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Conserved domains on  [gi|2462521184|ref|XP_054222807|]
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poly [ADP-ribose] polymerase tankyrase-2 isoform X6 [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 ...
467-689 7.33e-156

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: 449.35  E-value: 7.33e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 467 QGLNPYLTLNTSGSGTILIDLSPDDKEFQSVEEEMQSTVREHRDGGHAGGIFNRYNILKIQKVCNKKLWERYTHRRKEVS 546
Cdd:cd01438     1 QGRNPYLTFHCVNQGTILLDLAPDDKEYQSVEEEMQSTIREHRDGGNAGGIFNRYNIIRIQKVVNKKLRERYCHRQKEIA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 547 EENHNHANERMLFHGSPFVNAIIHKGFDERHAYIGGMFGAGIYFAENSSKSNQYVYGIGGGTGCPVHKDRSCYICHRQLL 626
Cdd:cd01438    81 EENHNHHNERMLFHGSPFINAIIHKGFDERHAYIGGMFGAGIYFAENSSKSNQYVYGIGGGTGCPTHKDRSCYVCHRQML 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462521184 627 FCRVTLGKSFLQFSAMKMAHSPPGHHSVTGRPSVNGLALAEYVIYRGEQAYPEYLITYQIMRP 689
Cdd:cd01438   161 FCRVTLGKSFLQFSAMKMAHAPPGHHSVIGRPSVNGLAYAEYVIYRGEQAYPEYLITYQIVKP 223
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
14-318 3.12e-51

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 179.76  E-value: 3.12e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184  14 ISLGNSEADRQLLEAAKAGDVETVKKLCTVQSVNCRDIEGRQSTPLHFAAGYNRVSVVEYLLQHGADVHAKDKGGLVPLH 93
Cdd:COG0666    13 AALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLH 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184  94 NACSYGHYEVAELLVKHGAVVNVADLWKFTPLHEAAAKGKYEICKLLLQHGADPTKKNRDGNtpldlvkdgdtdiqdllr 173
Cdd:COG0666    93 AAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGN------------------ 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 174 gdaalldaakkgclarvkklsspdnvncrdtqgrhsTPLHLAAGYNNLEVAEYLLQHGADVNAQDKGGLIPLHNAASYGH 253
Cdd:COG0666   155 ------------------------------------TPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGH 198
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462521184 254 VDVAALLIKYNACVNATDKWAFTPLHEAAQKGRTQLCALLLAHGADPTLKNQEGQTPLDLVSADD 318
Cdd:COG0666   199 LEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAG 263
SAM_tankyrase1,2 cd09524
SAM domain of tankyrase1,2 subfamily; SAM (sterile alpha motif) domain of Tankyrase1,2 ...
400-465 3.84e-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: 135.53  E-value: 3.84e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462521184 400 VPGVDFSITQFVRNLGLEHLMDIFEREQITLDVLVEMGHKELKEIGINAYGHRHKLIKGVERLISG 465
Cdd:cd09524     1 VNGTDFSISQFLSSLGLEHLREIFEREQITLDVLAEMGHEELKEIGINAYGHRHKLIKGVERLISG 66
Ank_4 pfam13637
Ankyrin repeats (many copies);
177-228 4.20e-05

Ankyrin repeats (many copies);


:

Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.49  E-value: 4.20e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462521184 177 ALLDAAKKGCLARVKKL-SSPDNVNCRDTQGRhsTPLHLAAGYNNLEVAEYLL 228
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 ...
467-689 7.33e-156

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: 449.35  E-value: 7.33e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 467 QGLNPYLTLNTSGSGTILIDLSPDDKEFQSVEEEMQSTVREHRDGGHAGGIFNRYNILKIQKVCNKKLWERYTHRRKEVS 546
Cdd:cd01438     1 QGRNPYLTFHCVNQGTILLDLAPDDKEYQSVEEEMQSTIREHRDGGNAGGIFNRYNIIRIQKVVNKKLRERYCHRQKEIA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 547 EENHNHANERMLFHGSPFVNAIIHKGFDERHAYIGGMFGAGIYFAENSSKSNQYVYGIGGGTGCPVHKDRSCYICHRQLL 626
Cdd:cd01438    81 EENHNHHNERMLFHGSPFINAIIHKGFDERHAYIGGMFGAGIYFAENSSKSNQYVYGIGGGTGCPTHKDRSCYVCHRQML 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462521184 627 FCRVTLGKSFLQFSAMKMAHSPPGHHSVTGRPSVNGLALAEYVIYRGEQAYPEYLITYQIMRP 689
Cdd:cd01438   161 FCRVTLGKSFLQFSAMKMAHAPPGHHSVIGRPSVNGLAYAEYVIYRGEQAYPEYLITYQIVKP 223
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
14-318 3.12e-51

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 179.76  E-value: 3.12e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184  14 ISLGNSEADRQLLEAAKAGDVETVKKLCTVQSVNCRDIEGRQSTPLHFAAGYNRVSVVEYLLQHGADVHAKDKGGLVPLH 93
Cdd:COG0666    13 AALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLH 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184  94 NACSYGHYEVAELLVKHGAVVNVADLWKFTPLHEAAAKGKYEICKLLLQHGADPTKKNRDGNtpldlvkdgdtdiqdllr 173
Cdd:COG0666    93 AAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGN------------------ 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 174 gdaalldaakkgclarvkklsspdnvncrdtqgrhsTPLHLAAGYNNLEVAEYLLQHGADVNAQDKGGLIPLHNAASYGH 253
Cdd:COG0666   155 ------------------------------------TPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGH 198
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462521184 254 VDVAALLIKYNACVNATDKWAFTPLHEAAQKGRTQLCALLLAHGADPTLKNQEGQTPLDLVSADD 318
Cdd:COG0666   199 LEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAG 263
SAM_tankyrase1,2 cd09524
SAM domain of tankyrase1,2 subfamily; SAM (sterile alpha motif) domain of Tankyrase1,2 ...
400-465 3.84e-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: 135.53  E-value: 3.84e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462521184 400 VPGVDFSITQFVRNLGLEHLMDIFEREQITLDVLVEMGHKELKEIGINAYGHRHKLIKGVERLISG 465
Cdd:cd09524     1 VNGTDFSISQFLSSLGLEHLREIFEREQITLDVLAEMGHEELKEIGINAYGHRHKLIKGVERLISG 66
PHA03095 PHA03095
ankyrin-like protein; Provisional
23-331 1.74e-34

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 137.46  E-value: 1.74e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184  23 RQLLEAAKAgDVETVKKLC-TVQSVNCRDIEGRqsTPLHFAAGYN---RVSVVEYLLQHGADVHAKDKGGLVPLH----N 94
Cdd:PHA03095   17 DYLLNASNV-TVEEVRRLLaAGADVNFRGEYGK--TPLHLYLHYSsekVKDIVRLLLEAGADVNAPERCGFTPLHlylyN 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184  95 ACSYghyEVAELLVKHGAVVNVADLWKFTPLHeAAAKGK---YEICKLLLQHGADPTKKNRDGNTPLD-LVKDGDTDIqD 170
Cdd:PHA03095   94 ATTL---DVIKLLIKAGADVNAKDKVGRTPLH-VYLSGFninPKVIRLLLRKGADVNALDLYGMTPLAvLLKSRNANV-E 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 171 LLRgdaALLDAakkGCLARVKklsspDNvncrdtqgRHSTPLHLAAGY--NNLEVAEYLLQHGADVNAQDKGGLIPLHNA 248
Cdd:PHA03095  169 LLR---LLIDA---GADVYAV-----DD--------RFRSLLHHHLQSfkPRARIVRELIRAGCDPAATDMLGNTPLHSM 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 249 ASYG---HVDVAALLIKyNACVNATDKWAFTPLHEAAQKGRTQLCALLLAHGADPTLKNQEGQTPLDLVSADDVSALLTA 325
Cdd:PHA03095  230 ATGSsckRSLVLPLLIA-GISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRA 308

                  ....*...
gi 2462521184 326 AMP--PSA 331
Cdd:PHA03095  309 ALAknPSA 316
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
492-684 3.03e-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: 103.57  E-value: 3.03e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 492 KEFQSVEEEMQSTvrehRDGGHAGGIFnrynILKIQKVCNKKLWERYTHRRKevseenhnHANERMLFHGSP--FVNAII 569
Cdd:pfam00644   2 EEYQIIEKYFLST----HDPTHGYPLF----ILEIFRVQRDGEWERFQPKKK--------LRNRRLLWHGSRltNFLGIL 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 570 HKGF--DERHAYIGG-MFGAGIYFAENSSKSNQYvygigggtgCPVHKDRScyicHRQLLFCRVTLGKSFLQFSAMKMAH 646
Cdd:pfam00644  66 SQGLriAPPEAPVTGyMFGKGIYFADDASKSANY---------CPPSEAHG----NGLMLLSEVALGDMNELKKADYAEK 132
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462521184 647 SPPGHHSV------------------TGRPSVNGLALA-----EYVIYRGEQAYPEYLITY 684
Cdd:pfam00644 133 LPPGKHSVkglgktapesfvdldgvpLGKLVATGYDSSvllynEYVVYNVNQVRPKYLLEV 193
Ank_2 pfam12796
Ankyrin repeats (3 copies);
59-151 4.30e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 93.64  E-value: 4.30e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184  59 LHFAAGYNRVSVVEYLLQHGADVHAKDKGGLVPLHNACSYGHYEVAELLVKHGAVVNVADLWkfTPLHEAAAKGKYEICK 138
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGR--TALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 2462521184 139 LLLQHGADPTKKN 151
Cdd:pfam12796  79 LLLEKGADINVKD 91
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
406-463 3.24e-13

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 64.98  E-value: 3.24e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462521184 406 SITQFVRNLGLEHLMDIFEREQIT-LDVLVEMGHKELKEIGINAYGHRHKLIKGVERLI 463
Cdd:pfam07647   8 SVADWLRSIGLEQYTDNFRDQGITgAELLLRLTLEDLKRLGITSVGHRRKILKKIQELK 66
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
25-229 4.80e-11

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 65.80  E-value: 4.80e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184  25 LLEAAKAGDVETVKKLCTVQSVncrDIEGRQS---TPLHFAAGYNRVSVVEYLLQHG---------ADVHAkdkgGLVPL 92
Cdd:cd22192    21 LLLAAKENDVQAIKKLLKCPSC---DLFQRGAlgeTALHVAALYDNLEAAVVLMEAApelvnepmtSDLYQ----GETAL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184  93 HNACSYGHYEVAELLVKHGAVVNVA------------DLWKFT--PLHEAAAKGKYEICKLLLQHGADPTKKNRDGNTPL 158
Cdd:cd22192    94 HIAVVNQNLNLVRELIARGADVVSPratgtffrpgpkNLIYYGehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462521184 159 D-LV----KDGDTDIQDLLrgdaalldaakkgcLARVKklssPDNVNCRDTQGRHS--TPLHLAAGYNNLEVAEYLLQ 229
Cdd:cd22192   174 HiLVlqpnKTFACQMYDLI--------------LSYDK----EDDLQPLDLVPNNQglTPFKLAAKEGNIVMFQHLVQ 233
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
406-462 5.21e-10

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: 55.76  E-value: 5.21e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462521184  406 SITQFVRNLGLEHLMDIFEREQITLDVLVEMGHKE-LKEIGINAYGHRHKLIKGVERL 462
Cdd:smart00454   8 SVADWLESIGLEQYADNFRKNGIDGALLLLLTSEEdLKELGITKLGHRKKILKAIQKL 65
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
100-313 4.59e-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: 4.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 100 HYEVAELLVKHGAVVNVADlwkfTPLHeAAAKGKYEICKLLLQHgadpTKKNRDGNTPLDLVKDGDTDiqDLLRGdaall 179
Cdd:TIGR00870  65 NLELTELLLNLSCRGAVGD----TLLH-AISLEYVDAVEAILLH----LLAAFRKSGPLELANDQYTS--EFTPG----- 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 180 daakkgclarvkklsspdnvncrdtqgrhSTPLHLAAGYNNLEVAEYLLQHGADVNAQDKG--------------GLIPL 245
Cdd:TIGR00870 129 -----------------------------ITALHLAAHRQNYEIVKLLLERGASVPARACGdffvksqgvdsfyhGESPL 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 246 HNAASYGHVDVAALLIKYNACVNATDKWAFTPLHEAA---------QKGRTQLCALLLAHGA--DPTLK-----NQEGQT 309
Cdd:TIGR00870 180 NAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVmenefkaeyEELSCQMYNFALSLLDklRDSKElevilNHQGLT 259

                  ....
gi 2462521184 310 PLDL 313
Cdd:TIGR00870 260 PLKL 263
PLN03123 PLN03123
poly [ADP-ribose] polymerase; Provisional
554-678 4.15e-06

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215590 [Multi-domain]  Cd Length: 981  Bit Score: 50.17  E-value: 4.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 554 NERMLFHGSPFVN--AIIHKGFdeRHA-----YIGGMFGAGIYFAENSSKSNQYvygigggtgcpvhkdrsCYICHRQ-- 624
Cdd:PLN03123  825 NRMLLWHGSRLTNfvGILSQGL--RIAppeapATGYMFGKGVYFADLVSKSAQY-----------------CYTDRKNpv 885
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462521184 625 --LLFCRVTLGKSFLQFSAMKMAHSPPGHHSVTGRPSVNGLAlAEYVIYRGEQAYP 678
Cdd:PLN03123  886 glMLLSEVALGEIYELKKAKYMDKPPRGKHSTKGLGKTVPQE-SEFVKWRDDVVVP 940
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
210-236 5.60e-06

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: 43.35  E-value: 5.60e-06
                           10        20
                   ....*....|....*....|....*..
gi 2462521184  210 TPLHLAAGYNNLEVAEYLLQHGADVNA 236
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
177-228 4.20e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.49  E-value: 4.20e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462521184 177 ALLDAAKKGCLARVKKL-SSPDNVNCRDTQGRhsTPLHLAAGYNNLEVAEYLL 228
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 ...
467-689 7.33e-156

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: 449.35  E-value: 7.33e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 467 QGLNPYLTLNTSGSGTILIDLSPDDKEFQSVEEEMQSTVREHRDGGHAGGIFNRYNILKIQKVCNKKLWERYTHRRKEVS 546
Cdd:cd01438     1 QGRNPYLTFHCVNQGTILLDLAPDDKEYQSVEEEMQSTIREHRDGGNAGGIFNRYNIIRIQKVVNKKLRERYCHRQKEIA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 547 EENHNHANERMLFHGSPFVNAIIHKGFDERHAYIGGMFGAGIYFAENSSKSNQYVYGIGGGTGCPVHKDRSCYICHRQLL 626
Cdd:cd01438    81 EENHNHHNERMLFHGSPFINAIIHKGFDERHAYIGGMFGAGIYFAENSSKSNQYVYGIGGGTGCPTHKDRSCYVCHRQML 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462521184 627 FCRVTLGKSFLQFSAMKMAHSPPGHHSVTGRPSVNGLALAEYVIYRGEQAYPEYLITYQIMRP 689
Cdd:cd01438   161 FCRVTLGKSFLQFSAMKMAHAPPGHHSVIGRPSVNGLAYAEYVIYRGEQAYPEYLITYQIVKP 223
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
14-318 3.12e-51

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 179.76  E-value: 3.12e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184  14 ISLGNSEADRQLLEAAKAGDVETVKKLCTVQSVNCRDIEGRQSTPLHFAAGYNRVSVVEYLLQHGADVHAKDKGGLVPLH 93
Cdd:COG0666    13 AALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLH 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184  94 NACSYGHYEVAELLVKHGAVVNVADLWKFTPLHEAAAKGKYEICKLLLQHGADPTKKNRDGNtpldlvkdgdtdiqdllr 173
Cdd:COG0666    93 AAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGN------------------ 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 174 gdaalldaakkgclarvkklsspdnvncrdtqgrhsTPLHLAAGYNNLEVAEYLLQHGADVNAQDKGGLIPLHNAASYGH 253
Cdd:COG0666   155 ------------------------------------TPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGH 198
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462521184 254 VDVAALLIKYNACVNATDKWAFTPLHEAAQKGRTQLCALLLAHGADPTLKNQEGQTPLDLVSADD 318
Cdd:COG0666   199 LEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAG 263
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
3-311 1.02e-50

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 178.22  E-value: 1.02e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184   3 NENVQQLLQEGISLGNSEADRQLLEAAKAGDVETVKKLCTVQSVNCRDIEGRQSTPLHFAAGYNRVSVVEYLLQHGADVH 82
Cdd:COG0666    35 LLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVN 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184  83 AKDKGGLVPLHNACSYGHYEVAELLVKHGAVVNVADLWKFTPLHEAAAKGKYEICKLLLQHGADPTKKNRDGNtpldlvk 162
Cdd:COG0666   115 ARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGE------- 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 163 dgdtdiqdllrgdaalldaakkgclarvkklsspdnvncrdtqgrhsTPLHLAAGYNNLEVAEYLLQHGADVNAQDKGGL 242
Cdd:COG0666   188 -----------------------------------------------TPLHLAAENGHLEIVKLLLEAGADVNAKDNDGK 220
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462521184 243 IPLHNAASYGHVDVAALLIKYNACVNATDKWAFTPLHEAAQKGRTQLCALLLAHGADPTLKNQEGQTPL 311
Cdd:COG0666   221 TALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
SAM_tankyrase1,2 cd09524
SAM domain of tankyrase1,2 subfamily; SAM (sterile alpha motif) domain of Tankyrase1,2 ...
400-465 3.84e-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: 135.53  E-value: 3.84e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462521184 400 VPGVDFSITQFVRNLGLEHLMDIFEREQITLDVLVEMGHKELKEIGINAYGHRHKLIKGVERLISG 465
Cdd:cd09524     1 VNGTDFSISQFLSSLGLEHLREIFEREQITLDVLAEMGHEELKEIGINAYGHRHKLIKGVERLISG 66
PHA03095 PHA03095
ankyrin-like protein; Provisional
23-331 1.74e-34

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 137.46  E-value: 1.74e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184  23 RQLLEAAKAgDVETVKKLC-TVQSVNCRDIEGRqsTPLHFAAGYN---RVSVVEYLLQHGADVHAKDKGGLVPLH----N 94
Cdd:PHA03095   17 DYLLNASNV-TVEEVRRLLaAGADVNFRGEYGK--TPLHLYLHYSsekVKDIVRLLLEAGADVNAPERCGFTPLHlylyN 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184  95 ACSYghyEVAELLVKHGAVVNVADLWKFTPLHeAAAKGK---YEICKLLLQHGADPTKKNRDGNTPLD-LVKDGDTDIqD 170
Cdd:PHA03095   94 ATTL---DVIKLLIKAGADVNAKDKVGRTPLH-VYLSGFninPKVIRLLLRKGADVNALDLYGMTPLAvLLKSRNANV-E 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 171 LLRgdaALLDAakkGCLARVKklsspDNvncrdtqgRHSTPLHLAAGY--NNLEVAEYLLQHGADVNAQDKGGLIPLHNA 248
Cdd:PHA03095  169 LLR---LLIDA---GADVYAV-----DD--------RFRSLLHHHLQSfkPRARIVRELIRAGCDPAATDMLGNTPLHSM 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 249 ASYG---HVDVAALLIKyNACVNATDKWAFTPLHEAAQKGRTQLCALLLAHGADPTLKNQEGQTPLDLVSADDVSALLTA 325
Cdd:PHA03095  230 ATGSsckRSLVLPLLIA-GISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRA 308

                  ....*...
gi 2462521184 326 AMP--PSA 331
Cdd:PHA03095  309 ALAknPSA 316
PHA03100 PHA03100
ankyrin repeat protein; Provisional
54-272 1.04e-29

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 122.47  E-value: 1.04e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184  54 RQSTPLHFAAGYNRVSVVEYLLQHGADVHAKDKGGLVPLHNACSYGHY-----EVAELLVKHGAVVNVADLWKFTPLHEA 128
Cdd:PHA03100   34 KPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYA 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 129 AAK--GKYEICKLLLQHGADPTKKNRDGNTPLDLVKDG---DTDIQDLLRGDAALLDAAKkgclaRVKKL-SSPDNVNCR 202
Cdd:PHA03100  114 ISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESnkiDLKILKLLIDKGVDINAKN-----RVNYLlSYGVPINIK 188
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 203 DTQGrhSTPLHLAAGYNNLEVAEYLLQHGADVNAQDKGGLIPLHNAASYGHVDVAALLIKYNACVNATDK 272
Cdd:PHA03100  189 DVYG--FTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
492-684 3.03e-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: 103.57  E-value: 3.03e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 492 KEFQSVEEEMQSTvrehRDGGHAGGIFnrynILKIQKVCNKKLWERYTHRRKevseenhnHANERMLFHGSP--FVNAII 569
Cdd:pfam00644   2 EEYQIIEKYFLST----HDPTHGYPLF----ILEIFRVQRDGEWERFQPKKK--------LRNRRLLWHGSRltNFLGIL 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 570 HKGF--DERHAYIGG-MFGAGIYFAENSSKSNQYvygigggtgCPVHKDRScyicHRQLLFCRVTLGKSFLQFSAMKMAH 646
Cdd:pfam00644  66 SQGLriAPPEAPVTGyMFGKGIYFADDASKSANY---------CPPSEAHG----NGLMLLSEVALGDMNELKKADYAEK 132
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462521184 647 SPPGHHSV------------------TGRPSVNGLALA-----EYVIYRGEQAYPEYLITY 684
Cdd:pfam00644 133 LPPGKHSVkglgktapesfvdldgvpLGKLVATGYDSSvllynEYVVYNVNQVRPKYLLEV 193
PHA02874 PHA02874
ankyrin repeat protein; Provisional
31-312 2.27e-24

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 106.59  E-value: 2.27e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184  31 AGDVETVKKLCTVQSvNCRDIEGRQS-TPLHFAAGYNRVSVVEYLLQHGADVHAKDKGGLVPLHNACSYGHYEVAELLVK 109
Cdd:PHA02874   11 SGDIEAIEKIIKNKG-NCINISVDETtTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLID 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 110 HGA-----------------------VVNVADLWKFTPLHEAAAKGKYEICKLLLQHGADPTKKNRDGNTPLDL-VKDGD 165
Cdd:PHA02874   90 NGVdtsilpipciekdmiktildcgiDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIaIKHNF 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 166 TDIQDLLrgdaalldaAKKGCLARVKKlsspDNVNcrdtqgrhsTPLHLAAGYNNLEVAEYLLQHGADVNAQDKGGLIPL 245
Cdd:PHA02874  170 FDIIKLL---------LEKGAYANVKD----NNGE---------SPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPL 227
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462521184 246 HNAASYGHvDVAALLIKyNACVNATDKWAFTPLHEAAQ-KGRTQLCALLLAHGADPTLKNQEGQTPLD 312
Cdd:PHA02874  228 HNAIIHNR-SAIELLIN-NASINDQDIDGSTPLHHAINpPCDIDIIDILLYHKADISIKDNKGENPID 293
Ank_2 pfam12796
Ankyrin repeats (3 copies);
59-151 4.30e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 93.64  E-value: 4.30e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184  59 LHFAAGYNRVSVVEYLLQHGADVHAKDKGGLVPLHNACSYGHYEVAELLVKHGAVVNVADLWkfTPLHEAAAKGKYEICK 138
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGR--TALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 2462521184 139 LLLQHGADPTKKN 151
Cdd:pfam12796  79 LLLEKGADINVKD 91
ADP_ribosyl cd01341
ADP_ribosylating enzymes catalyze the transfer of ADP_ribose from NAD+ to substrates. ...
557-680 5.06e-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: 5.06e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 557 MLFHGSPFVNAIIHKGFDERHAYIG-----GMFGAGIYFAENSSKSNQYVYGIGGGTGCPVHKDRSCyichrqllfCRVT 631
Cdd:cd01341     1 FLFHGSPPGNVISILKLGLRPASYGvllngGMFGKGIYSAPNISKSNGYSVGCDGQHVFQNGKPKVC---------GREL 71
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462521184 632 LGKSFLQFSAMKMAH-------------SPPGHHSVTGRPSV---NGLALAEYVIYRG-EQAYPEY 680
Cdd:cd01341    72 CVFGFLTLGVMSGATeessrvlfprnfrGATGAEVVDLLVAMcrdALLLPREYIIFEPySQVSIRY 137
PHA02874 PHA02874
ankyrin repeat protein; Provisional
35-251 1.13e-22

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 101.58  E-value: 1.13e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184  35 ETVKKL--CTVQsVNCRDIEGRqsTPLHFAAGYNRVSVVEYLLQHGADVHAKDKGGLVPLHNACSYGHYEVAELLVKHGA 112
Cdd:PHA02874  105 DMIKTIldCGID-VNIKDAELK--TFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGA 181
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 113 VVNVADLWKFTPLHEAAAKGKYEICKLLLQHGADPTKKNRDGNTPLDLVKDGDTDIQDLLRGDAAlldaakkgclarvkk 192
Cdd:PHA02874  182 YANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAIELLINNAS--------------- 246
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 193 lsspdnVNCRDTQGrhSTPLHLAAGYN-NLEVAEYLLQHGADVNAQDKGGLIPLHNAASY 251
Cdd:PHA02874  247 ------INDQDIDG--STPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTAFKY 298
Ank_2 pfam12796
Ankyrin repeats (3 copies);
212-304 1.63e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.10  E-value: 1.63e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 212 LHLAAGYNNLEVAEYLLQHGADVNAQDKGGLIPLHNAASYGHVDVAALLIKYNACVNATDKWafTPLHEAAQKGRTQLCA 291
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGR--TALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 2462521184 292 LLLAHGADPTLKN 304
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA02878 PHA02878
ankyrin repeat protein; Provisional
58-314 5.66e-22

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 99.57  E-value: 5.66e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184  58 PLHFAAGYNRVSVVEYLLQHGADVHAKDKGGLVPLHNAC-------------SYGHYEVAELLVKHGAVVNVADLWKFTP 124
Cdd:PHA02878   40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICkepnklgmkemirSINKCSVFYTLVAIKDAFNNRNVEIFKI 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 125 LHEAAAKGKY------------------EICKLLLQHGADPTKKNRD-GNTPLDLVKDG-DTDIQDLLrgdaalldaakk 184
Cdd:PHA02878  120 ILTNRYKNIQtidlvyidkkskddiieaEITKLLLSYGADINMKDRHkGNTALHYATENkDQRLTELL------------ 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 185 gcLARVKKLSSPDNVNcrdtqgrhSTPLHLAAGYNNLEVAEYLLQHGADVNAQDKGGLIPLHNAASY-GHVDVAALLIKY 263
Cdd:PHA02878  188 --LSYGANVNIPDKTN--------NSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEH 257
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462521184 264 NACVNATDK-WAFTPLHEAAQKgrTQLCALLLAHGADPTLKNQEGQTPLDLV 314
Cdd:PHA02878  258 GVDVNAKSYiLGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSA 307
PHA02876 PHA02876
ankyrin repeat protein; Provisional
46-311 1.09e-21

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 100.14  E-value: 1.09e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184  46 VNCRDIEGRqsTPLHFAAGYNRVSVVEYLLQHGADVHAKDKGGL-----------------------------VPLHNAC 96
Cdd:PHA02876  171 VNAKDIYCI--TPIHYAAERGNAKMVNLLLSYGADVNIIALDDLsvlecavdsknidtikaiidnrsninkndLSLLKAI 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184  97 SYGHYEVAELLVKHGAVVNVADLWKFTPLHEAA-AKGKYEICKLLLQHGADPTKKNRDGNTPLDLV-KDG-DTDIQDLLR 173
Cdd:PHA02876  249 RNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASqAPSLSRLVPKLLERGADVNAKNIKGETPLYLMaKNGyDTENIRTLI 328
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 174 GDAALLDAAKKGCLARVKKLSSPD--------------NVNCRDTQGRhsTPLHLAAGYNNLEVAEYLLQHGADVNAQDK 239
Cdd:PHA02876  329 MLGADVNAADRLYITPLHQASTLDrnkdivitllelgaNVNARDYCDK--TPIHYAAVRNNVVIINTLLDYGADIEALSQ 406
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462521184 240 GGLIPLHNAAsYGHVDVAAL--LIKYNACVNATDKWAFTPLHEAAQKG-RTQLCALLLAHGADPTLKNQEGQTPL 311
Cdd:PHA02876  407 KIGTALHFAL-CGTNPYMSVktLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPL 480
PHA02876 PHA02876
ankyrin repeat protein; Provisional
66-311 6.70e-20

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 94.36  E-value: 6.70e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184  66 NRVSVVEYLLQHGADVHAKDKGGLVPLHNACSYGHYEVAELLVKHGAVVNVADLWKFTPLHEAAAKGKYEICKLLLQHGA 145
Cdd:PHA02876  156 DELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRS 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 146 DPTK---------KNRDGNTPLDLVKDG-DTDIQDLLRgDAALLDAAKKGCLARV--KKLSSPDNVNCRDTQGRhsTPLH 213
Cdd:PHA02876  236 NINKndlsllkaiRNEDLETSLLLYDAGfSVNSIDDCK-NTPLHHASQAPSLSRLvpKLLERGADVNAKNIKGE--TPLY 312
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 214 LAA--GYNNlEVAEYLLQHGADVNAQDKGGLIPLHNAASYG-HVDVAALLIKYNACVNATDKWAFTPLHEAAQKGRTQLC 290
Cdd:PHA02876  313 LMAknGYDT-ENIRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVII 391
                         250       260
                  ....*....|....*....|.
gi 2462521184 291 ALLLAHGADPTLKNQEGQTPL 311
Cdd:PHA02876  392 NTLLDYGADIEALSQKIGTAL 412
PHA02878 PHA02878
ankyrin repeat protein; Provisional
15-307 5.40e-19

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 90.71  E-value: 5.40e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184  15 SLGNSEadRQLLEAAKAGDVETVKKLCTVQSVNCRDIEGRQSTPLHFAAGYNrVSVVEYLLQHGADVHAKDK-GGLVPLH 93
Cdd:PHA02878   97 SVFYTL--VAIKDAFNNRNVEIFKIILTNRYKNIQTIDLVYIDKKSKDDIIE-AEITKLLLSYGADINMKDRhKGNTALH 173
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184  94 NACSYGHYEVAELLVKHGAVVNVADLWKFTPLHEAAAKGKYEICKLLLQHGADPTKKNRDGNTPLdlvkdgdtdiqdllr 173
Cdd:PHA02878  174 YATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPL--------------- 238
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 174 gdaalldaakkgclarvkklsspdnvncrdtqgrhstplHLAAGY-NNLEVAEYLLQHGADVNAQDK-GGLIPLHnaASY 251
Cdd:PHA02878  239 ---------------------------------------HISVGYcKDYDILKLLLEHGVDVNAKSYiLGLTALH--SSI 277
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462521184 252 GHVDVAALLIKYNACVNATDKWAFTPLHEAAQK------GRTQLCALLLAHGADPTLKNQEG 307
Cdd:PHA02878  278 KSERKLKLLLEYGADINSLNSYKLTPLSSAVKQylciniGRILISNICLLKRIKPDIKNSEG 339
PHA02875 PHA02875
ankyrin repeat protein; Provisional
90-300 2.24e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 85.04  E-value: 2.24e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184  90 VPLHNACSYGHYEVAELLVKHGAVVNVADLWKFTPLHEAAAKGKYEICKLLLQHGADPTKKNRDGNTPL-DLVKDGDT-D 167
Cdd:PHA02875    4 VALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELhDAVEEGDVkA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 168 IQDLLRGDAALLDAA-KKGclarvkklsspdnvncrdtqgrhSTPLHLAAGYNNLEVAEYLLQHGADVNAQDKGGLIPLH 246
Cdd:PHA02875   84 VEELLDLGKFADDVFyKDG-----------------------MTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLH 140
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462521184 247 NAASYGHVDVAALLIKYNACVNATDKWAFTPLHEAAQKGRTQLCALLLAHGADP 300
Cdd:PHA02875  141 LAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANI 194
Ank_2 pfam12796
Ankyrin repeats (3 copies);
125-238 2.57e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.46  E-value: 2.57e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 125 LHEAAAKGKYEICKLLLQHGADPTKKNRDGNTPLDLvkdgdtdiqdllrgdaalldAAKKGCLARVKKLSSPDNVNCRDt 204
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHL--------------------AAKNGHLEIVKLLLEHADVNLKD- 59
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2462521184 205 qgRHSTPLHLAAGYNNLEVAEYLLQHGADVNAQD 238
Cdd:pfam12796  60 --NGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
TCCD_inducible_PARP_like cd01439
Poly(ADP-ribose) polymerases catalyse the covalent attachment of ADP-ribose units from NAD+ to ...
557-684 2.78e-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: 2.78e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 557 MLFHG--SPFVNAIIHKGFDER-HAYIGGMFGAGIYFAENSSKSNQYVYGIGGGTGcpvhkdrscyicHRQLLFCRVTLG 633
Cdd:cd01439     1 LLFHGtsADAVEAICRHGFDRRfCGKHGTMYGKGSYFAKNASYSHQYSKKSPKADG------------LKEMFLARVLTG 68
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462521184 634 KsFLQFSAMKMA-------HSPPGHHSVTGR---PSVnglalaeYVIYRGEQAYPEYLITY 684
Cdd:cd01439    69 D-YTQGHPGYRRpplkpsgVELDRYDSCVDNvsnPSI-------FVIFSDVQAYPEYLITY 121
PHA02876 PHA02876
ankyrin repeat protein; Provisional
22-265 5.74e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 81.65  E-value: 5.74e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184  22 DRQLLEAAKAGDVETVKKLCTVQ-SVNcrDIEGRQSTPLHFAAGYNRVS-VVEYLLQHGADVHAKDKGGLVPLHNACSYG 99
Cdd:PHA02876  241 DLSLLKAIRNEDLETSLLLYDAGfSVN--SIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMAKNG 318
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 100 H-YEVAELLVKHGAVVNVADLWKFTPLHEAAAKGKY-EICKLLLQHGADPTKKNRDGNTPL------------DLVKDGD 165
Cdd:PHA02876  319 YdTENIRTLIMLGADVNAADRLYITPLHQASTLDRNkDIVITLLELGANVNARDYCDKTPIhyaavrnnvviiNTLLDYG 398
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 166 TDIQDLLRGDAALLDAAKKGC--LARVKKL-SSPDNVNCRDTQgrHSTPLHLAAGYN-NLEVAEYLLQHGADVNAQDKGG 241
Cdd:PHA02876  399 ADIEALSQKIGTALHFALCGTnpYMSVKTLiDRGANVNSKNKD--LSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQN 476
                         250       260
                  ....*....|....*....|....
gi 2462521184 242 LIPLHNAASYGhvDVAALLIKYNA 265
Cdd:PHA02876  477 QYPLLIALEYH--GIVNILLHYGA 498
PHA02875 PHA02875
ankyrin repeat protein; Provisional
62-320 8.89e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 80.04  E-value: 8.89e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184  62 AAGYNRVSVVEYLLQHGADVHAKDKGGLVPLHNACSYGHYEVAELLVKHGAVVNVADLWKFTPLHEAAAKGKYEICKLLL 141
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 142 QHGA---DPTKKnrDGNTPLDL-VKDGDTDIQDLLrgdaalldaakkgclarVKKLSSPDNVNCRDTqgrhsTPLHLAAG 217
Cdd:PHA02875   89 DLGKfadDVFYK--DGMTPLHLaTILKKLDIMKLL-----------------IARGADPDIPNTDKF-----SPLHLAVM 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 218 YNNLEVAEYLLQHGADVNAQDKGGLIPLHNAASYGHVDVAALLIKYNACVNATDKWA-FTPLHEAAQKGRTQLCALLLAH 296
Cdd:PHA02875  145 MGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKR 224
                         250       260
                  ....*....|....*....|....*...
gi 2462521184 297 GADP----TLKNQEgQTPLDLVSADDVS 320
Cdd:PHA02875  225 GADCnimfMIEGEE-CTILDMICNMCTN 251
PHA02875 PHA02875
ankyrin repeat protein; Provisional
24-158 1.04e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 76.57  E-value: 1.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184  24 QLLEAAKAGDVETVKKLCTVQSVNCRDIEGRQSTPLHFAAGYNRVSVVEYLLQHGADVHAKDKGGLVPLHNACSYGHYEV 103
Cdd:PHA02875   71 ELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKG 150
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2462521184 104 AELLVKHGAVVNVADLWKFTPLHEAAAKGKYEICKLLLQHGADPTKKNRDGNTPL 158
Cdd:PHA02875  151 IELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAA 205
PHA03100 PHA03100
ankyrin repeat protein; Provisional
207-314 3.51e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 75.09  E-value: 3.51e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 207 RHSTPLHLAAGYNNLEVAEYLLQHGADVNAQDKGGLIPLHNAASYGHV-----DVAALLIKYNACVNATDKWAFTPLHEA 281
Cdd:PHA03100   34 KPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYA 113
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2462521184 282 AQKGRTQ--LCALLLAHGADPTLKNQEGQTPLDLV 314
Cdd:PHA03100  114 ISKKSNSysIVEYLLDNGANVNIKNSDGENLLHLY 148
Ank_4 pfam13637
Ankyrin repeats (many copies);
208-261 4.41e-14

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 66.91  E-value: 4.41e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462521184 208 HSTPLHLAAGYNNLEVAEYLLQHGADVNAQDKGGLIPLHNAASYGHVDVAALLI 261
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
57-268 2.88e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 72.33  E-value: 2.88e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184  57 TPLHFAAGYNRVSVVEYLLQHGADVHAKDKGGLVPLHNACSYGHYEVAELLVKHGAVVNVAdLWK--FTPLHEAAAKGKY 134
Cdd:PHA02875   37 SPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDV-FYKdgMTPLHLATILKKL 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 135 EICKLLLQHGADPTKKNRDGNTPLDL-VKDGDTDIQDLLRGDAALLDAAkkgclarvkklsspDNVNCrdtqgrhsTPLH 213
Cdd:PHA02875  116 DIMKLLIARGADPDIPNTDKFSPLHLaVMMGDIKGIELLIDHKACLDIE--------------DCCGC--------TPLI 173
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462521184 214 LAAGYNNLEVAEYLLQHGADVNAQDKGGLIPLH-NAASYGHVDVAALLIKYNACVN 268
Cdd:PHA02875  174 IAMAKGDIAICKMLLDSGANIDYFGKNGCVAALcYAIENNKIDIVRLFIKRGADCN 229
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
406-463 3.24e-13

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 64.98  E-value: 3.24e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462521184 406 SITQFVRNLGLEHLMDIFEREQIT-LDVLVEMGHKELKEIGINAYGHRHKLIKGVERLI 463
Cdd:pfam07647   8 SVADWLRSIGLEQYTDNFRDQGITgAELLLRLTLEDLKRLGITSVGHRRKILKKIQELK 66
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
51-284 6.05e-13

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 72.21  E-value: 6.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184  51 IEGRQSTPlhfaagYNRVSVVEYLLQHGADVHAKDKGGLV--------------PLHNACSYGHYEVAELLVKHGAVVNV 116
Cdd:PLN03192  480 IEAMQTRQ------EDNVVILKNFLQHHKELHDLNVGDLLgdnggehddpnmasNLLTVASTGNAALLEELLKAKLDPDI 553
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 117 ADLWKFTPLHEAAAKGkYEICKL-LLQHGADPTKKNRDGNTPL-DLVKDGDTDIQDLLRGDAALLDAAKKGCLarvkkls 194
Cdd:PLN03192  554 GDSKGRTPLHIAASKG-YEDCVLvLLKHACNVHIRDANGNTALwNAISAKHHKIFRILYHFASISDPHAAGDL------- 625
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 195 spdnvncrdtqgrhstpLHLAAGYNNLEVAEYLLQHGADVNAQDKGGLIPLHNAASYGHVDVAALLIKYNA---CVNATD 271
Cdd:PLN03192  626 -----------------LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGAdvdKANTDD 688
                         250
                  ....*....|...
gi 2462521184 272 KWAFTPLHEAAQK 284
Cdd:PLN03192  689 DFSPTELRELLQK 701
Ank_4 pfam13637
Ankyrin repeats (many copies);
55-108 8.76e-13

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 63.06  E-value: 8.76e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462521184  55 QSTPLHFAAGYNRVSVVEYLLQHGADVHAKDKGGLVPLHNACSYGHYEVAELLV 108
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
4-85 1.83e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 63.60  E-value: 1.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184   4 ENVQQLLQEGISLGNSEADRQ--LLEAAKAGDVETVKKLCTVQSVNCRDiegRQSTPLHFAAGYNRVSVVEYLLQHGADV 81
Cdd:pfam12796  11 ELVKLLLENGADANLQDKNGRtaLHLAAKNGHLEIVKLLLEHADVNLKD---NGRTALHYAARSGHLEIVKLLLEKGADI 87

                  ....
gi 2462521184  82 HAKD 85
Cdd:pfam12796  88 NVKD 91
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
406-461 4.33e-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: 61.49  E-value: 4.33e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462521184 406 SITQFVRNLGLEHLMDIFEREQITLDVLVEMGHKELKEIGINAYGHRHKLIKGVER 461
Cdd:cd09487     1 DVAEWLESLGLEQYADLFRKNEIDGDALLLLTDEDLKELGITSPGHRKKILRAIQR 56
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
25-229 4.80e-11

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 65.80  E-value: 4.80e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184  25 LLEAAKAGDVETVKKLCTVQSVncrDIEGRQS---TPLHFAAGYNRVSVVEYLLQHG---------ADVHAkdkgGLVPL 92
Cdd:cd22192    21 LLLAAKENDVQAIKKLLKCPSC---DLFQRGAlgeTALHVAALYDNLEAAVVLMEAApelvnepmtSDLYQ----GETAL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184  93 HNACSYGHYEVAELLVKHGAVVNVA------------DLWKFT--PLHEAAAKGKYEICKLLLQHGADPTKKNRDGNTPL 158
Cdd:cd22192    94 HIAVVNQNLNLVRELIARGADVVSPratgtffrpgpkNLIYYGehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462521184 159 D-LV----KDGDTDIQDLLrgdaalldaakkgcLARVKklssPDNVNCRDTQGRHS--TPLHLAAGYNNLEVAEYLLQ 229
Cdd:cd22192   174 HiLVlqpnKTFACQMYDLI--------------LSYDK----EDDLQPLDLVPNNQglTPFKLAAKEGNIVMFQHLVQ 233
parp_like cd01437
Poly(ADP-ribose) polymerase (parp) catalytic domain catalyses the covalent attachment of ...
487-657 5.44e-11

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


Pssm-ID: 238717 [Multi-domain]  Cd Length: 347  Bit Score: 64.60  E-value: 5.44e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 487 LSPDDKEFQSVEEEMQSTvrehrdggHAGGIFNRYNILKIQKVCNKKLWERYTHRRKevseeNHNHaneRMLFHGSPFVN 566
Cdd:cd01437   143 LDKDSEEYKIIEKYLKNT--------HAPTTEYTVEVQEIFRVEREGETDRFKPFKK-----LGNR---KLLWHGSRLTN 206
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 567 --AIIHKGF--DERHAYIGG-MFGAGIYFAENSSKSNQYVY-GIGGGTGCpvhkdrscyichrqLLFCRVTLGKSFLQFS 640
Cdd:cd01437   207 fvGILSQGLriAPPEAPVTGyMFGKGIYFADMFSKSANYCHaSASDPTGL--------------LLLCEVALGKMNELKK 272
                         170
                  ....*....|....*...
gi 2462521184 641 AMKMAHSPP-GHHSVTGR 657
Cdd:cd01437   273 ADYMAKELPkGKHSVKGL 290
PHA03100 PHA03100
ankyrin repeat protein; Provisional
30-146 8.01e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 64.69  E-value: 8.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184  30 KAGDVETVKKL----CTVQSVNCRDIegrqsTPLHFAAGYNRVSV------------------VEYLLQHGADVHAKDKG 87
Cdd:PHA03100  117 KSNSYSIVEYLldngANVNIKNSDGE-----NLLHLYLESNKIDLkilkllidkgvdinaknrVNYLLSYGVPINIKDVY 191
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462521184  88 GLVPLHNACSYGHYEVAELLVKHGAVVNVADLWKFTPLHEAAAKGKYEICKLLLQHGAD 146
Cdd:PHA03100  192 GFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
404-462 1.07e-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: 1.07e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462521184 404 DFSITQFVRNLGLEHLMDIFEREQITLDVLVEMGHKELKEIGINAYGHRHKLIKGVERL 462
Cdd:pfam00536   5 VEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRL 63
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
123-317 2.10e-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: 2.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 123 TPLHEAAAKGKYE-ICKLLLQHGADPTKKNRDGNTPLDLVKDGDTDiqdllrgDAA--LLDAAkkgclarvkklssPDNV 199
Cdd:cd22192    19 SPLLLAAKENDVQaIKKLLKCPSCDLFQRGALGETALHVAALYDNL-------EAAvvLMEAA-------------PELV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 200 NCRDT----QGRhsTPLHLAAGYNNLEVAEYLLQHGADVNA---------QDKGGLI-----PLHNAASYGHVDVAALLI 261
Cdd:cd22192    79 NEPMTsdlyQGE--TALHIAVVNQNLNLVRELIARGADVVSpratgtffrPGPKNLIyygehPLSFAACVGNEEIVRLLI 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462521184 262 KYNACVNATDKWAFTPLH----EAAQKGRTQLCALLLAhgADP--------TLKNQEGQTPLDLVSAD 317
Cdd:cd22192   157 EHGADIRAQDSLGNTVLHilvlQPNKTFACQMYDLILS--YDKeddlqpldLVPNNQGLTPFKLAAKE 222
PHA02876 PHA02876
ankyrin repeat protein; Provisional
45-181 2.25e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 63.93  E-value: 2.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184  45 SVNCRDIegRQSTPLHFAAGYNRVSVVEYLLQHGADVHAKDKGGLVPLHNA-CSYGHYEVAELLVKHGAVVNVADLWKFT 123
Cdd:PHA02876  367 NVNARDY--CDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLST 444
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462521184 124 PLHEAAAKG-KYEICKLLLQHGADPTKKNRDGNTPLDLVKDGDTDIQDLLRGDAALLDA 181
Cdd:PHA02876  445 PLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIALEYHGIVNILLHYGAELRDS 503
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
406-462 5.21e-10

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: 55.76  E-value: 5.21e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462521184  406 SITQFVRNLGLEHLMDIFEREQITLDVLVEMGHKE-LKEIGINAYGHRHKLIKGVERL 462
Cdd:smart00454   8 SVADWLESIGLEQYADNFRKNGIDGALLLLLTSEEdLKELGITKLGHRKKILKAIQKL 65
Ank_4 pfam13637
Ankyrin repeats (many copies);
91-141 7.09e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.97  E-value: 7.09e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462521184  91 PLHNACSYGHYEVAELLVKHGAVVNVADLWKFTPLHEAAAKGKYEICKLLL 141
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
24-110 8.94e-10

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 61.84  E-value: 8.94e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184  24 QLLEAAKAGDVETVKKLCTVQS-VNCRDIEGRqsTPLHFAAGYNRVSVVEYLLQHGADVHAKDKGGLVPLHNACSYGHYE 102
Cdd:PTZ00322   85 ELCQLAASGDAVGARILLTGGAdPNCRDYDGR--TPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFRE 162

                  ....*...
gi 2462521184 103 VAELLVKH 110
Cdd:PTZ00322  163 VVQLLSRH 170
Ank_5 pfam13857
Ankyrin repeats (many copies);
197-246 3.43e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 53.12  E-value: 3.43e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462521184 197 DNVNCRDTQGRHSTPLHLAAGYNNLEVAEYLLQHGADVNAQDKGGLIPLH 246
Cdd:pfam13857   5 GPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
100-313 4.59e-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: 4.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 100 HYEVAELLVKHGAVVNVADlwkfTPLHeAAAKGKYEICKLLLQHgadpTKKNRDGNTPLDLVKDGDTDiqDLLRGdaall 179
Cdd:TIGR00870  65 NLELTELLLNLSCRGAVGD----TLLH-AISLEYVDAVEAILLH----LLAAFRKSGPLELANDQYTS--EFTPG----- 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 180 daakkgclarvkklsspdnvncrdtqgrhSTPLHLAAGYNNLEVAEYLLQHGADVNAQDKG--------------GLIPL 245
Cdd:TIGR00870 129 -----------------------------ITALHLAAHRQNYEIVKLLLERGASVPARACGdffvksqgvdsfyhGESPL 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 246 HNAASYGHVDVAALLIKYNACVNATDKWAFTPLHEAA---------QKGRTQLCALLLAHGA--DPTLK-----NQEGQT 309
Cdd:TIGR00870 180 NAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVmenefkaeyEELSCQMYNFALSLLDklRDSKElevilNHQGLT 259

                  ....
gi 2462521184 310 PLDL 313
Cdd:TIGR00870 260 PLKL 263
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
96-266 7.75e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 58.76  E-value: 7.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184  96 CSYGHYEVAELLVKhGAVVNVADLWKFTPLHEAAAKgKYEICKLLLQHGADPTKKNRDGNTPLDLVKDGDTD--IQDLLR 173
Cdd:PTZ00322    6 CSVASSAFAAQLFF-GTEGSRKRRAKPISFERMAAI-QEEIARIDTHLEALEATENKDATPDHNLTTEEVIDpvVAHMLT 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 174 GDAALLDAAKKGCLARVKkLSSPDNVNCRDTQGRhsTPLHLAAGYNNLEVAEYLLQHGADVNAQDKGGLIPLHNAASYGH 253
Cdd:PTZ00322   84 VELCQLAASGDAVGARIL-LTGGADPNCRDYDGR--TPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGF 160
                         170
                  ....*....|...
gi 2462521184 254 VDVAALLIKYNAC 266
Cdd:PTZ00322  161 REVVQLLSRHSQC 173
Ank_4 pfam13637
Ankyrin repeats (many copies);
244-294 7.95e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.89  E-value: 7.95e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462521184 244 PLHNAASYGHVDVAALLIKYNACVNATDKWAFTPLHEAAQKGRTQLCALLL 294
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
213-296 1.74e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 57.60  E-value: 1.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 213 HLAAGYNNLEvAEYLLQHGADVNAQDKGGLIPLHNAASYGHVDVAALLIKYNACVNATDKWAFTPLHEAAQKGRTQLCAL 292
Cdd:PTZ00322   88 QLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166

                  ....
gi 2462521184 293 LLAH 296
Cdd:PTZ00322  167 LSRH 170
Ank_5 pfam13857
Ankyrin repeats (many copies);
45-93 2.00e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 50.81  E-value: 2.00e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2462521184  45 SVNCRDIEGRQSTPLHFAAGYNRVSVVEYLLQHGADVHAKDKGGLVPLH 93
Cdd:pfam13857   6 PIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
246-346 2.10e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 57.60  E-value: 2.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 246 HNAASyGHVDVAALLIKYNACVNATDKWAFTPLHEAAQKGRTQLCALLLAHGADPTLKNQEGQTPLDLVSADD----VSA 321
Cdd:PTZ00322   88 QLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGfrevVQL 166
                          90       100
                  ....*....|....*....|....*
gi 2462521184 322 LLTAAMPPSALPSCYKPQVLNGVRS 346
Cdd:PTZ00322  167 LSRHSQCHFELGANAKPDSFTGKPP 191
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
55-289 2.71e-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: 2.71e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184  55 QSTPLHFAAGYNRVSVVEYLL-QHGADVHAKDKGGLVPLHNACSYGHYEVAELLVKHG-AVVNVA---DLWK-FTPLHEA 128
Cdd:cd22192    17 SESPLLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAApELVNEPmtsDLYQgETALHIA 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 129 AAKGKYEICKLLLQHGADPTKknrdgntpldlvkdgdtdiqdllrgdaalldaakkgclARVKKLSSPDNVNCRDTQGRH 208
Cdd:cd22192    97 VVNQNLNLVRELIARGADVVS--------------------------------------PRATGTFFRPGPKNLIYYGEH 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 209 stPLHLAAGYNNLEVAEYLLQHGADVNAQDKGGLIPLHNAASYGHVDVAA----LLIKYNACVNA------TDKWAFTPL 278
Cdd:cd22192   139 --PLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTFACqmydLILSYDKEDDLqpldlvPNNQGLTPF 216
                         250
                  ....*....|.
gi 2462521184 279 HEAAQKGRTQL 289
Cdd:cd22192   217 KLAAKEGNIVM 227
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
210-239 8.44e-08

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: 48.44  E-value: 8.44e-08
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2462521184 210 TPLHLAAG-YNNLEVAEYLLQHGADVNAQDK 239
Cdd:pfam00023   4 TPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
107-161 8.52e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 49.27  E-value: 8.52e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462521184 107 LVKHGAV-VNVADLWKFTPLHEAAAKGKYEICKLLLQHGADPTKKNRDGNTPLDLV 161
Cdd:pfam13857   1 LLEHGPIdLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02798 PHA02798
ankyrin-like protein; Provisional
102-279 1.08e-07

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 54.84  E-value: 1.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 102 EVAELLVKHGAVVNVADLWKFTPLHEAAA-----KGKYEICKLLLQHGADPTKKNRDGNTPLdlvkdgdtdiqdllrgda 176
Cdd:PHA02798   52 DIVKLFINLGANVNGLDNEYSTPLCTILSnikdyKHMLDIVKILIENGADINKKNSDGETPL------------------ 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 177 alldaakkGCLarvkklsspdnvncrdtqgrhstplhLAAGY-NNLEVAEYLLQHGADVNAQDKGGLIPLHNAASYGH-- 253
Cdd:PHA02798  114 --------YCL--------------------------LSNGYiNNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHhi 159
                         170       180
                  ....*....|....*....|....*...
gi 2462521184 254 -VDVAALLIKYNACVNATDKW-AFTPLH 279
Cdd:PHA02798  160 dIEIIKLLLEKGVDINTHNNKeKYDTLH 187
Ank_5 pfam13857
Ankyrin repeats (many copies);
227-281 1.30e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.50  E-value: 1.30e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462521184 227 LLQHG-ADVNAQDKGGLIPLHNAASYGHVDVAALLIKYNACVNATDKWAFTPLHEA 281
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
123-159 1.69e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.42  E-value: 1.69e-07
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2462521184 123 TPLHEAAAKGKYEICKLLLQHGADPTKKNRDGNTPLD 159
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALH 39
SAM_BOI-like_fungal cd09535
SAM domain of BOI-like fungal subfamily; SAM (sterile alpha motif) domain of BOI-like fungal ...
407-462 1.76e-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: 1.76e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462521184 407 ITQFVRNLGLE-HLMDIFEREQITLDVLVEMGHKELKEIGINAYGHRHKLIKGVERL 462
Cdd:cd09535     8 VAEWLLSAGFDdSVCEKFRENEITGDILLELDLEDLKELDIGSFGKRFKLWNEIKSL 64
SAM_Ste50-like_fungal cd09533
SAM domain of Ste50_like (ubc2) subfamily; SAM (sterile alpha motif) domain of Ste50-like (or ...
409-462 1.80e-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: 1.80e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462521184 409 QFVRNLGLEHLMDIFEREQITLDVLVEMGHKELKEIGINAYGHRHKLIKGVERL 462
Cdd:cd09533     4 DWLSSLGLPQYEDQFIENGITGDVLVALDHEDLKEMGITSVGHRLTILKAVYEL 57
Ank_5 pfam13857
Ankyrin repeats (many copies);
267-314 2.10e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.11  E-value: 2.10e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2462521184 267 VNATDKWAFTPLHEAAQKGRTQLCALLLAHGADPTLKNQEGQTPLDLV 314
Cdd:pfam13857   9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02876 PHA02876
ankyrin repeat protein; Provisional
219-317 4.29e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 53.14  E-value: 4.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 219 NNLEVAEYLLQHGADVNAQDKGGLIPLHNAASYGHVDVAALLIKYNA--------------------------------- 265
Cdd:PHA02876  156 DELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGAdvniialddlsvlecavdsknidtikaiidnrs 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 266 -----------------------------CVNATDKWAFTPLHEAAQK-GRTQLCALLLAHGADPTLKNQEGQTPLDLVS 315
Cdd:PHA02876  236 ninkndlsllkairnedletslllydagfSVNSIDDCKNTPLHHASQApSLSRLVPKLLERGADVNAKNIKGETPLYLMA 315

                  ..
gi 2462521184 316 AD 317
Cdd:PHA02876  316 KN 317
PHA02798 PHA02798
ankyrin-like protein; Provisional
68-311 4.67e-07

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 52.91  E-value: 4.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184  68 VSVVEYLLQHGADVHAKDKGGLVPL----HNACSYGH-YEVAELLVKHGAVVNVADLWKFTPLHEAAAKG---KYEICKL 139
Cdd:PHA02798   51 TDIVKLFINLGANVNGLDNEYSTPLctilSNIKDYKHmLDIVKILIENGADINKKNSDGETPLYCLLSNGyinNLEILLF 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 140 LLQHGADPTKKNRDGNTPLDL-VKDG---DTDIQDLLrgdaalldaakkgclarvkkLSSPDNVNCRDTQGRHSTpLHLA 215
Cdd:PHA02798  131 MIENGADTTLLDKDGFTMLQVyLQSNhhiDIEIIKLL--------------------LEKGVDINTHNNKEKYDT-LHCY 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 216 AGYN----NLEVAEYLLQHGADVNAQDKGG-------LIPLHNAASYGHVDVAALLIKYnACVNATDKWAFTPLHEAAQK 284
Cdd:PHA02798  190 FKYNidriDADILKLFVDNGFIINKENKSHkkkfmeyLNSLLYDNKRFKKNILDFIFSY-IDINQVDELGFNPLYYSVSH 268
                         250       260
                  ....*....|....*....|....*..
gi 2462521184 285 GRTQLCALLLAHGADPTLKNQEGQTPL 311
Cdd:PHA02798  269 NNRKIFEYLLQLGGDINIITELGNTCL 295
Ank_5 pfam13857
Ankyrin repeats (many copies);
74-128 6.17e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.57  E-value: 6.17e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462521184  74 LLQHG-ADVHAKDKGGLVPLHNACSYGHYEVAELLVKHGAVVNVADLWKFTPLHEA 128
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
SAM_BICC1 cd09520
SAM domain of BICC1 (bicaudal) subfamily; SAM (sterile alpha motif) domain of BICC1 (bicaudal) ...
406-456 7.22e-07

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: 7.22e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462521184 406 SITQFVRNLGLEHLMDIFEREQITLDVLVEMGHKELKEIGINAYGHRHKLI 456
Cdd:cd09520     6 DLPELLAKLGLEKYIDLFAQQEIDLQTFLTLTDQDLKELGITAFGARRKML 56
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
6-295 1.08e-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: 1.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184   6 VQQLLQEGISLGNSEADR----QLLEAAKAGDVETVKKLctVQSVNCRDIEGRqsTPLHfAAGYNRVSVVEYLLQHGADV 81
Cdd:TIGR00870  33 VYRDLEEPKKLNINCPDRlgrsALFVAAIENENLELTEL--LLNLSCRGAVGD--TLLH-AISLEYVDAVEAILLHLLAA 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184  82 HAKdkGGLVPLHNACSYGHYEVAEllvkhgavvnvadlwkfTPLHEAAAKGKYEICKLLLQHGAD-PTKKNRDgntplDL 160
Cdd:TIGR00870 108 FRK--SGPLELANDQYTSEFTPGI-----------------TALHLAAHRQNYEIVKLLLERGASvPARACGD-----FF 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 161 VKdgdTDIQDLLRgdaalldaakkgclarvkklsspdnvncrdtQGRHstPLHLAAGYNNLEVAEYLLQHGADVNAQDKG 240
Cdd:TIGR00870 164 VK---SQGVDSFY-------------------------------HGES--PLNAAACLGSPSIVALLSEDPADILTADSL 207
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462521184 241 GLIPLH-------NAASY------------GHVDVAALLIKYNACVNATDkwaFTPLHEAAQKGRTQLCALLLA 295
Cdd:TIGR00870 208 GNTLLHllvmeneFKAEYeelscqmynfalSLLDKLRDSKELEVILNHQG---LTPLKLAAKEGRIVLFRLKLA 278
PHA02798 PHA02798
ankyrin-like protein; Provisional
46-235 1.19e-06

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 51.76  E-value: 1.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184  46 VNCRDIEgrQSTPL-----HFAAGYNRVSVVEYLLQHGADVHAKDKGGLVPLHNACSYGHY---EVAELLVKHGAVVNVA 117
Cdd:PHA02798   64 VNGLDNE--YSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYInnlEILLFMIENGADTTLL 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 118 DLWKFTPLHEAAAKGKY---EICKLLLQHGAD-PTKKNRDGNTPLDL-----VKDGDTDIQDLLRGDAALLD----AAKK 184
Cdd:PHA02798  142 DKDGFTMLQVYLQSNHHidiEIIKLLLEKGVDiNTHNNKEKYDTLHCyfkynIDRIDADILKLFVDNGFIINkenkSHKK 221
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462521184 185 GCLA----------RVKK-----LSSPDNVNCRDTQGrhSTPLHLAAGYNNLEVAEYLLQHGADVN 235
Cdd:PHA02798  222 KFMEylnsllydnkRFKKnildfIFSYIDINQVDELG--FNPLYYSVSHNNRKIFEYLLQLGGDIN 285
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
57-86 1.49e-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: 44.97  E-value: 1.49e-06
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2462521184  57 TPLHFAAG-YNRVSVVEYLLQHGADVHAKDK 86
Cdd:pfam00023   4 TPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
PHA02859 PHA02859
ankyrin repeat protein; Provisional
32-158 2.08e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 49.05  E-value: 2.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184  32 GDVETVKK-LCTVQSVNcrdieGRQSTPLH--FAAGYNRVSVVEYLLQHGADVHAKDKG-GLVPLHNACSYG---HYEVA 104
Cdd:PHA02859   32 DDIEGVKKwIKFVNDCN-----DLYETPIFscLEKDKVNVEILKFLIENGADVNFKTRDnNLSALHHYLSFNknvEPEIL 106
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462521184 105 ELLVKHGAVVNVADLWKFTPLHE--AAAKGKYEICKLLLQHGADPTKKNRDGNTPL 158
Cdd:PHA02859  107 KILIDSGSSITEEDEDGKNLLHMymCNFNVRINVIKLLIDSGVSFLNKDFDNNNIL 162
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
210-236 3.82e-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.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 43.79  E-value: 3.82e-06
                          10        20
                  ....*....|....*....|....*..
gi 2462521184 210 TPLHLAAGYNNLEVAEYLLQHGADVNA 236
Cdd:pfam13606   4 TPLHLAARNGRLEIVKLLLENGADINA 30
PLN03123 PLN03123
poly [ADP-ribose] polymerase; Provisional
554-678 4.15e-06

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215590 [Multi-domain]  Cd Length: 981  Bit Score: 50.17  E-value: 4.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 554 NERMLFHGSPFVN--AIIHKGFdeRHA-----YIGGMFGAGIYFAENSSKSNQYvygigggtgcpvhkdrsCYICHRQ-- 624
Cdd:PLN03123  825 NRMLLWHGSRLTNfvGILSQGL--RIAppeapATGYMFGKGVYFADLVSKSAQY-----------------CYTDRKNpv 885
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462521184 625 --LLFCRVTLGKSFLQFSAMKMAHSPPGHHSVTGRPSVNGLAlAEYVIYRGEQAYP 678
Cdd:PLN03123  886 glMLLSEVALGEIYELKKAKYMDKPPRGKHSTKGLGKTVPQE-SEFVKWRDDVVVP 940
SAM_TAL cd09523
SAM domain of TAL subfamily; SAM (sterile alpha motif) domain of TAL (Tsg101-associated ligase) ...
402-462 4.96e-06

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


Pssm-ID: 188922  Cd Length: 65  Bit Score: 44.59  E-value: 4.96e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462521184 402 GVDFSITQFVRNLGLEHLMDIFEREQITLDVLVEMGHKELKEIGINAYGHRHKLIKGVERL 462
Cdd:cd09523     3 GVDPQLVNLLNELSAEHYLPVFARHRITMETLSTMTDEDLKKIGIHEIGLRKEILRAAQEL 63
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
210-236 5.60e-06

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: 43.35  E-value: 5.60e-06
                           10        20
                   ....*....|....*....|....*..
gi 2462521184  210 TPLHLAAGYNNLEVAEYLLQHGADVNA 236
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
SAM_ASZ1 cd09521
SAM domain of ASZ1 subfamily; SAM (sterile alpha motif) domain of ASZ1 (Ankyrin, SAM, leucine ...
410-462 8.47e-06

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


Pssm-ID: 188920  Cd Length: 64  Bit Score: 43.81  E-value: 8.47e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462521184 410 FVRNLGLEHLMDIFEREQITLDVLVEMGHKELKEIGINAYGHRHKLIKGVERL 462
Cdd:cd09521    11 FLHGLELGHLTPLFKEHDVTFSQLLKMTEEDLEKIGITQPGDQKKILDAIKEV 63
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
17-229 1.63e-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: 47.95  E-value: 1.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184  17 GNSEADRQLLEAAKAGDV--ETVKKLCTvqsvnCRDIEGRqsTPLHFAAGYNRVSVVEYLLQHGADVHAKDKGGLVPLH- 93
Cdd:cd21882    40 GVNEAIMLLLEAAPDSGNpkELVNAPCT-----DEFYQGQ--TALHIAIENRNLNLVRLLVENGADVSARATGRFFRKSp 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184  94 -NACSYGHYevaellvkhgavvnvadlwkftPLHEAAAKGKYEICKLLLQHGADP-TKKNRD--GNTPLDLVkdgdTDIQ 169
Cdd:cd21882   113 gNLFYFGEL----------------------PLSLAACTNQEEIVRLLLENGAQPaALEAQDslGNTVLHAL----VLQA 166
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462521184 170 DLLRGDAALLDAAKKGCL---ARVKKLSSPDNVNCRdtQGRhsTPLHLAAGYNNLEVAEYLLQ 229
Cdd:cd21882   167 DNTPENSAFVCQMYNLLLsygAHLDPTQQLEEIPNH--QGL--TPLKLAAVEGKIVMFQHILQ 225
Ank_4 pfam13637
Ankyrin repeats (many copies);
25-75 1.64e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.65  E-value: 1.64e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462521184  25 LLEAAKAGDVETVKKL-CTVQSVNCRDIEGRqsTPLHFAAGYNRVSVVEYLL 75
Cdd:pfam13637   5 LHAAAASGHLELLRLLlEKGADINAVDGNGE--TALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
208-315 2.00e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 47.68  E-value: 2.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 208 HSTPLHLAAGYNNLEVAEYLLQHGADVNAQDKGGLIPLHNAASYGHVDVAALLIKYNACVNATDKWAFTPLHEAAQKGRT 287
Cdd:PHA02875    2 DQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDV 81
                          90       100       110
                  ....*....|....*....|....*....|
gi 2462521184 288 QLCALLLAHG--ADPTLKnQEGQTPLDLVS 315
Cdd:PHA02875   82 KAVEELLDLGkfADDVFY-KDGMTPLHLAT 110
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
57-83 2.13e-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: 41.86  E-value: 2.13e-05
                          10        20
                  ....*....|....*....|....*..
gi 2462521184  57 TPLHFAAGYNRVSVVEYLLQHGADVHA 83
Cdd:pfam13606   4 TPLHLAARNGRLEIVKLLLENGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
122-152 2.34e-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: 2.34e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2462521184 122 FTPLHEAAAK-GKYEICKLLLQHGADPTKKNR 152
Cdd:pfam00023   3 NTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
161-313 2.35e-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: 2.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 161 VKDGDTDIQDLLrgdaalLDAAKKGclarvKKLSSPDNVNCRDTQGRHSTPLHLAAGYNNLEVAEYLLQHGADVNAQDKG 240
Cdd:cd22196    58 LHNGQNDTISLL------LDIAEKT-----GNLKEFVNAAYTDSYYKGQTALHIAIERRNMHLVELLVQNGADVHARASG 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 241 --------------GLIPLHNAASYGHVDVAALLIK---YNACVNATDKWAFTPLH---EAAQ------KGRTQLCALLL 294
Cdd:cd22196   127 effkkkkggpgfyfGELPLSLAACTNQLDIVKFLLEnphSPADISARDSMGNTVLHalvEVADntpentKFVTKMYNEIL 206
                         170       180
                  ....*....|....*....|....*.
gi 2462521184 295 AHGAD--PTLK-----NQEGQTPLDL 313
Cdd:cd22196   207 ILGAKirPLLKleeitNKKGLTPLKL 232
PHA02876 PHA02876
ankyrin repeat protein; Provisional
256-322 3.05e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 47.37  E-value: 3.05e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462521184 256 VAALLIKYNACVNATDKWAFTPLHEAAQKGRTQLCALLLAHGADptlknqegqtpLDLVSADDVSAL 322
Cdd:PHA02876  160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGAD-----------VNIIALDDLSVL 215
SAM_Ste11_fungal cd09534
SAM domain of Ste11_fungal subfamily; SAM (sterile alpha motif) domain of Ste11 subfamily is a ...
406-462 3.93e-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: 3.93e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462521184 406 SITQFVRNLGLEHLMDIFEREQITLDVLVEMGHKELKEIGINAYGHRHKLIKGVERL 462
Cdd:cd09534     5 FVEEWLNELNCGQYLDIFEKNLITGDLLLELDKEALKELGITKVGDRIRLLRAIKSL 61
Ank_4 pfam13637
Ankyrin repeats (many copies);
177-228 4.20e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.49  E-value: 4.20e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462521184 177 ALLDAAKKGCLARVKKL-SSPDNVNCRDTQGRhsTPLHLAAGYNNLEVAEYLL 228
Cdd:pfam13637   4 ALHAAAASGHLELLRLLlEKGADINAVDGNGE--TALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
1-160 6.40e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 46.40  E-value: 6.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184   1 MGNEN-VQQLLQEGIS--LGNSEADRQLLEAAKAGDVETV----KKLCtvqSVNCRDIEGRQSTPLHFAAGYNRVSVVEY 73
Cdd:PLN03192  535 TGNAAlLEELLKAKLDpdIGDSKGRTPLHIAASKGYEDCVlvllKHAC---NVHIRDANGNTALWNAISAKHHKIFRILY 611
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184  74 LLQHGADVHAkdkGGLVpLHNACSYGHYEVAELLVKHGAVVNVADLWKFTPLHEAAAKGKYEICKLLLQHGADPTKKNRD 153
Cdd:PLN03192  612 HFASISDPHA---AGDL-LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTD 687

                  ....*...
gi 2462521184 154 GN-TPLDL 160
Cdd:PLN03192  688 DDfSPTEL 695
SAM_sec23ip-like cd09516
SAM domain of sec23ip-like subfamily; SAM (sterile alpha motif) domain of Sec23ip-like (Sec23 ...
393-456 7.42e-05

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


Pssm-ID: 188915  Cd Length: 69  Bit Score: 41.24  E-value: 7.42e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462521184 393 SSLEKKEVPGVDFSITQfvrnLGLEHLMDIFEREQITLDVLVEMGHKELKEIGInAYGHRHKLI 456
Cdd:cd09516     2 SVEEQEEPLTLEEDLEK----LGLSEYFDTFEKEKIDMESLLLCSESDLKEMGI-PMGPRKKLL 60
PHA02859 PHA02859
ankyrin repeat protein; Provisional
208-279 9.44e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 44.04  E-value: 9.44e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462521184 208 HSTPLH--LAAGYNNLEVAEYLLQHGADVNAQDKG-GLIPLHNAASYG---HVDVAALLIKYNACVNATDKWAFTPLH 279
Cdd:PHA02859   51 YETPIFscLEKDKVNVEILKFLIENGADVNFKTRDnNLSALHHYLSFNknvEPEILKILIDSGSSITEEDEDGKNLLH 128
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
122-149 1.11e-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: 1.11e-04
                           10        20
                   ....*....|....*....|....*...
gi 2462521184  122 FTPLHEAAAKGKYEICKLLLQHGADPTK 149
Cdd:smart00248   3 RTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
276-322 1.12e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 40.34  E-value: 1.12e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2462521184 276 TPLHEAAQKGRTQLCALLLAHGADPTLKNQEGQTPLDL-VSADDVSAL 322
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFaASNGNVEVL 50
PHA02743 PHA02743
Viral ankyrin protein; Provisional
50-145 1.24e-04

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 43.27  E-value: 1.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184  50 DIEGRQSTplHFAAGYNRVSVV---EYLLQHGADVHAKDKG-GLVPLHNACSYGHYEVAELLVKH-GAVVNVADLWKFTP 124
Cdd:PHA02743   54 DHHGRQCT--HMVAWYDRANAVmkiELLVNMGADINARELGtGNTLLHIAASTKNYELAEWLCRQlGVNLGAINYQHETA 131
                          90       100
                  ....*....|....*....|.
gi 2462521184 125 LHEAAAKGKYEICKLLLQHGA 145
Cdd:PHA02743  132 YHIAYKMRDRRMMEILRANGA 152
SAM_ANKS3 cd09519
SAM domain of ANKS3 subfamily; SAM (sterile alpha motif) domain of ANKS3 subfamily is a ...
407-464 1.57e-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: 1.57e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462521184 407 ITQFVRNLGLEHLMDIFEREQITLDVLVEMGHKELKEIGINAYGHRHKLIKGVERLIS 464
Cdd:cd09519     7 LSELLEQIGCSKYLPIFEEQDIDLRIFLTLTESDLKEIGITLFGPKRKMTSAIARWHS 64
SAM_Arap1,2,3 cd09490
SAM domain of Arap1,2,3 (angiotensin receptor-associated protein); SAM (sterile alpha motif) ...
402-461 1.66e-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: 1.66e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462521184 402 GVDFSITQFVRNLGLEHLMDIFEREQ-ITLDVLVEMGHKELKEIGINAYGHRHKLIKGVER 461
Cdd:cd09490     1 EADLDIAEWLASIHLEQYLDLFREHGyVTATDCQGINDSRLKQIGISPTGHRRRILKQLPI 61
PLN03124 PLN03124
poly [ADP-ribose] polymerase; Provisional
484-682 2.47e-04

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215591 [Multi-domain]  Cd Length: 643  Bit Score: 44.44  E-value: 2.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 484 LIDLSPDDKEFQSVEEEMQSTvrehRDGGHAGGIFNRYNILKIQKvcnkklwERYTHRRKEVSEeNHNhaneRML-FHGS 562
Cdd:PLN03124  430 LEPLDTDSEEFSMIAKYLENT----HGQTHSGYTLEIVQIFKVSR-------EGEDERFQKFSS-TKN----RMLlWHGS 493
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 563 PFVN--AIIHKGFdeRHA-----YIGGMFGAGIYFAENSSKSNQYVYgigGGTGCPVHkdrscyichrQLLFCRVTLGK- 634
Cdd:PLN03124  494 RLTNwtGILSQGL--RIAppeapSTGYMFGKGVYFADMFSKSANYCY---ASAANPDG----------VLLLCEVALGDm 558
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462521184 635 -SFLQFS--AMKMahsPPGHHSVTG---------------------------RPSVNG-LALAEYVIYRGEQAYPEYLI 682
Cdd:PLN03124  559 nELLQADynANKL---PPGKLSTKGvgrtvpdpseaktledgvvvplgkpveSPYSKGsLEYNEYIVYNVDQIRMRYVL 634
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
57-83 2.80e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.34  E-value: 2.80e-04
                           10        20
                   ....*....|....*....|....*..
gi 2462521184   57 TPLHFAAGYNRVSVVEYLLQHGADVHA 83
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02946 PHA02946
ankyin-like protein; Provisional
18-172 3.35e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 43.50  E-value: 3.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184  18 NSEADRQLLEAAK-AGDVETVKKLCTVQSVNCRDIE-------------GRQSTPLHFAAGYNRVSVVEYLLQHGADVHA 83
Cdd:PHA02946   21 NLDVFRNMLQAIEpSGNYHILHAYCGIKGLDERFVEellhrgyspnetdDDGNYPLHIASKINNNRIVAMLLTHGADPNA 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184  84 KDKGGLVPLHnACSYGHYEVAE---LLVKHGAVVNVA-DLWKFTPL---------------------------------- 125
Cdd:PHA02946  101 CDKQHKTPLY-YLSGTDDEVIErinLLVQYGAKINNSvDEEGCGPLlactdpservfkkimsigfearivdkfgknhihr 179
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462521184 126 HEAAAKGKYEICKLLLQHGADPTKKNRDGNTPLDLVKD---GDTDIQDLL 172
Cdd:PHA02946  180 HLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIVCSktvKNVDIINLL 229
SAM_ANKS6 cd09518
SAM domain of ANKS6 (or SamCystin) subfamily; SAM (sterile alpha motif) domain of ANKS6 (or ...
407-462 3.50e-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: 3.50e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462521184 407 ITQFVRNLGLEHLMDIFEREQITLDVLVEMGHKELKEIGINAYGHRHKLIKGVERL 462
Cdd:cd09518     8 LSGILRKLSLEKYQPIFEEQEVDMEAFLTLTDGDLKELGIKTDGPRQQILAAISEL 63
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
187-313 4.99e-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: 4.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 187 LARVKKLSSPD---NVNCRDTQGRHSTPLHLAAGYNNLEVAEYLLQHGADVNAQDKG--------------GLIPLHNAA 249
Cdd:cd22193    52 LDIAEKTDNLKrfiNAEYTDEYYEGQTALHIAIERRQGDIVALLVENGADVHAHAKGrffqpkyqgegfyfGELPLSLAA 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 250 SYGHVDVAALLIK---YNACVNATDKWAFTPLH---EAAQKGRTQ------LCALLLAHGAD--PTLK-----NQEGQTP 310
Cdd:cd22193   132 CTNQPDIVQYLLEnehQPADIEAQDSRGNTVLHalvTVADNTKENtkfvtrMYDMILIRGAKlcPTVEleeirNNDGLTP 211

                  ...
gi 2462521184 311 LDL 313
Cdd:cd22193   212 LQL 214
Ank_2 pfam12796
Ankyrin repeats (3 copies);
278-311 7.20e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 39.33  E-value: 7.20e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2462521184 278 LHEAAQKGRTQLCALLLAHGADPTLKNQEGQTPL 311
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTAL 34
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
123-313 7.25e-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: 42.94  E-value: 7.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 123 TPLHEAA---AKGKYEICKLLLQhgADPtkknrDGNTPLDLVKDGDTDiqDLLRGDAALLDAAKKGCLARVKKL-SSPDN 198
Cdd:cd21882    28 TCLHKAAlnlNDGVNEAIMLLLE--AAP-----DSGNPKELVNAPCTD--EFYQGQTALHIAIENRNLNLVRLLvENGAD 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 199 VNCRDTQ-------------GRHstPLHLAAGYNNLEVAEYLLQHGAD---VNAQDKGGLIPLHnaasyghvdvaALLIK 262
Cdd:cd21882    99 VSARATGrffrkspgnlfyfGEL--PLSLAACTNQEEIVRLLLENGAQpaaLEAQDSLGNTVLH-----------ALVLQ 165
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462521184 263 YNacvNATDKWAFTplheaaqkgrTQLCALLLAHGA--DPTLK-----NQEGQTPLDL 313
Cdd:cd21882   166 AD---NTPENSAFV----------CQMYNLLLSYGAhlDPTQQleeipNHQGLTPLKL 210
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
123-147 7.28e-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: 37.24  E-value: 7.28e-04
                          10        20
                  ....*....|....*....|....*
gi 2462521184 123 TPLHEAAAKGKYEICKLLLQHGADP 147
Cdd:pfam13606   4 TPLHLAARNGRLEIVKLLLENGADI 28
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
91-116 8.18e-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: 37.18  E-value: 8.18e-04
                           10        20
                   ....*....|....*....|....*.
gi 2462521184   91 PLHNACSYGHYEVAELLVKHGAVVNV 116
Cdd:smart00248   5 PLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
241-272 8.21e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 37.27  E-value: 8.21e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2462521184 241 GLIPLHNAA-SYGHVDVAALLIKYNACVNATDK 272
Cdd:pfam00023   2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PHA02946 PHA02946
ankyin-like protein; Provisional
71-245 9.31e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 42.35  E-value: 9.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184  71 VEYLLQHGADVHAKDKGGLVPLHNACSYGHYEVAELLVKHGAVVNVADLWKFTPLHEAAAKGK--YEICKLLLQHGADPT 148
Cdd:PHA02946   55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYGAKIN 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 149 KK-NRDGNTPLDLVKDGDTDIQDLLRG---DAALLDAAKKGCLARVKKLSSPD--------NVNCRDTQGRH--STPLHL 214
Cdd:PHA02946  135 NSvDEEGCGPLLACTDPSERVFKKIMSigfEARIVDKFGKNHIHRHLMSDNPKastiswmmKLGISPSKPDHdgNTPLHI 214
                         170       180       190
                  ....*....|....*....|....*....|...
gi 2462521184 215 AAG--YNNLEVAEYLLQhGADVNAQDKGGLIPL 245
Cdd:PHA02946  215 VCSktVKNVDIINLLLP-STDVNKQNKFGDSPL 246
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
91-116 1.31e-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.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 36.47  E-value: 1.31e-03
                          10        20
                  ....*....|....*....|....*.
gi 2462521184  91 PLHNACSYGHYEVAELLVKHGAVVNV 116
Cdd:pfam13606   5 PLHLAARNGRLEIVKLLLENGADINA 30
PHA02946 PHA02946
ankyin-like protein; Provisional
200-278 1.73e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 41.58  E-value: 1.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 200 NCRDTQGRHstPLHLAAGYNNLEVAEYLLQHGADVNAQDKGGLIPLHNAASYGH--VDVAALLIKYNACV-NATDKWAFT 276
Cdd:PHA02946   66 NETDDDGNY--PLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYGAKInNSVDEEGCG 143

                  ..
gi 2462521184 277 PL 278
Cdd:PHA02946  144 PL 145
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
88-118 2.09e-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: 2.09e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2462521184  88 GLVPLHNAC-SYGHYEVAELLVKHGAVVNVAD 118
Cdd:pfam00023   2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PHA02946 PHA02946
ankyin-like protein; Provisional
268-318 2.17e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 41.19  E-value: 2.17e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462521184 268 NATDKWAFTPLHEAAQKGRTQLCALLLAHGADPTLKNQEGQTPLDLVSADD 318
Cdd:PHA02946   66 NETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTD 116
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
275-304 2.24e-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: 2.24e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2462521184 275 FTPLHEAA-QKGRTQLCALLLAHGADPTLKN 304
Cdd:pfam00023   3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
63-158 2.87e-03

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 41.05  E-value: 2.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184  63 AGYNRVSVVEYLLQHGADVHAKDKGGLVPLHNAC--SYGHYEVAELLVKHGAVVNVADLWKFTPLH-------------- 126
Cdd:PHA02716  292 ARNIDISVVYSFLQPGVKLHYKDSAGRTCLHQYIlrHNISTDIIKLLHEYGNDLNEPDNIGNTVLHtylsmlsvvnildp 371
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2462521184 127 EAAAKGKYEICKLLLQHGADPTKKNRDGNTPL 158
Cdd:PHA02716  372 ETDNDIRLDVIQCLISLGADITAVNCLGYTPL 403
PHA02884 PHA02884
ankyrin repeat protein; Provisional
222-315 3.61e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 39.97  E-value: 3.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 222 EVAEYLLQHGADVNAQDKGGLI----PLHNAASYGHVDVAALLIKYNACVNATDKWA-FTPLHEAAQKGRTQLCALLLAH 296
Cdd:PHA02884   47 DIIDAILKLGADPEAPFPLSENsktnPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAkITPLYISVLHGCLKCLEILLSY 126
                          90
                  ....*....|....*....
gi 2462521184 297 GADPTLKNQEGQTPLDLVS 315
Cdd:PHA02884  127 GADINIQTNDMVTPIELAL 145
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
215-300 3.70e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 40.62  E-value: 3.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 215 AAGYNNLEVAEYLLQHGADVNAQDKGGLIPLHNAASYGHVDVAALLIKYNACVNATDKWAFTPLHEAAQKGRTQLCALL- 293
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILy 611

                  ....*...
gi 2462521184 294 -LAHGADP 300
Cdd:PLN03192  612 hFASISDP 619
SAM_DDHD2 cd09585
SAM domain of DDHD2; SAM (sterile alpha motif) domain of DDHD2 group is a potential ...
407-461 3.95e-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: 3.95e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2462521184 407 ITQFVRNLGLEHLMDIFEREQITLDVLVEMGHKELKEIGInAYGHRHKLIKGVER 461
Cdd:cd09585    12 LEETLKKLGLSEYCDVFEKEKIDLEALALCQERDLKDLGI-PLGPRKKILNYIRR 65
SAM_WDSUB1 cd09505
SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins ...
412-462 4.35e-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: 36.53  E-value: 4.35e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462521184 412 RNLGLEHLMDIFEREQITLDVLVEMGHKEL-KEIGINAYGHRHKLIKGVERL 462
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 ...
402-462 5.06e-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: 5.06e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462521184 402 GVDFSITQFVRNlglehlmdiFEREQITLDVLVEMGHKELKEIGINAYGHRHKLIKGVERL 462
Cdd:cd09511    15 GLDDCLQQYIYT---------FEREKVTGEQLLNLSPQDLENLGVTKIGHQELILEAVELL 66
PHA02946 PHA02946
ankyin-like protein; Provisional
105-278 5.15e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 40.04  E-value: 5.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 105 ELLVKHGAVVNVADLWKFTPLHEAAAKGKYEICKLLLQHGADPTKKNRDGNTPLDLVKDGDTDIQD----LLRGDAALLD 180
Cdd:PHA02946   56 EELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIErinlLVQYGAKINN 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521184 181 AA-KKGC---LA------RV--KKLSSPDNVNCRDTQGRHSTPLHLAAGYNNLEVAEYLLQHGADVNAQDKGGLIPLHNA 248
Cdd:PHA02946  136 SVdEEGCgplLActdpseRVfkKIMSIGFEARIVDKFGKNHIHRHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIV 215
                         170       180       190
                  ....*....|....*....|....*....|..
gi 2462521184 249 AS--YGHVDVAALLIKyNACVNATDKWAFTPL 278
Cdd:PHA02946  216 CSktVKNVDIINLLLP-STDVNKQNKFGDSPL 246
 
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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