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Conserved domains on  [gi|190587828|gb|EDV27870|]
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hypothetical protein TRIADDRAFT_52847 [Trichoplax adhaerens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FAM220 pfam15487
FAM220 family; This protein family is a domain of unknown function which is found in ...
 6-283 6.32e-116

FAM220 family; This protein family is a domain of unknown function which is found in eukaryotes. Proteins in this family are typically between 217 and 277 amino acids in length. There are two completely conserved residues (S and L) that may be functionally important.


:

Pssm-ID: 464743  Cd Length: 275  Bit Score: 341.78  E-value: 6.32e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190587828    6 EEIRDLLCVSRLSYSAIDDEDFSQQDVPHVTLAKHPFHRSSSYPFQQPtpPPGASGTVKSN-SAKVRSGRVLSPLSDITK 84
Cdd:pfam15487   1 RDLRDLLCVSRLSVKDSDEEDFSQDSLKLACKLKKRSQKRSPSPSDAP--SWTAQPVVDSNkRSRAKEAKSLEMKRDQSK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190587828   85 KkEDIRPNSGPVRPLHTINSKATSKTPQTIAKQQAVLPSIqpliKTEDLESIITRVDSNILENWLKESNKLVMRLHEWWQ 164
Cdd:pfam15487  79 A-GLLRHSGGKVLPPLKESSRRSSTSAATRVKAVALSPAP----KEENFDGILCYIDEAVVSDWLGRANKSVDNLTDWCH 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190587828  165 TGDNMTQFSHFWISVFPSQQKLDLLKMELEIIRDHLIILL--GGQQSQLEESTLEQLIYAIIPEFPTRFAVNR-QLFFLD 241
Cdd:pfam15487 154 KGDNFVQFAHFWLSGLPDHQKLDLIQMEVGIIRDEPQSAFpkGLQGTELELSDLRSLLSAILHEYPEVLLNDEtKYVFLD 233

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 190587828  242 VVYTLSSGRHKAYKKLLSAVKCKTSNRTCAQIVLAIRSHALL 283
Cdd:pfam15487 234 YLNPLTSERTTEYKKLLSDVKCTTDNKQFAQWVLAMRSFALL 275
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
295-473 3.70e-24

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 101.95  E-value: 3.70e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190587828 295 KLQQENSRFQHDKVSNITEIICQAIQLQYLDVIQYILDDQVlSITSLLPEDYNRLFFTgVMANSSSILTYLIQKhpgKID 374
Cdd:COG0666   71 LLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGA-DVNARDKDGETPLHLA-AYNGNLEIVKLLLEA---GAD 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190587828 375 INHHGESGNTPLHAAIGRGDTLMVKWLLKIGAKVNVINEqcNNATPLHLAVMNGDDAMVRSLVAAGADVYAKMGD-LTPL 453
Cdd:COG0666  146 VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDN--DGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDgKTAL 223

                        170       180
                 ....*....|....*....|
gi 190587828 454 DIAKDFEMDNLIELLNAIHL 473
Cdd:COG0666  224 DLAAENGNLEIVKLLLEAGA 243
 
Name Accession Description Interval E-value
FAM220 pfam15487
FAM220 family; This protein family is a domain of unknown function which is found in ...
 6-283 6.32e-116

FAM220 family; This protein family is a domain of unknown function which is found in eukaryotes. Proteins in this family are typically between 217 and 277 amino acids in length. There are two completely conserved residues (S and L) that may be functionally important.


Pssm-ID: 464743  Cd Length: 275  Bit Score: 341.78  E-value: 6.32e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190587828    6 EEIRDLLCVSRLSYSAIDDEDFSQQDVPHVTLAKHPFHRSSSYPFQQPtpPPGASGTVKSN-SAKVRSGRVLSPLSDITK 84
Cdd:pfam15487   1 RDLRDLLCVSRLSVKDSDEEDFSQDSLKLACKLKKRSQKRSPSPSDAP--SWTAQPVVDSNkRSRAKEAKSLEMKRDQSK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190587828   85 KkEDIRPNSGPVRPLHTINSKATSKTPQTIAKQQAVLPSIqpliKTEDLESIITRVDSNILENWLKESNKLVMRLHEWWQ 164
Cdd:pfam15487  79 A-GLLRHSGGKVLPPLKESSRRSSTSAATRVKAVALSPAP----KEENFDGILCYIDEAVVSDWLGRANKSVDNLTDWCH 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190587828  165 TGDNMTQFSHFWISVFPSQQKLDLLKMELEIIRDHLIILL--GGQQSQLEESTLEQLIYAIIPEFPTRFAVNR-QLFFLD 241
Cdd:pfam15487 154 KGDNFVQFAHFWLSGLPDHQKLDLIQMEVGIIRDEPQSAFpkGLQGTELELSDLRSLLSAILHEYPEVLLNDEtKYVFLD 233

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 190587828  242 VVYTLSSGRHKAYKKLLSAVKCKTSNRTCAQIVLAIRSHALL 283
Cdd:pfam15487 234 YLNPLTSERTTEYKKLLSDVKCTTDNKQFAQWVLAMRSFALL 275
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
295-473 3.70e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 101.95  E-value: 3.70e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190587828 295 KLQQENSRFQHDKVSNITEIICQAIQLQYLDVIQYILDDQVlSITSLLPEDYNRLFFTgVMANSSSILTYLIQKhpgKID 374
Cdd:COG0666   71 LLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGA-DVNARDKDGETPLHLA-AYNGNLEIVKLLLEA---GAD 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190587828 375 INHHGESGNTPLHAAIGRGDTLMVKWLLKIGAKVNVINEqcNNATPLHLAVMNGDDAMVRSLVAAGADVYAKMGD-LTPL 453
Cdd:COG0666  146 VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDN--DGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDgKTAL 223

                        170       180
                 ....*....|....*....|
gi 190587828 454 DIAKDFEMDNLIELLNAIHL 473
Cdd:COG0666  224 DLAAENGNLEIVKLLLEAGA 243
Ank_2 pfam12796
Ankyrin repeats (3 copies);
354-446 2.33e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 71.30  E-value: 2.33e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190587828  354 VMANSSSILTYLIQKHPgkiDINHHGESGNTPLHAAIGRGDTLMVKWLLKigakVNVINEQCNNATPLHLAVMNGDDAMV 433
Cdd:pfam12796   5 AKNGNLELVKLLLENGA---DANLQDKNGRTALHLAAKNGHLEIVKLLLE----HADVNLKDNGRTALHYAARSGHLEIV 77

                          90
                  ....*....|...
gi 190587828  434 RSLVAAGADVYAK 446
Cdd:pfam12796  78 KLLLEKGADINVK 90
PHA03095 PHA03095
ankyrin-like protein; Provisional
 374-455 5.69e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 58.11  E-value: 5.69e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190587828 374 DINHHGESGNTPLHAAIGRG---DTLMVKWLLKIGAKVNVInEQCnNATPLHLAVMNGDDA-MVRSLVAAGADVYAKMG- 448
Cdd:PHA03095  39 DVNFRGEYGKTPLHLYLHYSsekVKDIVRLLLEAGADVNAP-ERC-GFTPLHLYLYNATTLdVIKLLIKAGADVNAKDKv 116


                 ....*..
gi 190587828 449 DLTPLDI 455
Cdd:PHA03095 117 GRTPLHV 123
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 373-443 5.78e-04

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 42.31  E-value: 5.78e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 190587828 373 IDINHHGESGNTPLHAAIGRGDTLMVKWLLKigAKVNVINEQCNNA-----TPLHLAVMNGDDAMVRSLVAAGADV 443
Cdd:cd22192   42 CDLFQRGALGETALHVAALYDNLEAAVVLME--AAPELVNEPMTSDlyqgeTALHIAVVNQNLNLVRELIARGADV 115
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 382-410 1.04e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.41  E-value: 1.04e-03
                           10        20
                   ....*....|....*....|....*....
gi 190587828   382 GNTPLHAAIGRGDTLMVKWLLKIGAKVNV 410
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
FAM220 pfam15487
FAM220 family; This protein family is a domain of unknown function which is found in ...
 6-283 6.32e-116

FAM220 family; This protein family is a domain of unknown function which is found in eukaryotes. Proteins in this family are typically between 217 and 277 amino acids in length. There are two completely conserved residues (S and L) that may be functionally important.


Pssm-ID: 464743  Cd Length: 275  Bit Score: 341.78  E-value: 6.32e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190587828    6 EEIRDLLCVSRLSYSAIDDEDFSQQDVPHVTLAKHPFHRSSSYPFQQPtpPPGASGTVKSN-SAKVRSGRVLSPLSDITK 84
Cdd:pfam15487   1 RDLRDLLCVSRLSVKDSDEEDFSQDSLKLACKLKKRSQKRSPSPSDAP--SWTAQPVVDSNkRSRAKEAKSLEMKRDQSK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190587828   85 KkEDIRPNSGPVRPLHTINSKATSKTPQTIAKQQAVLPSIqpliKTEDLESIITRVDSNILENWLKESNKLVMRLHEWWQ 164
Cdd:pfam15487  79 A-GLLRHSGGKVLPPLKESSRRSSTSAATRVKAVALSPAP----KEENFDGILCYIDEAVVSDWLGRANKSVDNLTDWCH 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190587828  165 TGDNMTQFSHFWISVFPSQQKLDLLKMELEIIRDHLIILL--GGQQSQLEESTLEQLIYAIIPEFPTRFAVNR-QLFFLD 241
Cdd:pfam15487 154 KGDNFVQFAHFWLSGLPDHQKLDLIQMEVGIIRDEPQSAFpkGLQGTELELSDLRSLLSAILHEYPEVLLNDEtKYVFLD 233

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 190587828  242 VVYTLSSGRHKAYKKLLSAVKCKTSNRTCAQIVLAIRSHALL 283
Cdd:pfam15487 234 YLNPLTSERTTEYKKLLSDVKCTTDNKQFAQWVLAMRSFALL 275
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
295-473 3.70e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 101.95  E-value: 3.70e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190587828 295 KLQQENSRFQHDKVSNITEIICQAIQLQYLDVIQYILDDQVlSITSLLPEDYNRLFFTgVMANSSSILTYLIQKhpgKID 374
Cdd:COG0666   71 LLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGA-DVNARDKDGETPLHLA-AYNGNLEIVKLLLEA---GAD 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190587828 375 INHHGESGNTPLHAAIGRGDTLMVKWLLKIGAKVNVINEqcNNATPLHLAVMNGDDAMVRSLVAAGADVYAKMGD-LTPL 453
Cdd:COG0666  146 VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDN--DGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDgKTAL 223

                        170       180
                 ....*....|....*....|
gi 190587828 454 DIAKDFEMDNLIELLNAIHL 473
Cdd:COG0666  224 DLAAENGNLEIVKLLLEAGA 243
Ank_2 pfam12796
Ankyrin repeats (3 copies);
354-446 2.33e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 71.30  E-value: 2.33e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190587828  354 VMANSSSILTYLIQKHPgkiDINHHGESGNTPLHAAIGRGDTLMVKWLLKigakVNVINEQCNNATPLHLAVMNGDDAMV 433
Cdd:pfam12796   5 AKNGNLELVKLLLENGA---DANLQDKNGRTALHLAAKNGHLEIVKLLLE----HADVNLKDNGRTALHYAARSGHLEIV 77

                          90
                  ....*....|...
gi 190587828  434 RSLVAAGADVYAK 446
Cdd:pfam12796  78 KLLLEKGADINVK 90
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
354-474 9.18e-15

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 74.61  E-value: 9.18e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190587828 354 VMANSSSILTYLIQKhpgKIDINHHGESGNTPLHAAIGRGDTLMVKWLLKIGAKVNVINEqcNNATPLHLAVMNGDDAMV 433
Cdd:COG0666  161 AANGNLEIVKLLLEA---GADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN--DGKTALDLAAENGNLEIV 235

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 190587828 434 RSLVAAGADVYAKMGD-LTPLDIAKDFEMDNLIELLNAIHLE 474
Cdd:COG0666  236 KLLLEAGADLNAKDKDgLTALLLAAAAGAALIVKLLLLALLL 277
Ank_2 pfam12796
Ankyrin repeats (3 copies);
386-468 3.97e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 59.36  E-value: 3.97e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190587828  386 LHAAIGRGDTLMVKWLLKIGAKVNVINeqCNNATPLHLAVMNGDDAMVRSLVaAGADVYAKMGDLTPLDIAKDFEMDNLI 465
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQD--KNGRTALHLAAKNGHLEIVKLLL-EHADVNLKDNGRTALHYAARSGHLEIV 77


                  ...
gi 190587828  466 ELL 468
Cdd:pfam12796  78 KLL 80
PHA03095 PHA03095
ankyrin-like protein; Provisional
 374-455 5.69e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 58.11  E-value: 5.69e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190587828 374 DINHHGESGNTPLHAAIGRG---DTLMVKWLLKIGAKVNVInEQCnNATPLHLAVMNGDDA-MVRSLVAAGADVYAKMG- 448
Cdd:PHA03095  39 DVNFRGEYGKTPLHLYLHYSsekVKDIVRLLLEAGADVNAP-ERC-GFTPLHLYLYNATTLdVIKLLIKAGADVNAKDKv 116


                 ....*..
gi 190587828 449 DLTPLDI 455
Cdd:PHA03095 117 GRTPLHV 123
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
347-468 1.27e-08

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 56.12  E-value: 1.27e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190587828 347 NRLFFTGVMANSSSILTYLIQKHPGKIDINHHGESGNTPLHAAIGRGDTLMVKWLLKIGAKVNVINEqcNNATPLHLAVM 426
Cdd:COG0666   19 LLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD--GGNTLLHAAAR 96

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 190587828 427 NGDDAMVRSLVAAGADVYAKMGD-LTPLDIAKDFEMDNLIELL 468
Cdd:COG0666   97 NGDLEIVKLLLEAGADVNARDKDgETPLHLAAYNGNLEIVKLL 139
Ank_4 pfam13637
Ankyrin repeats (many copies);
382-437 7.30e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.81  E-value: 7.30e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 190587828  382 GNTPLHAAIGRGDTLMVKWLLKIGAKVNVINEQCNnaTPLHLAVMNGDDAMVRSLV 437
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGE--TALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 373-455 9.35e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 54.26  E-value: 9.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190587828 373 IDINHHGESGNTPLHAAIGRGDTL-MVKWLLKIGAKVNVINEqcNNATPLH--LAVMNGDDAMVRSLVAAGADVYA-KMG 448
Cdd:PHA03095  74 ADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAGADVNAKDK--VGRTPLHvyLSGFNINPKVIRLLLRKGADVNAlDLY 151


                 ....*..
gi 190587828 449 DLTPLDI 455
Cdd:PHA03095 152 GMTPLAV 158
PHA03095 PHA03095
ankyrin-like protein; Provisional
 356-459 1.34e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 53.88  E-value: 1.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190587828 356 ANSSSILTYLIQKhpgKIDINHHGESGNTPLHAAIG--RGDTLMVKWLLKIGAKVNVINeqCNNATPLHLAVMNG--DDA 431
Cdd:PHA03095  94 ATTLDVIKLLIKA---GADVNAKDKVGRTPLHVYLSgfNINPKVIRLLLRKGADVNALD--LYGMTPLAVLLKSRnaNVE 168

                         90       100
                 ....*....|....*....|....*....
gi 190587828 432 MVRSLVAAGADVYAK-MGDLTPLDIAKDF 459
Cdd:PHA03095 169 LLRLLIDAGADVYAVdDRFRSLLHHHLQS 197
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 315-468 6.18e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 51.53  E-value: 6.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190587828 315 ICQAIQLQYLDVIQYILDDQVlSITSLLPEDYNRLffTGVMANSSSILTYLIQKHPGKIDINHHGEsgNTPLHAAIGRGD 394
Cdd:PHA02875   6 LCDAILFGELDIARRLLDIGI-NPNFEIYDGISPI--KLAMKFRDSEAIKLLMKHGAIPDVKYPDI--ESELHDAVEEGD 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 190587828 395 TLMVKWLLKIGAKVN-VINEQCNnaTPLHLAVMNGDDAMVRSLVAAGADVYAKMGD-LTPLDIAKDFEMDNLIELL 468
Cdd:PHA02875  81 VKAVEELLDLGKFADdVFYKDGM--TPLHLATILKKLDIMKLLIARGADPDIPNTDkFSPLHLAVMMGDIKGIELL 154
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 309-456 1.13e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 50.73  E-value: 1.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190587828 309 SNITEIICQAIQLQYLDVIQYILDDQVlsITSLLP------EDYNRLFFTGVMAN-----SSSILTYLIQKHPGKI---- 373
Cdd:PHA02874  66 TKIPHPLLTAIKIGAHDIIKLLIDNGV--DTSILPipciekDMIKTILDCGIDVNikdaeLKTFLHYAIKKGDLESikml 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190587828 374 -----DINHHGESGNTPLHAAIGRGDTLMVKWLLKIGAKVNVINEQCNnaTPLHLAVMNGDDAMVRSLVAAGADVYAKMG 448
Cdd:PHA02874 144 feygaDVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGE--SPLHNAAEYGDYACIKLLIDHGNHIMNKCK 221


                 ....*....
gi 190587828 449 D-LTPLDIA 456
Cdd:PHA02874 222 NgFTPLHNA 230
Ank_2 pfam12796
Ankyrin repeats (3 copies);
315-412 1.64e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 46.26  E-value: 1.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190587828  315 ICQAIQLQYLDVIQYILDDQVlSITSLLPEDYNRLFFTgVMANSSSILTYLIQKHPGKIDinhhgESGNTPLHAAIGRGD 394
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGA-DANLQDKNGRTALHLA-AKNGHLEIVKLLLEHADVNLK-----DNGRTALHYAARSGH 73

                          90
                  ....*....|....*...
gi 190587828  395 TLMVKWLLKIGAKVNVIN 412
Cdd:pfam12796  74 LEIVKLLLEKGADINVKD 91
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 382-413 3.80e-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: 43.43  E-value: 3.80e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 190587828  382 GNTPLHAAIGR-GDTLMVKWLLKIGAKVNVINE 413
Cdd:pfam00023   2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
365-424 1.20e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.72  E-value: 1.20e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 190587828  365 LIQKHPgkIDINHHGESGNTPLHAAIGRGDTLMVKWLLKIGAKVNVINEQCNnaTPLHLA 424
Cdd:pfam13857   1 LLEHGP--IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGL--TALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
346-402 1.34e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.26  E-value: 1.34e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 190587828  346 YNRLFFTGVMANSSSILTYLIQKhpgKIDINHHGESGNTPLHAAIGRGDTLMVKWLL 402
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEK---GADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 373-434 4.88e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 45.79  E-value: 4.88e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 190587828 373 IDINHHGESGNTPLHAAIGRGDTLMVKWLLKIGAKVNVINEqcNNATPLHLAVMNGDDAMVR 434
Cdd:PHA03095 248 ISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSS--DGNTPLSLMVRNNNGRAVR 307
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 384-468 6.46e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 44.98  E-value: 6.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190587828 384 TPLHAAIGRGDTLMVKWLLKIGAKVNVinEQCNNATPLHLAVMNGDDAMVRSLVAAGA--DVYAKMGDLTPLDIAKDFEM 461
Cdd:PHA02875 137 SPLHLAVMMGDIKGIELLIDHKACLDI--EDCCGCTPLIIAMAKGDIAICKMLLDSGAniDYFGKNGCVAALCYAIENNK 214


                 ....*..
gi 190587828 462 DNLIELL 468
Cdd:PHA02875 215 IDIVRLF 221
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 364-461 8.07e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 45.04  E-value: 8.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190587828 364 YLIQKhpgKIDINHHGESGNTPLHAAIGRGDTLMVKWLLKIGAKVNVINEQCNnaTPLHLAVMNGDDAMVRSLVAAGADV 443
Cdd:PHA03100 177 YLLSY---GVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGD--TPLHIAILNNNKEIFKLLLNNGPSI 251

                         90       100
                 ....*....|....*....|...
gi 190587828 444 -----YAKMGDLTPLDIAKDFEM 461
Cdd:PHA03100 252 ktiieTLLYFKDKDLNTITKIKM 274
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 381-456 1.34e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 44.10  E-value: 1.34e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 190587828 381 SGNTPLHAAIGRGDTLMVKWLLKIGAKVNVINeQCNNaTPLHLAVMNGDDAMVRSLVAAGA--DVYAKMGDlTPLDIA 456
Cdd:PHA02878 167 KGNTALHYATENKDQRLTELLLSYGANVNIPD-KTNN-SPLHHAVKHYNKPIVHILLENGAstDARDKCGN-TPLHIS 241
Ank_5 pfam13857
Ankyrin repeats (many copies);
401-456 1.40e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.64  E-value: 1.40e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 190587828  401 LLKIGAkVNVINEQCNNATPLHLAVMNGDDAMVRSLVAAGADVYAKMGD-LTPLDIA 456
Cdd:pfam13857   1 LLEHGP-IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEgLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 393-468 1.42e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.50  E-value: 1.42e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 190587828 393 GDTLMVKWLLKIGAKVNVINEqcNNATPLHLAVMNGDDAMVRSLVAAGADVYA-KMGDLTPLDIAKDFEMDNLIELL 468
Cdd:PTZ00322  93 GDAVGARILLTGGADPNCRDY--DGRTPLHIACANGHVQVVRVLLEFGADPTLlDKDGKTPLELAEENGFREVVQLL 167
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 382-456 1.74e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 43.83  E-value: 1.74e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 190587828 382 GNTPLHAAIGRGDTLMVKWLLKIGAKVNVINEqcNNATPLHLAVMNGDDAMVRSLVAAGADVYAKMG-DLTPLDIA 456
Cdd:PHA02875 102 GMTPLHLATILKKLDIMKLLIARGADPDIPNT--DKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCcGCTPLIIA 175
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 382-410 2.35e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 38.39  E-value: 2.35e-04
                          10        20
                  ....*....|....*....|....*....
gi 190587828  382 GNTPLHAAIGRGDTLMVKWLLKIGAKVNV 410
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
ActA pfam05058
ActA Protein; The ActA family is found in Listeria and is associated with motility. ActA ...
 57-126 2.37e-04

ActA Protein; The ActA family is found in Listeria and is associated with motility. ActA protein acts as a scaffold to assemble and activate host cell actin cytoskeletal factors at the bacterial surface, resulting in directional actin polymerization and propulsion of the bacterium through the cytoplasm of the host cell.


Pssm-ID: 282861 [Multi-domain]  Cd Length: 633  Bit Score: 43.80  E-value: 2.37e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 190587828   57 PGASGTVKSNSAKVRSGRVLSPLSDITKKKedirPNSGPVRPLHTINSKATSK------TPQTIAKQQAVLPSIQP 126
Cdd:pfam05058 441 PFASSPVPSLSPKVSKISAPALISDITKKT----PFKNPSQPLNVFNKKTTTKtvtkkpTPVKTAPKLAELPATKP 512
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 357-468 2.70e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 43.12  E-value: 2.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190587828 357 NSSSILTYLIQKHpgkIDINHHGESGNTPLHAAI--GRGDTLMVKWLLKIGAKVNVINE---------------QCNNaT 419
Cdd:PHA03100 119 NSYSIVEYLLDNG---ANVNIKNSDGENLLHLYLesNKIDLKILKLLIDKGVDINAKNRvnyllsygvpinikdVYGF-T 194

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 190587828 420 PLHLAVMNGDDAMVRSLVAAGADVYAKMGD-LTPLDIAKDFEMDNLIELL 468
Cdd:PHA03100 195 PLHYAVYNNNPEFVKYLLDLGANPNLVNKYgDTPLHIAILNNNKEIFKLL 244
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 373-443 5.78e-04

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 42.31  E-value: 5.78e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 190587828 373 IDINHHGESGNTPLHAAIGRGDTLMVKWLLKigAKVNVINEQCNNA-----TPLHLAVMNGDDAMVRSLVAAGADV 443
Cdd:cd22192   42 CDLFQRGALGETALHVAALYDNLEAAVVLME--AAPELVNEPMTSDlyqgeTALHIAVVNQNLNLVRELIARGADV 115
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 416-446 7.62e-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: 36.88  E-value: 7.62e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 190587828  416 NNATPLHLAV-MNGDDAMVRSLVAAGADVYAK 446
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNAR 32
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 416-445 9.94e-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: 36.47  E-value: 9.94e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 190587828  416 NNATPLHLAVMNGDDAMVRSLVAAGADVYA 445
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 382-410 1.04e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.41  E-value: 1.04e-03
                           10        20
                   ....*....|....*....|....*....
gi 190587828   382 GNTPLHAAIGRGDTLMVKWLLKIGAKVNV 410
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA03095 PHA03095
ankyrin-like protein; Provisional
 381-443 1.16e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 41.16  E-value: 1.16e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 190587828 381 SGNTPLHAAIGRG---DTLMVKWLLKiGAKVNVINEqcNNATPLHLAVMNGDDAMVRSLVAAGADV 443
Cdd:PHA03095 221 LGNTPLHSMATGSsckRSLVLPLLIA-GISINARNR--YGQTPLHYAAVFNNPRACRRLIALGADI 283
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 375-456 1.39e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 41.02  E-value: 1.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190587828 375 INHHGESGNTPLHAAIGR-GDTLMVKWLLKIGAKVNvINEQCNNATPLHLAVMngDDAMVRSLVAAGADVYAKMGD-LTP 452
Cdd:PHA02878 227 TDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVN-AKSYILGLTALHSSIK--SERKLKLLLEYGADINSLNSYkLTP 303


                 ....
gi 190587828 453 LDIA 456
Cdd:PHA02878 304 LSSA 307
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 379-446 1.71e-03

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 41.02  E-value: 1.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190587828 379 GESGNTPLHAAI-----GRGDTLMVkwLLKIGAKVN----VINEQCNNA-----TPLHLAVMNGDDAMVRSLVAAGADVY 444
Cdd:cd21882   23 GATGKTCLHKAAlnlndGVNEAIML--LLEAAPDSGnpkeLVNAPCTDEfyqgqTALHIAIENRNLNLVRLLVENGADVS 100


                 ..
gi 190587828 445 AK 446
Cdd:cd21882  101 AR 102
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 365-465 1.78e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 41.01  E-value: 1.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190587828 365 LIQKHPGKIDINHHGESGNTP------LHAAIGRGDTLMVKWLLKIGakVNVINEQCNNATPLHLAVMNGDDAMVRSLVA 438
Cdd:PLN03192 599 ISAKHHKIFRILYHFASISDPhaagdlLCTAAKRNDLTAMKELLKQG--LNVDSEDHQGATALQVAMAEDHVDMVRLLIM 676

                         90       100       110
                 ....*....|....*....|....*....|..
gi 190587828 439 AGADV-----YAKMGDLTPLDIAKDFEMDNLI 465
Cdd:PLN03192 677 NGADVdkantDDDFSPTELRELLQKRELGHSI 708
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 416-445 1.86e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.64  E-value: 1.86e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 190587828   416 NNATPLHLAVMNGDDAMVRSLVAAGADVYA 445
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02741 PHA02741
hypothetical protein; Provisional
 374-436 3.33e-03

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 38.49  E-value: 3.33e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 190587828 374 DIN-HHGESGNTPLHAAIGRGDTLMVKWLL-KIGAKVNVINeqCNNATPLHLAVMNGDDAMVRSL 436
Cdd:PHA02741  89 DINaQEMLEGDTALHLAAHRRDHDLAEWLCcQPGIDLHFCN--ADNKSPFELAIDNEDVAMMQIL 151
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 374-446 4.00e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 39.65  E-value: 4.00e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 190587828 374 DINHHGESGNTPLHAAIGR--GDTLMVKWLLKIGAKVNVINeqCNNATPLHLAVMNGDD--AMVRSLVAAGADVYAK 446
Cdd:PHA03100  98 NVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKN--SDGENLLHLYLESNKIdlKILKLLIDKGVDINAK 172
Ank_4 pfam13637
Ankyrin repeats (many copies);
419-456 6.09e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 34.94  E-value: 6.09e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 190587828  419 TPLHLAVMNGDDAMVRSLVAAGADVYAKMGD-LTPLDIA 456
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNgETALHFA 41
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 362-471 6.62e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 38.82  E-value: 6.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190587828 362 LTYLIQKHPGKIDINHHgeSGNTPLHAAIGRGDTLMVKWLLKIGAKVNVINEQcNNATPLHLAVMNGDDAMVRSLVAAGA 441
Cdd:PHA02875 150 GIELLIDHKACLDIEDC--CGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKN-GCVAALCYAIENNKIDIVRLFIKRGA 226

                         90       100       110
                 ....*....|....*....|....*....|....
gi 190587828 442 D---VYAKMGDL-TPLDIAKDFEMDNLIELLNAI 471
Cdd:PHA02875 227 DcniMFMIEGEEcTILDMICNMCTNLESEAIDAL 260
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 383-468 7.76e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 38.89  E-value: 7.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190587828 383 NTPLHAAIGRGD-TLMVKWLLKIGAKVNVINeqCNNATPLHLAVMNG-DDAMVRSLVAAGADVYAKMG-DLTPLDIAK-- 457
Cdd:PHA02876 274 NTPLHHASQAPSlSRLVPKLLERGADVNAKN--IKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRlYITPLHQAStl 351

                         90
                 ....*....|.
gi 190587828 458 DFEMDNLIELL 468
Cdd:PHA02876 352 DRNKDIVITLL 362
 
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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