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Conserved domains on  [gi|157823313|ref|NP_001102459|]
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KN motif and ankyrin repeat domain-containing protein 3 [Rattus norvegicus]

Protein Classification

ankyrin repeat domain-containing protein( domain architecture ID 13778391)

ankyrin (ANK) repeat domain-containing protein may be involved in mediating protein-protein interactions; ankyrin (ANK) repeat domain-containing protein may be involved in mediating protein-protein interactions; similar to Homo sapiens ankyrin repeat and SOCS box protein 7 isoform 1; ankyrin repeat (ANK) domain-containing protein may be involved in mediating protein-protein interactions

Gene Ontology:  GO:0005515
PubMed:  15152081|17176038

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
604-792 7.69e-42

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 154.73  E-value: 7.69e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823313 604 LLAHVVNLADGNGNTALHYSVSHGNLAISSLLLDTGVcDVNHQNRAGYSALMLAAltsvgkEEEDMAVVQRLFSMG-DVN 682
Cdd:COG0666   75 AAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGA-DVNARDKDGETPLHLAA------YNGNLEIVKLLLEAGaDVN 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823313 683 AKASQtGQTALMLAISHGHQDMVAALLECGADVNVQDADGATALMCASEYGRLDTVQLLLAQpGCDLTILDNEGTSALAI 762
Cdd:COG0666  148 AQDND-GNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA-GADVNAKDNDGKTALDL 225

                        170       180       190
                 ....*....|....*....|....*....|
gi 157823313 763 ALEAEQDEVAALLHAHLTSNHHDSQEQSTP 792
Cdd:COG0666  226 AAENGNLEIVKLLLEAGADLNAKDKDGLTA 255
KN_motif pfam12075
KN motif; This small motif is found at the N-terminus of Kank proteins and has been called the ...
 32-73 4.09e-18

KN motif; This small motif is found at the N-terminus of Kank proteins and has been called the KN (for Kank N-terminal) motif. This protein is found in eukaryotes. Proteins in this family are typically between 413 to 1202 amino acids in length. This protein is found associated with pfam00023. This protein has two conserved sequence motifs: TPYG and LDLDF. Kank1 was obtained by positional cloning of a tumor suppressor gene in renal cell carcinoma, while the other members were found by homology search. The family is involved in the regulation of actin polymerization and cell motility through signaling pathways containing PI3K/Akt and/or unidentified modulators/effectors.


:

Pssm-ID: 432311  Cd Length: 39  Bit Score: 78.16  E-value: 4.09e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 157823313   32 PYSVETPYGFHLDLDFLKYVEEIERGPASRRApgpPHARRPR 73
Cdd:pfam12075   1 PYSVETPYGFHLDLDFLKYVEDIESGQTIRRA---RVQRRPR 39
COG4913 super family cl25907
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
129-322 1.10e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


The actual alignment was detected with superfamily member COG4913:

Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.59  E-value: 1.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823313  129 VEH--TLLETSRRLEQAQAQERALSPARAATRSpRGSGRSSPAPNPALASPSPVLAspGPAQLQLVREQMAVALRRLREL 206
Cdd:COG4913   231 VEHfdDLERAHEALEDAREQIELLEPIRELAER-YAAARERLAELEYLRAALRLWF--AQRRLELLEAELEELRAELARL 307

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823313  207 EDQARALP----ELQEQVRALRAEKARLLAGRVQP-EQDVEievrpDKLSQLRRLTERLATSDRGVRSRASPRAEDPDGL 281
Cdd:COG4913   308 EAELERLEarldALREELDELEAQIRGNGGDRLEQlEREIE-----RLERELEERERRRARLEALLAALGLPLPASAEEF 382

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 157823313  282 AARRSEGALQVLDPASRTPDGEPQTREAGTEVVPETREVDA 322
Cdd:COG4913   383 AALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRE 423
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
604-792 7.69e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 154.73  E-value: 7.69e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823313 604 LLAHVVNLADGNGNTALHYSVSHGNLAISSLLLDTGVcDVNHQNRAGYSALMLAAltsvgkEEEDMAVVQRLFSMG-DVN 682
Cdd:COG0666   75 AAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGA-DVNARDKDGETPLHLAA------YNGNLEIVKLLLEAGaDVN 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823313 683 AKASQtGQTALMLAISHGHQDMVAALLECGADVNVQDADGATALMCASEYGRLDTVQLLLAQpGCDLTILDNEGTSALAI 762
Cdd:COG0666  148 AQDND-GNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA-GADVNAKDNDGKTALDL 225

                        170       180       190
                 ....*....|....*....|....*....|
gi 157823313 763 ALEAEQDEVAALLHAHLTSNHHDSQEQSTP 792
Cdd:COG0666  226 AAENGNLEIVKLLLEAGADLNAKDKDGLTA 255
Ank_2 pfam12796
Ankyrin repeats (3 copies);
620-719 3.00e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.16  E-value: 3.00e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823313  620 LHYSVSHGNLAISSLLLDTGvCDVNHQNRAGYSALMLAALTsvGKEEedmaVVQRLFSMGDVNAKASqtGQTALMLAISH 699
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENG-ADANLQDKNGRTALHLAAKN--GHLE----IVKLLLEHADVNLKDN--GRTALHYAARS 71

                          90       100
                  ....*....|....*....|
gi 157823313  700 GHQDMVAALLECGADVNVQD 719
Cdd:pfam12796  72 GHLEIVKLLLEKGADINVKD 91
KN_motif pfam12075
KN motif; This small motif is found at the N-terminus of Kank proteins and has been called the ...
 32-73 4.09e-18

KN motif; This small motif is found at the N-terminus of Kank proteins and has been called the KN (for Kank N-terminal) motif. This protein is found in eukaryotes. Proteins in this family are typically between 413 to 1202 amino acids in length. This protein is found associated with pfam00023. This protein has two conserved sequence motifs: TPYG and LDLDF. Kank1 was obtained by positional cloning of a tumor suppressor gene in renal cell carcinoma, while the other members were found by homology search. The family is involved in the regulation of actin polymerization and cell motility through signaling pathways containing PI3K/Akt and/or unidentified modulators/effectors.


Pssm-ID: 432311  Cd Length: 39  Bit Score: 78.16  E-value: 4.09e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 157823313   32 PYSVETPYGFHLDLDFLKYVEEIERGPASRRApgpPHARRPR 73
Cdd:pfam12075   1 PYSVETPYGFHLDLDFLKYVEDIESGQTIRRA---RVQRRPR 39
PHA03095 PHA03095
ankyrin-like protein; Provisional
 609-765 5.84e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 62.35  E-value: 5.84e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823313 609 VNLADGNGNTALHYSVSHGN---LAISSLLLDTGVcDVNHQNRAGYSALMLAALTSvgkEEEDmaVVQRLFSMG-DVNAK 684
Cdd:PHA03095  40 VNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGA-DVNAPERCGFTPLHLYLYNA---TTLD--VIKLLIKAGaDVNAK 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823313 685 aSQTGQTAL--MLAISHGHQDMVAALLECGADVNVQDADGATALMCASEYGR--LDTVQLLLAQpGCDLTILDNEGTSAL 760
Cdd:PHA03095 114 -DKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanVELLRLLIDA-GADVYAVDDRFRSLL 191


                 ....*
gi 157823313 761 AIALE 765
Cdd:PHA03095 192 HHHLQ 196
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 689-717 3.31e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.42  E-value: 3.31e-05
                           10        20
                   ....*....|....*....|....*....
gi 157823313   689 GQTALMLAISHGHQDMVAALLECGADVNV 717
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 616-726 7.02e-05

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: 46.16  E-value: 7.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823313 616 GNTALHYSVSHGNLAISSLLLDTGVCDVNH----QNRAGYSALMLAALTsvgkeeEDMAVVQRLFSMG-DV-NAKASQT- 688
Cdd:cd22192   51 GETALHVAALYDNLEAAVVLMEAAPELVNEpmtsDLYQGETALHIAVVN------QNLNLVRELIARGaDVvSPRATGTf 124

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 157823313 689 -----------GQTALMLAISHGHQDMVAALLECGADVNVQDADGATAL 726
Cdd:cd22192  125 frpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
129-322 1.10e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.59  E-value: 1.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823313  129 VEH--TLLETSRRLEQAQAQERALSPARAATRSpRGSGRSSPAPNPALASPSPVLAspGPAQLQLVREQMAVALRRLREL 206
Cdd:COG4913   231 VEHfdDLERAHEALEDAREQIELLEPIRELAER-YAAARERLAELEYLRAALRLWF--AQRRLELLEAELEELRAELARL 307

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823313  207 EDQARALP----ELQEQVRALRAEKARLLAGRVQP-EQDVEievrpDKLSQLRRLTERLATSDRGVRSRASPRAEDPDGL 281
Cdd:COG4913   308 EAELERLEarldALREELDELEAQIRGNGGDRLEQlEREIE-----RLERELEERERRRARLEALLAALGLPLPASAEEF 382

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 157823313  282 AARRSEGALQVLDPASRTPDGEPQTREAGTEVVPETREVDA 322
Cdd:COG4913   383 AALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRE 423
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
63-326 5.42e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 40.22  E-value: 5.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823313  63 APGPPHARRPRASGKGLAGARSPGAWTSSESLASDDGGASGALSP-GAFPGLSLPPLSPRSfsRNPRVEHTLLETSRRLE 141
Cdd:PRK07003 368 PGGGVPARVAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPkAAAAAAATRAEAPPA--APAPPATADRGDDAADG 445

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823313 142 QAQAQERAlsPARAATRSPRGSGRSSPAPNPALAS-------------PSPVLASPGPAQLQLVREQMAVAL-RRLRELE 207
Cdd:PRK07003 446 DAPVPAKA--NARASADSRCDERDAQPPADSGSASapasdappdaafePAPRAAAPSAATPAAVPDARAPAAaSREDAPA 523

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823313 208 DQARALPELQEQVRALRAEKARllAGRVQPEQDVeievrpdklsqLRRLTERLaTSDRGVRSRASPRAEDPDGLAARRSE 287
Cdd:PRK07003 524 AAAPPAPEARPPTPAAAAPAAR--AGGAAAALDV-----------LRNAGMRV-SSDRGARAAAAAKPAAAPAAAPKPAA 589

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 157823313 288 GALQVLDPASRTPDGEPQTREAGTEVVPETREvDAQAVP 326
Cdd:PRK07003 590 PRVAVQVPTPRARAATGDAPPNGAARAEQAAE-SRGAPP 627
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 616-717 8.26e-03

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 39.68  E-value: 8.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823313  616 GNTALHYSVSHG-NLAISSLLLdtgvcdvNHQNRA--GYSALMLAALTSVGKEEEDMAVVQRLFSMGD----VNAKASQT 688
Cdd:TIGR00870  52 GRSALFVAAIENeNLELTELLL-------NLSCRGavGDTLLHAISLEYVDAVEAILLHLLAAFRKSGplelANDQYTSE 124

                          90       100       110
                  ....*....|....*....|....*....|..
gi 157823313  689 ---GQTALMLAISHGHQDMVAALLECGADVNV 717
Cdd:TIGR00870 125 ftpGITALHLAAHRQNYEIVKLLLERGASVPA 156
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
604-792 7.69e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 154.73  E-value: 7.69e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823313 604 LLAHVVNLADGNGNTALHYSVSHGNLAISSLLLDTGVcDVNHQNRAGYSALMLAAltsvgkEEEDMAVVQRLFSMG-DVN 682
Cdd:COG0666   75 AAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGA-DVNARDKDGETPLHLAA------YNGNLEIVKLLLEAGaDVN 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823313 683 AKASQtGQTALMLAISHGHQDMVAALLECGADVNVQDADGATALMCASEYGRLDTVQLLLAQpGCDLTILDNEGTSALAI 762
Cdd:COG0666  148 AQDND-GNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA-GADVNAKDNDGKTALDL 225

                        170       180       190
                 ....*....|....*....|....*....|
gi 157823313 763 ALEAEQDEVAALLHAHLTSNHHDSQEQSTP 792
Cdd:COG0666  226 AAENGNLEIVKLLLEAGADLNAKDKDGLTA 255
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
603-775 1.53e-34

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 133.54  E-value: 1.53e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823313 603 ELLAH--VVNLADGNGNTALHYSVSHGNLAISSLLLDTGVcDVNHQNRAGYSALMLAAltsvgkEEEDMAVVQRLFSMG- 679
Cdd:COG0666  105 LLLEAgaDVNARDKDGETPLHLAAYNGNLEIVKLLLEAGA-DVNAQDNDGNTPLHLAA------ANGNLEIVKLLLEAGa 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823313 680 DVNAKaSQTGQTALMLAISHGHQDMVAALLECGADVNVQDADGATALMCASEYGRLDTVQLLLAQpGCDLTILDNEGTSA 759
Cdd:COG0666  178 DVNAR-DNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA-GADLNAKDKDGLTA 255

                        170
                 ....*....|....*.
gi 157823313 760 LAIALEAEQDEVAALL 775
Cdd:COG0666  256 LLLAAAAGAALIVKLL 271
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
604-778 6.91e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 128.92  E-value: 6.91e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823313 604 LLAHVVNLADGNGNTALHYSVSHGNLAISSLLLDTGVcDVNHQNRAGYSALMLAAltsvgkEEEDMAVVQRLFSMG-DVN 682
Cdd:COG0666   42 LALLALALADALGALLLLAAALAGDLLVALLLLAAGA-DINAKDDGGNTLLHAAA------RNGDLEIVKLLLEAGaDVN 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823313 683 AKASQtGQTALMLAISHGHQDMVAALLECGADVNVQDADGATALMCASEYGRLDTVQLLLAQpGCDLTILDNEGTSALAI 762
Cdd:COG0666  115 ARDKD-GETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEA-GADVNARDNDGETPLHL 192

                        170
                 ....*....|....*.
gi 157823313 763 ALEAEQDEVAALLHAH 778
Cdd:COG0666  193 AAENGHLEIVKLLLEA 208
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
604-757 5.57e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 103.11  E-value: 5.57e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823313 604 LLAH--VVNLADGNGNTALHYSVSHGNLAISSLLLDTGVcDVNHQNRAGYSALMLAAltsvgkEEEDMAVVQRLFSMG-D 680
Cdd:COG0666  139 LLEAgaDVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGA-DVNARDNDGETPLHLAA------ENGHLEIVKLLLEAGaD 211

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157823313 681 VNAKASQtGQTALMLAISHGHQDMVAALLECGADVNVQDADGATALMCASEYGRLDTVQLLLAQPGCDLTILDNEGT 757
Cdd:COG0666  212 VNAKDND-GKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
603-775 2.62e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 100.80  E-value: 2.62e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823313 603 ELLAHVVNLADGNGNTALHYSVSHGNLAISSLLLDTGVCDVNHQNRAGYSALMLAAltsvgkEEEDMAVVQRLFSMGDVN 682
Cdd:COG0666    7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAA------LAGDLLVALLLLAAGADI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823313 683 AKASQTGQTALMLAISHGHQDMVAALLECGADVNVQDADGATALMCASEYGRLDTVQLLLAQpGCDLTILDNEGTSALAI 762
Cdd:COG0666   81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA-GADVNAQDNDGNTPLHL 159

                        170
                 ....*....|...
gi 157823313 763 ALEAEQDEVAALL 775
Cdd:COG0666  160 AAANGNLEIVKLL 172
Ank_2 pfam12796
Ankyrin repeats (3 copies);
620-719 3.00e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.16  E-value: 3.00e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823313  620 LHYSVSHGNLAISSLLLDTGvCDVNHQNRAGYSALMLAALTsvGKEEedmaVVQRLFSMGDVNAKASqtGQTALMLAISH 699
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENG-ADANLQDKNGRTALHLAAKN--GHLE----IVKLLLEHADVNLKDN--GRTALHYAARS 71

                          90       100
                  ....*....|....*....|
gi 157823313  700 GHQDMVAALLECGADVNVQD 719
Cdd:pfam12796  72 GHLEIVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
693-775 3.86e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.77  E-value: 3.86e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823313  693 LMLAISHGHQDMVAALLECGADVNVQDADGATALMCASEYGRLDTVQLLLAQPGCDltiLDNEGTSALAIALEAEQDEVA 772
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN---LKDNGRTALHYAARSGHLEIV 77


                  ...
gi 157823313  773 ALL 775
Cdd:pfam12796  78 KLL 80
KN_motif pfam12075
KN motif; This small motif is found at the N-terminus of Kank proteins and has been called the ...
 32-73 4.09e-18

KN motif; This small motif is found at the N-terminus of Kank proteins and has been called the KN (for Kank N-terminal) motif. This protein is found in eukaryotes. Proteins in this family are typically between 413 to 1202 amino acids in length. This protein is found associated with pfam00023. This protein has two conserved sequence motifs: TPYG and LDLDF. Kank1 was obtained by positional cloning of a tumor suppressor gene in renal cell carcinoma, while the other members were found by homology search. The family is involved in the regulation of actin polymerization and cell motility through signaling pathways containing PI3K/Akt and/or unidentified modulators/effectors.


Pssm-ID: 432311  Cd Length: 39  Bit Score: 78.16  E-value: 4.09e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 157823313   32 PYSVETPYGFHLDLDFLKYVEEIERGPASRRApgpPHARRPR 73
Cdd:pfam12075   1 PYSVETPYGFHLDLDFLKYVEDIESGQTIRRA---RVQRRPR 39
Ank_2 pfam12796
Ankyrin repeats (3 copies);
654-753 1.25e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 78.62  E-value: 1.25e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823313  654 LMLAAltsvgkEEEDMAVVQRLFSMG-DVNAKaSQTGQTALMLAISHGHQDMVAALLECgADVNVQDaDGATALMCASEY 732
Cdd:pfam12796   1 LHLAA------KNGNLELVKLLLENGaDANLQ-DKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARS 71

                          90       100
                  ....*....|....*....|.
gi 157823313  733 GRLDTVQLLLaQPGCDLTILD 753
Cdd:pfam12796  72 GHLEIVKLLL-EKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
653-778 2.03e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 68.83  E-value: 2.03e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823313 653 ALMLAALTSVGKEEEDMAVVQRLFSMGDVNAKASQTGQTALMLAISHGHQDMVAALLECGADVNVQDADGATALMCASEY 732
Cdd:COG0666   18 LLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARN 97

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 157823313 733 GRLDTVQLLLAQpGCDLTILDNEGTSALAIALEAEQDEVAALLHAH 778
Cdd:COG0666   98 GDLEIVKLLLEA-GADVNARDKDGETPLHLAAYNGNLEIVKLLLEA 142
Ank_4 pfam13637
Ankyrin repeats (many copies);
691-742 1.23e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 57.28  E-value: 1.23e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 157823313  691 TALMLAISHGHQDMVAALLECGADVNVQDADGATALMCASEYGRLDTVQLLL 742
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 609-765 5.84e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 62.35  E-value: 5.84e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823313 609 VNLADGNGNTALHYSVSHGN---LAISSLLLDTGVcDVNHQNRAGYSALMLAALTSvgkEEEDmaVVQRLFSMG-DVNAK 684
Cdd:PHA03095  40 VNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGA-DVNAPERCGFTPLHLYLYNA---TTLD--VIKLLIKAGaDVNAK 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823313 685 aSQTGQTAL--MLAISHGHQDMVAALLECGADVNVQDADGATALMCASEYGR--LDTVQLLLAQpGCDLTILDNEGTSAL 760
Cdd:PHA03095 114 -DKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanVELLRLLIDA-GADVYAVDDRFRSLL 191


                 ....*
gi 157823313 761 AIALE 765
Cdd:PHA03095 192 HHHLQ 196
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 609-742 1.11e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 58.14  E-value: 1.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823313 609 VNLADGNGNTALHYSVSH--GNLAISSLLLDTGvCDVNHQNRAGYSALMLAalTSVGKEEEDMavVQRLFSMG-DVNAKA 685
Cdd:PHA03100  99 VNAPDNNGITPLLYAISKksNSYSIVEYLLDNG-ANVNIKNSDGENLLHLY--LESNKIDLKI--LKLLIDKGvDINAKN 173

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157823313 686 S---------------QTGQTALMLAISHGHQDMVAALLECGADVNVQDADGATALMCASEYGRLDTVQLLL 742
Cdd:PHA03100 174 RvnyllsygvpinikdVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLL 245
PHA03095 PHA03095
ankyrin-like protein; Provisional
 589-733 1.55e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 57.73  E-value: 1.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823313 589 PVAGVLRGVKSLGPELLAhvvnlADGNGNTALHYSVSHGNLAISSL--LLDTGVcDVNHQNRAGYSALMLAAltsvgKEE 666
Cdd:PHA03095 200 PRARIVRELIRAGCDPAA-----TDMLGNTPLHSMATGSSCKRSLVlpLLIAGI-SINARNRYGQTPLHYAA-----VFN 268

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157823313 667 EDMAVVqRLFSMG-DVNAkASQTGQTALMLAISHGHQDMVAALLECGADVNVQDAdgatALMCASEYG 733
Cdd:PHA03095 269 NPRACR-RLIALGaDINA-VSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAA----TLNTASVAG 330
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 703-808 3.02e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 57.22  E-value: 3.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823313 703 DMVAA--LLECGADVNVQDADGATALMCASEYGRLDTVQLLLaQPGCDLTILDNEGTSALAIALEAEQDEVAALLHAHLT 780
Cdd:PTZ00322  94 DAVGAriLLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLL-EFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQ 172

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 157823313 781 SNHH----------DSQEQSTPGSPTATLQRDTG--PQPL 808
Cdd:PTZ00322 173 CHFElganakpdsfTGKPPSLEDSPISSHHPDFSavPQPM 212
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 609-765 5.45e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 56.13  E-value: 5.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823313 609 VNLADGNGNTALHYSVSHGNLAISSLLLDTGVCdVNHQNRAGYSALMLAAltsvgkEEEDMAVVQRLFSMGDVNAKASQT 688
Cdd:PHA02874 150 VNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAY-ANVKDNNGESPLHNAA------EYGDYACIKLLIDHGNHIMNKCKN 222

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157823313 689 GQTALMLAISHGHQdmVAALLECGADVNVQDADGATALMCASEYG-RLDTVQLLLAQPGcDLTILDNEGTSALAIALE 765
Cdd:PHA02874 223 GFTPLHNAIIHNRS--AIELLINNASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKA-DISIKDNKGENPIDTAFK 297
Ank_5 pfam13857
Ankyrin repeats (many copies);
708-763 1.89e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.50  E-value: 1.89e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 157823313  708 LLECG-ADVNVQDADGATALMCASEYGRLDTVQLLLAqPGCDLTILDNEGTSALAIA 763
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLA-YGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
680-726 4.07e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.34  E-value: 4.07e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 157823313  680 DVNAKaSQTGQTALMLAISHGHQDMVAALLECGADVNVQDADGATAL 726
Cdd:pfam13857   8 DLNRL-DGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 635-764 5.28e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 53.04  E-value: 5.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823313 635 LLDTGVcDVNHQNRAGYSALMLAAltsvgkEEEDMAVVQRLFSMG-DVNAKaSQTGQTALMLAISHGHQDMVAALLECGA 713
Cdd:PHA02874 110 ILDCGI-DVNIKDAELKTFLHYAI------KKGDLESIKMLFEYGaDVNIE-DDNGCYPIHIAIKHNFFDIIKLLLEKGA 181

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 157823313 714 DVNVQDADGATALMCASEYGRLDTVQLLLAQpGCDLTILDNEGTSALAIAL 764
Cdd:PHA02874 182 YANVKDNNGESPLHNAAEYGDYACIKLLIDH-GNHIMNKCKNGFTPLHNAI 231
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 609-729 6.65e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 52.57  E-value: 6.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823313 609 VNLADGNGNTALHYSVSHGNLAISSLLLDTGvCDVNHQNRAGYSALMLaaltSVGKEEeDMAVVQRLFSMG-DVNAKASQ 687
Cdd:PHA02878 194 VNIPDKTNNSPLHHAVKHYNKPIVHILLENG-ASTDARDKCGNTPLHI----SVGYCK-DYDILKLLLEHGvDVNAKSYI 267

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 157823313 688 TGQTALMLAISHghQDMVAALLECGADVNVQDADGATALMCA 729
Cdd:PHA02878 268 LGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSA 307
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 689-719 7.44e-07

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 46.13  E-value: 7.44e-07
                          10        20        30
                  ....*....|....*....|....*....|..
gi 157823313  689 GQTALMLAISH-GHQDMVAALLECGADVNVQD 719
Cdd:pfam00023   2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 689-748 2.51e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.05  E-value: 2.51e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823313 689 GQTALMLAISHGHQDMVAALLECGADVNVQDADGATALMCASEYGRLDTVQLLLAQPGCD 748
Cdd:PTZ00322 115 GRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCH 174
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 610-742 2.73e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 51.02  E-value: 2.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823313 610 NLADGNGNTALHYSVSHGNLAISSLLLDTGvCDVNHQNRAGYSALMLAAltsvgkeeedMAVVQRLFSMGDVNAKAS--Q 687
Cdd:PLN03192 552 DIGDSKGRTPLHIAASKGYEDCVLVLLKHA-CNVHIRDANGNTALWNAI----------SAKHHKIFRILYHFASISdpH 620

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 157823313 688 TGQTALMLAISHGHQDMVAALLECGADVNVQDADGATALMCASEYGRLDTVQLLL 742
Cdd:PLN03192 621 AAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLI 675
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 609-775 4.83e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 49.96  E-value: 4.83e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823313 609 VNLADGNGNTALHYSVSHGNLAISSLLLDTGVcDVNHQNRAGYSALMLAalTSVGKEEedmaVVQRLFSmgdvnakasqT 688
Cdd:PHA02874  28 INISVDETTTPLIDAIRSGDAKIVELFIKHGA-DINHINTKIPHPLLTA--IKIGAHD----IIKLLID----------N 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823313 689 GQTALMLAISHGHQDMVAALLECGADVNVQDADGATALMCASEYGRLDTVQLLLaQPGCDLTILDNEGTSALAIALEAEQ 768
Cdd:PHA02874  91 GVDTSILPIPCIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLF-EYGADVNIEDDNGCYPIHIAIKHNF 169


                 ....*..
gi 157823313 769 DEVAALL 775
Cdd:PHA02874 170 FDIIKLL 176
Ank_2 pfam12796
Ankyrin repeats (3 copies);
726-792 6.45e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 45.11  E-value: 6.45e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157823313  726 LMCASEYGRLDTVQLLLaQPGCDLTILDNEGTSALAIALEAEQDEVAALLHAHLTSNHHDSQEqsTP 792
Cdd:pfam12796   1 LHLAAKNGNLELVKLLL-ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGR--TA 64
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 620-775 6.97e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 49.87  E-value: 6.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823313 620 LHYSVSHGNLAISSLLLDTGVcdvNHQNRAGYSALMLAALTSVGKEEEDMAVVQRLFSMGDvnakasQTGQTALMLAISH 699
Cdd:PLN03192 498 LQHHKELHDLNVGDLLGDNGG---EHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGD------SKGRTPLHIAASK 568

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823313 700 GHQDMVAALLECGADVNVQDADGATAL------------------------------MC-ASEYGRLDTVQLLLAQpGCD 748
Cdd:PLN03192 569 GYEDCVLVLLKHACNVHIRDANGNTALwnaisakhhkifrilyhfasisdphaagdlLCtAAKRNDLTAMKELLKQ-GLN 647

                        170       180
                 ....*....|....*....|....*..
gi 157823313 749 LTILDNEGTSALAIALEAEQDEVAALL 775
Cdd:PLN03192 648 VDSEDHQGATALQVAMAEDHVDMVRLL 674
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 620-742 7.09e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 49.28  E-value: 7.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823313 620 LHYSVSHGNLAISSLLLDTGvCDVNhQNRAGYSALMLAALTSVGKEEEDMAVVQRLFSMG-DVNAKaSQTGQTALMLAIS 698
Cdd:PHA03100  39 LYLAKEARNIDVVKILLDNG-ADIN-SSTKNNSTPLHYLSNIKYNLTDVKEIVKLLLEYGaNVNAP-DNNGITPLLYAIS 115

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 157823313 699 H--GHQDMVAALLECGADVNVQDADGATALMCASEYGR--LDTVQLLL 742
Cdd:PHA03100 116 KksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLI 163
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 604-715 1.06e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 49.10  E-value: 1.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823313 604 LLAHV--VNLADGNGNTALHYSVSHGNLAISSLLLDTGVCDVNHqnrAGYSALMLAAltsvgkEEEDMAVVQRLFSMG-D 680
Cdd:PLN03192 577 LLKHAcnVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPH---AAGDLLCTAA------KRNDLTAMKELLKQGlN 647

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 157823313 681 VNAKASQtGQTALMLAISHGHQDMVAALLECGADV 715
Cdd:PLN03192 648 VDSEDHQ-GATALQVAMAEDHVDMVRLLIMNGADV 681
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 607-781 1.70e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 48.34  E-value: 1.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823313 607 HVVNLADGNGNTALHYSVSHGN-LAISSLLLDTGVCDVNHQ---------NRAGYSALMLaaLTSVGKEEEDMAVVQ--- 673
Cdd:PHA02878  61 HNVNQPDHRDLTPLHIICKEPNkLGMKEMIRSINKCSVFYTlvaikdafnNRNVEIFKII--LTNRYKNIQTIDLVYidk 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823313 674 -------------RLFSMG-DVNAKASQTGQTALMLAISHGHQDMVAALLECGADVNVQDADGATALMCASEYGRLDTVQ 739
Cdd:PHA02878 139 kskddiieaeitkLLLSYGaDINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVH 218

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 157823313 740 LLLaQPGCDLTILDNEGTSALAIALEAEQD-EVAALLHAHLTS 781
Cdd:PHA02878 219 ILL-ENGASTDARDKCGNTPLHISVGYCKDyDILKLLLEHGVD 260
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 689-717 3.31e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.42  E-value: 3.31e-05
                           10        20
                   ....*....|....*....|....*....
gi 157823313   689 GQTALMLAISHGHQDMVAALLECGADVNV 717
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 615-752 4.03e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 46.91  E-value: 4.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823313 615 NGNTALHYSVSHGNLAISSLLLDTGVcDVNHQNRAGYSALMLAALTSvgkeeeDMAVVQRLFSMGDVNAKASQTGQTALM 694
Cdd:PHA02875 101 DGMTPLHLATILKKLDIMKLLIARGA-DPDIPNTDKFSPLHLAVMMG------DIKGIELLIDHKACLDIEDCCGCTPLI 173

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 157823313 695 LAISHGHQDMVAALLECGADVNVQDADGATALMC-ASEYGRLDTVQLLLAQpGCDLTIL 752
Cdd:PHA02875 174 IAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCyAIENNKIDIVRLFIKR-GADCNIM 231
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 646-783 4.63e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 47.17  E-value: 4.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823313 646 QNRAGYSALMLAALTSVGKEEEDMAVVQRLFSMG----DVNAKASqtgqtaLMLAISHGHQDMVAALLECGADVNVQDAD 721
Cdd:PLN03192 484 QTRQEDNVVILKNFLQHHKELHDLNVGDLLGDNGgehdDPNMASN------LLTVASTGNAALLEELLKAKLDPDIGDSK 557

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157823313 722 GATALMCASEYGRLDTVQLLLAQpGCDLTILDNEGTSALAIALEAEQDEVAALLH--AHLTSNH 783
Cdd:PLN03192 558 GRTPLHIAASKGYEDCVLVLLKH-ACNVHIRDANGNTALWNAISAKHHKIFRILYhfASISDPH 620
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 616-726 7.02e-05

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: 46.16  E-value: 7.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823313 616 GNTALHYSVSHGNLAISSLLLDTGVCDVNH----QNRAGYSALMLAALTsvgkeeEDMAVVQRLFSMG-DV-NAKASQT- 688
Cdd:cd22192   51 GETALHVAALYDNLEAAVVLMEAAPELVNEpmtsDLYQGETALHIAVVN------QNLNLVRELIARGaDVvSPRATGTf 124

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 157823313 689 -----------GQTALMLAISHGHQDMVAALLECGADVNVQDADGATAL 726
Cdd:cd22192  125 frpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
PHA03095 PHA03095
ankyrin-like protein; Provisional
 612-726 1.13e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 45.40  E-value: 1.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823313 612 ADGNGNTALHY--SVSHGNLAISSLLLDTGvCDVNHQNRAGYSALMLAALTSVGKEeedmAVVQRLFSMG-DVNAKaSQT 688
Cdd:PHA03095 183 VDDRFRSLLHHhlQSFKPRARIVRELIRAG-CDPAATDMLGNTPLHSMATGSSCKR----SLVLPLLIAGiSINAR-NRY 256

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 157823313 689 GQTALMLAISHGHQDMVAALLECGADVNVQDADGATAL 726
Cdd:PHA03095 257 GQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPL 294
Ank_2 pfam12796
Ankyrin repeats (3 copies);
603-647 1.24e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 41.64  E-value: 1.24e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 157823313  603 ELLAHVVNLADGNGNTALHYSVSHGNLAISSLLLDTGvCDVNHQN 647
Cdd:pfam12796  48 LLLEHADVNLKDNGRTALHYAARSGHLEIVKLLLEKG-ADINVKD 91
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 689-717 1.43e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 39.55  E-value: 1.43e-04
                          10        20
                  ....*....|....*....|....*....
gi 157823313  689 GQTALMLAISHGHQDMVAALLECGADVNV 717
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 665-742 2.68e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 44.67  E-value: 2.68e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157823313 665 EEEDMAVVQRLFSMG-DVNAKASQTgQTALMLAISHGHQDMVAALLECGADVNVQDADGATALMCASEYGRLDTVQLLL 742
Cdd:PHA02876 154 QQDELLIAEMLLEGGaDVNAKDIYC-ITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAII 231
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 615-775 3.04e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 44.21  E-value: 3.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823313 615 NGNTALHYSVSHGNLAISSLLLDTGVcDVNHQNRAGYSALMLAA----------LTSVGK-----------------EEE 667
Cdd:PHA02875   1 MDQVALCDAILFGELDIARRLLDIGI-NPNFEIYDGISPIKLAMkfrdseaiklLMKHGAipdvkypdieselhdavEEG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823313 668 DMAVVQRLFSMGD-VNAKASQTGQTALMLAISHGHQDMVAALLECGADVNVQDADGATALMCASEYGRLDTVQLLLAQPG 746
Cdd:PHA02875  80 DVKAVEELLDLGKfADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKA 159

                        170       180
                 ....*....|....*....|....*....
gi 157823313 747 CdLTILDNEGTSALAIALEAEQDEVAALL 775
Cdd:PHA02875 160 C-LDIEDCCGCTPLIIAMAKGDIAICKML 187
PHA02798 PHA02798
ankyrin-like protein; Provisional
 703-788 4.07e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 43.67  E-value: 4.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823313 703 DMVAALLECGADVNVQDADGATALMCASEYGRLDTVQLLL--AQPGCDLTILDNEGTSALAIALEA----EQDEVAALLH 776
Cdd:PHA02798  90 DIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLfmIENGADTTLLDKDGFTMLQVYLQSnhhiDIEIIKLLLE 169

                         90
                 ....*....|..
gi 157823313 777 AHLTSNHHDSQE 788
Cdd:PHA02798 170 KGVDINTHNNKE 181
PHA03095 PHA03095
ankyrin-like protein; Provisional
 644-764 5.82e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 43.09  E-value: 5.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823313 644 NHQNRAGYSALMLAALTSvgkEEEDMAVVQRLFSMG-DVNAKASqTGQTALMLAISHGHQ---DMVAALLECGADVNVQD 719
Cdd:PHA03095   5 ESVDIIMEAALYDYLLNA---SNVTVEEVRRLLAAGaDVNFRGE-YGKTPLHLYLHYSSEkvkDIVRLLLEAGADVNAPE 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 157823313 720 ADGATALMCASEYG-RLDTVQLLLaQPGCDLTILDNEGTSALAIAL 764
Cdd:PHA03095  81 RCGFTPLHLYLYNAtTLDVIKLLI-KAGADVNAKDKVGRTPLHVYL 125
Ank_4 pfam13637
Ankyrin repeats (many copies);
616-659 1.03e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.64  E-value: 1.03e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 157823313  616 GNTALHYSVSHGNLAISSLLLDTGVcDVNHQNRAGYSALMLAAL 659
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGA-DINAVDGNGETALHFAAS 43
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
129-322 1.10e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.59  E-value: 1.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823313  129 VEH--TLLETSRRLEQAQAQERALSPARAATRSpRGSGRSSPAPNPALASPSPVLAspGPAQLQLVREQMAVALRRLREL 206
Cdd:COG4913   231 VEHfdDLERAHEALEDAREQIELLEPIRELAER-YAAARERLAELEYLRAALRLWF--AQRRLELLEAELEELRAELARL 307

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823313  207 EDQARALP----ELQEQVRALRAEKARLLAGRVQP-EQDVEievrpDKLSQLRRLTERLATSDRGVRSRASPRAEDPDGL 281
Cdd:COG4913   308 EAELERLEarldALREELDELEAQIRGNGGDRLEQlEREIE-----RLERELEERERRRARLEALLAALGLPLPASAEEF 382

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 157823313  282 AARRSEGALQVLDPASRTPDGEPQTREAGTEVVPETREVDA 322
Cdd:COG4913   383 AALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRE 423
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 615-648 1.33e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.88  E-value: 1.33e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 157823313  615 NGNTALHYSVSH-GNLAISSLLLDTGvCDVNHQNR 648
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKG-ADVNARDK 34
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 650-770 1.39e-03

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 42.05  E-value: 1.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823313 650 GYSALMLAALTSVGKEEEdmaVVQRLFSMGDVNA------KASQT-----GQTALMLAISHGHQDMVAALLECGADVNVQ 718
Cdd:cd22194   94 GKTCLMKALLNINENTKE---IVRILLAFAEENGildrfiNAEYTeeayeGQTALNIAIERRQGDIVKLLIAKGADVNAH 170

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157823313 719 DAD--------------GATALMCASEYGRLDTVQLLLAQPGCDLTILDNEGTSAL-AIALEAEQDE 770
Cdd:cd22194  171 AKGvffnpkykhegfyfGETPLALAACTNQPEIVQLLMEKESTDITSQDSRGNTVLhALVTVAEDSK 237
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 631-768 1.66e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 41.79  E-value: 1.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823313 631 ISSLLLDTGVcDVNHQNR-AGYSALMLAAltsvgkEEEDMAVVQRLFSMG-DVNAkASQTGQTALMLAISHGHQDMVAAL 708
Cdd:PHA02878 149 ITKLLLSYGA-DINMKDRhKGNTALHYAT------ENKDQRLTELLLSYGaNVNI-PDKTNNSPLHHAVKHYNKPIVHIL 220

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157823313 709 LECGADVNVQDADGATALMCASEYGRLDTVQLLLAQPGCDL----TILdneGTSALAIALEAEQ 768
Cdd:PHA02878 221 LENGASTDARDKCGNTPLHISVGYCKDYDILKLLLEHGVDVnaksYIL---GLTALHSSIKSER 281
Ank_4 pfam13637
Ankyrin repeats (many copies);
609-636 1.85e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.87  E-value: 1.85e-03
                          10        20
                  ....*....|....*....|....*...
gi 157823313  609 VNLADGNGNTALHYSVSHGNLAISSLLL 636
Cdd:pfam13637  27 INAVDGNGETALHFAASNGNVEVLKLLL 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 615-644 2.69e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.03  E-value: 2.69e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 157823313   615 NGNTALHYSVSHGNLAISSLLLDTGVcDVN 644
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGA-DIN 29
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 708-785 2.83e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 41.20  E-value: 2.83e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157823313 708 LLECGADVNVQDADGATALMCASEYGRLDTVQLLLAQpGCDLTILDNEGTSALAIALEAEQ-DEVAALLHAHLTSNHHD 785
Cdd:PHA02876 164 LLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSY-GADVNIIALDDLSVLECAVDSKNiDTIKAIIDNRSNINKND 241
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
63-326 5.42e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 40.22  E-value: 5.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823313  63 APGPPHARRPRASGKGLAGARSPGAWTSSESLASDDGGASGALSP-GAFPGLSLPPLSPRSfsRNPRVEHTLLETSRRLE 141
Cdd:PRK07003 368 PGGGVPARVAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPkAAAAAAATRAEAPPA--APAPPATADRGDDAADG 445

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823313 142 QAQAQERAlsPARAATRSPRGSGRSSPAPNPALAS-------------PSPVLASPGPAQLQLVREQMAVAL-RRLRELE 207
Cdd:PRK07003 446 DAPVPAKA--NARASADSRCDERDAQPPADSGSASapasdappdaafePAPRAAAPSAATPAAVPDARAPAAaSREDAPA 523

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823313 208 DQARALPELQEQVRALRAEKARllAGRVQPEQDVeievrpdklsqLRRLTERLaTSDRGVRSRASPRAEDPDGLAARRSE 287
Cdd:PRK07003 524 AAAPPAPEARPPTPAAAAPAAR--AGGAAAALDV-----------LRNAGMRV-SSDRGARAAAAAKPAAAPAAAPKPAA 589

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 157823313 288 GALQVLDPASRTPDGEPQTREAGTEVVPETREvDAQAVP 326
Cdd:PRK07003 590 PRVAVQVPTPRARAATGDAPPNGAARAEQAAE-SRGAPP 627
Ank_5 pfam13857
Ankyrin repeats (many copies);
604-657 7.50e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.40  E-value: 7.50e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 157823313  604 LLAHV---VNLADGNGNTALHYSVSHGNLAISSLLLDTGvCDVNHQNRAGYSALMLA 657
Cdd:pfam13857   1 LLEHGpidLNRLDGEGYTPLHVAAKYGALEIVRVLLAYG-VDLNLKDEEGLTALDLA 56
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
137-366 7.52e-03

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 39.61  E-value: 7.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823313 137 SRRLEQAQAQERALSPARAATRSPRGSGRSSPAPNPALASPSPVLASPGPAqlqlvREQMAVALRRLRELEDQARALPEL 216
Cdd:COG0515  252 EERYQSAAELAAALRAVLRSLAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA-----AAAAAAAAAAAAAAAAAAAAPAAA 326

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823313 217 QEQVRALRAEKARLLAGRVQPEQDVEIEVRPDKLSQLRRLTERLATSDRGVRSRASPRAEDPDGLAARRSEGALQVLDPA 296
Cdd:COG0515  327 AAAAAAAAALAAAAAAAAAAAAAALLAAAAALAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAALAAAAAA 406

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823313 297 SRTPDGEPQTREAGTEVVPETREVDAQAVPETREAGVEVVPETVEVDTWVTEALLGLPEAAERELELLRT 366
Cdd:COG0515  407 AAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAAAARLLAAAAAAAAAAAAAPLLAALLAAAALAAAAAA 476
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 616-717 8.26e-03

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 39.68  E-value: 8.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823313  616 GNTALHYSVSHG-NLAISSLLLdtgvcdvNHQNRA--GYSALMLAALTSVGKEEEDMAVVQRLFSMGD----VNAKASQT 688
Cdd:TIGR00870  52 GRSALFVAAIENeNLELTELLL-------NLSCRGavGDTLLHAISLEYVDAVEAILLHLLAAFRKSGplelANDQYTSE 124

                          90       100       110
                  ....*....|....*....|....*....|..
gi 157823313  689 ---GQTALMLAISHGHQDMVAALLECGADVNV 717
Cdd:TIGR00870 125 ftpGITALHLAAHRQNYEIVKLLLERGASVPA 156
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 604-717 8.28e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 39.59  E-value: 8.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823313 604 LLAH--VVNLADGNGNTALHYSVSHGNLAISSLLLDTGvcdvnhqnragysalmlAALTSVGKEeedmavvqrlfsmGDV 681
Cdd:PHA02875 154 LIDHkaCLDIEDCCGCTPLIIAMAKGDIAICKMLLDSG-----------------ANIDYFGKN-------------GCV 203

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 157823313 682 nakasqtgqTALMLAISHGHQDMVAALLECGADVNV 717
Cdd:PHA02875 204 ---------AALCYAIENNKIDIVRLFIKRGADCNI 230
PHA02741 PHA02741
hypothetical protein; Provisional
 696-790 8.45e-03

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 38.10  E-value: 8.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823313 696 AISHGHQ---DMVAALLECGADVNVQDA-DGATALMCASEYGRLDTVQLLLAQPGCDLTILDNEGTSALAIALEAEQDEV 771
Cdd:PHA02741  68 AEKHEAQlaaEIIDHLIELGADINAQEMlEGDTALHLAAHRRDHDLAEWLCCQPGIDLHFCNADNKSPFELAIDNEDVAM 147

                         90
                 ....*....|....*....
gi 157823313 772 AALLHAHLTSNHHDSQEQS 790
Cdd:PHA02741 148 MQILREIVATSRGFSNENT 166
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 721-754 9.09e-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: 34.57  E-value: 9.09e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 157823313  721 DGATALMCAS-EYGRLDTVQLLLaQPGCDLTILDN 754
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLL-SKGADVNARDK 34
 
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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