLLRKGANINEKTKEFLTPLHVASE 409
Cdd:PHA02876  240 NDLSLLKAIRNEDLeTSLLLYDAGFSVN-SIDDCKNTPLHHASQAPSLSR--LVPKLLERGADVNAKNIKGETPLYLMAK 316
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   410 KAHN-DVVEVVVKHEAKVNALDNLGQTSLHRAaycghlqtcrlllsygcdpniislqgfTALQMGNENVQQLLQEGislg 488
Cdd:PHA02876  317 NGYDtENIRTLIMLGADVNAADRLYITPLHQA---------------------------STLDRNKDIVITLLELG---- 365
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   489 nseadrqlleaakagdvetvkklctvQSVNCRDIegRQSTPLHFAAGYNRVSVVEYLLQHGADVHAKDKGGLVPLHNA-C 567
Cdd:PHA02876  366 --------------------------ANVNARDY--CDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlC 417
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   568 SYGHYEVAELLVKHGAVVNVADLWKFTPLHEAAAKG-KYEICKLLLQHGADPTKKNRDGNTPLDLVKDGDTDIQDLLRGD 646
Cdd:PHA02876  418 GTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIALEYHGIVNILLHYG 497

                  ....*.
gi 13376842   647 AALLDA 652
Cdd:PHA02876  498 AELRDS 503
PHA03095 PHA03095
ankyrin-like protein; Provisional
356-653 5.21e-23

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 103.95  E-value: 5.21e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   356 VNFKHPQThETALHCAAASPYPKRKQICELLLRKGANINEKTKEFLTPLHV-ASEKAHNDVVEVVVKHEAKVNALDNLGQ 434
Cdd:PHA03095   40 VNFRGEYG-KTPLHLYLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLyLYNATTLDVIKLLIKAGADVNAKDKVGR 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   435 TSLHraAYCG----HLQTCRLLLSYGCDPNIISLQGFTALqmgnenvqqllqeGISLGNSEAdrqlleaakagDVETVKK 510
Cdd:PHA03095  119 TPLH--VYLSgfniNPKVIRLLLRKGADVNALDLYGMTPL-------------AVLLKSRNA-----------NVELLRL 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   511 LCTVQS-VNCRDIEGRqsTPLHFAAGY--NRVSVVEYLLQHGADVHAKDKGGLVPLHNA---CSYGHYEVAELLVKhGAV 584
Cdd:PHA03095  173 LIDAGAdVYAVDDRFR--SLLHHHLQSfkPRARIVRELIRAGCDPAATDMLGNTPLHSMatgSSCKRSLVLPLLIA-GIS 249
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13376842   585 VNVADLWKFTPLHEAAAKGKYEICKLLLQHGADPTKKNRDGNTPLDLVkdgdtdiqdLLRGDAALLDAA 653
Cdd:PHA03095  250 INARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLM---------VRNNNGRAVRAA 309
ADP_ribosyl cd01341
ADP_ribosylating enzymes catalyze the transfer of ADP_ribose from NAD+ to substrates. ...
1028-1151 8.94e-23

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: 95.32  E-value: 8.94e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842 1028 MLFHGSPFVNAIIHKGFDERHAYIG-----GMFGAGIYFAENSSKSNQYVYGIGGGTGCPVHKDRSCyichrqllfCRVT 1102
Cdd:cd01341    1 FLFHGSPPGNVISILKLGLRPASYGvllngGMFGKGIYSAPNISKSNGYSVGCDGQHVFQNGKPKVC---------GREL 71
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13376842 1103 LGKSFLQFSAMKMAH-------------SPPGHHSVTGRPSV---NGLALAEYVIYRG-EQAYPEY 1151
Cdd:cd01341   72 CVFGFLTLGVMSGATeessrvlfprnfrGATGAEVVDLLVAMcrdALLLPREYIIFEPySQVSIRY 137
Ank_2 pfam12796
Ankyrin repeats (3 copies);
530-622 3.06e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.10  E-value: 3.06e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842    530 LHFAAGYNRVSVVEYLLQHGADVHAKDKGGLVPLHNACSYGHYEVAELLVKHGAVVNVADLWkfTPLHEAAAKGKYEICK 609
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGR--TALHYAARSGHLEIVK 78
                           90
                   ....*....|...
gi 13376842    610 LLLQHGADPTKKN 622
Cdd:pfam12796   79 LLLEKGADINVKD 91
PHA02878 PHA02878
ankyrin repeat protein; Provisional
401-778 7.52e-22

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 100.34  E-value: 7.52e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   401 LTPLHVASEKAHNDVVEVVVKHEAKVNALDNLGQTSLHRAayCGHlqtcrlllsygcdPNIISLQgftalqmgnenvqQL 480
Cdd:PHA02878   38 FIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHII--CKE-------------PNKLGMK-------------EM 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   481 LQEGISLGNSEADRQLLEAAKAGDVETVKKLCTVQSVNCRDIEGRQSTPLHFAAGYNrVSVVEYLLQHGADVHAKDK-GG 559
Cdd:PHA02878   90 IRSINKCSVFYTLVAIKDAFNNRNVEIFKIILTNRYKNIQTIDLVYIDKKSKDDIIE-AEITKLLLSYGADINMKDRhKG 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   560 LVPLHNACSYGHYEVAELLVKHGAVVNVADLWKFTPLHEAAAKGKYEICKLLLQHGADPTKKNRDGNTPLdlvkdgdtdi 639
Cdd:PHA02878  169 NTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPL---------- 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   640 qdllrgdaalldaakkgclarvkklsspdnvncrdtqgrhstplHLAAGY-NNLEVAEYLLQHGADVNAQDK-GGLIPLH 717
Cdd:PHA02878  239 --------------------------------------------HISVGYcKDYDILKLLLEHGVDVNAKSYiLGLTALH 274
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13376842   718 naASYGHVDVAALLIKYNACVNATDKWAFTPLHEAAQK------GRTQLCALLLAHGADPTLKNQEG 778
Cdd:PHA02878  275 --SSIKSERKLKLLLEYGADINSLNSYKLTPLSSAVKQylciniGRILISNICLLKRIKPDIKNSEG 339
Ank_2 pfam12796
Ankyrin repeats (3 copies);
683-775 1.15e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 90.56  E-value: 1.15e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842    683 LHLAAGYNNLEVAEYLLQHGADVNAQDKGGLIPLHNAASYGHVDVAALLIKYNACVNATDKWafTPLHEAAQKGRTQLCA 762
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGR--TALHYAARSGHLEIVK 78
                           90
                   ....*....|...
gi 13376842    763 LLLAHGADPTLKN 775
Cdd:pfam12796   79 LLLEKGADINVKD 91
PHA02878 PHA02878
ankyrin repeat protein; Provisional
529-785 2.91e-21

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 98.80  E-value: 2.91e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   529 PLHFAAGYNRVSVVEYLLQHGADVHAKDKGGLVPLHNAC-------------SYGHYEVAELLVKHGAVVNVADLWKFTP 595
Cdd:PHA02878   40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICkepnklgmkemirSINKCSVFYTLVAIKDAFNNRNVEIFKI 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   596 LHEAAAKGKY------------------EICKLLLQHGADPTKKNRD-GNTPLDLVKDG-DTDIQDLLrgdaalldaakk 655
Cdd:PHA02878  120 ILTNRYKNIQtidlvyidkkskddiieaEITKLLLSYGADINMKDRHkGNTALHYATENkDQRLTELL------------ 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   656 gcLARVKKLSSPDNVNcrdtqgrhSTPLHLAAGYNNLEVAEYLLQHGADVNAQDKGGLIPLHNAASY-GHVDVAALLIKY 734
Cdd:PHA02878  188 --LSYGANVNIPDKTN--------NSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEH 257
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 13376842   735 NACVNATDK-WAFTPLHEAAQKgrTQLCALLLAHGADPTLKNQEGQTPLDLV 785
Cdd:PHA02878  258 GVDVNAKSYiLGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSA 307
Ank_2 pfam12796
Ankyrin repeats (3 copies);
62-154 7.14e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 88.25  E-value: 7.14e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842     62 LHFAAGFGRKDVVEYLLQNGANVQARDDGGLIPLHNACSFGHAEVVNLLLRHgADPNARDNwNYTPLHEAAIKGKIDVCI 141
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78
                           90
                   ....*....|...
gi 13376842    142 VLLQHGAEPTIRN 154
Cdd:pfam12796   79 LLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
28-161 8.70e-21

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 94.25  E-value: 8.70e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   28 LFEACRNGDVERVKRLVtpEK---VNSRDTAGRksTPLHFAAGFGRKDVVEYLLQNGANVQARDDGGLIPLHNACSFGHA 104
Cdd:COG0666  157 LHLAAANGNLEIVKLLL--EAgadVNARDNDGE--TPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNL 232
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 13376842  105 EVVNLLLRHGADPNARDNWNYTPLHEAAIKGKIDVCIVLLQHGAEPTIRNTDGRTAL 161
Cdd:COG0666  233 EIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA02875 PHA02875
ankyrin repeat protein; Provisional
65-303 1.38e-20

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 95.83  E-value: 1.38e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842    65 AAGFGRKDVVEYLLQNGANVQARDDGGLIPLHNACSFGHAEVVNLLLRHGADPNARDNWNYTPLHEAAIKGKIdvcivll 144
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDV------- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   145 qhgaeptirntdgrtaldladpsaKAVltgeykkDELLESARSGNEekmmalltplnvnCHASDGrkSTPLHLAAGYNRV 224
Cdd:PHA02875   82 ------------------------KAV-------EELLDLGKFADD-------------VFYKDG--MTPLHLATILKKL 115
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13376842   225 KIVQLLLQHGADVHAKDKGDLVPLHNACSYGHYEVTELLVKHGACVNAMDLWQFTPLHEAASKNRVEVCSLLLSYGADP 303
Cdd:PHA02875  116 DIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANI 194
Ank_2 pfam12796
Ankyrin repeats (3 copies);
215-307 1.06e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 84.78  E-value: 1.06e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842    215 LHLAAGYNRVKIVQLLLQHGADVHAKDKGDLVPLHNACSYGHYEVTELLVKHgACVNaMDLWQFTPLHEAASKNRVEVCS 294
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVN-LKDNGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|...
gi 13376842    295 LLLSYGADPTLLN 307
Cdd:pfam12796   79 LLLEKGADINVKD 91
PHA02876 PHA02876
ankyrin repeat protein; Provisional
110-617 5.03e-19

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 92.82  E-value: 5.03e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   110 LLRHGADPNARDNWNYTPLHEAAIKGKIDVCIVLLQHGAEpTIRNTDGR------------TALDLA-----------DP 166
Cdd:PHA02876   27 LHKHGANQCENESIPFTAIHQALQLRQIDIVEEIIQQNPE-LIYITDHKchstlhticiipNVMDIVisltldcdiilDI 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   167 SAKAVLTGEYKKDE----LLESARSGNE-----------------------EKMMA-LLTPLNVNCHASDGRKSTPLHLA 218
Cdd:PHA02876  106 KYASIILNKHKLDEacihILKEAISGNDihydkinesieymklikeriqqdELLIAeMLLEGGADVNAKDIYCITPIHYA 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   219 AGYNRVKIVQLLLQHGADVHAKDKGDLVPLHNACSYGHYEVTELLVKHGACVNAMDLwqftPLHEAASKNRVEVCSLLLS 298
Cdd:PHA02876  186 AERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKNDL----SLLKAIRNEDLETSLLLYD 261
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   299 YGADPTLLN-CHNKSAIDLAPTPQLkERLAYEfkghsLLQAAREADVTRIKKhlslemvnfkhpqthETALHCAAASPYP 377
Cdd:PHA02876  262 AGFSVNSIDdCKNTPLHHASQAPSL-SRLVPK-----LLERGADVNAKNIKG---------------ETPLYLMAKNGYD 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   378 KRKqiCELLLRKGANINEKTKEFLTPLHVASEKAHN-DVVEVVVKHEAKVNALDNLGQTSLHRAAYCGHLQTCRLLLSYG 456
Cdd:PHA02876  321 TEN--IRTLIMLGADVNAADRLYITPLHQASTLDRNkDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYG 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   457 CDPNIISlqgftalqmgnenvqqllqegislgnseadrqlleaakagdvetvKKLCTVqsvncrdiegrqstpLHFA-AG 535
Cdd:PHA02876  399 ADIEALS---------------------------------------------QKIGTA---------------LHFAlCG 418
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   536 YNRVSVVEYLLQHGADVHAKDKGGLVPLHNACSYG-HYEVAELLVKHGAVVNVADLWKFTPLheAAAKGKYEICKLLLQH 614
Cdd:PHA02876  419 TNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPL--LIALEYHGIVNILLHY 496

                  ...
gi 13376842   615 GAD 617
Cdd:PHA02876  497 GAE 499
Ank_2 pfam12796
Ankyrin repeats (3 copies);
28-121 2.62e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.93  E-value: 2.62e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842     28 LFEACRNGDVERVKRLVTPEK-VNSRDTAGRksTPLHFAAGFGRKDVVEYLLQNgANVQARDDgGLIPLHNACSFGHAEV 106
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGAdANLQDKNGR--TALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEI 76
                           90
                   ....*....|....*
gi 13376842    107 VNLLLRHGADPNARD 121
Cdd:pfam12796   77 VKLLLEKGADINVKD 91
PHA02875 PHA02875
ankyrin repeat protein; Provisional
437-629 1.31e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 86.58  E-value: 1.31e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   437 LHRAAYC-----GHLQTCRLLLSYGCDPNIISLQGFTALQMG-----NENVQQLLQEGI--SLGNSEADRQLLEAAKAGD 504
Cdd:PHA02875    1 MDQVALCdailfGELDIARRLLDIGINPNFEIYDGISPIKLAmkfrdSEAIKLLMKHGAipDVKYPDIESELHDAVEEGD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   505 VETVKKLCTVQSVNCRDIEGRQSTPLHFAAGYNRVSVVEYLLQHGADVHAKDKGGLVPLHNACSYGHYEVAELLVKHGAV 584
Cdd:PHA02875   81 VKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKAC 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 13376842   585 VNVADLWKFTPLHEAAAKGKYEICKLLLQHGADPTKKNRDGNTPL 629
Cdd:PHA02875  161 LDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAA 205
Ank_2 pfam12796
Ankyrin repeats (3 copies);
437-556 2.82e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.85  E-value: 2.82e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842    437 LHRAAYCGHLQTCRLLLSYGCDPNIISLQGFTALQMgnenvqqllqegislgnseadrqlleAAKAGDVETVKKLCTVQS 516
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHL--------------------------AAKNGHLEIVKLLLEHAD 54
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 13376842    517 VNCRDiegRQSTPLHFAAGYNRVSVVEYLLQHGADVHAKD 556
Cdd:pfam12796   55 VNLKD---NGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA02875 PHA02875
ankyrin repeat protein; Provisional
561-771 4.79e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 85.04  E-value: 4.79e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   561 VPLHNACSYGHYEVAELLVKHGAVVNVADLWKFTPLHEAAAKGKYEICKLLLQHGADPTKKNRDGNTPL-DLVKDGDT-D 638
Cdd:PHA02875    4 VALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELhDAVEEGDVkA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   639 IQDLLRGDAALLDAA-KKGclarvkklsspdnvncrdtqgrhSTPLHLAAGYNNLEVAEYLLQHGADVNAQDKGGLIPLH 717
Cdd:PHA02875   84 VEELLDLGKFADDVFyKDG-----------------------MTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLH 140
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 13376842   718 NAASYGHVDVAALLIKYNACVNATDKWAFTPLHEAAQKGRTQLCALLLAHGADP 771
Cdd:PHA02875  141 LAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANI 194
TCCD_inducible_PARP_like cd01439
Poly(ADP-ribose) polymerases catalyse the covalent attachment of ADP-ribose units from NAD+ to ...
1028-1155 4.85e-17

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: 78.13  E-value: 4.85e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842 1028 MLFHG--SPFVNAIIHKGFDER-HAYIGGMFGAGIYFAENSSKSNQYVYGIGGGTGcpvhkdrscyicHRQLLFCRVTLG 1104
Cdd:cd01439    1 LLFHGtsADAVEAICRHGFDRRfCGKHGTMYGKGSYFAKNASYSHQYSKKSPKADG------------LKEMFLARVLTG 68
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13376842 1105 KsFLQFSAMKMA-------HSPPGHHSVTGR---PSVnglalaeYVIYRGEQAYPEYLITY 1155
Cdd:cd01439   69 D-YTQGHPGYRRpplkpsgVELDRYDSCVDNvsnPSI-------FVIFSDVQAYPEYLITY 121
PHA02878 PHA02878
ankyrin repeat protein; Provisional
348-632 7.64e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 84.93  E-value: 7.64e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   348 KKHLSLEMVNFKHPQTHETALHCAAASPY-----PKRKQICELLLRKGANINEKTKEFLTPLHVA-------------SE 409
Cdd:PHA02878   13 YETILKYIEYIDHTENYSTSASLIPFIPLhqaveARNLDVVKSLLTRGHNVNQPDHRDLTPLHIIckepnklgmkemiRS 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   410 KAHNDVVEVVVK-----HEAKVNALDNL-------GQTS----LHRAAYCGHLQT--CRLLLSYGCDPNIISL-QGFTAL 470
Cdd:PHA02878   93 INKCSVFYTLVAikdafNNRNVEIFKIIltnryknIQTIdlvyIDKKSKDDIIEAeiTKLLLSYGADINMKDRhKGNTAL 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   471 QMGNENVQQLLQEGIslgnseadrqLLEAAKagdvetvkklctvqsVNCRDIEgrQSTPLHFAAGYNRVSVVEYLLQHGA 550
Cdd:PHA02878  173 HYATENKDQRLTELL----------LSYGAN---------------VNIPDKT--NNSPLHHAVKHYNKPIVHILLENGA 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   551 DVHAKDKGGLVPLHNACSY-GHYEVAELLVKHGAVVNV-ADLWKFTPLHEAAAKGKyeICKLLLQHGADPTKKNRDGNTP 628
Cdd:PHA02878  226 STDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAkSYILGLTALHSSIKSER--KLKLLLEYGADINSLNSYKLTP 303

                  ....
gi 13376842   629 LDLV 632
Cdd:PHA02878  304 LSSA 307
PHA02874 PHA02874
ankyrin repeat protein; Provisional
247-676 1.29e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 83.86  E-value: 1.29e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   247 PLHNACSYGHYEVTELLVKHGACVNAMDLWQFTPLHEAASKNRVEVCSLLLSYGADPTLLnchnksaidlaPTPQLKERL 326
Cdd:PHA02874   38 PLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSIL-----------PIPCIEKDM 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   327 AyefkgHSLLQAAREadvtrikkhlslemVNFKHPQThETALHCAAASpypKRKQICELLLRKGANINEKTKEFLTPLHV 406
Cdd:PHA02874  107 I-----KTILDCGID--------------VNIKDAEL-KTFLHYAIKK---GDLESIKMLFEYGADVNIEDDNGCYPIHI 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   407 ASEKAHNDVVEVVVKHEAKVNALDNLGQTSLHRAAYCGHLQTCRLLLSYGCDPNIISLQGFTALQ---MGNENVQQLLqe 483
Cdd:PHA02874  164 AIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHnaiIHNRSAIELL-- 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   484 gisLGNSeadrqlleaakagdvetvkklctvqSVNCRDIEGrqSTPLHFAAGYN-RVSVVEYLLQHGADVHAKDKGGLVP 562
Cdd:PHA02874  242 ---INNA-------------------------SINDQDIDG--STPLHHAINPPcDIDIIDILLYHKADISIKDNKGENP 291
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   563 LHNACSY-GHYEVAELLVKHGAVVNVADLWKFTPLHEaaakgkyeicklllqhgadptKKNRDGNTPL-DLVKDGDTDIQ 640
Cdd:PHA02874  292 IDTAFKYiNKDPVIKDIIANAVLIKEADKLKDSDFLE---------------------HIEIKDNKEFsDFIKECNEEIE 350
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 13376842   641 DLLR----GDAALLDAakkgCLARVK------KLSSPDNVNCRDTQ 676
Cdd:PHA02874  351 DMKKtkcgCDKNIFDL----CLIRIKhkfdgnEDSIKDYLNCLDDN 392
Ank_2 pfam12796
Ankyrin repeats (3 copies);
596-709 1.81e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.54  E-value: 1.81e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842    596 LHEAAAKGKYEICKLLLQHGADPTKKNRDGNTPLDLvkdgdtdiqdllrgdaalldAAKKGCLARVKKLSSPDNVNCRDt 675
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHL--------------------AAKNGHLEIVKLLLEHADVNLKD- 59
                           90       100       110
                   ....*....|....*....|....*....|....
gi 13376842    676 qgRHSTPLHLAAGYNNLEVAEYLLQHGADVNAQD 709
Cdd:pfam12796   60 --NGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
72-289 3.95e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 82.32  E-value: 3.95e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842    72 DVVEYLLQNGAN-VQARDDGGLIPLHNACSFGHAEVVNLLLRHGADPNARDNWNYTPLHEAAIKGKIDVCIVLLQHGAE- 149
Cdd:PHA02874   15 EAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDt 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   150 -----PTIRNTDGRTALDladpSAKAVLTGEYKKDELLESARSGNEEKMMALLTPLNVNCHASDGRKSTPLHLAAGYNRV 224
Cdd:PHA02874   95 silpiPCIEKDMIKTILD----CGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFF 170
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13376842   225 KIVQLLLQHGADVHAKDKGDLVPLHNACSYGHYEVTELLVKHGACVNAMDLWQFTPLHEAASKNR 289
Cdd:PHA02874  171 DIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR 235
Ank_2 pfam12796
Ankyrin repeats (3 copies);
368-461 4.39e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 74.38  E-value: 4.39e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842    368 LHCAAASPYPkrkQICELLLRKGANINEKTKEFLTPLHVASEKAHNDVVEVVVKHeAKVNALDNlGQTSLHRAAYCGHLQ 447
Cdd:pfam12796    1 LHLAAKNGNL---ELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLE 75
                           90
                   ....*....|....
gi 13376842    448 TCRLLLSYGCDPNI 461
Cdd:pfam12796   76 IVKLLLEKGADINV 89
PHA02874 PHA02874
ankyrin repeat protein; Provisional
34-327 4.93e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 81.93  E-value: 4.93e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842    34 NGDVERVKRLVTPEKVNSRDTAGRKSTPLHFAAGFGRKDVVEYLLQNGANVQARDDGGLIPLHNACSFGHAEVVNLLLRH 113
Cdd:PHA02874   11 SGDIEAIEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDN 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   114 GADP-----------------------NARDNWNYTPLHEAAIKGKIDVCIVLLQHGAEPTIRNTDGRTALDLADPSaka 170
Cdd:PHA02874   91 GVDTsilpipciekdmiktildcgidvNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKH--- 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   171 vltgeykkdellesarsgNEEKMMALLTPLNVNCHASDGRKSTPLHLAAGYNRVKIVQLLLQHGADVHAKDKGDLVPLHN 250
Cdd:PHA02874  168 ------------------NFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHN 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   251 ACSYGHyEVTELLVKHgACVNAMDLWQFTPLHEAASKN-RVEVCSLLLSYGADPTLLNCHNKSAIDLA-----PTPQLKE 324
Cdd:PHA02874  230 AIIHNR-SAIELLINN-ASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTAfkyinKDPVIKD 307

                  ...
gi 13376842   325 RLA 327
Cdd:PHA02874  308 IIA 310
PHA02878 PHA02878
ankyrin repeat protein; Provisional
271-614 4.96e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 82.24  E-value: 4.96e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   271 NAMDLWQFTPLHEAASKNRVEVCSLLLSYGAD----------PTLLNCH--NKSAIDLAPTPQLKERLAYEFKGHSLLQA 338
Cdd:PHA02878   31 TSASLIPFIPLHQAVEARNLDVVKSLLTRGHNvnqpdhrdltPLHIICKepNKLGMKEMIRSINKCSVFYTLVAIKDAFN 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   339 AREADVTRIkkhlsLEMVNFKHPQTHETALHCAAASPYPKRKQICELLLRKGANINEKTKEFL-TPLHVASEKAHNDVVE 417
Cdd:PHA02878  111 NRNVEIFKI-----ILTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDRHKGnTALHYATENKDQRLTE 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   418 VVVKHEAKVNALDNLGQTSLHRAAYCGHLQTCRLLLSYGCDPNIISLQGftalqmgnenvqqllqegislgnseadrqll 497
Cdd:PHA02878  186 LLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCG------------------------------- 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   498 eaakagdvetvkklctvqsvncrdiegrqSTPLHFAAGY-NRVSVVEYLLQHGADVHAKDK-GGLVPLHnaCSYGHYEVA 575
Cdd:PHA02878  235 -----------------------------NTPLHISVGYcKDYDILKLLLEHGVDVNAKSYiLGLTALH--SSIKSERKL 283
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 13376842   576 ELLVKHGAVVNVADLWKFTPLHEAAAK-GKYEICKLLLQH 614
Cdd:PHA02878  284 KLLLEYGADINSLNSYKLTPLSSAVKQyLCINIGRILISN 323
Ank_2 pfam12796
Ankyrin repeats (3 copies);
95-241 8.11e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 73.61  E-value: 8.11e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842     95 LHNACSFGHAEVVNLLLRHGADPNARDNWNYTPLHEAAIKGKIDVCIVLLQHGaeptirntdgrtaldladpsakavltg 174
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA--------------------------- 53
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13376842    175 eykkdellesarsgneekmmalltplNVNChasDGRKSTPLHLAAGYNRVKIVQLLLQHGADVHAKD 241
Cdd:pfam12796   54 --------------------------DVNL---KDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA02878 PHA02878
ankyrin repeat protein; Provisional
214-501 1.47e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 81.08  E-value: 1.47e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   214 PLHLAAGYNRVKIVQLLLQHGADVHAKDKGDLVPLHNACSYGHYE-VTELLvkhgACVNAMDL-WQFTPLHEAASKNRVE 291
Cdd:PHA02878   40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLgMKEMI----RSINKCSVfYTLVAIKDAFNNRNVE 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   292 VCSLLLSYGADptllnchNKSAIDLAPTPQLKERLAYEFKGHSLLqAAREADVTRIKKHlslemvnfkhpqTHETALHCA 371
Cdd:PHA02878  116 IFKIILTNRYK-------NIQTIDLVYIDKKSKDDIIEAEITKLL-LSYGADINMKDRH------------KGNTALHYA 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   372 AASPypkRKQICELLLRKGANINEKTKEFLTPLHVASEKAHNDVVEVVVKHEAKVNALDNLGQTSLHRA-AYCGHLQTCR 450
Cdd:PHA02878  176 TENK---DQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILK 252
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 13376842   451 LLLSYGCDPNIIS-LQGFTALQMG--NENVQQLLQE---GISLGNSEADRQLLEAAK 501
Cdd:PHA02878  253 LLLEHGVDVNAKSyILGLTALHSSikSERKLKLLLEygaDINSLNSYKLTPLSSAVK 309
PHA02875 PHA02875
ankyrin repeat protein; Provisional
533-791 1.87e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 80.04  E-value: 1.87e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   533 AAGYNRVSVVEYLLQHGADVHAKDKGGLVPLHNACSYGHYEVAELLVKHGAVVNVADLWKFTPLHEAAAKGKYEICKLLL 612
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   613 QHGA---DPTKKnrDGNTPLDL-VKDGDTDIQDLLrgdaalldaakkgclarVKKLSSPDNVNCRDTqgrhsTPLHLAAG 688
Cdd:PHA02875   89 DLGKfadDVFYK--DGMTPLHLaTILKKLDIMKLL-----------------IARGADPDIPNTDKF-----SPLHLAVM 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   689 YNNLEVAEYLLQHGADVNAQDKGGLIPLHNAASYGHVDVAALLIKYNACVNATDKWA-FTPLHEAAQKGRTQLCALLLAH 767
Cdd:PHA02875  145 MGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKR 224
                         250       260
                  ....*....|....*....|....*...
gi 13376842   768 GADP----TLKNQEgQTPLDLVSADDVS 791
Cdd:PHA02875  225 GADCnimfMIEGEE-CTILDMICNMCTN 251
PHA02878 PHA02878
ankyrin repeat protein; Provisional
61-410 2.00e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 80.31  E-value: 2.00e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842    61 PLHFAAGFGRKDVVEYLLQNGANVQARDDGGLIPLHNACSFGHAEVVNLLLRhgaDPNARDNWN-YTPLHEAAIKGKIDV 139
Cdd:PHA02878   40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIR---SINKCSVFYtLVAIKDAFNNRNVEI 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   140 CIVLLqhgaeptIRNTDGRTALDLadpsakaVLTGEYKKDELLESarsgneeKMMALLTPLNVNCHASDGRK-STPLHLA 218
Cdd:PHA02878  117 FKIIL-------TNRYKNIQTIDL-------VYIDKKSKDDIIEA-------EITKLLLSYGADINMKDRHKgNTALHYA 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   219 AGYNRVKIVQLLLQHGADVHAKDKGDLVPLHNACSYGHYEVTELLVKHGACVNAMDLWQFTPLHEAASK-NRVEVCSLLL 297
Cdd:PHA02878  176 TENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLL 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   298 SYGADptllnchnksaidlaptpqlkerlayefkghsllqaareadvtrikkhlslemVNFKHPQTHETALHCAAASPyp 377
Cdd:PHA02878  256 EHGVD-----------------------------------------------------VNAKSYILGLTALHSSIKSE-- 280
                         330       340       350
                  ....*....|....*....|....*....|...
gi 13376842   378 krkQICELLLRKGANINEKTKEFLTPLHVASEK 410
Cdd:PHA02878  281 ---RKLKLLLEYGADINSLNSYKLTPLSSAVKQ 310
PHA03100 PHA03100
ankyrin repeat protein; Provisional
71-184 2.62e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 79.71  E-value: 2.62e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842    71 KDVVEYLLQNGANVQARDDGGLIPLHNACSFGHAEVVNLLLRHGADPNARDNWNYTPLHEAAIKGKIDVCIVLLQHGA-- 148
Cdd:PHA03100  172 KNRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPsi 251
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 13376842   149 ---EPTI-----RNTDGRTALDLADPSAKAVLT---GEYKKDELLES 184
Cdd:PHA03100  252 ktiIETLlyfkdKDLNTITKIKMLKKSIMYMFLldpGFYKNRKLIEN 298
PHA02878 PHA02878
ankyrin repeat protein; Provisional
30-298 1.89e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 77.23  E-value: 1.89e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842    30 EACRNGDVERVKRLVTPEKVNSRDTAGRKSTPLHFAAGFGRKdVVEYLLQNGANVQARD-DGGLIPLHNACSFGHAEVVN 108
Cdd:PHA02878  107 DAFNNRNVEIFKIILTNRYKNIQTIDLVYIDKKSKDDIIEAE-ITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTE 185
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   109 LLLRHGADPNARDNWNYTPLHEAAIKGKIDVCIVLLQHGAEPTIRNTDGrtaldladpsakavltgeykkdellesarsg 188
Cdd:PHA02878  186 LLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCG------------------------------- 234
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   189 neekmmalltplnvnchasdgrkSTPLHLAAGY-NRVKIVQLLLQHGADVHAKDK-GDLVPLHnaCSYGHYEVTELLVKH 266
Cdd:PHA02878  235 -----------------------NTPLHISVGYcKDYDILKLLLEHGVDVNAKSYiLGLTALH--SSIKSERKLKLLLEY 289
                         250       260       270
                  ....*....|....*....|....*....|...
gi 13376842   267 GACVNAMDLWQFTPLHEAASKNR-VEVCSLLLS 298
Cdd:PHA02878  290 GADINSLNSYKLTPLSSAVKQYLcINIGRILIS 322
PHA03100 PHA03100
ankyrin repeat protein; Provisional
678-785 7.35e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 75.09  E-value: 7.35e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   678 RHSTPLHLAAGYNNLEVAEYLLQHGADVNAQDKGGLIPLHNAASYGHV-----DVAALLIKYNACVNATDKWAFTPLHEA 752
Cdd:PHA03100   34 KPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYA 113
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 13376842   753 AQKGRTQ--LCALLLAHGADPTLKNQEGQTPLDLV 785
Cdd:PHA03100  114 ISKKSNSysIVEYLLDNGANVNIKNSDGENLLHLY 148
Ank_4 pfam13637
Ankyrin repeats (many copies);
679-732 2.28e-13

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 65.37  E-value: 2.28e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 13376842    679 HSTPLHLAAGYNNLEVAEYLLQHGADVNAQDKGGLIPLHNAASYGHVDVAALLI 732
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
59-269 2.76e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 73.76  E-value: 2.76e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842    59 STPLHFAAGFGRKDVVEYLLQNGANVQARDDGGLIPLHNACSFGHAEVVNLLLRHGADPNARDNWNYTPLHEAAIKGK-I 137
Cdd:PHA02878  169 NTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKdY 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   138 DVCIVLLQHGaeptirntdgrtaldlADPSAKAVLTGeykkdellesarsgneekmmalLTPLNVNCHASDgrkstplhl 217
Cdd:PHA02878  249 DILKLLLEHG----------------VDVNAKSYILG----------------------LTALHSSIKSER--------- 281
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 13376842   218 aagynrvkIVQLLLQHGADVHAKDKGDLVPLHNAC-SYGHYEVTELLVKHGAC 269
Cdd:PHA02878  282 --------KLKLLLEYGADINSLNSYKLTPLSSAVkQYLCINIGRILISNICL 326
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
877-934 6.36e-13

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 64.60  E-value: 6.36e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 13376842    877 SITQFVRNLGLEHLMDIFEREQIT-LDVLVEMGHKELKEIGINAYGHRHKLIKGVERLI 934
Cdd:pfam07647    8 SVADWLRSIGLEQYTDNFRDQGITgAELLLRLTLEDLKRLGITSVGHRRKILKKIQELK 66
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
522-755 1.32e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 72.21  E-value: 1.32e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   522 IEGRQSTPlhfaagYNRVSVVEYLLQHGADVHAKDKGGLV--------------PLHNACSYGHYEVAELLVKHGAVVNV 587
Cdd:PLN03192  480 IEAMQTRQ------EDNVVILKNFLQHHKELHDLNVGDLLgdnggehddpnmasNLLTVASTGNAALLEELLKAKLDPDI 553
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   588 ADLWKFTPLHEAAAKGkYEICKL-LLQHGADPTKKNRDGNTPL-DLVKDGDTDIQDLLRGDAALLDAAKKGCLarvkkls 665
Cdd:PLN03192  554 GDSKGRTPLHIAASKG-YEDCVLvLLKHACNVHIRDANGNTALwNAISAKHHKIFRILYHFASISDPHAAGDL------- 625
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   666 spdnvncrdtqgrhstpLHLAAGYNNLEVAEYLLQHGADVNAQDKGGLIPLHNAASYGHVDVAALLIKYNA---CVNATD 742
Cdd:PLN03192  626 -----------------LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGAdvdKANTDD 688
                         250
                  ....*....|...
gi 13376842   743 KWAFTPLHEAAQK 755
Cdd:PLN03192  689 DFSPTELRELLQK 701
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
79-281 2.18e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 71.44  E-value: 2.18e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842    79 QNGANVQARDDGGLIplhNACSFGHAEVVNLLLRHGADPNARDNWNYTPLHEAAIKGKIDVCIVLLQHGAEPTIRNTDGR 158
Cdd:PLN03192  516 NGGEHDDPNMASNLL---TVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGN 592
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   159 TALdladpsAKAVLTGEYKKDELL-ESARSGNEEKMMALLtplnvnChasdgrkstplhLAAGYNRVKIVQLLLQHGADV 237
Cdd:PLN03192  593 TAL------WNAISAKHHKIFRILyHFASISDPHAAGDLL------C------------TAAKRNDLTAMKELLKQGLNV 648
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 13376842   238 HAKDKGDLVPLHNACSYGHYEVTELLVKHGACVNAMDLWQ-FTPL 281
Cdd:PLN03192  649 DSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDDdFSPT 693
Ank_4 pfam13637
Ankyrin repeats (many copies);
59-111 2.78e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 62.29  E-value: 2.78e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 13376842     59 STPLHFAAGFGRKDVVEYLLQNGANVQARDDGGLIPLHNACSFGHAEVVNLLL 111
Cdd:pfam13637    2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
526-579 4.07e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 61.91  E-value: 4.07e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 13376842    526 QSTPLHFAAGYNRVSVVEYLLQHGADVHAKDKGGLVPLHNACSYGHYEVAELLV 579
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
877-932 9.99e-12

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: 61.10  E-value: 9.99e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 13376842  877 SITQFVRNLGLEHLMDIFEREQITLDVLVEMGHKELKEIGINAYGHRHKLIKGVER 932
Cdd:cd09487    1 DVAEWLESLGLEQYADLFRKNEIDGDALLLLTDEDLKELGITSPGHRKKILRAIQR 56
PHA02875 PHA02875
ankyrin repeat protein; Provisional
60-306 1.08e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 68.48  E-value: 1.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842    60 TPLHFAAGFGRKDVVEYLLQNGANVQARDDGGLIPLHNACSFGHAEVVNLLLRHGA---DPNARDnwNYTPLHEAAIKGK 136
Cdd:PHA02875   37 SPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKfadDVFYKD--GMTPLHLATILKK 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   137 IDVCIVLLQHGAEPTIRNTDgrtaldladpsakavltgeykkdellesarsgneekmmalltplnvnchasdgrKSTPLH 216
Cdd:PHA02875  115 LDIMKLLIARGADPDIPNTD------------------------------------------------------KFSPLH 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   217 LAAGYNRVKIVQLLLQHGADVHAKDKGDLVPLHNACSYGHYEVTELLVKHGACVNAMDL-WQFTPLHEAASKNRVEVCSL 295
Cdd:PHA02875  141 LAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKnGCVAALCYAIENNKIDIVRL 220
                         250
                  ....*....|.
gi 13376842   296 LLSYGADPTLL 306
Cdd:PHA02875  221 FIKRGADCNIM 231
PHA02798 PHA02798
ankyrin-like protein; Provisional
224-476 1.43e-11

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 68.32  E-value: 1.43e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   224 VKIVQLLLQHGADVHAKDKGDLVPL----HNACSYGH-YEVTELLVKHGACVNAMDLWQFTPLHEAASK---NRVEVCSL 295
Cdd:PHA02798   51 TDIVKLFINLGANVNGLDNEYSTPLctilSNIKDYKHmLDIVKILIENGADINKKNSDGETPLYCLLSNgyiNNLEILLF 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   296 LLSYGADPTLLNCHNKSAIDLaptpqlkerlayefkghsLLQAAREADVTRIKkhLSLEM---VNFKHPQTHETALHCAA 372
Cdd:PHA02798  131 MIENGADTTLLDKDGFTMLQV------------------YLQSNHHIDIEIIK--LLLEKgvdINTHNNKEKYDTLHCYF 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   373 ASPYPK-RKQICELLLRKGANINEKTK-------EFLTPLHVASEKAHNDVVEVVVKHeAKVNALDNLGQTSLHRAAYCG 444
Cdd:PHA02798  191 KYNIDRiDADILKLFVDNGFIINKENKshkkkfmEYLNSLLYDNKRFKKNILDFIFSY-IDINQVDELGFNPLYYSVSHN 269
                         250       260       270
                  ....*....|....*....|....*....|..
gi 13376842   445 HLQTCRLLLSYGCDPNIISLQGFTALQMGNEN 476
Cdd:PHA02798  270 NRKIFEYLLQLGGDINIITELGNTCLFTAFEN 301
PHA02878 PHA02878
ankyrin repeat protein; Provisional
189-472 2.93e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 67.21  E-value: 2.93e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   189 NEEKMMALLTpLNVNCHASDGRKSTPLHLAAGY-NRVKIVQLLLQHGADvhaKDKGDLVPLHNACSYGHYEVTE-LLVKH 266
Cdd:PHA02878   49 NLDVVKSLLT-RGHNVNQPDHRDLTPLHIICKEpNKLGMKEMIRSINKC---SVFYTLVAIKDAFNNRNVEIFKiILTNR 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   267 GACVNAMDLWQFTPLHEAASKNrVEVCSLLLSYGADPTLLNCHnksaidlaptpqlkerlayefKGHSLLQAAREADVTR 346
Cdd:PHA02878  125 YKNIQTIDLVYIDKKSKDDIIE-AEITKLLLSYGADINMKDRH---------------------KGNTALHYATENKDQR 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   347 IKKHLSLEMVNFKHP-QTHETALHCAAASpypKRKQICELLLRKGANINEKTKEFLTPLHVASEKAHN-DVVEVVVKHEA 424
Cdd:PHA02878  183 LTELLLSYGANVNIPdKTNNSPLHHAVKH---YNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDyDILKLLLEHGV 259
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 13376842   425 KVNALDN-LGQTSLHRAAYCGhlQTCRLLLSYGCDPNIISLQGFTALQM 472
Cdd:PHA02878  260 DVNAKSYiLGLTALHSSIKSE--RKLKLLLEYGADINSLNSYKLTPLSS 306
PHA02875 PHA02875
ankyrin repeat protein; Provisional
28-150 3.05e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 66.94  E-value: 3.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842    28 LFEACRNGDVERVKRLVTPEKVNSRDTAGRKSTPLHFAAGFGRKDVVEYLLQNGANVQARDDGGLIPLHNACSFGHAEVV 107
Cdd:PHA02875   72 LHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGI 151
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 13376842   108 NLLLRHGADPNARDNWNYTPLHEAAIKGKIDVCIVLLQHGAEP 150
Cdd:PHA02875  152 ELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANI 194
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
496-700 1.00e-10

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: 65.80  E-value: 1.00e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842  496 LLEAAKAGDVETVKKLCTVQSVncrDIEGRQS---TPLHFAAGYNRVSVVEYLLQHG---------ADVHAkdkgGLVPL 563
Cdd:cd22192   21 LLLAAKENDVQAIKKLLKCPSC---DLFQRGAlgeTALHVAALYDNLEAAVVLMEAApelvnepmtSDLYQ----GETAL 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842  564 HNACSYGHYEVAELLVKHGAVVNVA------------DLWKFT--PLHEAAAKGKYEICKLLLQHGADPTKKNRDGNTPL 629
Cdd:cd22192   94 HIAVVNQNLNLVRELIARGADVVSPratgtffrpgpkNLIYYGehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13376842  630 D-LV----KDGDTDIQDLLrgdaalldaakkgcLARVKklssPDNVNCRDTQGRHS--TPLHLAAGYNNLEVAEYLLQ 700
Cdd:cd22192  174 HiLVlqpnKTFACQMYDLI--------------LSYDK----EDDLQPLDLVPNNQglTPFKLAAKEGNIVMFQHLVQ 233
parp_like cd01437
Poly(ADP-ribose) polymerase (parp) catalytic domain catalyses the covalent attachment of ...
958-1128 1.18e-10

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: 64.60  E-value: 1.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842  958 LSPDDKEFQSVEEEMQSTvrehrdggHAGGIFNRYNILKIQKVCNKKLWERYTHRRKevseeNHNHaneRMLFHGSPFVN 1037
Cdd:cd01437  143 LDKDSEEYKIIEKYLKNT--------HAPTTEYTVEVQEIFRVEREGETDRFKPFKK-----LGNR---KLLWHGSRLTN 206
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842 1038 --AIIHKGF--DERHAYIGG-MFGAGIYFAENSSKSNQYVY-GIGGGTGCpvhkdrscyichrqLLFCRVTLGKSFLQFS 1111
Cdd:cd01437  207 fvGILSQGLriAPPEAPVTGyMFGKGIYFADMFSKSANYCHaSASDPTGL--------------LLLCEVALGKMNELKK 272
                        170
                 ....*....|....*...
gi 13376842 1112 AMKMAHSPP-GHHSVTGR 1128
Cdd:cd01437  273 ADYMAKELPkGKHSVKGL 290
Ank_4 pfam13637
Ankyrin repeats (many copies);
212-264 1.32e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 57.67  E-value: 1.32e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 13376842    212 STPLHLAAGYNRVKIVQLLLQHGADVHAKDKGDLVPLHNACSYGHYEVTELLV 264
Cdd:pfam13637    2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
574-788 1.55e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 65.47  E-value: 1.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   574 VAELLVKHGAVVNVADLWKFTPLHEAAAKGKYEICKLLLQHGADPTKKNRDGNTPLDLVKDGdtdiqdllrgdaalldaa 653
Cdd:PHA02876  160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDS------------------ 221
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   654 kkgclarvkklsspdnvncrdtqgrhstplhlaagyNNLEVAEYLLQHGADVNAQDkgglIPLHNAASYGHVDVAALLIK 733
Cdd:PHA02876  222 ------------------------------------KNIDTIKAIIDNRSNINKND----LSLLKAIRNEDLETSLLLYD 261
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 13376842   734 YNACVNATDKWAFTPLHEAAQK-GRTQLCALLLAHGADPTLKNQEGQTPLDLVSAD 788
Cdd:PHA02876  262 AGFSVNSIDDCKNTPLHHASQApSLSRLVPKLLERGADVNAKNIKGETPLYLMAKN 317
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
875-933 1.76e-10

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: 57.66  E-value: 1.76e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 13376842    875 DFSITQFVRNLGLEHLMDIFEREQITLDVLVEMGHKELKEIGINAYGHRHKLIKGVERL 933
Cdd:pfam00536    5 VEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRL 63
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
594-788 4.34e-10

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: 63.88  E-value: 4.34e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842  594 TPLHEAAAKGKYE-ICKLLLQHGADPTKKNRDGNTPLDLVKDGDTDiqdllrgDAA--LLDAAkkgclarvkklssPDNV 670
Cdd:cd22192   19 SPLLLAAKENDVQaIKKLLKCPSCDLFQRGALGETALHVAALYDNL-------EAAvvLMEAA-------------PELV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842  671 NCRDT----QGRhsTPLHLAAGYNNLEVAEYLLQHGADVNA---------QDKGGLI-----PLHNAASYGHVDVAALLI 732
Cdd:cd22192   79 NEPMTsdlyQGE--TALHIAVVNQNLNLVRELIARGADVVSpratgtffrPGPKNLIyygehPLSFAACVGNEEIVRLLI 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13376842  733 KYNACVNATDKWAFTPLH----EAAQKGRTQLCALLLAhgADP--------TLKNQEGQTPLDLVSAD 788
Cdd:cd22192  157 EHGADIRAQDSLGNTVLHilvlQPNKTFACQMYDLILS--YDKeddlqpldLVPNNQGLTPFKLAAKE 222
Ank_4 pfam13637
Ankyrin repeats (many copies);
247-297 9.82e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.36  E-value: 9.82e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 13376842    247 PLHNACSYGHYEVTELLVKHGACVNAMDLWQFTPLHEAASKNRVEVCSLLL 297
Cdd:pfam13637    4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
877-933 1.09e-09

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: 55.38  E-value: 1.09e-09
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 13376842     877 SITQFVRNLGLEHLMDIFEREQITLDVLVEMGHKE-LKEIGINAYGHRHKLIKGVERL 933
Cdd:smart00454    8 SVADWLESIGLEQYADNFRKNGIDGALLLLLTSEEdLKELGITKLGHRKKILKAIQKL 65
PHA02876 PHA02876
ankyrin repeat protein; Provisional
28-268 1.19e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 62.39  E-value: 1.19e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842    28 LFEACRNG-DVERVKRLVT-PEKVNSRDTAgrKSTPLHFAAGFGR-KDVVEYLLQNGANVqarddggliplhnacsfgha 104
Cdd:PHA02876  311 LYLMAKNGyDTENIRTLIMlGADVNAADRL--YITPLHQASTLDRnKDIVITLLELGANV-------------------- 368
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   105 evvnlllrhgadpNARDNWNYTPLHEAAIKGKIDVCIVLLQHGAEPTIRNTDGRTALDLAdpsakavLTGEykkdelles 184
Cdd:PHA02876  369 -------------NARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFA-------LCGT--------- 419
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   185 arsgNEEKMMALLTPLNVNCHASDGRKSTPLHLAAGYN-RVKIVQLLLQHGADVHAKDKGDLVPLHNACSYghYEVTELL 263
Cdd:PHA02876  420 ----NPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIALEY--HGIVNIL 493

                  ....*
gi 13376842   264 VKHGA 268
Cdd:PHA02876  494 LHYGA 498
Ank_5 pfam13857
Ankyrin repeats (many copies);
77-131 1.41e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 55.05  E-value: 1.41e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 13376842     77 LLQNG-ANVQARDDGGLIPLHNACSFGHAEVVNLLLRHGADPNARDNWNYTPLHEA 131
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
53-164 1.53e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 62.19  E-value: 1.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842    53 DTAGRksTPLHFAAGFGRKDVVEYLLQNGANVQARDDGGLIPLHNACSFGHAEVVNLL--LRHGADPNARDNWnytpLHE 130
Cdd:PLN03192  555 DSKGR--TPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILyhFASISDPHAAGDL----LCT 628
                          90       100       110
                  ....*....|....*....|....*....|....
gi 13376842   131 AAIKGKIDVCIVLLQHGAEPTIRNTDGRTALDLA 164
Cdd:PLN03192  629 AAKRNDLTAMKELLKQGLNVDSEDHQGATALQVA 662
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
102-167 1.80e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 61.84  E-value: 1.80e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13376842   102 GHAEVVNLLLRHGADPNARDNWNYTPLHEAAIKGKIDVCIVLLQHGAEPTIRNTDGRTALDLADPS 167
Cdd:PTZ00322   93 GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEEN 158
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
495-581 2.25e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 61.45  E-value: 2.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   495 QLLEAAKAGDVETVKKLCTVQS-VNCRDIEGRqsTPLHFAAGYNRVSVVEYLLQHGADVHAKDKGGLVPLHNACSYGHYE 573
Cdd:PTZ00322   85 ELCQLAASGDAVGARILLTGGAdPNCRDYDGR--TPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFRE 162

                  ....*...
gi 13376842   574 VAELLVKH 581
Cdd:PTZ00322  163 VVQLLSRH 170
PHA02946 PHA02946
ankyin-like protein; Provisional
74-248 2.89e-09

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 60.84  E-value: 2.89e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842    74 VEYLLQNGANVQARDDGGLIPLHNACSFGHAEVVNLLLRHGADPNARDNWNYTPLHeaAIKGKIDVCI----VLLQHGAE 149
Cdd:PHA02946   55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLY--YLSGTDDEVIerinLLVQYGAK 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   150 ptIRNTDGRTA----LDLADPSAK-----------AVLTGEYKKDELLESARSGN-EEKMMALLTPLNVNCHASDGRKST 213
Cdd:PHA02946  133 --INNSVDEEGcgplLACTDPSERvfkkimsigfeARIVDKFGKNHIHRHLMSDNpKASTISWMMKLGISPSKPDHDGNT 210
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 13376842   214 PLHLAAG--YNRVKIVQLLLQhGADVHAKDKGDLVPL 248
Cdd:PHA02946  211 PLHIVCSktVKNVDIINLLLP-STDVNKQNKFGDSPL 246
Ank_4 pfam13637
Ankyrin repeats (many copies);
562-612 2.94e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.82  E-value: 2.94e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 13376842    562 PLHNACSYGHYEVAELLVKHGAVVNVADLWKFTPLHEAAAKGKYEICKLLL 612
Cdd:pfam13637    4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
110-164 3.06e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 53.89  E-value: 3.06e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 13376842    110 LLRHG-ADPNARDNWNYTPLHEAAIKGKIDVCIVLLQHGAEPTIRNTDGRTALDLA 164
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
384-596 3.57e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 61.04  E-value: 3.57e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   384 ELLLRKGANINEKTKEFLTPLHVASEKAHNDVVEVVVKHEAKVNALDNLGQTSLHRAAYCGHLQTCRLLLSYGcdpniis 463
Cdd:PLN03192  542 EELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFA------- 614
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   464 lqgftalqmgnenvqqllqegiSLGNSEAdrqlleaakAGDVetvkkLCTvqsvncrdiegrqstplhfAAGYNRVSVVE 543
Cdd:PLN03192  615 ----------------------SISDPHA---------AGDL-----LCT-------------------AAKRNDLTAMK 639
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 13376842   544 YLLQHGADVHAKDKGGLVPLHNACSYGHYEVAELLVKHGAVVNVADLW-KFTPL 596
Cdd:PLN03192  640 ELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDdDFSPT 693
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
28-164 4.87e-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: 4.87e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   28 LFEACRNGDVERVKRLVT------------------------------------PEKVNSRDT----AGRksTPLHFAAG 67
Cdd:cd22192   21 LLLAAKENDVQAIKKLLKcpscdlfqrgalgetalhvaalydnleaavvlmeaaPELVNEPMTsdlyQGE--TALHIAVV 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   68 FGRKDVVEYLLQNGANVQ-ARDDG--------GLI-----PLHNACSFGHAEVVNLLLRHGADPNARDNWNYTPLHE-AA 132
Cdd:cd22192   99 NQNLNLVRELIARGADVVsPRATGtffrpgpkNLIyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHIlVL 178
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 13376842  133 IKGKIDVCIV---LLQHGAE------PTIRNTDGRTALDLA 164
Cdd:cd22192  179 QPNKTFACQMydlILSYDKEddlqplDLVPNNQGLTPFKLA 219
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
162-269 6.43e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 60.30  E-value: 6.43e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   162 DLADPSAKAVLTGEykkdeLLESARSGNEEKMMALLTP-LNVNCHASDGRksTPLHLAAGYNRVKIVQLLLQHGADVHAK 240
Cdd:PTZ00322   72 EVIDPVVAHMLTVE-----LCQLAASGDAVGARILLTGgADPNCRDYDGR--TPLHIACANGHVQVVRVLLEFGADPTLL 144
                          90       100
                  ....*....|....*....|....*....
gi 13376842   241 DKGDLVPLHNACSYGHYEVTELLVKHGAC 269
Cdd:PTZ00322  145 DKDGKTPLELAEENGFREVVQLLSRHSQC 173
PHA02875 PHA02875
ankyrin repeat protein; Provisional
244-470 6.48e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 59.62  E-value: 6.48e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   244 DLVPLHNACSYGHYEVTELLVKHGACVNAMDLWQFTPLHEAASKNRVEVCSLLLSYGADPTLlnchnksaidlaPTPQLK 323
Cdd:PHA02875    2 DQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDV------------KYPDIE 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   324 ERLAyefkghsllQAAREADVTRIKKHLSL-EMVNFKHPQTHETALHCAAASpypKRKQICELLLRKGANINEKTKEFLT 402
Cdd:PHA02875   70 SELH---------DAVEEGDVKAVEELLDLgKFADDVFYKDGMTPLHLATIL---KKLDIMKLLIARGADPDIPNTDKFS 137
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13376842   403 PLHVASEKAHNDVVEVVVKHEAKVNALDNLGQTSLHRAAYCGHLQTCRLLLSYGCDPNIISLQGFTAL 470
Cdd:PHA02875  138 PLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAA 205
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
571-784 9.31e-09

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: 59.71  E-value: 9.31e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842    571 HYEVAELLVKHGAVVNVADlwkfTPLHeAAAKGKYEICKLLLQHgadpTKKNRDGNTPLDLVKDGDTDiqDLLRGdaall 650
Cdd:TIGR00870   65 NLELTELLLNLSCRGAVGD----TLLH-AISLEYVDAVEAILLH----LLAAFRKSGPLELANDQYTS--EFTPG----- 128
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842    651 daakkgclarvkklsspdnvncrdtqgrhSTPLHLAAGYNNLEVAEYLLQHGADVNAQDKG--------------GLIPL 716
Cdd:TIGR00870  129 -----------------------------ITALHLAAHRQNYEIVKLLLERGASVPARACGdffvksqgvdsfyhGESPL 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842    717 HNAASYGHVDVAALLIKYNACVNATDKWAFTPLHEAA---------QKGRTQLCALLLAHGA--DPTLK-----NQEGQT 780
Cdd:TIGR00870  180 NAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVmenefkaeyEELSCQMYNFALSLLDklRDSKElevilNHQGLT 259

                   ....
gi 13376842    781 PLDL 784
Cdd:TIGR00870  260 PLKL 263
PHA02798 PHA02798
ankyrin-like protein; Provisional
72-306 9.66e-09

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 59.08  E-value: 9.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842    72 DVVEYLLQNGANVQARDDGGLIP----LHNACSFGHA-EVVNLLLRHGADPNARDNWNYTP----LHEAAIKGKiDVCIV 142
Cdd:PHA02798   52 DIVKLFINLGANVNGLDNEYSTPlctiLSNIKDYKHMlDIVKILIENGADINKKNSDGETPlyclLSNGYINNL-EILLF 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   143 LLQHGAEPTIRNTDGRTALDLadpsakAVLTGEYKKDELLEsarsgneekmMALLTPLNVNCHaSDGRKSTPLHLAAGYN 222
Cdd:PHA02798  131 MIENGADTTLLDKDGFTMLQV------YLQSNHHIDIEIIK----------LLLEKGVDINTH-NNKEKYDTLHCYFKYN 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   223 ----RVKIVQLLLQHGADVHAKDKGD-------LVPLHNACSYGHYEVTELLVKHgACVNAMDLWQFTPLHEAASKNRVE 291
Cdd:PHA02798  194 idriDADILKLFVDNGFIINKENKSHkkkfmeyLNSLLYDNKRFKKNILDFIFSY-IDINQVDELGFNPLYYSVSHNNRK 272
                         250
                  ....*....|....*
gi 13376842   292 VCSLLLSYGADPTLL 306
Cdd:PHA02798  273 IFEYLLQLGGDINII 287
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
74-149 1.04e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 59.53  E-value: 1.04e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13376842    74 VEYLLQNGANVQARDDGGLIPLHNACSFGHAEVVNLLLRHGADPNARDNWNYTPLHEAAIKGKIDVCIVLLQHGAE 149
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQC 173
Ank_5 pfam13857
Ankyrin repeats (many copies);
668-717 1.30e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 51.96  E-value: 1.30e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 13376842    668 DNVNCRDTQGRHSTPLHLAAGYNNLEVAEYLLQHGADVNAQDKGGLIPLH 717
Cdd:pfam13857    5 GPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
94-144 1.33e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.89  E-value: 1.33e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 13376842     94 PLHNACSFGHAEVVNLLLRHGADPNARDNWNYTPLHEAAIKGKIDVCIVLL 144
Cdd:pfam13637    4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
567-737 1.87e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 58.76  E-value: 1.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   567 CSYGHYEVAELLVKhGAVVNVADLWKFTPLHEAAAKgKYEICKLLLQHGADPTKKNRDGNTPLDLVKDGDTD--IQDLLR 644
Cdd:PTZ00322    6 CSVASSAFAAQLFF-GTEGSRKRRAKPISFERMAAI-QEEIARIDTHLEALEATENKDATPDHNLTTEEVIDpvVAHMLT 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   645 GDAALLDAAKKGCLARVKkLSSPDNVNCRDTQGRhsTPLHLAAGYNNLEVAEYLLQHGADVNAQDKGGLIPLHNAASYGH 724
Cdd:PTZ00322   84 VELCQLAASGDAVGARIL-LTGGADPNCRDYDGR--TPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGF 160
                         170
                  ....*....|...
gi 13376842   725 VDVAALLIKYNAC 737
Cdd:PTZ00322  161 REVVQLLSRHSQC 173
Ank_4 pfam13637
Ankyrin repeats (many copies);
715-765 3.17e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.12  E-value: 3.17e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 13376842    715 PLHNAASYGHVDVAALLIKYNACVNATDKWAFTPLHEAAQKGRTQLCALLL 765
Cdd:pfam13637    4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
684-767 4.03e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 57.60  E-value: 4.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   684 HLAAGYNNLEvAEYLLQHGADVNAQDKGGLIPLHNAASYGHVDVAALLIKYNACVNATDKWAFTPLHEAAQKGRTQLCAL 763
Cdd:PTZ00322   88 QLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166

                  ....
gi 13376842   764 LLAH 767
Cdd:PTZ00322  167 LSRH 170
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
717-817 4.87e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 57.22  E-value: 4.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   717 HNAASyGHVDVAALLIKYNACVNATDKWAFTPLHEAAQKGRTQLCALLLAHGADPTLKNQEGQTPLDLVSADD----VSA 792
Cdd:PTZ00322   88 QLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGfrevVQL 166
                          90       100
                  ....*....|....*....|....*
gi 13376842   793 LLTAAMPPSALPSCYKPQVLNGVRS 817
Cdd:PTZ00322  167 LSRHSQCHFELGANAKPDSFTGKPP 191
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
526-760 5.40e-08

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 56.94  E-value: 5.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842  526 QSTPLHFAAGYNRVSVVEYLL-QHGADVHAKDKGGLVPLHNACSYGHYEVAELLVKHG-AVVNVA---DLWK-FTPLHEA 599
Cdd:cd22192   17 SESPLLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAApELVNEPmtsDLYQgETALHIA 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842  600 AAKGKYEICKLLLQHGADPTKknrdgntpldlvkdgdtdiqdllrgdaalldaakkgclARVKKLSSPDNVNCRDTQGRH 679
Cdd:cd22192   97 VVNQNLNLVRELIARGADVVS--------------------------------------PRATGTFFRPGPKNLIYYGEH 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842  680 stPLHLAAGYNNLEVAEYLLQHGADVNAQDKGGLIPLHNAASYGHVDVAA----LLIKYNACVNA------TDKWAFTPL 749
Cdd:cd22192  139 --PLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTFACqmydLILSYDKEDDLqpldlvPNNQGLTPF 216
                        250
                 ....*....|.
gi 13376842  750 HEAAQKGRTQL 760
Cdd:cd22192  217 KLAAKEGNIVM 227
PHA02875 PHA02875
ankyrin repeat protein; Provisional
384-649 6.10e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 56.54  E-value: 6.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   384 ELLLRKGANINEKTKEFLTPLHVASEKAHNDVVEVVVKHEAKVN-ALDNLGQTSLHRAAYCGHLQTCRLLLSYGCDPNIi 462
Cdd:PHA02875   52 KLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDI- 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   463 slqgftalqmgnenvqqllqegislgnSEADRqlleaakagdvetvkklctvqsvncrdiegrqSTPLHFAAGYNRVSVV 542
Cdd:PHA02875  131 ---------------------------PNTDK--------------------------------FSPLHLAVMMGDIKGI 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   543 EYLLQHGADVHAKDKGGLVPLHNACSYGHYEVAELLVKHGAVVN-VADLWKFTPLHEAAAKGKYEICKLLLQHGADP--- 618
Cdd:PHA02875  152 ELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDyFGKNGCVAALCYAIENNKIDIVRLFIKRGADCnim 231
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 13376842   619 TKKNRDGNTPLDLVKDGDTDIQ----DLLRGDAAL 649
Cdd:PHA02875  232 FMIEGEECTILDMICNMCTNLEseaiDALIADIAI 266
Ank_4 pfam13637
Ankyrin repeats (many copies);
401-453 6.55e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.97  E-value: 6.55e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 13376842    401 LTPLHVASEKAHNDVVEVVVKHEAKVNALDNLGQTSLHRAAYCGHLQTCRLLL 453
Cdd:pfam13637    2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
516-564 7.38e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 50.04  E-value: 7.38e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 13376842    516 SVNCRDIEGRQSTPLHFAAGYNRVSVVEYLLQHGADVHAKDKGGLVPLH 564
Cdd:pfam13857    6 PIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
216-299 7.79e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.45  E-value: 7.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   216 HLAAGYNRVKIvQLLLQHGADVHAKDKGDLVPLHNACSYGHYEVTELLVKHGACVNAMDLWQFTPLHEAASKNRVEVCSL 295
Cdd:PTZ00322   88 QLAASGDAVGA-RILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166

                  ....
gi 13376842   296 LLSY 299
Cdd:PTZ00322  167 LSRH 170
Ank_2 pfam12796
Ankyrin repeats (3 copies);
335-430 8.55e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 50.88  E-value: 8.55e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842    335 LLQAAREADVTRIKKHLSLEMVNFKHPQTHETALHCAAASpypKRKQICELLLRKgANINEKTKEFlTPLHVASEKAHND 414
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKN---GHLEIVKLLLEH-ADVNLKDNGR-TALHYAARSGHLE 75
                           90
                   ....*....|....*.
gi 13376842    415 VVEVVVKHEAKVNALD 430
Cdd:pfam12796   76 IVKLLLEKGADINVKD 91
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
126-299 1.24e-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: 1.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842  126 TPLHEAAIKGKID-VCIVLLQHGAEPTIRNTDGRTALDLAdpsakaVLtgeYKKDE----LLESARsgneekmmallTPL 200
Cdd:cd22192   19 SPLLLAAKENDVQaIKKLLKCPSCDLFQRGALGETALHVA------AL---YDNLEaavvLMEAAP-----------ELV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842  201 NVNCHASDGRKSTPLHLAAGYNRVKIVQLLLQHGADVHA---------KDKGDLV-----PLHNACSYGHYEVTELLVKH 266
Cdd:cd22192   79 NEPMTSDLYQGETALHIAVVNQNLNLVRELIARGADVVSpratgtffrPGPKNLIyygehPLSFAACVGNEEIVRLLIEH 158
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 13376842  267 GACVNAMDLWQFTPLH---EAASKNRV-EVCSLLLSY 299
Cdd:cd22192  159 GADIRAQDSLGNTVLHilvLQPNKTFAcQMYDLILSY 195
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
60-172 1.75e-07

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: 55.47  E-value: 1.75e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842     60 TPLHFAAGFGRKDVVEYLLQNGANVQARDDG--------------GLIPLHNACSFGHAEVVNLLLRHGADPNARDNWNY 125
Cdd:TIGR00870  130 TALHLAAHRQNYEIVKLLLERGASVPARACGdffvksqgvdsfyhGESPLNAAACLGSPSIVALLSEDPADILTADSLGN 209
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13376842    126 TPLHEAAIKGKID------VCIV---LLQHGAEP-------TIRNTDGRTALDLADPSAKAVL 172
Cdd:TIGR00870  210 TLLHLLVMENEFKaeyeelSCQMynfALSLLDKLrdskeleVILNHQGLTPLKLAAKEGRIVL 272
PHA02798 PHA02798
ankyrin-like protein; Provisional
573-750 2.12e-07

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 54.84  E-value: 2.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   573 EVAELLVKHGAVVNVADLWKFTPLHEAAA-----KGKYEICKLLLQHGADPTKKNRDGNTPLdlvkdgdtdiqdllrgda 647
Cdd:PHA02798   52 DIVKLFINLGANVNGLDNEYSTPLCTILSnikdyKHMLDIVKILIENGADINKKNSDGETPL------------------ 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   648 alldaakkGCLarvkklsspdnvncrdtqgrhstplhLAAGY-NNLEVAEYLLQHGADVNAQDKGGLIPLHNAASYGH-- 724
Cdd:PHA02798  114 --------YCL--------------------------LSNGYiNNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHhi 159
                         170       180
                  ....*....|....*....|....*...
gi 13376842   725 -VDVAALLIKYNACVNATDKW-AFTPLH 750
Cdd:PHA02798  160 dIEIIKLLLEKGVDINTHNNKeKYDTLH 187
SAM_Ste50-like_fungal cd09533
SAM domain of Ste50_like (ubc2) subfamily; SAM (sterile alpha motif) domain of Ste50-like (or ...
880-933 2.55e-07

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: 48.47  E-value: 2.55e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 13376842  880 QFVRNLGLEHLMDIFEREQITLDVLVEMGHKELKEIGINAYGHRHKLIKGVERL 933
Cdd:cd09533    4 DWLSSLGLPQYEDQFIENGITGDVLVALDHEDLKEMGITSVGHRLTILKAVYEL 57
SAM_BOI-like_fungal cd09535
SAM domain of BOI-like fungal subfamily; SAM (sterile alpha motif) domain of BOI-like fungal ...
878-933 2.98e-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: 2.98e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 13376842  878 ITQFVRNLGLE-HLMDIFEREQITLDVLVEMGHKELKEIGINAYGHRHKLIKGVERL 933
Cdd:cd09535    8 VAEWLLSAGFDdSVCEKFRENEITGDILLELDLEDLKELDIGSFGKRFKLWNEIKSL 64
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
681-710 3.05e-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: 47.67  E-value: 3.05e-07
                           10        20        30
                   ....*....|....*....|....*....|.
gi 13376842    681 TPLHLAAG-YNNLEVAEYLLQHGADVNAQDK 710
Cdd:pfam00023    4 TPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
578-632 3.41e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.11  E-value: 3.41e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 13376842    578 LVKHGAV-VNVADLWKFTPLHEAAAKGKYEICKLLLQHGADPTKKNRDGNTPLDLV 632
Cdd:pfam13857    1 LLEHGPIdLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
698-752 4.99e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.73  E-value: 4.99e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 13376842    698 LLQHG-ADVNAQDKGGLIPLHNAASYGHVDVAALLIKYNACVNATDKWAFTPLHEA 752
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
531-614 5.22e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.13  E-value: 5.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   531 HFAAGYNRVSVvEYLLQHGADVHAKDKGGLVPLHNACSYGHYEVAELLVKHGAVVNVADLWKFTPLHEAAAKGKYEICKL 610
Cdd:PTZ00322   88 QLAASGDAVGA-RILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166

                  ....
gi 13376842   611 LLQH 614
Cdd:PTZ00322  167 LSRH 170
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
181-335 5.26e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 54.10  E-value: 5.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   181 LLESARSGN----EEKMMALLTPlnvncHASDGRKSTPLHLAAGYNRVKIVQLLLQHGADVHAKDKGDLVPLHNACSYGH 256
Cdd:PLN03192  529 LLTVASTGNaallEELLKAKLDP-----DIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKH 603
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   257 YEVTEL-------------------------------LVKHGACVNAMDLWQFTPLHEAASKNRVEVCSLLLSYGADPTL 305
Cdd:PLN03192  604 HKIFRIlyhfasisdphaagdllctaakrndltamkeLLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDK 683
                         170       180       190
                  ....*....|....*....|....*....|
gi 13376842   306 LNCHNksaiDLAPTpQLKERLAYEFKGHSL 335
Cdd:PLN03192  684 ANTDD----DFSPT-ELRELLQKRELGHSI 708
Ank_4 pfam13637
Ankyrin repeats (many copies);
594-630 6.06e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.27  E-value: 6.06e-07
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 13376842    594 TPLHEAAAKGKYEICKLLLQHGADPTKKNRDGNTPLD 630
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALH 39
Ank_5 pfam13857
Ankyrin repeats (many copies);
738-785 7.32e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.34  E-value: 7.32e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 13376842    738 VNATDKWAFTPLHEAAQKGRTQLCALLLAHGADPTLKNQEGQTPLDLV 785
Cdd:pfam13857    9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_2 pfam12796
Ankyrin repeats (3 copies);
281-396 8.07e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 48.19  E-value: 8.07e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842    281 LHEAASKNRVEVCSLLLSYGADPTLLNChnksaidlaptpqlkerlayefKGHSLLQAAREADVTRIKKHLsLEMVNFKH 360
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDK----------------------NGRTALHLAAKNGHLEIVKLL-LEHADVNL 57
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 13376842    361 PQTHETALHCAAASpypKRKQICELLLRKGANINEK 396
Cdd:pfam12796   58 KDNGRTALHYAARS---GHLEIVKLLLEKGADINVK 90
PHA02798 PHA02798
ankyrin-like protein; Provisional
539-782 9.10e-07

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 52.91  E-value: 9.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   539 VSVVEYLLQHGADVHAKDKGGLVPL----HNACSYGH-YEVAELLVKHGAVVNVADLWKFTPLHEAAAKG---KYEICKL 610
Cdd:PHA02798   51 TDIVKLFINLGANVNGLDNEYSTPLctilSNIKDYKHmLDIVKILIENGADINKKNSDGETPLYCLLSNGyinNLEILLF 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   611 LLQHGADPTKKNRDGNTPLDL-VKDG---DTDIQDLLrgdaalldaakkgclarvkkLSSPDNVNCRDTQGRHSTpLHLA 686
Cdd:PHA02798  131 MIENGADTTLLDKDGFTMLQVyLQSNhhiDIEIIKLL--------------------LEKGVDINTHNNKEKYDT-LHCY 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   687 AGYN----NLEVAEYLLQHGADVNAQDKGG-------LIPLHNAASYGHVDVAALLIKYnACVNATDKWAFTPLHEAAQK 755
Cdd:PHA02798  190 FKYNidriDADILKLFVDNGFIINKENKSHkkkfmeyLNSLLYDNKRFKKNILDFIFSY-IDINQVDELGFNPLYYSVSH 268
                         250       260
                  ....*....|....*....|....*..
gi 13376842   756 GRTQLCALLLAHGADPTLKNQEGQTPL 782
Cdd:PHA02798  269 NNRKIFEYLLQLGGDINIITELGNTCL 295
PHA03095 PHA03095
ankyrin-like protein; Provisional
60-171 1.06e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 52.72  E-value: 1.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842    60 TPLHFAAGFG--RKDVVEYLLQNGANVQARDDGGLIPLHNACSFGHAEVVNLLLRHGADPNARDNWNYTPLHEAAIKGki 137
Cdd:PHA03095  224 TPLHSMATGSscKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNN-- 301
                          90       100       110
                  ....*....|....*....|....*....|....
gi 13376842   138 DVCIVllqhgaeptirntdgRTALDLAdPSAKAV 171
Cdd:PHA03095  302 NGRAV---------------RAALAKN-PSAETV 319
SAM_BICC1 cd09520
SAM domain of BICC1 (bicaudal) subfamily; SAM (sterile alpha motif) domain of BICC1 (bicaudal) ...
877-927 1.22e-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: 46.90  E-value: 1.22e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 13376842  877 SITQFVRNLGLEHLMDIFEREQITLDVLVEMGHKELKEIGINAYGHRHKLI 927
Cdd:cd09520    6 DLPELLAKLGLEKYIDLFAQQEIDLQTFLTLTDQDLKELGITAFGARRKML 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
213-242 1.33e-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: 45.74  E-value: 1.33e-06
                           10        20        30
                   ....*....|....*....|....*....|.
gi 13376842    213 TPLHLAAG-YNRVKIVQLLLQHGADVHAKDK 242
Cdd:pfam00023    4 TPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
PHA02798 PHA02798
ankyrin-like protein; Provisional
446-706 1.39e-06

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 52.14  E-value: 1.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   446 LQTCRLLLSyGCDPNIISLQgFTALQmgnenvQQLLQEGISLGNSEADRQLLEAAKAGDVETVKKLCTVQSvNCRDiegr 525
Cdd:PHA02798   18 LSTVKLLIK-SCNPNEIVNE-YSIFQ------KYLQRDSPSTDIVKLFINLGANVNGLDNEYSTPLCTILS-NIKD---- 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   526 qstplhfaagYN-RVSVVEYLLQHGADVHAKDKGGLVPLHNACSYGHY---EVAELLVKHGAVVNVADLWKFTPLHEAAA 601
Cdd:PHA02798   85 ----------YKhMLDIVKILIENGADINKKNSDGETPLYCLLSNGYInnlEILLFMIENGADTTLLDKDGFTMLQVYLQ 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   602 KGKY---EICKLLLQHGAD-PTKKNRDGNTPLDL-----VKDGDTDIQDLLRGDAALLD----AAKKGCLA--------- 659
Cdd:PHA02798  155 SNHHidiEIIKLLLEKGVDiNTHNNKEKYDTLHCyfkynIDRIDADILKLFVDNGFIINkenkSHKKKFMEylnsllydn 234
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 13376842   660 -RVKK-----LSSPDNVNCRDTQGrhSTPLHLAAGYNNLEVAEYLLQHGADVN 706
Cdd:PHA02798  235 kRFKKnildfIFSYIDINQVDELG--FNPLYYSVSHNNRKIFEYLLQLGGDIN 285
Ank_5 pfam13857
Ankyrin repeats (many copies);
196-249 1.59e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.19  E-value: 1.59e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 13376842    196 LLTPLNVNCHASDGRKSTPLHLAAGYNRVKIVQLLLQHGADVHAKDKGDLVPLH 249
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
50-113 1.98e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.21  E-value: 1.98e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13376842    50 NSRDTAGRksTPLHFAAGFGRKDVVEYLLQNGANVQARDDGGLIPLHNACSFGHAEVVNLLLRH 113
Cdd:PTZ00322  109 NCRDYDGR--TPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
477-766 2.12e-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: 52.01  E-value: 2.12e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842    477 VQQLLQEGISLGNSEADR----QLLEAAKAGDVETVKKLctVQSVNCRDIEGRqsTPLHfAAGYNRVSVVEYLLQHGADV 552
Cdd:TIGR00870   33 VYRDLEEPKKLNINCPDRlgrsALFVAAIENENLELTEL--LLNLSCRGAVGD--TLLH-AISLEYVDAVEAILLHLLAA 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842    553 HAKdkGGLVPLHNACSYGHYEVAEllvkhgavvnvadlwkfTPLHEAAAKGKYEICKLLLQHGAD-PTKKNRDgntplDL 631
Cdd:TIGR00870  108 FRK--SGPLELANDQYTSEFTPGI-----------------TALHLAAHRQNYEIVKLLLERGASvPARACGD-----FF 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842    632 VKdgdTDIQDLLRgdaalldaakkgclarvkklsspdnvncrdtQGRHstPLHLAAGYNNLEVAEYLLQHGADVNAQDKG 711
Cdd:TIGR00870  164 VK---SQGVDSFY-------------------------------HGES--PLNAAACLGSPSIVALLSEDPADILTADSL 207
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13376842    712 GLIPLH-------NAASY------------GHVDVAALLIKYNACVNATDkwaFTPLHEAAQKGRTQLCALLLA 766
Cdd:TIGR00870  208 GNTLLHllvmeneFKAEYeelscqmynfalSLLDKLRDSKELEVILNHQG---LTPLKLAAKEGRIVLFRLKLA 278
Ank_5 pfam13857
Ankyrin repeats (many copies);
545-599 2.33e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.80  E-value: 2.33e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 13376842    545 LLQHG-ADVHAKDKGGLVPLHNACSYGHYEVAELLVKHGAVVNVADLWKFTPLHEA 599
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02859 PHA02859
ankyrin repeat protein; Provisional
503-629 3.61e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 49.05  E-value: 3.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   503 GDVETVKK-LCTVQSVNcrdieGRQSTPLH--FAAGYNRVSVVEYLLQHGADVHAKDKG-GLVPLHNACSYG---HYEVA 575
Cdd:PHA02859   32 DDIEGVKKwIKFVNDCN-----DLYETPIFscLEKDKVNVEILKFLIENGADVNFKTRDnNLSALHHYLSFNknvEPEIL 106
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 13376842   576 ELLVKHGAVVNVADLWKFTPLHE--AAAKGKYEICKLLLQHGADPTKKNRDGNTPL 629
Cdd:PHA02859  107 KILIDSGSSITEEDEDGKNLLHMymCNFNVRINVIKLLIDSGVSFLNKDFDNNNIL 162
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
528-557 5.09e-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: 44.20  E-value: 5.09e-06
                           10        20        30
                   ....*....|....*....|....*....|.
gi 13376842    528 TPLHFAAG-YNRVSVVEYLLQHGADVHAKDK 557
Cdd:pfam00023    4 TPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
PLN03123 PLN03123
poly [ADP-ribose] polymerase; Provisional
1025-1149 8.06e-06

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215590 [Multi-domain]  Cd Length: 981  Bit Score: 50.17  E-value: 8.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842  1025 NERMLFHGSPFVN--AIIHKGFdeRHA-----YIGGMFGAGIYFAENSSKSNQYvygigggtgcpvhkdrsCYICHRQ-- 1095
Cdd:PLN03123  825 NRMLLWHGSRLTNfvGILSQGL--RIAppeapATGYMFGKGVYFADLVSKSAQY-----------------CYTDRKNpv 885
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 13376842  1096 --LLFCRVTLGKSFLQFSAMKMAHSPPGHHSVTGRPSVNGLAlAEYVIYRGEQAYP 1149
Cdd:PLN03123  886 glMLLSEVALGEIYELKKAKYMDKPPRGKHSTKGLGKTVPQE-SEFVKWRDDVVVP 940
SAM_TAL cd09523
SAM domain of TAL subfamily; SAM (sterile alpha motif) domain of TAL (Tsg101-associated ligase) ...
873-933 1.09e-05

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: 44.20  E-value: 1.09e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13376842  873 GVDFSITQFVRNLGLEHLMDIFEREQITLDVLVEMGHKELKEIGINAYGHRHKLIKGVERL 933
Cdd:cd09523    3 GVDPQLVNLLNELSAEHYLPVFARHRITMETLSTMTDEDLKKIGIHEIGLRKEILRAAQEL 63
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
681-707 1.14e-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: 43.01  E-value: 1.14e-05
                           10        20
                   ....*....|....*....|....*..
gi 13376842    681 TPLHLAAGYNNLEVAEYLLQHGADVNA 707
Cdd:pfam13606    4 TPLHLAARNGRLEIVKLLLENGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
263-317 1.36e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.49  E-value: 1.36e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 13376842    263 LVKHGAC-VNAMDLWQFTPLHEAASKNRVEVCSLLLSYGADPTLLNCHNKSAIDLA 317
Cdd:pfam13857    1 LLEHGPIdLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
681-707 1.57e-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: 1.57e-05
                            10        20
                    ....*....|....*....|....*..
gi 13376842     681 TPLHLAAGYNNLEVAEYLLQHGADVNA 707
Cdd:smart00248    4 TPLHLAAENGNLEVVKLLLDKGADINA 30
SAM_ASZ1 cd09521
SAM domain of ASZ1 subfamily; SAM (sterile alpha motif) domain of ASZ1 (Ankyrin, SAM, leucine ...
881-933 1.57e-05

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: 43.81  E-value: 1.57e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 13376842  881 FVRNLGLEHLMDIFEREQITLDVLVEMGHKELKEIGINAYGHRHKLIKGVERL 933
Cdd:cd09521   11 FLHGLELGHLTPLFKEHDVTFSQLLKMTEEDLEKIGITQPGDQKKILDAIKEV 63
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
91-122 1.75e-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: 1.75e-05
                           10        20        30
                   ....*....|....*....|....*....|...
gi 13376842     91 GLIPLHNAC-SFGHAEVVNLLLRHGADPNARDN 122
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
Ank_4 pfam13637
Ankyrin repeats (many copies);
124-164 1.85e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.03  E-value: 1.85e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 13376842    124 NYTPLHEAAIKGKIDVCIVLLQHGAEPTIRNTDGRTALDLA 164
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFA 41
PHA02875 PHA02875
ankyrin repeat protein; Provisional
58-152 2.46e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 48.06  E-value: 2.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842    58 KSTPLHFAAGFGRKDVVEYLLQNGANVQARDDGGLIPLHNACSFGHAEVVNLLLRHGADPN-ARDNWNYTPLHEAAIKGK 136
Cdd:PHA02875  135 KFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDyFGKNGCVAALCYAIENNK 214
                          90
                  ....*....|....*.
gi 13376842   137 IDVCIVLLQHGAEPTI 152
Cdd:PHA02875  215 IDIVRLFIKRGADCNI 230
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
466-700 2.72e-05

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 48.34  E-value: 2.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842  466 GFTALQMGNENVQQLLQEGISLgnseadrqLLEAAKAGDV--ETVKKLCTvqsvnCRDIEGRqsTPLHFAAGYNRVSVVE 543
Cdd:cd21882   26 GKTCLHKAALNLNDGVNEAIML--------LLEAAPDSGNpkELVNAPCT-----DEFYQGQ--TALHIAIENRNLNLVR 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842  544 YLLQHGADVHAKDKGGLVPLH--NACSYGHYevaellvkhgavvnvadlwkftPLHEAAAKGKYEICKLLLQHGADP-TK 620
Cdd:cd21882   91 LLVENGADVSARATGRFFRKSpgNLFYFGEL----------------------PLSLAACTNQEEIVRLLLENGAQPaAL 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842  621 KNRD--GNTPLDLVkdgdTDIQDLLRGDAALLDAAKKGCL---ARVKKLSSPDNVNCRdtQGRhsTPLHLAAGYNNLEVA 695
Cdd:cd21882  149 EAQDslGNTVLHAL----VLQADNTPENSAFVCQMYNLLLsygAHLDPTQQLEEIPNH--QGL--TPLKLAAVEGKIVMF 220

                 ....*
gi 13376842  696 EYLLQ 700
Cdd:cd21882  221 QHILQ 225
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
458-631 2.78e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 48.33  E-value: 2.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   458 DPNIISlQGFTALQMGNEN-VQQLLQEGIS--LGNSEADRQLLEAAKAGDVETV----KKLCtvqSVNCRDIEGRQSTPL 530
Cdd:PLN03192  522 DPNMAS-NLLTVASTGNAAlLEELLKAKLDpdIGDSKGRTPLHIAASKGYEDCVlvllKHAC---NVHIRDANGNTALWN 597
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   531 HFAAGYNRVSVVEYLLQHGADVHAkdkGGLVpLHNACSYGHYEVAELLVKHGAVVNVADLWKFTPLHEAAAKGKYEICKL 610
Cdd:PLN03192  598 AISAKHHKIFRILYHFASISDPHA---AGDL-LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRL 673
                         170       180
                  ....*....|....*....|..
gi 13376842   611 LLQHGADPTKKNRDGN-TPLDL 631
Cdd:PLN03192  674 LIMNGADVDKANTDDDfSPTEL 695
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
213-301 2.79e-05

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 48.54  E-value: 2.79e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842    213 TPLHLAAGYNRVKIVQLLLQHGADVHAKDKGDLV---PLHNACSYGHY-----------EVTELLVKHGACVNAMDLWQF 278
Cdd:TIGR00870  130 TALHLAAHRQNYEIVKLLLERGASVPARACGDFFvksQGVDSFYHGESplnaaaclgspSIVALLSEDPADILTADSLGN 209
                           90       100       110
                   ....*....|....*....|....*....|..
gi 13376842    279 TPLH------EAASKNRVEVCS---LLLSYGA 301
Cdd:TIGR00870  210 TLLHllvmenEFKAEYEELSCQmynFALSLLD 241
Ank_5 pfam13857
Ankyrin repeats (many copies);
426-472 3.24e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.72  E-value: 3.24e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 13376842    426 VNALDNLGQTSLHRAAYCGHLQTCRLLLSYGCDPNIISLQGFTALQM 472
Cdd:pfam13857    9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
PHA02875 PHA02875
ankyrin repeat protein; Provisional
679-786 3.80e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 47.68  E-value: 3.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   679 HSTPLHLAAGYNNLEVAEYLLQHGADVNAQDKGGLIPLHNAASYGHVDVAALLIKYNACVNATDKWAFTPLHEAAQKGRT 758
Cdd:PHA02875    2 DQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDV 81
                          90       100       110
                  ....*....|....*....|....*....|
gi 13376842   759 QLCALLLAHG--ADPTLKnQEGQTPLDLVS 786
Cdd:PHA02875   82 KAVEELLDLGkfADDVFY-KDGMTPLHLAT 110
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
60-89 4.11e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 41.51  E-value: 4.11e-05
                           10        20        30
                   ....*....|....*....|....*....|.
gi 13376842     60 TPLHFAAG-FGRKDVVEYLLQNGANVQARDD 89
Cdd:pfam00023    4 TPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
43-96 4.22e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.33  E-value: 4.22e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 13376842     43 LVTPEKVNSRDTAGRKSTPLHFAAGFGRKDVVEYLLQNGANVQARDDGGLIPLH 96
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
213-239 4.23e-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: 41.47  E-value: 4.23e-05
                           10        20
                   ....*....|....*....|....*..
gi 13376842    213 TPLHLAAGYNRVKIVQLLLQHGADVHA 239
Cdd:pfam13606    4 TPLHLAARNGRLEIVKLLLENGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
435-481 4.30e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.26  E-value: 4.30e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 13376842    435 TSLHRAAYCGHLQTCRLLLSYGCDPNIISLQGFTALQM----GNENVQQLL 481
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFaasnGNVEVLKLL 53
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
262-317 4.33e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.59  E-value: 4.33e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 13376842   262 LLVKHGACVNAMDLWQFTPLHEAASKNRVEVCSLLLSYGADPTLLNCHNKSAIDLA 317
Cdd:PTZ00322  100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELA 155
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
632-784 4.50e-05

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: 47.49  E-value: 4.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842  632 VKDGDTDIQDLLrgdaalLDAAKKGclarvKKLSSPDNVNCRDTQGRHSTPLHLAAGYNNLEVAEYLLQHGADVNAQDKG 711
Cdd:cd22196   58 LHNGQNDTISLL------LDIAEKT-----GNLKEFVNAAYTDSYYKGQTALHIAIERRNMHLVELLVQNGADVHARASG 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842  712 --------------GLIPLHNAASYGHVDVAALLIK---YNACVNATDKWAFTPLH---EAAQ------KGRTQLCALLL 765
Cdd:cd22196  127 effkkkkggpgfyfGELPLSLAACTNQLDIVKFLLEnphSPADISARDSMGNTVLHalvEVADntpentKFVTKMYNEIL 206
                        170       180
                 ....*....|....*....|....*.
gi 13376842  766 AHGAD--PTLK-----NQEGQTPLDL 784
Cdd:cd22196  207 ILGAKirPLLKleeitNKKGLTPLKL 232
PHA02798 PHA02798
ankyrin-like protein; Provisional
376-553 4.93e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 47.14  E-value: 4.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   376 YPKRKQICELLLRKGANINEKTKEFLTPLH-VASEKAHN--DVVEVVVKHEAKVNALDNLGQTSLHRAAYCGH---LQTC 449
Cdd:PHA02798   85 YKHMLDIVKILIENGADINKKNSDGETPLYcLLSNGYINnlEILLFMIENGADTTLLDKDGFTMLQVYLQSNHhidIEII 164
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   450 RLLLSYGCDPNIIS-LQGFTALQMG--------NENVQQLLQEG---ISLGNSEADRQLLEA-------AKAGDVETVKK 510
Cdd:PHA02798  165 KLLLEKGVDINTHNnKEKYDTLHCYfkynidriDADILKLFVDNgfiINKENKSHKKKFMEYlnsllydNKRFKKNILDF 244
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 13376842   511 LCTVQSVNCRDIEGrqSTPLHFAAGYNRVSVVEYLLQHGADVH 553
Cdd:PHA02798  245 IFSYIDINQVDELG--FNPLYYSVSHNNRKIFEYLLQLGGDIN 285
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
528-554 6.20e-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: 41.09  E-value: 6.20e-05
                           10        20
                   ....*....|....*....|....*..
gi 13376842    528 TPLHFAAGYNRVSVVEYLLQHGADVHA 554
Cdd:pfam13606    4 TPLHLAARNGRLEIVKLLLENGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
496-546 6.43e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.49  E-value: 6.43e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 13376842    496 LLEAAKAGDVETVKKL-CTVQSVNCRDIEGRqsTPLHFAAGYNRVSVVEYLL 546
Cdd:pfam13637    5 LHAAAASGHLELLRLLlEKGADINAVDGNGE--TALHFAASNGNVEVLKLLL 54
SAM_Ste11_fungal cd09534
SAM domain of Ste11_fungal subfamily; SAM (sterile alpha motif) domain of Ste11 subfamily is a ...
877-933 6.72e-05

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: 41.81  E-value: 6.72e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 13376842  877 SITQFVRNLGLEHLMDIFEREQITLDVLVEMGHKELKEIGINAYGHRHKLIKGVERL 933
Cdd:cd09534    5 FVEEWLNELNCGQYLDIFEKNLITGDLLLELDKEALKELGITKVGDRIRLLRAIKSL 61
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
60-172 6.97e-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: 6.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   60 TPLHFAAGFGRKDVVEYLLQNGANVQARDDG-------------GLIPLHNACSFGHAEVVNLLLRHGADP---NARDNW 123
Cdd:cd21882   75 TALHIAIENRNLNLVRLLVENGADVSARATGrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQPaalEAQDSL 154
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13376842  124 NYTPLH---EAAIKGKIDVCIV------LLQHGA--EPT-----IRNTDGRTALDLADPSAKAVL 172
Cdd:cd21882  155 GNTVLHalvLQADNTPENSAFVcqmynlLLSYGAhlDPTqqleeIPNHQGLTPLKLAAVEGKIVM 219
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
593-623 7.20e-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: 40.74  E-value: 7.20e-05
                           10        20        30
                   ....*....|....*....|....*....|..
gi 13376842    593 FTPLHEAAAK-GKYEICKLLLQHGADPTKKNR 623
Cdd:pfam00023    3 NTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
416-492 7.29e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.82  E-value: 7.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   416 VEVVVKHEAKVNALDNLGQTSLHRAAYCGHLQTCRLLLSYGCDPNIISLQGFTALQMGNEN-----VQQLLQEGISLGNS 490
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENgfrevVQLLSRHSQCHFEL 177

                  ..
gi 13376842   491 EA 492
Cdd:PTZ00322  178 GA 179
PHA02876 PHA02876
ankyrin repeat protein; Provisional
727-793 7.40e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.98  E-value: 7.40e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13376842   727 VAALLIKYNACVNATDKWAFTPLHEAAQKGRTQLCALLLAHGADptlknqegqtpLDLVSADDVSAL 793
Cdd:PHA02876  160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGAD-----------VNIIALDDLSVL 215
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
157-278 9.14e-05

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: 46.72  E-value: 9.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842  157 GRTALdladpsAKAVLTGEYKKDE----LLESARSGNEEKMMalltplnVNCHASDG--RKSTPLHLAAGYNRVKIVQLL 230
Cdd:cd22196   47 GKTCL------LKAMLNLHNGQNDtislLLDIAEKTGNLKEF-------VNAAYTDSyyKGQTALHIAIERRNMHLVELL 113
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 13376842  231 LQHGADVHAKDKGDLVPLhNACSYGHYeVTELLVKHGACVNAMDLWQF 278
Cdd:cd22196  114 VQNGADVHARASGEFFKK-KKGGPGFY-FGELPLSLAACTNQLDIVKF 159
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
91-119 9.45e-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: 40.65  E-value: 9.45e-05
                            10        20
                    ....*....|....*....|....*....
gi 13376842      91 GLIPLHNACSFGHAEVVNLLLRHGADPNA 119
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
SAM_sec23ip-like cd09516
SAM domain of sec23ip-like subfamily; SAM (sterile alpha motif) domain of Sec23ip-like (Sec23 ...
864-927 1.26e-04

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: 41.24  E-value: 1.26e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13376842  864 SSLEKKEVPGVDFSITQfvrnLGLEHLMDIFEREQITLDVLVEMGHKELKEIGInAYGHRHKLI 927
Cdd:cd09516    2 SVEEQEEPLTLEEDLEK----LGLSEYFDTFEKEKIDMESLLLCSESDLKEMGI-PMGPRKKLL 60
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
105-308 1.28e-04

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 46.06  E-value: 1.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   105 EVVNLLLRHGADPNARDNWNYTPLHEAAIKGKIDVCIV--LLQHGAEPTIRNTDGRTaldladpsakAVLTgeykkdeLL 182
Cdd:PHA02716  193 DILEWLCNNGVNVNLQNNHLITPLHTYLITGNVCASVIkkIIELGGDMDMKCVNGMS----------PIMT-------YI 255
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   183 ESARSGNEEkmmalLTPLNVNCHASDGRKSTP--LHL---AAGYNRVKIVQLLLQHGADVHAKDKGDLVPLHNAC--SYG 255
Cdd:PHA02716  256 INIDNINPE-----ITNIYIESLDGNKVKNIPmiLHSyitLARNIDISVVYSFLQPGVKLHYKDSAGRTCLHQYIlrHNI 330
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13376842   256 HYEVTELLVKHGACVNAMDLWQFTPLH--------------EAASKNRVEVCSLLLSYGADPTLLNC 308
Cdd:PHA02716  331 STDIIKLLHEYGNDLNEPDNIGNTVLHtylsmlsvvnildpETDNDIRLDVIQCLISLGADITAVNC 397
Ank_4 pfam13637
Ankyrin repeats (many copies);
648-699 1.59e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 40.34  E-value: 1.59e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 13376842    648 ALLDAAKKGCLARVKKL-SSPDNVNCRDTQGRhsTPLHLAAGYNNLEVAEYLL 699
Cdd:pfam13637    4 ALHAAAASGHLELLRLLlEKGADINAVDGNGE--TALHFAASNGNVEVLKLLL 54
PHA02859 PHA02859
ankyrin repeat protein; Provisional
679-750 1.66e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 44.04  E-value: 1.66e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13376842   679 HSTPLH--LAAGYNNLEVAEYLLQHGADVNAQDKG-GLIPLHNAASYG---HVDVAALLIKYNACVNATDKWAFTPLH 750
Cdd:PHA02859   51 YETPIFscLEKDKVNVEILKFLIENGADVNFKTRDnNLSALHHYLSFNknvEPEILKILIDSGSSITEEDEDGKNLLH 128
PHA02946 PHA02946
ankyin-like protein; Provisional
380-568 1.93e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 45.43  E-value: 1.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   380 KQICELLLRKGANINEKTKEFLTPLHVASEKAHNDVVEVVVKHEAKVNALDNLGQTSLHRAAycghlqtcrlllsyGCDP 459
Cdd:PHA02946   52 ERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLS--------------GTDD 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   460 NIIslqgftalqmgnENVQQLLQEGISLGNS--EADRQLLEAAKAGDVETVKKLCTVQ-SVNCRDIEGRQSTPLHFAAGY 536
Cdd:PHA02946  118 EVI------------ERINLLVQYGAKINNSvdEEGCGPLLACTDPSERVFKKIMSIGfEARIVDKFGKNHIHRHLMSDN 185
                         170       180       190
                  ....*....|....*....|....*....|..
gi 13376842   537 NRVSVVEYLLQHGADVHAKDKGGLVPLHNACS 568
Cdd:PHA02946  186 PKASTISWMMKLGISPSKPDHDGNTPLHIVCS 217
Ank_5 pfam13857
Ankyrin repeats (many copies);
385-440 1.99e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.41  E-value: 1.99e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 13376842    385 LLLRKGANINEKTKEFLTPLHVASEKAHNDVVEVVVKHEAKVNALDNLGQTSLHRA 440
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
230-284 2.36e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.02  E-value: 2.36e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 13376842    230 LLQHG-ADVHAKDKGDLVPLHNACSYGHYEVTELLVKHGACVNAMDLWQFTPLHEA 284
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
213-239 2.42e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.49  E-value: 2.42e-04
                            10        20
                    ....*....|....*....|....*..
gi 13376842     213 TPLHLAAGYNRVKIVQLLLQHGADVHA 239
Cdd:smart00248    4 TPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02743 PHA02743
Viral ankyrin protein; Provisional
521-616 2.66e-04

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 42.88  E-value: 2.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   521 DIEGRQSTplHFAAGYNRVSVV---EYLLQHGADVHAKDKG-GLVPLHNACSYGHYEVAELLVKH-GAVVNVADLWKFTP 595
Cdd:PHA02743   54 DHHGRQCT--HMVAWYDRANAVmkiELLVNMGADINARELGtGNTLLHIAASTKNYELAEWLCRQlGVNLGAINYQHETA 131
                          90       100
                  ....*....|....*....|.
gi 13376842   596 LHEAAAKGKYEICKLLLQHGA 616
Cdd:PHA02743  132 YHIAYKMRDRRMMEILRANGA 152
SAM_ANKS3 cd09519
SAM domain of ANKS3 subfamily; SAM (sterile alpha motif) domain of ANKS3 subfamily is a ...
878-935 2.67e-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: 40.17  E-value: 2.67e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 13376842  878 ITQFVRNLGLEHLMDIFEREQITLDVLVEMGHKELKEIGINAYGHRHKLIKGVERLIS 935
Cdd:cd09519    7 LSELLEQIGCSKYLPIFEEQDIDLRIFLTLTESDLKEIGITLFGPKRKMTSAIARWHS 64
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
153-305 2.88e-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: 44.87  E-value: 2.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842  153 RNTDGRTALdladpsAKAVLTGEYKKDE----LLESARSGNEEKMMAlltplNVNCHASDGRKSTPLHLAAGYNRVKIVQ 228
Cdd:cd21882   22 RGATGKTCL------HKAALNLNDGVNEaimlLLEAAPDSGNPKELV-----NAPCTDEFYQGQTALHIAIENRNLNLVR 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842  229 LLLQHGADVHAKDKGDL-------------VPLHNACSYGHYEVTELLVKHG---ACVNAMDLWQFTPLH---EAASK-- 287
Cdd:cd21882   91 LLVENGADVSARATGRFfrkspgnlfyfgeLPLSLAACTNQEEIVRLLLENGaqpAALEAQDSLGNTVLHalvLQADNtp 170
                        170       180
                 ....*....|....*....|....
gi 13376842  288 -NRVEVCS---LLLSYGA--DPTL 305
Cdd:cd21882  171 eNSAFVCQmynLLLSYGAhlDPTQ 194
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
593-620 2.92e-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: 2.92e-04
                            10        20
                    ....*....|....*....|....*...
gi 13376842     593 FTPLHEAAAKGKYEICKLLLQHGADPTK 620
Cdd:smart00248    3 RTPLHLAAENGNLEVVKLLLDKGADINA 30
SAM_Arap1,2,3 cd09490
SAM domain of Arap1,2,3 (angiotensin receptor-associated protein); SAM (sterile alpha motif) ...
873-932 3.35e-04

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: 39.97  E-value: 3.35e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13376842  873 GVDFSITQFVRNLGLEHLMDIFEREQ-ITLDVLVEMGHKELKEIGINAYGHRHKLIKGVER 932
Cdd:cd09490    1 EADLDIAEWLASIHLEQYLDLFREHGyVTATDCQGINDSRLKQIGISPTGHRRRILKQLPI 61
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
212-302 3.72e-04

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: 44.62  E-value: 3.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842  212 STPLHLAAGYNRVKIVQ-LLLQHGADVHAKDKGDLVPLHNACSYGHYEVTELLVKhgaCV-----NAM--DLWQ-FTPLH 282
Cdd:cd22192   18 ESPLLLAAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME---AApelvnEPMtsDLYQgETALH 94
                         90       100
                 ....*....|....*....|
gi 13376842  283 EAASKNRVEVCSLLLSYGAD 302
Cdd:cd22192   95 IAVVNQNLNLVRELIARGAD 114
PHA02946 PHA02946
ankyin-like protein; Provisional
188-271 3.75e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 44.27  E-value: 3.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   188 GNEEKMMALLTPLNVNCHASDGRKSTPLHLAAGYNRVKIVQLLLQHGADVHAKDKGDLVPLHnACSYGHYEVTE---LLV 264
Cdd:PHA02946   49 GLDERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLY-YLSGTDDEVIErinLLV 127

                  ....*..
gi 13376842   265 KHGACVN 271
Cdd:PHA02946  128 QYGAKIN 134
Ank_4 pfam13637
Ankyrin repeats (many copies);
747-793 3.89e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.57  E-value: 3.89e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 13376842    747 TPLHEAAQKGRTQLCALLLAHGADPTLKNQEGQTPLDL-VSADDVSAL 793
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFaASNGNVEVL 50
PLN03124 PLN03124
poly [ADP-ribose] polymerase; Provisional
955-1153 4.66e-04

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215591 [Multi-domain]  Cd Length: 643  Bit Score: 44.44  E-value: 4.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   955 LIDLSPDDKEFQSVEEEMQSTvrehRDGGHAGGIFNRYNILKIQKvcnkklwERYTHRRKEVSEeNHNhaneRML-FHGS 1033
Cdd:PLN03124  430 LEPLDTDSEEFSMIAKYLENT----HGQTHSGYTLEIVQIFKVSR-------EGEDERFQKFSS-TKN----RMLlWHGS 493
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842  1034 PFVN--AIIHKGFdeRHA-----YIGGMFGAGIYFAENSSKSNQYVYgigGGTGCPVHkdrscyichrQLLFCRVTLGK- 1105
Cdd:PLN03124  494 RLTNwtGILSQGL--RIAppeapSTGYMFGKGVYFADMFSKSANYCY---ASAANPDG----------VLLLCEVALGDm 558
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13376842  1106 -SFLQFS--AMKMahsPPGHHSVTG---------------------------RPSVNG-LALAEYVIYRGEQAYPEYLI 1153
Cdd:PLN03124  559 nELLQADynANKL---PPGKLSTKGvgrtvpdpseaktledgvvvplgkpveSPYSKGsLEYNEYIVYNVDQIRMRYVL 634
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
49-186 5.57e-04

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: 44.02  E-value: 5.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   49 VNS--RDTAGRKSTPLHFAAGFGRKDVVEYLLQNGANVQARDDG--------------GLIPLHNACSFGHAEVVNLLLR 112
Cdd:cd22193   65 INAeyTDEYYEGQTALHIAIERRQGDIVALLVENGADVHAHAKGrffqpkyqgegfyfGELPLSLAACTNQPDIVQYLLE 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842  113 HG---ADPNARDNWNYTPLH---EAAIKGKIDVCIV------LLQHGAE-------PTIRNTDGRTALDLADPSAKA--- 170
Cdd:cd22193  145 NEhqpADIEAQDSRGNTVLHalvTVADNTKENTKFVtrmydmILIRGAKlcptvelEEIRNNDGLTPLQLAAKMGKIeil 224
                        170
                 ....*....|....*...
gi 13376842  171 --VLTGEYKKDELLESAR 186
Cdd:cd22193  225 kyILQREIKEPELRHLSR 242
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
94-119 5.82e-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: 5.82e-04
                           10        20
                   ....*....|....*....|....*.
gi 13376842     94 PLHNACSFGHAEVVNLLLRHGADPNA 119
Cdd:pfam13606    5 PLHLAARNGRLEIVKLLLENGADINA 30
SAM_ANKS6 cd09518
SAM domain of ANKS6 (or SamCystin) subfamily; SAM (sterile alpha motif) domain of ANKS6 (or ...
878-933 5.93e-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: 5.93e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 13376842  878 ITQFVRNLGLEHLMDIFEREQITLDVLVEMGHKELKEIGINAYGHRHKLIKGVERL 933
Cdd:cd09518    8 LSGILRKLSLEKYQPIFEEQEVDMEAFLTLTDGDLKELGIKTDGPRQQILAAISEL 63
PHA02859 PHA02859
ankyrin repeat protein; Provisional
213-310 5.98e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 42.50  E-value: 5.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   213 TPLH--LAAGYNRVKIVQLLLQHGADVHAKDKGD-LVPLHNACSYG---HYEVTELLVKHGACVNAMDLWQFTPLHEAAS 286
Cdd:PHA02859   53 TPIFscLEKDKVNVEILKFLIENGADVNFKTRDNnLSALHHYLSFNknvEPEILKILIDSGSSITEEDEDGKNLLHMYMC 132
                          90       100
                  ....*....|....*....|....*.
gi 13376842   287 K--NRVEVCSLLLSYGADPTLLNCHN 310
Cdd:PHA02859  133 NfnVRINVIKLLIDSGVSFLNKDFDN 158
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
60-86 6.48e-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.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 38.01  E-value: 6.48e-04
                           10        20
                   ....*....|....*....|....*..
gi 13376842     60 TPLHFAAGFGRKDVVEYLLQNGANVQA 86
Cdd:pfam13606    4 TPLHLAARNGRLEIVKLLLENGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
528-554 7.35e-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: 37.95  E-value: 7.35e-04
                            10        20
                    ....*....|....*....|....*..
gi 13376842     528 TPLHFAAGYNRVSVVEYLLQHGADVHA 554
Cdd:smart00248    4 TPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
658-784 9.37e-04

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: 43.25  E-value: 9.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842  658 LARVKKLSSPD---NVNCRDTQGRHSTPLHLAAGYNNLEVAEYLLQHGADVNAQDKG--------------GLIPLHNAA 720
Cdd:cd22193   52 LDIAEKTDNLKrfiNAEYTDEYYEGQTALHIAIERRQGDIVALLVENGADVHAHAKGrffqpkyqgegfyfGELPLSLAA 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842  721 SYGHVDVAALLIK---YNACVNATDKWAFTPLH---EAAQKGRTQ------LCALLLAHGAD--PTLK-----NQEGQTP 781
Cdd:cd22193  132 CTNQPDIVQYLLEnehQPADIEAQDSRGNTVLHalvTVADNTKENtkfvtrMYDMILIRGAKlcPTVEleeirNNDGLTP 211

                 ...
gi 13376842  782 LDL 784
Cdd:cd22193  212 LQL 214
Ank_4 pfam13637
Ankyrin repeats (many copies);
364-417 1.06e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.02  E-value: 1.06e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 13376842    364 HETALHCAAASPypkRKQICELLLRKGANINEKTKEFLTPLHVASEKAHNDVVE 417
Cdd:pfam13637    1 ELTALHAAAASG---HLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLK 51
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
47-169 1.06e-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: 43.26  E-value: 1.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   47 EKVNS--RDTAGRKSTPLHFAAGFGRKDVVEYLLQNGANVQARDDG--------------GLIPLHNACSFGHAEVVNLL 110
Cdd:cd22196   81 EFVNAayTDSYYKGQTALHIAIERRNMHLVELLVQNGADVHARASGeffkkkkggpgfyfGELPLSLAACTNQLDIVKFL 160
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13376842  111 LRH---GADPNARDNWNYTPLH---EAAIKGKIDVCIV------LLQHGAE--PTIR-----NTDGRTALDLADPSAK 169
Cdd:cd22196  161 LENphsPADISARDSMGNTVLHalvEVADNTPENTKFVtkmyneILILGAKirPLLKleeitNKKGLTPLKLAAKTGK 238
PHA02743 PHA02743
Viral ankyrin protein; Provisional
170-301 1.17e-03

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 40.95  E-value: 1.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   170 AVLTGEYKKDELLESARSGNEEKMMALLTPLNVNCHA-----SDGRKSTplHLAAGYNR---VKIVQLLLQHGADVHAKD 241
Cdd:PHA02743   13 AVEIDEDEQNTFLRICRTGNIYELMEVAPFISGDGHLlhrydHHGRQCT--HMVAWYDRanaVMKIELLVNMGADINARE 90
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13376842   242 K--GDLVpLHNACSYGHYEVTELLVKH-GACVNAMDLWQFTPLHEAASKNRVEVCSLLLSYGA 301
Cdd:PHA02743   91 LgtGNTL-LHIAASTKNYELAEWLCRQlGVNLGAINYQHETAYHIAYKMRDRRMMEILRANGA 152
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
594-784 1.36e-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: 42.94  E-value: 1.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842  594 TPLHEAA---AKGKYEICKLLLQhgADPtkknrDGNTPLDLVKDGDTDiqDLLRGDAALLDAAKKGCLARVKKL-SSPDN 669
Cdd:cd21882   28 TCLHKAAlnlNDGVNEAIMLLLE--AAP-----DSGNPKELVNAPCTD--EFYQGQTALHIAIENRNLNLVRLLvENGAD 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842  670 VNCRDTQ-------------GRHstPLHLAAGYNNLEVAEYLLQHGAD---VNAQDKGGLIPLHnaasyghvdvaALLIK 733
Cdd:cd21882   99 VSARATGrffrkspgnlfyfGEL--PLSLAACTNQEEIVRLLLENGAQpaaLEAQDSLGNTVLH-----------ALVLQ 165
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 13376842  734 YNacvNATDKWAFTplheaaqkgrTQLCALLLAHGA--DPTLK-----NQEGQTPLDL 784
Cdd:cd21882  166 AD---NTPENSAFV----------CQMYNLLLSYGAhlDPTQQleeipNHQGLTPLKL 210
PHA02859 PHA02859
ankyrin repeat protein; Provisional
364-459 1.43e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 41.34  E-value: 1.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   364 HETALHCAAASPYPKrKQICELLLRKGANINEKTKEF-LTPLH---VASEKAHNDVVEVVVKHEAKVNALDNLGQTSLHR 439
Cdd:PHA02859   51 YETPIFSCLEKDKVN-VEILKFLIENGADVNFKTRDNnLSALHhylSFNKNVEPEILKILIDSGSSITEEDEDGKNLLHM 129
                          90       100
                  ....*....|....*....|....*..
gi 13376842   440 aaycgHLQTC-------RLLLSYGCDP 459
Cdd:PHA02859  130 -----YMCNFnvrinviKLLIDSGVSF 151
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
594-618 1.97e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 36.85  E-value: 1.97e-03
                           10        20
                   ....*....|....*....|....*
gi 13376842    594 TPLHEAAAKGKYEICKLLLQHGADP 618
Cdd:pfam13606    4 TPLHLAARNGRLEIVKLLLENGADI 28
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
562-587 2.06e-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: 2.06e-03
                            10        20
                    ....*....|....*....|....*.
gi 13376842     562 PLHNACSYGHYEVAELLVKHGAVVNV 587
Cdd:smart00248    5 PLHLAAENGNLEVVKLLLDKGADINA 30
Ank_2 pfam12796
Ankyrin repeats (3 copies);
749-782 2.14e-03

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 38.56  E-value: 2.14e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 13376842    749 LHEAAQKGRTQLCALLLAHGADPTLKNQEGQTPL 782
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTAL 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
60-84 2.21e-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: 2.21e-03
                            10        20
                    ....*....|....*....|....*
gi 13376842      60 TPLHFAAGFGRKDVVEYLLQNGANV 84
Cdd:smart00248    4 TPLHLAAENGNLEVVKLLLDKGADI 28
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
712-743 2.48e-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: 36.50  E-value: 2.48e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 13376842    712 GLIPLHNAA-SYGHVDVAALLIKYNACVNATDK 743
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
181-275 2.68e-03

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: 41.76  E-value: 2.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842  181 LLESARSGNEEKMmalltpLNVNCHASDGRKSTPLHLAAGYNRVKIVQLLLQHGADVHAKDKGDLVPLHNA-CSYghyeV 259
Cdd:cd22197   70 LEIDKDSGNPKPL------VNAQCTDEYYRGHSALHIAIEKRSLQCVKLLVENGADVHARACGRFFQKKQGtCFY----F 139
                         90
                 ....*....|....*.
gi 13376842  260 TELLVKHGACVNAMDL 275
Cdd:cd22197  140 GELPLSLAACTKQWDV 155
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
358-598 2.71e-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: 2.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842  358 FKHPQTHETALHCAAASPYPKRKQiCELLLRKGANINEKTKEFL------------TPLHVASEKAHNDVVEVVVKHEAK 425
Cdd:cd21882   20 YQRGATGKTCLHKAALNLNDGVNE-AIMLLLEAAPDSGNPKELVnapctdefyqgqTALHIAIENRNLNLVRLLVENGAD 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842  426 VNALDN-------------LGQTSLHRAAYCGHLQTCRLLLSYGCDPNIISLQGftalQMGNENVQQLLQEGislGNSEA 492
Cdd:cd21882   99 VSARATgrffrkspgnlfyFGELPLSLAACTNQEEIVRLLLENGAQPAALEAQD----SLGNTVLHALVLQA---DNTPE 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842  493 DRQLLEAAKAGDVETVKKLCTVQSVNcrDIEGRQS-TPLHFAAGYNRVSVVEYLLQ---HGADVHAKDK----------G 558
Cdd:cd21882  172 NSAFVCQMYNLLLSYGAHLDPTQQLE--EIPNHQGlTPLKLAAVEGKIVMFQHILQrefSGPYQPLSRKftewtygpvtS 249
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 13376842  559 GLVPLHNACSYGHYEVAELLVKHGAVVNVADLWKFTPLHE 598
Cdd:cd21882  250 SLYDLSEIDSWEKNSVLELIAFSKKREARHQMLVQEPLNE 289
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
41-196 3.00e-03

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 41.67  E-value: 3.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   41 KRLVTPEKVNSrdtAGRKSTPLHFAAGFGRKDVVEYLLQNGANVQA-----------RDDG---GLIPLHNACSFGHAEV 106
Cdd:cd22194  127 DRFINAEYTEE---AYEGQTALNIAIERRQGDIVKLLIAKGADVNAhakgvffnpkyKHEGfyfGETPLALAACTNQPEI 203
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842  107 VNLLLRHGADPNA-RDNWNYTPLHEAAI-----KGKIDVCI-----VLLQHGAE--PTIRNTDGRTALDLAdpsAKavlt 173
Cdd:cd22194  204 VQLLMEKESTDITsQDSRGNTVLHALVTvaedsKTQNDFVKrmydmILLKSENKnlETIRNNEGLTPLQLA---AK---- 276
                        170       180
                 ....*....|....*....|....*
gi 13376842  174 geYKKDELLES--ARSGNEEKMMAL 196
Cdd:cd22194  277 --MGKAEILKYilSREIKEKPNRSL 299
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
433-461 3.14e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.11  E-value: 3.14e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 13376842    433 GQTSLHRAAY-CGHLQTCRLLLSYGCDPNI 461
Cdd:pfam00023    2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNA 31
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
562-587 3.52e-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.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 36.08  E-value: 3.52e-03
                           10        20
                   ....*....|....*....|....*.
gi 13376842    562 PLHNACSYGHYEVAELLVKHGAVVNV 587
Cdd:pfam13606    5 PLHLAARNGRLEIVKLLLENGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
385-455 3.58e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.42  E-value: 3.58e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13376842   385 LLLRKGANINEKTKEFLTPLHVASEKAHNDVVEVVVKHEAKVNALDNLGQTSLHRAAYCGHLQTCRLLLSY 455
Cdd:PTZ00322  100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
278-305 3.62e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.03  E-value: 3.62e-03
                            10        20
                    ....*....|....*....|....*...
gi 13376842     278 FTPLHEAASKNRVEVCSLLLSYGADPTL 305
Cdd:smart00248    3 RTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02859 PHA02859
ankyrin repeat protein; Provisional
28-161 3.94e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 40.19  E-value: 3.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842    28 LFEACRNGDVERVKRLVTpekvNSRDTAGRKSTPLH--FAAGFGRKDVVEYLLQNGANVQARDDG-GLIPLHNACSFG-- 102
Cdd:PHA02859   25 LFYYVEKDDIEGVKKWIK----FVNDCNDLYETPIFscLEKDKVNVEILKFLIENGADVNFKTRDnNLSALHHYLSFNkn 100
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13376842   103 -HAEVVNLLLRHGADPNARDNWNYTPLHE--AAIKGKIDVCIVLLQHGAEPTIRNTDGRTAL 161
Cdd:PHA02859  101 vEPEILKILIDSGSSITEEDEDGKNLLHMymCNFNVRINVIKLLIDSGVSFLNKDFDNNNIL 162
PHA02946 PHA02946
ankyin-like protein; Provisional
682-749 3.96e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 41.19  E-value: 3.96e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13376842   682 PLHLAAGYNNLEVAEYLLQHGADVNAQDKGGLIPLHNAASYGH--VDVAALLIKYNACV-NATDKWAFTPL 749
Cdd:PHA02946   75 PLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYGAKInNSVDEEGCGPL 145
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
365-398 4.39e-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: 4.39e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 13376842    365 ETALHCAAASPypKRKQICELLLRKGANINEKTK 398
Cdd:pfam00023    3 NTPLHLAAGRR--GNLEIVKLLLSKGADVNARDK 34
PHA02946 PHA02946
ankyin-like protein; Provisional
739-789 4.79e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 40.81  E-value: 4.79e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 13376842   739 NATDKWAFTPLHEAAQKGRTQLCALLLAHGADPTLKNQEGQTPLDLVSADD 789
Cdd:PHA02946   66 NETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTD 116
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
61-145 5.04e-03

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 41.22  E-value: 5.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842     61 PLHFAAGFGRKDVVEYLLQNGANVQARDDGGLIPLH-----NACSFGHAEVV----NLLLRHGAD----------PNARD 121
Cdd:TIGR00870  178 PLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHllvmeNEFKAEYEELScqmyNFALSLLDKlrdskeleviLNHQG 257
                           90       100
                   ....*....|....*....|....
gi 13376842    122 NwnyTPLHEAAIKGKIDVCIVLLQ 145
Cdd:TIGR00870  258 L---TPLKLAAKEGRIVLFRLKLA 278
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
433-461 5.64e-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: 35.31  E-value: 5.64e-03
                           10        20
                   ....*....|....*....|....*....
gi 13376842    433 GQTSLHRAAYCGHLQTCRLLLSYGCDPNI 461
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
278-307 6.01e-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: 6.01e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 13376842    278 FTPLHEAASK-NRVEVCSLLLSYGADPTLLN 307
Cdd:pfam00023    3 NTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
534-629 6.14e-03

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 40.67  E-value: 6.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   534 AGYNRVSVVEYLLQHGADVHAKDKGGLVPLHNAC--SYGHYEVAELLVKHGAVVNVADLWKFTPLH-------------- 597
Cdd:PHA02716  292 ARNIDISVVYSFLQPGVKLHYKDSAGRTCLHQYIlrHNISTDIIKLLHEYGNDLNEPDNIGNTVLHtylsmlsvvnildp 371
                          90       100       110
                  ....*....|....*....|....*....|..
gi 13376842   598 EAAAKGKYEICKLLLQHGADPTKKNRDGNTPL 629
Cdd:PHA02716  372 ETDNDIRLDVIQCLISLGADITAVNCLGYTPL 403
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
559-589 6.31e-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: 6.31e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 13376842    559 GLVPLHNAC-SYGHYEVAELLVKHGAVVNVAD 589
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
746-775 6.57e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 35.34  E-value: 6.57e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 13376842    746 FTPLHEAA-QKGRTQLCALLLAHGADPTLKN 775
Cdd:pfam00023    3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PHA02884 PHA02884
ankyrin repeat protein; Provisional
693-786 6.63e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 39.97  E-value: 6.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   693 EVAEYLLQHGADVNAQDKGGLI----PLHNAASYGHVDVAALLIKYNACVNATDKWA-FTPLHEAAQKGRTQLCALLLAH 767
Cdd:PHA02884   47 DIIDAILKLGADPEAPFPLSENsktnPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAkITPLYISVLHGCLKCLEILLSY 126
                          90
                  ....*....|....*....
gi 13376842   768 GADPTLKNQEGQTPLDLVS 786
Cdd:PHA02884  127 GADINIQTNDMVTPIELAL 145
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
346-428 6.88e-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: 6.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842  346 RIKKHLSLEmvNFKHPQTHETALHCAAASPYPKRKQICELLLrkgaNINEKT---KEFL------------TPLHVASEK 410
Cdd:cd22196   31 RTKKRLTDS--EFKDPETGKTCLLKAMLNLHNGQNDTISLLL----DIAEKTgnlKEFVnaaytdsyykgqTALHIAIER 104
                         90
                 ....*....|....*...
gi 13376842  411 AHNDVVEVVVKHEAKVNA 428
Cdd:cd22196  105 RNMHLVELLVQNGADVHA 122
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
686-771 6.89e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 40.62  E-value: 6.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842   686 AAGYNNLEVAEYLLQHGADVNAQDKGGLIPLHNAASYGHVDVAALLIKYNACVNATDKWAFTPLHEAAQKGRTQLCALL- 764
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILy 611

                  ....*...
gi 13376842   765 -LAHGADP 771
Cdd:PLN03192  612 hFASISDP 619
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
124-152 7.13e-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: 7.13e-03
                            10        20
                    ....*....|....*....|....*....
gi 13376842     124 NYTPLHEAAIKGKIDVCIVLLQHGAEPTI 152
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
247-274 7.39e-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: 7.39e-03
                           10        20
                   ....*....|....*....|....*....
gi 13376842    247 PLHNAC-SYGHYEVTELLVKHGACVNAMD 274
Cdd:pfam00023    5 PLHLAAgRRGNLEIVKLLLSKGADVNARD 33
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
200-303 7.52e-03

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 40.51  E-value: 7.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376842  200 LNVNCHASDGRKSTPLHLAAGYNRVKIVQLLLQHGADVHAKDKGDLV-PLHNacsyghyevtellvkhgacvnaMDLWQF 278
Cdd:cd22194  130 INAEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGVFFnPKYK----------------------HEGFYF 187
                         90       100
                 ....*....|....*....|....*..
gi 13376842  279 --TPLHEAASKNRVEVCSLLLSYGADP 303
Cdd:cd22194  188 geTPLALAACTNQPEIVQLLMEKESTD 214
SAM_DDHD2 cd09585
SAM domain of DDHD2; SAM (sterile alpha motif) domain of DDHD2 group is a potential ...
878-932 7.79e-03

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: 36.27  E-value: 7.79e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 13376842  878 ITQFVRNLGLEHLMDIFEREQITLDVLVEMGHKELKEIGInAYGHRHKLIKGVER 932
Cdd:cd09585   12 LEETLKKLGLSEYCDVFEKEKIDLEALALCQERDLKDLGI-PLGPRKKILNYIRR 65
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
125-154 8.16e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. 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: 34.96  E-value: 8.16e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 13376842    125 YTPLHEAAIK-GKIDVCIVLLQHGAEPTIRN 154
Cdd:pfam00023    3 NTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
SAM_WDSUB1 cd09505
SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins ...
883-933 8.66e-03

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: 36.14  E-value: 8.66e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 13376842  883 RNLGLEHLMDIFEREQITLDVLVEMGHKEL-KEIGINAYGHRHKLIKGVERL 933
Cdd:cd09505   15 RSIGLEQYVEVFRANNIDGKELLNLTKESLsKDLKIESLGHRNKILRKIEEL 66
SAM_CNK1,2,3-suppressor cd09511
SAM domain of CNK1,2,3-suppressor subfamily; SAM (sterile alpha motif) domain of CNK ...
873-933 8.86e-03

SAM domain of CNK1,2,3-suppressor subfamily; SAM (sterile alpha motif) domain of CNK (connector enhancer of kinase suppressor of ras (Ksr)) subfamily is a protein-protein interaction domain. CNK proteins are multidomain scaffold proteins containing a few protein-protein interaction domains and are required for connecting Rho and Ras signaling pathways. In Drosophila, the SAM domain of CNK is known to interact with the SAM domain of the aveugle protein, forming a heterodimer. Mutation of the SAM domain in human CNK1 abolishes the ability to cooperate with the Ras effector, supporting the idea that this interaction is necessary for proper Ras signal transduction.


Pssm-ID: 188910  Cd Length: 69  Bit Score: 36.11  E-value: 8.86e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13376842  873 GVDFSITQFVRNlglehlmdiFEREQITLDVLVEMGHKELKEIGINAYGHRHKLIKGVERL 933
Cdd:cd09511   15 GLDDCLQQYIYT---------FEREKVTGEQLLNLSPQDLENLGVTKIGHQELILEAVELL 66
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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