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Conserved domains on  [gi|672058128|ref|XP_008763424|]
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KN motif and ankyrin repeat domain-containing protein 3 isoform X1 [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];
614-802 3.97e-42

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 155.50  E-value: 3.97e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672058128 614 LLAHVVNLADGNGNTALHYSVSHGNLAISSLLLDTGVcDVNHQNRAGYSALMLAAltsvgkEEEDMAVVQRLFSMG-DVN 692
Cdd:COG0666   75 AAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGA-DVNARDKDGETPLHLAA------YNGNLEIVKLLLEAGaDVN 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672058128 693 AKASQtGQTALMLAISHGHQDMVAALLECGADVNVQDADGATALMCASEYGRLDTVQLLLAQpGCDLTILDNEGTSALAI 772
Cdd:COG0666  148 AQDND-GNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA-GADVNAKDNDGKTALDL 225

                        170       180       190
                 ....*....|....*....|....*....|
gi 672058128 773 ALEAEQDEVAALLHAHLTSNHHDSQEQSTP 802
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 3.37e-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: 78.55  E-value: 3.37e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 672058128   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 8.93e-04

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: 42.98  E-value: 8.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672058128  129 VEH--TLLETSRRLEQAQAQERALSPARAATRSpRGSGRSSPAPNPALASPSPVLAspGPAQLQLVREQMAVALRRLREL 206
Cdd:COG4913   231 VEHfdDLERAHEALEDAREQIELLEPIRELAER-YAAARERLAELEYLRAALRLWF--AQRRLELLEAELEELRAELARL 307

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672058128  207 EDQARALP----ELQEQVRALRAEKARLLAGRVQP-EQDVEievrpDKLSQLRRLTERLATSDRGVRSRASPRAEDPDGL 281
Cdd:COG4913   308 EAELERLEarldALREELDELEAQIRGNGGDRLEQlEREIE-----RLERELEERERRRARLEALLAALGLPLPASAEEF 382

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 672058128  282 AARRSEGALQVLDPASRTPDGEPQTREAGTEVVPETREVDA 322
Cdd:COG4913   383 AALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRE 423
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
614-802 3.97e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 155.50  E-value: 3.97e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672058128 614 LLAHVVNLADGNGNTALHYSVSHGNLAISSLLLDTGVcDVNHQNRAGYSALMLAAltsvgkEEEDMAVVQRLFSMG-DVN 692
Cdd:COG0666   75 AAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGA-DVNARDKDGETPLHLAA------YNGNLEIVKLLLEAGaDVN 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672058128 693 AKASQtGQTALMLAISHGHQDMVAALLECGADVNVQDADGATALMCASEYGRLDTVQLLLAQpGCDLTILDNEGTSALAI 772
Cdd:COG0666  148 AQDND-GNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA-GADVNAKDNDGKTALDL 225

                        170       180       190
                 ....*....|....*....|....*....|
gi 672058128 773 ALEAEQDEVAALLHAHLTSNHHDSQEQSTP 802
Cdd:COG0666  226 AAENGNLEIVKLLLEAGADLNAKDKDGLTA 255
Ank_2 pfam12796
Ankyrin repeats (3 copies);
630-729 3.04e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.16  E-value: 3.04e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672058128  630 LHYSVSHGNLAISSLLLDTGvCDVNHQNRAGYSALMLAALTsvGKEEedmaVVQRLFSMGDVNAKASqtGQTALMLAISH 709
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENG-ADANLQDKNGRTALHLAAKN--GHLE----IVKLLLEHADVNLKDN--GRTALHYAARS 71

                          90       100
                  ....*....|....*....|
gi 672058128  710 GHQDMVAALLECGADVNVQD 729
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 3.37e-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: 78.55  E-value: 3.37e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 672058128   32 PYSVETPYGFHLDLDFLKYVEEIERGPASRRApgpPHARRPR 73
Cdd:pfam12075   1 PYSVETPYGFHLDLDFLKYVEDIESGQTIRRA---RVQRRPR 39
PHA03095 PHA03095
ankyrin-like protein; Provisional
 619-775 5.94e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 62.35  E-value: 5.94e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672058128 619 VNLADGNGNTALHYSVSHGN---LAISSLLLDTGVcDVNHQNRAGYSALMLAALTSvgkEEEDmaVVQRLFSMG-DVNAK 694
Cdd:PHA03095  40 VNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGA-DVNAPERCGFTPLHLYLYNA---TTLD--VIKLLIKAGaDVNAK 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672058128 695 aSQTGQTAL--MLAISHGHQDMVAALLECGADVNVQDADGATALMCASEYGR--LDTVQLLLAQpGCDLTILDNEGTSAL 770
Cdd:PHA03095 114 -DKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanVELLRLLIDA-GADVYAVDDRFRSLL 191


                 ....*
gi 672058128 771 AIALE 775
Cdd:PHA03095 192 HHHLQ 196
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 699-727 3.35e-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: 3.35e-05
                           10        20
                   ....*....|....*....|....*....
gi 672058128   699 GQTALMLAISHGHQDMVAALLECGADVNV 727
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 626-736 7.13e-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: 7.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672058128 626 GNTALHYSVSHGNLAISSLLLDTGVCDVNH----QNRAGYSALMLAALTsvgkeeEDMAVVQRLFSMG-DV-NAKASQT- 698
Cdd:cd22192   51 GETALHVAALYDNLEAAVVLMEAAPELVNEpmtsDLYQGETALHIAVVN------QNLNLVRELIARGaDVvSPRATGTf 124

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 672058128 699 -----------GQTALMLAISHGHQDMVAALLECGADVNVQDADGATAL 736
Cdd:cd22192  125 frpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
129-322 8.93e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.98  E-value: 8.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672058128  129 VEH--TLLETSRRLEQAQAQERALSPARAATRSpRGSGRSSPAPNPALASPSPVLAspGPAQLQLVREQMAVALRRLREL 206
Cdd:COG4913   231 VEHfdDLERAHEALEDAREQIELLEPIRELAER-YAAARERLAELEYLRAALRLWF--AQRRLELLEAELEELRAELARL 307

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672058128  207 EDQARALP----ELQEQVRALRAEKARLLAGRVQP-EQDVEievrpDKLSQLRRLTERLATSDRGVRSRASPRAEDPDGL 281
Cdd:COG4913   308 EAELERLEarldALREELDELEAQIRGNGGDRLEQlEREIE-----RLERELEERERRRARLEALLAALGLPLPASAEEF 382

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 672058128  282 AARRSEGALQVLDPASRTPDGEPQTREAGTEVVPETREVDA 322
Cdd:COG4913   383 AALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRE 423
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
63-326 5.27e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 40.60  E-value: 5.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672058128  63 APGPPHARRPRASGKGLAGARSPGAWTSSESLASDDGGASGALSP-GAFPGLSLPPLSPRSfsRNPRVEHTLLETSRRLE 141
Cdd:PRK07003 368 PGGGVPARVAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPkAAAAAAATRAEAPPA--APAPPATADRGDDAADG 445

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672058128 142 QAQAQERAlsPARAATRSPRGSGRSSPAPNPALAS-------------PSPVLASPGPAQLQLVREQMAVAL-RRLRELE 207
Cdd:PRK07003 446 DAPVPAKA--NARASADSRCDERDAQPPADSGSASapasdappdaafePAPRAAAPSAATPAAVPDARAPAAaSREDAPA 523

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672058128 208 DQARALPELQEQVRALRAEKARllAGRVQPEQDVeievrpdklsqLRRLTERLaTSDRGVRSRASPRAEDPDGLAARRSE 287
Cdd:PRK07003 524 AAAPPAPEARPPTPAAAAPAAR--AGGAAAALDV-----------LRNAGMRV-SSDRGARAAAAAKPAAAPAAAPKPAA 589

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 672058128 288 GALQVLDPASRTPDGEPQTREAGTEVVPETREvDAQAVP 326
Cdd:PRK07003 590 PRVAVQVPTPRARAATGDAPPNGAARAEQAAE-SRGAPP 627
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 626-727 8.39e-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: 8.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672058128  626 GNTALHYSVSHG-NLAISSLLLdtgvcdvNHQNRA--GYSALMLAALTSVGKEEEDMAVVQRLFSMGD----VNAKASQT 698
Cdd:TIGR00870  52 GRSALFVAAIENeNLELTELLL-------NLSCRGavGDTLLHAISLEYVDAVEAILLHLLAAFRKSGplelANDQYTSE 124

                          90       100       110
                  ....*....|....*....|....*....|..
gi 672058128  699 ---GQTALMLAISHGHQDMVAALLECGADVNV 727
Cdd:TIGR00870 125 ftpGITALHLAAHRQNYEIVKLLLERGASVPA 156
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
614-802 3.97e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 155.50  E-value: 3.97e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672058128 614 LLAHVVNLADGNGNTALHYSVSHGNLAISSLLLDTGVcDVNHQNRAGYSALMLAAltsvgkEEEDMAVVQRLFSMG-DVN 692
Cdd:COG0666   75 AAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGA-DVNARDKDGETPLHLAA------YNGNLEIVKLLLEAGaDVN 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672058128 693 AKASQtGQTALMLAISHGHQDMVAALLECGADVNVQDADGATALMCASEYGRLDTVQLLLAQpGCDLTILDNEGTSALAI 772
Cdd:COG0666  148 AQDND-GNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA-GADVNAKDNDGKTALDL 225

                        170       180       190
                 ....*....|....*....|....*....|
gi 672058128 773 ALEAEQDEVAALLHAHLTSNHHDSQEQSTP 802
Cdd:COG0666  226 AAENGNLEIVKLLLEAGADLNAKDKDGLTA 255
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
613-785 9.97e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 134.31  E-value: 9.97e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672058128 613 ELLAH--VVNLADGNGNTALHYSVSHGNLAISSLLLDTGVcDVNHQNRAGYSALMLAAltsvgkEEEDMAVVQRLFSMG- 689
Cdd:COG0666  105 LLLEAgaDVNARDKDGETPLHLAAYNGNLEIVKLLLEAGA-DVNAQDNDGNTPLHLAA------ANGNLEIVKLLLEAGa 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672058128 690 DVNAKaSQTGQTALMLAISHGHQDMVAALLECGADVNVQDADGATALMCASEYGRLDTVQLLLAQpGCDLTILDNEGTSA 769
Cdd:COG0666  178 DVNAR-DNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA-GADLNAKDKDGLTA 255

                        170
                 ....*....|....*.
gi 672058128 770 LAIALEAEQDEVAALL 785
Cdd:COG0666  256 LLLAAAAGAALIVKLL 271
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
614-788 4.50e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 129.30  E-value: 4.50e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672058128 614 LLAHVVNLADGNGNTALHYSVSHGNLAISSLLLDTGVcDVNHQNRAGYSALMLAAltsvgkEEEDMAVVQRLFSMG-DVN 692
Cdd:COG0666   42 LALLALALADALGALLLLAAALAGDLLVALLLLAAGA-DINAKDDGGNTLLHAAA------RNGDLEIVKLLLEAGaDVN 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672058128 693 AKASQtGQTALMLAISHGHQDMVAALLECGADVNVQDADGATALMCASEYGRLDTVQLLLAQpGCDLTILDNEGTSALAI 772
Cdd:COG0666  115 ARDKD-GETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEA-GADVNARDNDGETPLHL 192

                        170
                 ....*....|....*.
gi 672058128 773 ALEAEQDEVAALLHAH 788
Cdd:COG0666  193 AAENGHLEIVKLLLEA 208
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
614-767 3.81e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 103.50  E-value: 3.81e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672058128 614 LLAH--VVNLADGNGNTALHYSVSHGNLAISSLLLDTGVcDVNHQNRAGYSALMLAAltsvgkEEEDMAVVQRLFSMG-D 690
Cdd:COG0666  139 LLEAgaDVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGA-DVNARDNDGETPLHLAA------ENGHLEIVKLLLEAGaD 211

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 672058128 691 VNAKASQtGQTALMLAISHGHQDMVAALLECGADVNVQDADGATALMCASEYGRLDTVQLLLAQPGCDLTILDNEGT 767
Cdd:COG0666  212 VNAKDND-GKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
613-785 1.83e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 101.57  E-value: 1.83e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672058128 613 ELLAHVVNLADGNGNTALHYSVSHGNLAISSLLLDTGVCDVNHQNRAGYSALMLAAltsvgkEEEDMAVVQRLFSMGDVN 692
Cdd:COG0666    7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAA------LAGDLLVALLLLAAGADI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672058128 693 AKASQTGQTALMLAISHGHQDMVAALLECGADVNVQDADGATALMCASEYGRLDTVQLLLAQpGCDLTILDNEGTSALAI 772
Cdd:COG0666   81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA-GADVNAQDNDGNTPLHL 159

                        170
                 ....*....|...
gi 672058128 773 ALEAEQDEVAALL 785
Cdd:COG0666  160 AAANGNLEIVKLL 172
Ank_2 pfam12796
Ankyrin repeats (3 copies);
630-729 3.04e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.16  E-value: 3.04e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672058128  630 LHYSVSHGNLAISSLLLDTGvCDVNHQNRAGYSALMLAALTsvGKEEedmaVVQRLFSMGDVNAKASqtGQTALMLAISH 709
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENG-ADANLQDKNGRTALHLAAKN--GHLE----IVKLLLEHADVNLKDN--GRTALHYAARS 71

                          90       100
                  ....*....|....*....|
gi 672058128  710 GHQDMVAALLECGADVNVQD 729
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 3.37e-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: 78.55  E-value: 3.37e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 672058128   32 PYSVETPYGFHLDLDFLKYVEEIERGPASRRApgpPHARRPR 73
Cdd:pfam12075   1 PYSVETPYGFHLDLDFLKYVEDIESGQTIRRA---RVQRRPR 39
Ank_2 pfam12796
Ankyrin repeats (3 copies);
703-785 3.91e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.77  E-value: 3.91e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672058128  703 LMLAISHGHQDMVAALLECGADVNVQDADGATALMCASEYGRLDTVQLLLAQPGCDltiLDNEGTSALAIALEAEQDEVA 782
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN---LKDNGRTALHYAARSGHLEIV 77


                  ...
gi 672058128  783 ALL 785
Cdd:pfam12796  78 KLL 80
Ank_2 pfam12796
Ankyrin repeats (3 copies);
664-763 1.27e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 78.62  E-value: 1.27e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672058128  664 LMLAAltsvgkEEEDMAVVQRLFSMG-DVNAKaSQTGQTALMLAISHGHQDMVAALLECgADVNVQDaDGATALMCASEY 742
Cdd:pfam12796   1 LHLAA------KNGNLELVKLLLENGaDANLQ-DKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARS 71

                          90       100
                  ....*....|....*....|.
gi 672058128  743 GRLDTVQLLLaQPGCDLTILD 763
Cdd:pfam12796  72 GHLEIVKLLL-EKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
663-788 1.61e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 68.83  E-value: 1.61e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672058128 663 ALMLAALTSVGKEEEDMAVVQRLFSMGDVNAKASQTGQTALMLAISHGHQDMVAALLECGADVNVQDADGATALMCASEY 742
Cdd:COG0666   18 LLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARN 97

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 672058128 743 GRLDTVQLLLAQpGCDLTILDNEGTSALAIALEAEQDEVAALLHAH 788
Cdd:COG0666   98 GDLEIVKLLLEA-GADVNARDKDGETPLHLAAYNGNLEIVKLLLEA 142
Ank_4 pfam13637
Ankyrin repeats (many copies);
701-752 1.24e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 57.28  E-value: 1.24e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 672058128  701 TALMLAISHGHQDMVAALLECGADVNVQDADGATALMCASEYGRLDTVQLLL 752
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 619-775 5.94e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 62.35  E-value: 5.94e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672058128 619 VNLADGNGNTALHYSVSHGN---LAISSLLLDTGVcDVNHQNRAGYSALMLAALTSvgkEEEDmaVVQRLFSMG-DVNAK 694
Cdd:PHA03095  40 VNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGA-DVNAPERCGFTPLHLYLYNA---TTLD--VIKLLIKAGaDVNAK 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672058128 695 aSQTGQTAL--MLAISHGHQDMVAALLECGADVNVQDADGATALMCASEYGR--LDTVQLLLAQpGCDLTILDNEGTSAL 770
Cdd:PHA03095 114 -DKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanVELLRLLIDA-GADVYAVDDRFRSLL 191


                 ....*
gi 672058128 771 AIALE 775
Cdd:PHA03095 192 HHHLQ 196
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 619-752 1.13e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 58.14  E-value: 1.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672058128 619 VNLADGNGNTALHYSVSH--GNLAISSLLLDTGvCDVNHQNRAGYSALMLAalTSVGKEEEDMavVQRLFSMG-DVNAKA 695
Cdd:PHA03100  99 VNAPDNNGITPLLYAISKksNSYSIVEYLLDNG-ANVNIKNSDGENLLHLY--LESNKIDLKI--LKLLIDKGvDINAKN 173

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 672058128 696 S---------------QTGQTALMLAISHGHQDMVAALLECGADVNVQDADGATALMCASEYGRLDTVQLLL 752
Cdd:PHA03100 174 RvnyllsygvpinikdVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLL 245
PHA03095 PHA03095
ankyrin-like protein; Provisional
 599-743 1.57e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 57.73  E-value: 1.57e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672058128 599 PVAGVLRGVKSLGPELLAhvvnlADGNGNTALHYSVSHGNLAISSL--LLDTGVcDVNHQNRAGYSALMLAAltsvgKEE 676
Cdd:PHA03095 200 PRARIVRELIRAGCDPAA-----TDMLGNTPLHSMATGSSCKRSLVlpLLIAGI-SINARNRYGQTPLHYAA-----VFN 268

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 672058128 677 EDMAVVqRLFSMG-DVNAkASQTGQTALMLAISHGHQDMVAALLECGADVNVQDAdgatALMCASEYG 743
Cdd:PHA03095 269 NPRACR-RLIALGaDINA-VSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAA----TLNTASVAG 330
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 713-818 2.99e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 57.22  E-value: 2.99e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672058128 713 DMVAA--LLECGADVNVQDADGATALMCASEYGRLDTVQLLLaQPGCDLTILDNEGTSALAIALEAEQDEVAALLHAHLT 790
Cdd:PTZ00322  94 DAVGAriLLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLL-EFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQ 172

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 672058128 791 SNHH----------DSQEQSTPGSPTATLQRDTG--PQPL 818
Cdd:PTZ00322 173 CHFElganakpdsfTGKPPSLEDSPISSHHPDFSavPQPM 212
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 619-775 5.54e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 56.13  E-value: 5.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672058128 619 VNLADGNGNTALHYSVSHGNLAISSLLLDTGVCdVNHQNRAGYSALMLAAltsvgkEEEDMAVVQRLFSMGDVNAKASQT 698
Cdd:PHA02874 150 VNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAY-ANVKDNNGESPLHNAA------EYGDYACIKLLIDHGNHIMNKCKN 222

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 672058128 699 GQTALMLAISHGHQdmVAALLECGADVNVQDADGATALMCASEYG-RLDTVQLLLAQPGcDLTILDNEGTSALAIALE 775
Cdd:PHA02874 223 GFTPLHNAIIHNRS--AIELLINNASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKA-DISIKDNKGENPIDTAFK 297
Ank_5 pfam13857
Ankyrin repeats (many copies);
718-773 1.79e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.50  E-value: 1.79e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 672058128  718 LLECG-ADVNVQDADGATALMCASEYGRLDTVQLLLAqPGCDLTILDNEGTSALAIA 773
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLA-YGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
690-736 3.92e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.34  E-value: 3.92e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 672058128  690 DVNAKaSQTGQTALMLAISHGHQDMVAALLECGADVNVQDADGATAL 736
Cdd:pfam13857   8 DLNRL-DGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 645-774 5.37e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 53.04  E-value: 5.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672058128 645 LLDTGVcDVNHQNRAGYSALMLAAltsvgkEEEDMAVVQRLFSMG-DVNAKaSQTGQTALMLAISHGHQDMVAALLECGA 723
Cdd:PHA02874 110 ILDCGI-DVNIKDAELKTFLHYAI------KKGDLESIKMLFEYGaDVNIE-DDNGCYPIHIAIKHNFFDIIKLLLEKGA 181

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 672058128 724 DVNVQDADGATALMCASEYGRLDTVQLLLAQpGCDLTILDNEGTSALAIAL 774
Cdd:PHA02874 182 YANVKDNNGESPLHNAAEYGDYACIKLLIDH-GNHIMNKCKNGFTPLHNAI 231
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 619-739 6.76e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 52.57  E-value: 6.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672058128 619 VNLADGNGNTALHYSVSHGNLAISSLLLDTGvCDVNHQNRAGYSALMLaaltSVGKEEeDMAVVQRLFSMG-DVNAKASQ 697
Cdd:PHA02878 194 VNIPDKTNNSPLHHAVKHYNKPIVHILLENG-ASTDARDKCGNTPLHI----SVGYCK-DYDILKLLLEHGvDVNAKSYI 267

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 672058128 698 TGQTALMLAISHghQDMVAALLECGADVNVQDADGATALMCA 739
Cdd:PHA02878 268 LGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSA 307
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 699-729 7.24e-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: 7.24e-07
                          10        20        30
                  ....*....|....*....|....*....|..
gi 672058128  699 GQTALMLAISH-GHQDMVAALLECGADVNVQD 729
Cdd:pfam00023   2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 699-758 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 672058128 699 GQTALMLAISHGHQDMVAALLECGADVNVQDADGATALMCASEYGRLDTVQLLLAQPGCD 758
Cdd:PTZ00322 115 GRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCH 174
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 620-752 2.77e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 51.02  E-value: 2.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672058128 620 NLADGNGNTALHYSVSHGNLAISSLLLDTGvCDVNHQNRAGYSALMLAAltsvgkeeedMAVVQRLFSMGDVNAKAS--Q 697
Cdd:PLN03192 552 DIGDSKGRTPLHIAASKGYEDCVLVLLKHA-CNVHIRDANGNTALWNAI----------SAKHHKIFRILYHFASISdpH 620

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 672058128 698 TGQTALMLAISHGHQDMVAALLECGADVNVQDADGATALMCASEYGRLDTVQLLL 752
Cdd:PLN03192 621 AAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLI 675
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 619-785 4.91e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 49.96  E-value: 4.91e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672058128 619 VNLADGNGNTALHYSVSHGNLAISSLLLDTGVcDVNHQNRAGYSALMLAalTSVGKEEedmaVVQRLFSmgdvnakasqT 698
Cdd:PHA02874  28 INISVDETTTPLIDAIRSGDAKIVELFIKHGA-DINHINTKIPHPLLTA--IKIGAHD----IIKLLID----------N 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672058128 699 GQTALMLAISHGHQDMVAALLECGADVNVQDADGATALMCASEYGRLDTVQLLLaQPGCDLTILDNEGTSALAIALEAEQ 778
Cdd:PHA02874  91 GVDTSILPIPCIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLF-EYGADVNIEDDNGCYPIHIAIKHNF 169


                 ....*..
gi 672058128 779 DEVAALL 785
Cdd:PHA02874 170 FDIIKLL 176
Ank_2 pfam12796
Ankyrin repeats (3 copies);
736-802 6.53e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 45.11  E-value: 6.53e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 672058128  736 LMCASEYGRLDTVQLLLaQPGCDLTILDNEGTSALAIALEAEQDEVAALLHAHLTSNHHDSQEqsTP 802
Cdd:pfam12796   1 LHLAAKNGNLELVKLLL-ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGR--TA 64
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 630-785 7.09e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 49.87  E-value: 7.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672058128 630 LHYSVSHGNLAISSLLLDTGVcdvNHQNRAGYSALMLAALTSVGKEEEDMAVVQRLFSMGDvnakasQTGQTALMLAISH 709
Cdd:PLN03192 498 LQHHKELHDLNVGDLLGDNGG---EHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGD------SKGRTPLHIAASK 568

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672058128 710 GHQDMVAALLECGADVNVQDADGATAL------------------------------MC-ASEYGRLDTVQLLLAQpGCD 758
Cdd:PLN03192 569 GYEDCVLVLLKHACNVHIRDANGNTALwnaisakhhkifrilyhfasisdphaagdlLCtAAKRNDLTAMKELLKQ-GLN 647

                        170       180
                 ....*....|....*....|....*..
gi 672058128 759 LTILDNEGTSALAIALEAEQDEVAALL 785
Cdd:PLN03192 648 VDSEDHQGATALQVAMAEDHVDMVRLL 674
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 630-752 7.21e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 49.28  E-value: 7.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672058128 630 LHYSVSHGNLAISSLLLDTGvCDVNhQNRAGYSALMLAALTSVGKEEEDMAVVQRLFSMG-DVNAKaSQTGQTALMLAIS 708
Cdd:PHA03100  39 LYLAKEARNIDVVKILLDNG-ADIN-SSTKNNSTPLHYLSNIKYNLTDVKEIVKLLLEYGaNVNAP-DNNGITPLLYAIS 115

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 672058128 709 H--GHQDMVAALLECGADVNVQDADGATALMCASEYGR--LDTVQLLL 752
Cdd:PHA03100 116 KksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLI 163
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 614-725 1.08e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 49.10  E-value: 1.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672058128 614 LLAHV--VNLADGNGNTALHYSVSHGNLAISSLLLDTGVCDVNHqnrAGYSALMLAAltsvgkEEEDMAVVQRLFSMG-D 690
Cdd:PLN03192 577 LLKHAcnVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPH---AAGDLLCTAA------KRNDLTAMKELLKQGlN 647

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 672058128 691 VNAKASQtGQTALMLAISHGHQDMVAALLECGADV 725
Cdd:PLN03192 648 VDSEDHQ-GATALQVAMAEDHVDMVRLLIMNGADV 681
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 617-791 1.73e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 48.34  E-value: 1.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672058128 617 HVVNLADGNGNTALHYSVSHGN-LAISSLLLDTGVCDVNHQ---------NRAGYSALMLaaLTSVGKEEEDMAVVQ--- 683
Cdd:PHA02878  61 HNVNQPDHRDLTPLHIICKEPNkLGMKEMIRSINKCSVFYTlvaikdafnNRNVEIFKII--LTNRYKNIQTIDLVYidk 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672058128 684 -------------RLFSMG-DVNAKASQTGQTALMLAISHGHQDMVAALLECGADVNVQDADGATALMCASEYGRLDTVQ 749
Cdd:PHA02878 139 kskddiieaeitkLLLSYGaDINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVH 218

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 672058128 750 LLLaQPGCDLTILDNEGTSALAIALEAEQD-EVAALLHAHLTS 791
Cdd:PHA02878 219 ILL-ENGASTDARDKCGNTPLHISVGYCKDyDILKLLLEHGVD 260
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 699-727 3.35e-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: 3.35e-05
                           10        20
                   ....*....|....*....|....*....
gi 672058128   699 GQTALMLAISHGHQDMVAALLECGADVNV 727
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 625-762 4.09e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 46.91  E-value: 4.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672058128 625 NGNTALHYSVSHGNLAISSLLLDTGVcDVNHQNRAGYSALMLAALTSvgkeeeDMAVVQRLFSMGDVNAKASQTGQTALM 704
Cdd:PHA02875 101 DGMTPLHLATILKKLDIMKLLIARGA-DPDIPNTDKFSPLHLAVMMG------DIKGIELLIDHKACLDIEDCCGCTPLI 173

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 672058128 705 LAISHGHQDMVAALLECGADVNVQDADGATALMC-ASEYGRLDTVQLLLAQpGCDLTIL 762
Cdd:PHA02875 174 IAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCyAIENNKIDIVRLFIKR-GADCNIM 231
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 656-793 4.71e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 47.17  E-value: 4.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672058128 656 QNRAGYSALMLAALTSVGKEEEDMAVVQRLFSMG----DVNAKASqtgqtaLMLAISHGHQDMVAALLECGADVNVQDAD 731
Cdd:PLN03192 484 QTRQEDNVVILKNFLQHHKELHDLNVGDLLGDNGgehdDPNMASN------LLTVASTGNAALLEELLKAKLDPDIGDSK 557

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 672058128 732 GATALMCASEYGRLDTVQLLLAQpGCDLTILDNEGTSALAIALEAEQDEVAALLH--AHLTSNH 793
Cdd:PLN03192 558 GRTPLHIAASKGYEDCVLVLLKH-ACNVHIRDANGNTALWNAISAKHHKIFRILYhfASISDPH 620
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 626-736 7.13e-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: 7.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672058128 626 GNTALHYSVSHGNLAISSLLLDTGVCDVNH----QNRAGYSALMLAALTsvgkeeEDMAVVQRLFSMG-DV-NAKASQT- 698
Cdd:cd22192   51 GETALHVAALYDNLEAAVVLMEAAPELVNEpmtsDLYQGETALHIAVVN------QNLNLVRELIARGaDVvSPRATGTf 124

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 672058128 699 -----------GQTALMLAISHGHQDMVAALLECGADVNVQDADGATAL 736
Cdd:cd22192  125 frpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
PHA03095 PHA03095
ankyrin-like protein; Provisional
 622-736 1.15e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 45.40  E-value: 1.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672058128 622 ADGNGNTALHY--SVSHGNLAISSLLLDTGvCDVNHQNRAGYSALMLAALTSVGKEeedmAVVQRLFSMG-DVNAKaSQT 698
Cdd:PHA03095 183 VDDRFRSLLHHhlQSFKPRARIVRELIRAG-CDPAATDMLGNTPLHSMATGSSCKR----SLVLPLLIAGiSINAR-NRY 256

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 672058128 699 GQTALMLAISHGHQDMVAALLECGADVNVQDADGATAL 736
Cdd:PHA03095 257 GQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPL 294
Ank_2 pfam12796
Ankyrin repeats (3 copies);
613-657 1.26e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 41.64  E-value: 1.26e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 672058128  613 ELLAHVVNLADGNGNTALHYSVSHGNLAISSLLLDTGvCDVNHQN 657
Cdd:pfam12796  48 LLLEHADVNLKDNGRTALHYAARSGHLEIVKLLLEKG-ADINVKD 91
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 699-727 1.45e-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: 1.45e-04
                          10        20
                  ....*....|....*....|....*....
gi 672058128  699 GQTALMLAISHGHQDMVAALLECGADVNV 727
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 675-752 2.72e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 44.67  E-value: 2.72e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 672058128 675 EEEDMAVVQRLFSMG-DVNAKASQTgQTALMLAISHGHQDMVAALLECGADVNVQDADGATALMCASEYGRLDTVQLLL 752
Cdd:PHA02876 154 QQDELLIAEMLLEGGaDVNAKDIYC-ITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAII 231
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 625-785 3.08e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 44.21  E-value: 3.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672058128 625 NGNTALHYSVSHGNLAISSLLLDTGVcDVNHQNRAGYSALMLAA----------LTSVGK-----------------EEE 677
Cdd:PHA02875   1 MDQVALCDAILFGELDIARRLLDIGI-NPNFEIYDGISPIKLAMkfrdseaiklLMKHGAipdvkypdieselhdavEEG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672058128 678 DMAVVQRLFSMGD-VNAKASQTGQTALMLAISHGHQDMVAALLECGADVNVQDADGATALMCASEYGRLDTVQLLLAQPG 756
Cdd:PHA02875  80 DVKAVEELLDLGKfADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKA 159

                        170       180
                 ....*....|....*....|....*....
gi 672058128 757 CdLTILDNEGTSALAIALEAEQDEVAALL 785
Cdd:PHA02875 160 C-LDIEDCCGCTPLIIAMAKGDIAICKML 187
PHA02798 PHA02798
ankyrin-like protein; Provisional
 713-798 4.13e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 43.67  E-value: 4.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672058128 713 DMVAALLECGADVNVQDADGATALMCASEYGRLDTVQLLL--AQPGCDLTILDNEGTSALAIALEA----EQDEVAALLH 786
Cdd:PHA02798  90 DIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLfmIENGADTTLLDKDGFTMLQVYLQSnhhiDIEIIKLLLE 169

                         90
                 ....*....|..
gi 672058128 787 AHLTSNHHDSQE 798
Cdd:PHA02798 170 KGVDINTHNNKE 181
PHA03095 PHA03095
ankyrin-like protein; Provisional
 654-774 5.91e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 43.09  E-value: 5.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672058128 654 NHQNRAGYSALMLAALTSvgkEEEDMAVVQRLFSMG-DVNAKASqTGQTALMLAISHGHQ---DMVAALLECGADVNVQD 729
Cdd:PHA03095   5 ESVDIIMEAALYDYLLNA---SNVTVEEVRRLLAAGaDVNFRGE-YGKTPLHLYLHYSSEkvkDIVRLLLEAGADVNAPE 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 672058128 730 ADGATALMCASEYG-RLDTVQLLLaQPGCDLTILDNEGTSALAIAL 774
Cdd:PHA03095  81 RCGFTPLHLYLYNAtTLDVIKLLI-KAGADVNAKDKVGRTPLHVYL 125
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
129-322 8.93e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.98  E-value: 8.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672058128  129 VEH--TLLETSRRLEQAQAQERALSPARAATRSpRGSGRSSPAPNPALASPSPVLAspGPAQLQLVREQMAVALRRLREL 206
Cdd:COG4913   231 VEHfdDLERAHEALEDAREQIELLEPIRELAER-YAAARERLAELEYLRAALRLWF--AQRRLELLEAELEELRAELARL 307

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672058128  207 EDQARALP----ELQEQVRALRAEKARLLAGRVQP-EQDVEievrpDKLSQLRRLTERLATSDRGVRSRASPRAEDPDGL 281
Cdd:COG4913   308 EAELERLEarldALREELDELEAQIRGNGGDRLEQlEREIE-----RLERELEERERRRARLEALLAALGLPLPASAEEF 382

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 672058128  282 AARRSEGALQVLDPASRTPDGEPQTREAGTEVVPETREVDA 322
Cdd:COG4913   383 AALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRE 423
Ank_4 pfam13637
Ankyrin repeats (many copies);
626-669 1.05e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.64  E-value: 1.05e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 672058128  626 GNTALHYSVSHGNLAISSLLLDTGVcDVNHQNRAGYSALMLAAL 669
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGA-DINAVDGNGETALHFAAS 43
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 625-658 1.31e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. 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: 1.31e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 672058128  625 NGNTALHYSVSH-GNLAISSLLLDTGvCDVNHQNR 658
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKG-ADVNARDK 34
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 660-780 1.41e-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: 1.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672058128 660 GYSALMLAALTSVGKEEEdmaVVQRLFSMGDVNA------KASQT-----GQTALMLAISHGHQDMVAALLECGADVNVQ 728
Cdd:cd22194   94 GKTCLMKALLNINENTKE---IVRILLAFAEENGildrfiNAEYTeeayeGQTALNIAIERRQGDIVKLLIAKGADVNAH 170

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 672058128 729 DAD--------------GATALMCASEYGRLDTVQLLLAQPGCDLTILDNEGTSAL-AIALEAEQDE 780
Cdd:cd22194  171 AKGvffnpkykhegfyfGETPLALAACTNQPEIVQLLMEKESTDITSQDSRGNTVLhALVTVAEDSK 237
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 641-778 1.68e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 41.79  E-value: 1.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672058128 641 ISSLLLDTGVcDVNHQNR-AGYSALMLAAltsvgkEEEDMAVVQRLFSMG-DVNAkASQTGQTALMLAISHGHQDMVAAL 718
Cdd:PHA02878 149 ITKLLLSYGA-DINMKDRhKGNTALHYAT------ENKDQRLTELLLSYGaNVNI-PDKTNNSPLHHAVKHYNKPIVHIL 220

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 672058128 719 LECGADVNVQDADGATALMCASEYGRLDTVQLLLAQPGCDL----TILdneGTSALAIALEAEQ 778
Cdd:PHA02878 221 LENGASTDARDKCGNTPLHISVGYCKDYDILKLLLEHGVDVnaksYIL---GLTALHSSIKSER 281
Ank_4 pfam13637
Ankyrin repeats (many copies);
619-646 1.87e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.87  E-value: 1.87e-03
                          10        20
                  ....*....|....*....|....*...
gi 672058128  619 VNLADGNGNTALHYSVSHGNLAISSLLL 646
Cdd:pfam13637  27 INAVDGNGETALHFAASNGNVEVLKLLL 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 625-654 2.73e-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: 2.73e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 672058128   625 NGNTALHYSVSHGNLAISSLLLDTGVcDVN 654
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGA-DIN 29
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 718-795 2.87e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 41.20  E-value: 2.87e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 672058128 718 LLECGADVNVQDADGATALMCASEYGRLDTVQLLLAQpGCDLTILDNEGTSALAIALEAEQ-DEVAALLHAHLTSNHHD 795
Cdd:PHA02876 164 LLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSY-GADVNIIALDDLSVLECAVDSKNiDTIKAIIDNRSNINKND 241
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
63-326 5.27e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 40.60  E-value: 5.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672058128  63 APGPPHARRPRASGKGLAGARSPGAWTSSESLASDDGGASGALSP-GAFPGLSLPPLSPRSfsRNPRVEHTLLETSRRLE 141
Cdd:PRK07003 368 PGGGVPARVAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPkAAAAAAATRAEAPPA--APAPPATADRGDDAADG 445

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672058128 142 QAQAQERAlsPARAATRSPRGSGRSSPAPNPALAS-------------PSPVLASPGPAQLQLVREQMAVAL-RRLRELE 207
Cdd:PRK07003 446 DAPVPAKA--NARASADSRCDERDAQPPADSGSASapasdappdaafePAPRAAAPSAATPAAVPDARAPAAaSREDAPA 523

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672058128 208 DQARALPELQEQVRALRAEKARllAGRVQPEQDVeievrpdklsqLRRLTERLaTSDRGVRSRASPRAEDPDGLAARRSE 287
Cdd:PRK07003 524 AAAPPAPEARPPTPAAAAPAAR--AGGAAAALDV-----------LRNAGMRV-SSDRGARAAAAAKPAAAPAAAPKPAA 589

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 672058128 288 GALQVLDPASRTPDGEPQTREAGTEVVPETREvDAQAVP 326
Cdd:PRK07003 590 PRVAVQVPTPRARAATGDAPPNGAARAEQAAE-SRGAPP 627
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
137-366 6.77e-03

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 40.00  E-value: 6.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672058128 137 SRRLEQAQAQERALSPARAATRSPRGSGRSSPAPNPALASPSPVLASPGPAqlqlvREQMAVALRRLRELEDQARALPEL 216
Cdd:COG0515  252 EERYQSAAELAAALRAVLRSLAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA-----AAAAAAAAAAAAAAAAAAAAPAAA 326

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672058128 217 QEQVRALRAEKARLLAGRVQPEQDVEIEVRPDKLSQLRRLTERLATSDRGVRSRASPRAEDPDGLAARRSEGALQVLDPA 296
Cdd:COG0515  327 AAAAAAAAALAAAAAAAAAAAAAALLAAAAALAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAALAAAAAA 406

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672058128 297 SRTPDGEPQTREAGTEVVPETREVDAQAVPETREAGVEVVPETVEVDTWVTEALLGLPEAAERELELLRT 366
Cdd:COG0515  407 AAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAAAARLLAAAAAAAAAAAAAPLLAALLAAAALAAAAAA 476
Ank_5 pfam13857
Ankyrin repeats (many copies);
614-667 7.23e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.40  E-value: 7.23e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 672058128  614 LLAHV---VNLADGNGNTALHYSVSHGNLAISSLLLDTGvCDVNHQNRAGYSALMLA 667
Cdd:pfam13857   1 LLEHGpidLNRLDGEGYTPLHVAAKYGALEIVRVLLAYG-VDLNLKDEEGLTALDLA 56
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 626-727 8.39e-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: 8.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672058128  626 GNTALHYSVSHG-NLAISSLLLdtgvcdvNHQNRA--GYSALMLAALTSVGKEEEDMAVVQRLFSMGD----VNAKASQT 698
Cdd:TIGR00870  52 GRSALFVAAIENeNLELTELLL-------NLSCRGavGDTLLHAISLEYVDAVEAILLHLLAAFRKSGplelANDQYTSE 124

                          90       100       110
                  ....*....|....*....|....*....|..
gi 672058128  699 ---GQTALMLAISHGHQDMVAALLECGADVNV 727
Cdd:TIGR00870 125 ftpGITALHLAAHRQNYEIVKLLLERGASVPA 156
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 614-727 8.41e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 39.59  E-value: 8.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672058128 614 LLAH--VVNLADGNGNTALHYSVSHGNLAISSLLLDTGvcdvnhqnragysalmlAALTSVGKEeedmavvqrlfsmGDV 691
Cdd:PHA02875 154 LIDHkaCLDIEDCCGCTPLIIAMAKGDIAICKMLLDSG-----------------ANIDYFGKN-------------GCV 203

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 672058128 692 nakasqtgqTALMLAISHGHQDMVAALLECGADVNV 727
Cdd:PHA02875 204 ---------AALCYAIENNKIDIVRLFIKRGADCNI 230
PHA02741 PHA02741
hypothetical protein; Provisional
 706-800 8.57e-03

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 38.10  E-value: 8.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672058128 706 AISHGHQ---DMVAALLECGADVNVQDA-DGATALMCASEYGRLDTVQLLLAQPGCDLTILDNEGTSALAIALEAEQDEV 781
Cdd:PHA02741  68 AEKHEAQlaaEIIDHLIELGADINAQEMlEGDTALHLAAHRRDHDLAEWLCCQPGIDLHFCNADNKSPFELAIDNEDVAM 147

                         90
                 ....*....|....*....
gi 672058128 782 AALLHAHLTSNHHDSQEQS 800
Cdd:PHA02741 148 MQILREIVATSRGFSNENT 166
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 731-764 8.84e-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: 8.84e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 672058128  731 DGATALMCAS-EYGRLDTVQLLLaQPGCDLTILDN 764
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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