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Conserved domains on  [gi|13507632|ref|NP_109622|]
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KN motif and ankyrin repeat domain-containing protein 3 isoform 1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
595-770 2.06e-40

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 150.49  E-value: 2.06e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507632 595 LLAYVVNLADGNGNTALHYSVSHGNLAISSLLLDTGVcDVNHQNRAGYSALMLAAltsvgqEEEDMAVAQRLFSMG-DVN 673
Cdd:COG0666  75 AAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGA-DVNARDKDGETPLHLAA------YNGNLEIVKLLLEAGaDVN 147

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507632 674 AKASQtGQTALMLAISHGHQDMVAALLECGADVNVQDADGATALMCASEYGRLDTVQLLLAQpGCDLTILDNEGTSALAI 753
Cdd:COG0666 148 AQDND-GNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA-GADVNAKDNDGKTALDL 225

                       170
                ....*....|....*..
gi 13507632 754 ALEAEQDEVAALLHAHL 770
Cdd:COG0666 226 AAENGNLEIVKLLLEAG 242
KN_motif pfam12075
KN motif; This small motif is found at the N-terminus of Kank proteins and has been called the ...
 32-73 6.03e-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: 77.78  E-value: 6.03e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 13507632    32 PYSVETPYGFHLDLDFLKYVEEIERGPASRRTpgpPHARRPR 73
Cdd:pfam12075   1 PYSVETPYGFHLDLDFLKYVEDIESGQTIRRA---RVQRRPR 39
SPS1 super family cl43163
Serine/threonine protein kinase [Signal transduction mechanisms];
187-401 8.74e-04

Serine/threonine protein kinase [Signal transduction mechanisms];


The actual alignment was detected with superfamily member COG0515:

Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 42.69  E-value: 8.74e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507632 187 EQMAAALRRLRELEDQARALPELQEQVRALRAEKARLLAGRVQPEQEVEIEARPDKLAQLRRLTERLATSDRGVRSRASP 266
Cdd:COG0515 259 AELAAALRAVLRSLAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAPAAAAAAAAAAAALAA 338

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507632 267 RAEDPDGLAARRSEGALQVLDPGSRTPDGEPRTRETGTEVVPETREVDAQAVPETGEAGVEVVPETVEVDTWVTEELLGL 346
Cdd:COG0515 339 AAAAAAAAAAAALLAAAAALAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAA 418

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 13507632 347 PEAAERELELLRTSLEHQRGVSELLRGRLRELEEAHEAAVTRPQSRDVAAQTTLG 401
Cdd:COG0515 419 ALAAAAAAAAAAAAAAAAAAAAAARLLAAAAAAAAAAAAAPLLAALLAAAALAAA 473
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
595-770 2.06e-40

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 150.49  E-value: 2.06e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507632 595 LLAYVVNLADGNGNTALHYSVSHGNLAISSLLLDTGVcDVNHQNRAGYSALMLAAltsvgqEEEDMAVAQRLFSMG-DVN 673
Cdd:COG0666  75 AAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGA-DVNARDKDGETPLHLAA------YNGNLEIVKLLLEAGaDVN 147

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507632 674 AKASQtGQTALMLAISHGHQDMVAALLECGADVNVQDADGATALMCASEYGRLDTVQLLLAQpGCDLTILDNEGTSALAI 753
Cdd:COG0666 148 AQDND-GNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA-GADVNAKDNDGKTALDL 225

                       170
                ....*....|....*..
gi 13507632 754 ALEAEQDEVAALLHAHL 770
Cdd:COG0666 226 AAENGNLEIVKLLLEAG 242
Ank_2 pfam12796
Ankyrin repeats (3 copies);
684-766 3.78e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.77  E-value: 3.78e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507632   684 LMLAISHGHQDMVAALLECGADVNVQDADGATALMCASEYGRLDTVQLLLAQPGCDltiLDNEGTSALAIALEAEQDEVA 763
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN---LKDNGRTALHYAARSGHLEIV 77


                  ...
gi 13507632   764 ALL 766
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 6.03e-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: 77.78  E-value: 6.03e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 13507632    32 PYSVETPYGFHLDLDFLKYVEEIERGPASRRTpgpPHARRPR 73
Cdd:pfam12075   1 PYSVETPYGFHLDLDFLKYVEDIESGQTIRRA---RVQRRPR 39
PHA03095 PHA03095
ankyrin-like protein; Provisional
 600-756 2.02e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 60.81  E-value: 2.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507632  600 VNLADGNGNTALHYSVSHGN---LAISSLLLDTGVcDVNHQNRAGYSALMLAALTSvgqEEEDmaVAQRLFSMG-DVNAK 675
Cdd:PHA03095  40 VNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGA-DVNAPERCGFTPLHLYLYNA---TTLD--VIKLLIKAGaDVNAK 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507632  676 aSQTGQTAL--MLAISHGHQDMVAALLECGADVNVQDADGATALMCASEYGR--LDTVQLLLAQpGCDLTILDNEGTSAL 751
Cdd:PHA03095 114 -DKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanVELLRLLIDA-GADVYAVDDRFRSLL 191


                 ....*
gi 13507632  752 AIALE 756
Cdd:PHA03095 192 HHHLQ 196
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 680-708 3.24e-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: 3.24e-05
                           10        20
                   ....*....|....*....|....*....
gi 13507632    680 GQTALMLAISHGHQDMVAALLECGADVNV 708
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 607-717 6.34e-04

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 43.08  E-value: 6.34e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507632 607 GNTALHYSVSHGNLAISSLLLDTGVCDVNH----QNRAGYSALMLAALTsvgqeeEDMAVAQRLFSMG-DV-NAKASQT- 679
Cdd:cd22192  51 GETALHVAALYDNLEAAVVLMEAAPELVNEpmtsDLYQGETALHIAVVN------QNLNLVRELIARGaDVvSPRATGTf 124

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 13507632 680 -----------GQTALMLAISHGHQDMVAALLECGADVNVQDADGATAL 717
Cdd:cd22192 125 frpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
187-401 8.74e-04

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 42.69  E-value: 8.74e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507632 187 EQMAAALRRLRELEDQARALPELQEQVRALRAEKARLLAGRVQPEQEVEIEARPDKLAQLRRLTERLATSDRGVRSRASP 266
Cdd:COG0515 259 AELAAALRAVLRSLAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAPAAAAAAAAAAAALAA 338

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507632 267 RAEDPDGLAARRSEGALQVLDPGSRTPDGEPRTRETGTEVVPETREVDAQAVPETGEAGVEVVPETVEVDTWVTEELLGL 346
Cdd:COG0515 339 AAAAAAAAAAAALLAAAAALAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAA 418

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 13507632 347 PEAAERELELLRTSLEHQRGVSELLRGRLRELEEAHEAAVTRPQSRDVAAQTTLG 401
Cdd:COG0515 419 ALAAAAAAAAAAAAAAAAAAAAAARLLAAAAAAAAAAAAAPLLAALLAAAALAAA 473
HpnN TIGR03480
hopanoid biosynthesis associated RND transporter like protein HpnN; The genomes containing ...
 187-286 6.60e-03

hopanoid biosynthesis associated RND transporter like protein HpnN; The genomes containing members of this family share the machinery for the biosynthesis of hopanoid lipids. Furthermore, the genes of this family are usually located proximal to other components of this biological process. The proteins appear to be related to the RND family of export proteins, particularly the hydrophobe/amphiphile efflux-3 (HAE3) family represented by TIGR00921.


Pssm-ID: 274598 [Multi-domain]  Cd Length: 862  Bit Score: 39.98  E-value: 6.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507632   187 EQMAAALRRLRELeDQARAL----PELQEQVRALRAEKARLLAGRVQPEQEVEIEARPDKLAQLRRLTERLAtsdrgvrs 262
Cdd:TIGR03480 514 RALTERLEALPEV-DQVVTLpdfvPDDQEAKLALIADLALVLGPTLNPGEADPAPSAEEVAAALRRLAARLR-------- 584

                          90       100
                  ....*....|....*....|....
gi 13507632   263 RASPRAEDPDGLAARRSEGALQVL 286
Cdd:TIGR03480 585 AAAAKSQDPDAAAAGRLAASLDRL 608
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
595-770 2.06e-40

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 150.49  E-value: 2.06e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507632 595 LLAYVVNLADGNGNTALHYSVSHGNLAISSLLLDTGVcDVNHQNRAGYSALMLAAltsvgqEEEDMAVAQRLFSMG-DVN 673
Cdd:COG0666  75 AAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGA-DVNARDKDGETPLHLAA------YNGNLEIVKLLLEAGaDVN 147

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507632 674 AKASQtGQTALMLAISHGHQDMVAALLECGADVNVQDADGATALMCASEYGRLDTVQLLLAQpGCDLTILDNEGTSALAI 753
Cdd:COG0666 148 AQDND-GNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA-GADVNAKDNDGKTALDL 225

                       170
                ....*....|....*..
gi 13507632 754 ALEAEQDEVAALLHAHL 770
Cdd:COG0666 226 AAENGNLEIVKLLLEAG 242
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
600-766 2.24e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 130.07  E-value: 2.24e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507632 600 VNLADGNGNTALHYSVSHGNLAISSLLLDTGVcDVNHQNRAGYSALMLAAltsvgqEEEDMAVAQRLFSMG-DVNAKaSQ 678
Cdd:COG0666 113 VNARDKDGETPLHLAAYNGNLEIVKLLLEAGA-DVNAQDNDGNTPLHLAA------ANGNLEIVKLLLEAGaDVNAR-DN 184

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507632 679 TGQTALMLAISHGHQDMVAALLECGADVNVQDADGATALMCASEYGRLDTVQLLLAQpGCDLTILDNEGTSALAIALEAE 758
Cdd:COG0666 185 DGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA-GADLNAKDKDGLTALLLAAAAG 263


                ....*...
gi 13507632 759 QDEVAALL 766
Cdd:COG0666 264 AALIVKLL 271
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
595-769 3.77e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 126.61  E-value: 3.77e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507632 595 LLAYVVNLADGNGNTALHYSVSHGNLAISSLLLDTGVcDVNHQNRAGYSALMLAAltsvgqEEEDMAVAQRLFSMG-DVN 673
Cdd:COG0666  42 LALLALALADALGALLLLAAALAGDLLVALLLLAAGA-DINAKDDGGNTLLHAAA------RNGDLEIVKLLLEAGaDVN 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507632 674 AKASQtGQTALMLAISHGHQDMVAALLECGADVNVQDADGATALMCASEYGRLDTVQLLLAQpGCDLTILDNEGTSALAI 753
Cdd:COG0666 115 ARDKD-GETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEA-GADVNARDNDGETPLHL 192

                       170
                ....*....|....*.
gi 13507632 754 ALEAEQDEVAALLHAH 769
Cdd:COG0666 193 AAENGHLEIVKLLLEA 208
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
600-748 4.62e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 100.03  E-value: 4.62e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507632 600 VNLADGNGNTALHYSVSHGNLAISSLLLDTGVcDVNHQNRAGYSALMLAAltsvgqEEEDMAVAQRLFSMG-DVNAKASQ 678
Cdd:COG0666 146 VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGA-DVNARDNDGETPLHLAA------ENGHLEIVKLLLEAGaDVNAKDND 218

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507632 679 tGQTALMLAISHGHQDMVAALLECGADVNVQDADGATALMCASEYGRLDTVQLLLAQPGCDLTILDNEGT 748
Cdd:COG0666 219 -GKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
594-766 5.43e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 100.03  E-value: 5.43e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507632 594 ELLAYVVNLADGNGNTALHYSVSHGNLAISSLLLDTGVCDVNHQNRAGYSALMLAAltsvgqEEEDMAVAQRLFSMGDVN 673
Cdd:COG0666   7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAA------LAGDLLVALLLLAAGADI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507632 674 AKASQTGQTALMLAISHGHQDMVAALLECGADVNVQDADGATALMCASEYGRLDTVQLLLAQpGCDLTILDNEGTSALAI 753
Cdd:COG0666  81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA-GADVNAQDNDGNTPLHL 159

                       170
                ....*....|...
gi 13507632 754 ALEAEQDEVAALL 766
Cdd:COG0666 160 AAANGNLEIVKLL 172
Ank_2 pfam12796
Ankyrin repeats (3 copies);
684-766 3.78e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.77  E-value: 3.78e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507632   684 LMLAISHGHQDMVAALLECGADVNVQDADGATALMCASEYGRLDTVQLLLAQPGCDltiLDNEGTSALAIALEAEQDEVA 763
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN---LKDNGRTALHYAARSGHLEIV 77


                  ...
gi 13507632   764 ALL 766
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 6.03e-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: 77.78  E-value: 6.03e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 13507632    32 PYSVETPYGFHLDLDFLKYVEEIERGPASRRTpgpPHARRPR 73
Cdd:pfam12075   1 PYSVETPYGFHLDLDFLKYVEDIESGQTIRRA---RVQRRPR 39
Ank_2 pfam12796
Ankyrin repeats (3 copies);
611-710 7.92e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.00  E-value: 7.92e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507632   611 LHYSVSHGNLAISSLLLDTGvCDVNHQNRAGYSALMLAALTsvGQEEedmaVAQRLFSMGDVNAKASqtGQTALMLAISH 690
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENG-ADANLQDKNGRTALHLAAKN--GHLE----IVKLLLEHADVNLKDN--GRTALHYAARS 71

                          90       100
                  ....*....|....*....|
gi 13507632   691 GHQDMVAALLECGADVNVQD 710
Cdd:pfam12796  72 GHLEIVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
645-744 6.12e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 76.31  E-value: 6.12e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507632   645 LMLAAltsvgqEEEDMAVAQRLFSMG-DVNAKaSQTGQTALMLAISHGHQDMVAALLECgADVNVQDaDGATALMCASEY 723
Cdd:pfam12796   1 LHLAA------KNGNLELVKLLLENGaDANLQ-DKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARS 71

                          90       100
                  ....*....|....*....|.
gi 13507632   724 GRLDTVQLLLaQPGCDLTILD 744
Cdd:pfam12796  72 GHLEIVKLLL-EKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
644-769 3.18e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 68.06  E-value: 3.18e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507632 644 ALMLAALTSVGQEEEDMAVAQRLFSMGDVNAKASQTGQTALMLAISHGHQDMVAALLECGADVNVQDADGATALMCASEY 723
Cdd:COG0666  18 LLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARN 97

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 13507632 724 GRLDTVQLLLAQpGCDLTILDNEGTSALAIALEAEQDEVAALLHAH 769
Cdd:COG0666  98 GDLEIVKLLLEA-GADVNARDKDGETPLHLAAYNGNLEIVKLLLEA 142
Ank_4 pfam13637
Ankyrin repeats (many copies);
682-733 1.20e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 57.28  E-value: 1.20e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 13507632   682 TALMLAISHGHQDMVAALLECGADVNVQDADGATALMCASEYGRLDTVQLLL 733
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 600-756 2.02e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 60.81  E-value: 2.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507632  600 VNLADGNGNTALHYSVSHGN---LAISSLLLDTGVcDVNHQNRAGYSALMLAALTSvgqEEEDmaVAQRLFSMG-DVNAK 675
Cdd:PHA03095  40 VNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGA-DVNAPERCGFTPLHLYLYNA---TTLD--VIKLLIKAGaDVNAK 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507632  676 aSQTGQTAL--MLAISHGHQDMVAALLECGADVNVQDADGATALMCASEYGR--LDTVQLLLAQpGCDLTILDNEGTSAL 751
Cdd:PHA03095 114 -DKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanVELLRLLIDA-GADVYAVDDRFRSLL 191


                 ....*
gi 13507632  752 AIALE 756
Cdd:PHA03095 192 HHHLQ 196
PHA03095 PHA03095
ankyrin-like protein; Provisional
 582-724 7.90e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 58.88  E-value: 7.90e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507632  582 AGVLRGVKSLGPELLAyvvnlADGNGNTALHYSVSHGNLAISSL--LLDTGVcDVNHQNRAGYSALMLAALTSvgqeeED 659
Cdd:PHA03095 202 ARIVRELIRAGCDPAA-----TDMLGNTPLHSMATGSSCKRSLVlpLLIAGI-SINARNRYGQTPLHYAAVFN-----NP 270

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13507632  660 MAVAqRLFSMG-DVNAkASQTGQTALMLAISHGHQDMVAALLECGADVNVQDAdgatALMCASEYG 724
Cdd:PHA03095 271 RACR-RLIALGaDINA-VSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAA----TLNTASVAG 330
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 694-787 1.43e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 58.37  E-value: 1.43e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507632  694 DMVAA--LLECGADVNVQDADGATALMCASEYGRLDTVQLLLaQPGCDLTILDNEGTSALAIALEAEQDEVAALLHAHLT 771
Cdd:PTZ00322  94 DAVGAriLLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLL-EFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQ 172

                         90       100
                 ....*....|....*....|..
gi 13507632  772 SNHQG------QSSTGSPTAKE 787
Cdd:PTZ00322 173 CHFELganakpDSFTGKPPSLE 194
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 600-733 3.17e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 56.60  E-value: 3.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507632  600 VNLADGNGNTALHYSVSH--GNLAISSLLLDTGvCDVNHQNRAGYSALMLAaltsVGQEEEDMAVAQRLFSMG-DVNAKA 676
Cdd:PHA03100  99 VNAPDNNGITPLLYAISKksNSYSIVEYLLDNG-ANVNIKNSDGENLLHLY----LESNKIDLKILKLLIDKGvDINAKN 173

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13507632  677 S---------------QTGQTALMLAISHGHQDMVAALLECGADVNVQDADGATALMCASEYGRLDTVQLLL 733
Cdd:PHA03100 174 RvnyllsygvpinikdVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLL 245
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 600-756 2.15e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 54.20  E-value: 2.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507632  600 VNLADGNGNTALHYSVSHGNLAISSLLLDTGVCdVNHQNRAGYSALMLAAltsvgqEEEDMAVAQRLFSMGDVNAKASQT 679
Cdd:PHA02874 150 VNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAY-ANVKDNNGESPLHNAA------EYGDYACIKLLIDHGNHIMNKCKN 222

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13507632  680 GQTALMLAISHGHQdmVAALLECGADVNVQDADGATALMCASEYG-RLDTVQLLLAQPGcDLTILDNEGTSALAIALE 756
Cdd:PHA02874 223 GFTPLHNAIIHNRS--AIELLINNASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKA-DISIKDNKGENPIDTAFK 297
Ank_5 pfam13857
Ankyrin repeats (many copies);
699-754 2.30e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.11  E-value: 2.30e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 13507632   699 LLECG-ADVNVQDADGATALMCASEYGRLDTVQLLLAqPGCDLTILDNEGTSALAIA 754
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLA-YGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
671-717 4.89e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.34  E-value: 4.89e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 13507632   671 DVNAKaSQTGQTALMLAISHGHQDMVAALLECGADVNVQDADGATAL 717
Cdd:pfam13857   8 DLNRL-DGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 680-710 8.19e-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: 45.74  E-value: 8.19e-07
                          10        20        30
                  ....*....|....*....|....*....|..
gi 13507632   680 GQTALMLAISH-GHQDMVAALLECGADVNVQD 710
Cdd:pfam00023   2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
Ank_2 pfam12796
Ankyrin repeats (3 copies);
717-780 1.16e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 47.42  E-value: 1.16e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13507632   717 LMCASEYGRLDTVQLLLaQPGCDLTILDNEGTSALAIALEAEQDEVAALLHAHLTSNHQGQSST 780
Cdd:pfam12796   1 LHLAAKNGNLELVKLLL-ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGRT 63
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 611-766 1.40e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 51.79  E-value: 1.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507632  611 LHYSVSHGNLAISSLLLDTGVcdvNHQNRAGYSALMLAALTSVGQEEEDMAVAQRLFSMGDvnakasQTGQTALMLAISH 690
Cdd:PLN03192 498 LQHHKELHDLNVGDLLGDNGG---EHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGD------SKGRTPLHIAASK 568

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507632  691 GHQDMVAALLECGADVNVQDADGATAL------------------------------MC-ASEYGRLDTVQLLLAQpGCD 739
Cdd:PLN03192 569 GYEDCVLVLLKHACNVHIRDANGNTALwnaisakhhkifrilyhfasisdphaagdlLCtAAKRNDLTAMKELLKQ-GLN 647

                        170       180
                 ....*....|....*....|....*..
gi 13507632  740 LTILDNEGTSALAIALEAEQDEVAALL 766
Cdd:PLN03192 648 VDSEDHQGATALQVAMAEDHVDMVRLL 674
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 601-733 1.69e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 51.79  E-value: 1.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507632  601 NLADGNGNTALHYSVSHGNLAISSLLLDTGvCDVNHQNRAGYSALMLAAltsvgqeeedMAVAQRLFSMGDVNAKAS--Q 678
Cdd:PLN03192 552 DIGDSKGRTPLHIAASKGYEDCVLVLLKHA-CNVHIRDANGNTALWNAI----------SAKHHKIFRILYHFASISdpH 620

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 13507632  679 TGQTALMLAISHGHQDMVAALLECGADVNVQDADGATALMCASEYGRLDTVQLLL 733
Cdd:PLN03192 621 AAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLI 675
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 600-720 1.83e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 51.42  E-value: 1.83e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507632  600 VNLADGNGNTALHYSVSHGNLAISSLLLDTGvCDVNHQNRAGYSALMLaaltSVGQeEEDMAVAQRLFSMG-DVNAKASQ 678
Cdd:PHA02878 194 VNIPDKTNNSPLHHAVKHYNKPIVHILLENG-ASTDARDKCGNTPLHI----SVGY-CKDYDILKLLLEHGvDVNAKSYI 267

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 13507632  679 TGQTALMLAIShgHQDMVAALLECGADVNVQDADGATALMCA 720
Cdd:PHA02878 268 LGLTALHSSIK--SERKLKLLLEYGADINSLNSYKLTPLSSA 307
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 626-755 2.08e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 51.12  E-value: 2.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507632  626 LLDTGVcDVNHQNRAGYSALMLAAltsvgqEEEDMAVAQRLFSMG-DVNAKaSQTGQTALMLAISHGHQDMVAALLECGA 704
Cdd:PHA02874 110 ILDCGI-DVNIKDAELKTFLHYAI------KKGDLESIKMLFEYGaDVNIE-DDNGCYPIHIAIKHNFFDIIKLLLEKGA 181

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 13507632  705 DVNVQDADGATALMCASEYGRLDTVQLLLAQpGCDLTILDNEGTSALAIAL 755
Cdd:PHA02874 182 YANVKDNNGESPLHNAAEYGDYACIKLLIDH-GNHIMNKCKNGFTPLHNAI 231
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 680-739 2.24e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.05  E-value: 2.24e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507632  680 GQTALMLAISHGHQDMVAALLECGADVNVQDADGATALMCASEYGRLDTVQLLLAQPGCD 739
Cdd:PTZ00322 115 GRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCH 174
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 600-766 6.42e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 49.58  E-value: 6.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507632  600 VNLADGNGNTALHYSVSHGNLAISSLLLDTGVcDVNHQNRAGYSALmlaaLTSVGQEEEDMAvaqRLFSMGDVNAKasqt 679
Cdd:PHA02874  28 INISVDETTTPLIDAIRSGDAKIVELFIKHGA-DINHINTKIPHPL----LTAIKIGAHDII---KLLIDNGVDTS---- 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507632  680 gqtalMLAISHGHQDMVAALLECGADVNVQDADGATALMCASEYGRLDTVQLLLaQPGCDLTILDNEGTSALAIALEAEQ 759
Cdd:PHA02874  96 -----ILPIPCIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLF-EYGADVNIEDDNGCYPIHIAIKHNF 169


                 ....*..
gi 13507632  760 DEVAALL 766
Cdd:PHA02874 170 FDIIKLL 176
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 611-733 2.33e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 47.74  E-value: 2.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507632  611 LHYSVSHGNLAISSLLLDTGvCDVNhQNRAGYSALMLAALTSVGQEEEDMAVAQRLFSMG-DVNAKaSQTGQTALMLAIS 689
Cdd:PHA03100  39 LYLAKEARNIDVVKILLDNG-ADIN-SSTKNNSTPLHYLSNIKYNLTDVKEIVKLLLEYGaNVNAP-DNNGITPLLYAIS 115

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 13507632  690 H--GHQDMVAALLECGADVNVQDADGATALMCASEYGR--LDTVQLLL 733
Cdd:PHA03100 116 KksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLI 163
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 680-708 3.24e-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: 3.24e-05
                           10        20
                   ....*....|....*....|....*....
gi 13507632    680 GQTALMLAISHGHQDMVAALLECGADVNV 708
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 637-776 3.43e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 47.56  E-value: 3.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507632  637 QNRAGYSALMLAALTSVGQEEEDMAVAQRLFSMG----DVNAKASqtgqtaLMLAISHGHQDMVAALLECGADVNVQDAD 712
Cdd:PLN03192 484 QTRQEDNVVILKNFLQHHKELHDLNVGDLLGDNGgehdDPNMASN------LLTVASTGNAALLEELLKAKLDPDIGDSK 557

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13507632  713 GATALMCASEYGRLDTVQLLLAQpGCDLTILDNEGTSALAIALEAEQDEVAALLH--AHLTSNHQG 776
Cdd:PLN03192 558 GRTPLHIAASKGYEDCVLVLLKH-ACNVHIRDANGNTALWNAISAKHHKIFRILYhfASISDPHAA 622
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 600-706 4.32e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 47.17  E-value: 4.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507632  600 VNLADGNGNTALHYSVSHGNLAISSLLLDTGVCDVNHqnrAGYSALMLAAltsvgqEEEDMAVAQRLFSMG-DVNAKASQ 678
Cdd:PLN03192 584 VHIRDANGNTALWNAISAKHHKIFRILYHFASISDPH---AAGDLLCTAA------KRNDLTAMKELLKQGlNVDSEDHQ 654

                         90       100
                 ....*....|....*....|....*...
gi 13507632  679 tGQTALMLAISHGHQDMVAALLECGADV 706
Cdd:PLN03192 655 -GATALQVAMAEDHVDMVRLLIMNGADV 681
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 656-733 6.87e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.60  E-value: 6.87e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13507632  656 EEEDMAVAQRLFSMG-DVNAKASQTgQTALMLAISHGHQDMVAALLECGADVNVQDADGATALMCASEYGRLDTVQLLL 733
Cdd:PHA02876 154 QQDELLIAEMLLEGGaDVNAKDIYC-ITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAII 231
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 606-781 7.26e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 46.14  E-value: 7.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507632  606 NGNTALHYSVSHGNLAISSLLLDTGVcDVNHQNRAGYSALMLAALTSvgqeeeDMAVAQRLFSMGDVNAKASQTGQTALM 685
Cdd:PHA02875 101 DGMTPLHLATILKKLDIMKLLIARGA-DPDIPNTDKFSPLHLAVMMG------DIKGIELLIDHKACLDIEDCCGCTPLI 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507632  686 LAISHGHQDMVAALLECGADVNVQDADGATALMC-ASEYGRLDTVQLLLAQpGCD---LTILDNEGTSALAI----ALEA 757
Cdd:PHA02875 174 IAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCyAIENNKIDIVRLFIKR-GADcniMFMIEGEECTILDMicnmCTNL 252

                        170       180
                 ....*....|....*....|....
gi 13507632  758 EQDEVAALLHAHLTSNHQGQSSTG 781
Cdd:PHA02875 253 ESEAIDALIADIAIRIHKKTIRRD 276
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 597-729 8.00e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 45.72  E-value: 8.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507632  597 AYVvNLADGNGNTALHYSVSHGNLAISSLLLDTGVCDVNHQNRaGYSALMLAALTSvgQEEEDMAVAQRLFSMGDVNaka 676
Cdd:PHA02874 181 AYA-NVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKN-GFTPLHNAIIHN--RSAIELLINNASINDQDID--- 253

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 13507632  677 sqtGQTALMLAISHG-HQDMVAALLECGADVNVQDADGATALMCASEYGRLDTV 729
Cdd:PHA02874 254 ---GSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTAFKYINKDPV 304
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 680-708 1.40e-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: 1.40e-04
                          10        20
                  ....*....|....*....|....*....
gi 13507632   680 GQTALMLAISHGHQDMVAALLECGADVNV 708
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_2 pfam12796
Ankyrin repeats (3 copies);
594-638 3.11e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 40.48  E-value: 3.11e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 13507632   594 ELLAYVVNLADGNGNTALHYSVSHGNLAISSLLLDTGvCDVNHQN 638
Cdd:pfam12796  48 LLLEHADVNLKDNGRTALHYAARSGHLEIVKLLLEKG-ADINVKD 91
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 600-772 3.96e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 43.72  E-value: 3.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507632  600 VNLADGNGNTALHYSVSHGN-LAISSLLLDTGVCDVNHQ---------NRAGYSALMLaaLTSVGQEEEDM--------- 660
Cdd:PHA02878  63 VNQPDHRDLTPLHIICKEPNkLGMKEMIRSINKCSVFYTlvaikdafnNRNVEIFKII--LTNRYKNIQTIdlvyidkks 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507632  661 -------AVAQRLFSMG-DVNAKASQTGQTALMLAISHGHQDMVAALLECGADVNVQDADGATALMCASEYGRLDTVQLL 732
Cdd:PHA02878 141 kddiieaEITKLLLSYGaDINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHIL 220

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 13507632  733 LaQPGCDLTILDNEGTSALAIALEAEQD-EVAALLHAHLTS 772
Cdd:PHA02878 221 L-ENGASTDARDKCGNTPLHISVGYCKDyDILKLLLEHGVD 260
PHA03095 PHA03095
ankyrin-like protein; Provisional
 603-717 5.06e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 43.47  E-value: 5.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507632  603 ADGNGNTALHY--SVSHGNLAISSLLLDTGvCDVNHQNRAGYSALMLAALTSvgqEEEDMAVAQRLFSMGDVNAKaSQTG 680
Cdd:PHA03095 183 VDDRFRSLLHHhlQSFKPRARIVRELIRAG-CDPAATDMLGNTPLHSMATGS---SCKRSLVLPLLIAGISINAR-NRYG 257

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 13507632  681 QTALMLAISHGHQDMVAALLECGADVNVQDADGATAL 717
Cdd:PHA03095 258 QTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPL 294
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 607-717 6.34e-04

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 43.08  E-value: 6.34e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507632 607 GNTALHYSVSHGNLAISSLLLDTGVCDVNH----QNRAGYSALMLAALTsvgqeeEDMAVAQRLFSMG-DV-NAKASQT- 679
Cdd:cd22192  51 GETALHVAALYDNLEAAVVLMEAAPELVNEpmtsDLYQGETALHIAVVN------QNLNLVRELIARGaDVvSPRATGTf 124

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 13507632 680 -----------GQTALMLAISHGHQDMVAALLECGADVNVQDADGATAL 717
Cdd:cd22192 125 frpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 598-652 6.95e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 42.73  E-value: 6.95e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 13507632  598 YVVNLADGNGNTALHYSVSHGNLAISSLLLDTGvCDVNHQNRAGYSALMLAALTS 652
Cdd:PHA03100 183 VPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLG-ANPNLVNKYGDTPLHIAILNN 236
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 622-759 7.43e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 42.95  E-value: 7.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507632  622 ISSLLLDTGVcDVNHQNR-AGYSALMLAAltsvgqEEEDMAVAQRLFSMG-DVNAkASQTGQTALMLAISHGHQDMVAAL 699
Cdd:PHA02878 149 ITKLLLSYGA-DINMKDRhKGNTALHYAT------ENKDQRLTELLLSYGaNVNI-PDKTNNSPLHHAVKHYNKPIVHIL 220

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13507632  700 LECGADVNVQDADGATALMCASEYGRLDTVQLLLAQPGCDL----TILdneGTSALAIALEAEQ 759
Cdd:PHA02878 221 LENGASTDARDKCGNTPLHISVGYCKDYDILKLLLEHGVDVnaksYIL---GLTALHSSIKSER 281
PHA02798 PHA02798
ankyrin-like protein; Provisional
 694-757 8.10e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 42.90  E-value: 8.10e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13507632  694 DMVAALLECGADVNVQDADGATALMCASEYGRLDTVQLLL--AQPGCDLTILDNEGTSALAIALEA 757
Cdd:PHA02798  90 DIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLfmIENGADTTLLDKDGFTMLQVYLQS 155
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
187-401 8.74e-04

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 42.69  E-value: 8.74e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507632 187 EQMAAALRRLRELEDQARALPELQEQVRALRAEKARLLAGRVQPEQEVEIEARPDKLAQLRRLTERLATSDRGVRSRASP 266
Cdd:COG0515 259 AELAAALRAVLRSLAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAPAAAAAAAAAAAALAA 338

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507632 267 RAEDPDGLAARRSEGALQVLDPGSRTPDGEPRTRETGTEVVPETREVDAQAVPETGEAGVEVVPETVEVDTWVTEELLGL 346
Cdd:COG0515 339 AAAAAAAAAAAALLAAAAALAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAA 418

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 13507632 347 PEAAERELELLRTSLEHQRGVSELLRGRLRELEEAHEAAVTRPQSRDVAAQTTLG 401
Cdd:COG0515 419 ALAAAAAAAAAAAAAAAAAAAAAARLLAAAAAAAAAAAAAPLLAALLAAAALAAA 473
Ank_4 pfam13637
Ankyrin repeats (many copies);
607-650 1.01e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.64  E-value: 1.01e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 13507632   607 GNTALHYSVSHGNLAISSLLLDTGVcDVNHQNRAGYSALMLAAL 650
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGA-DINAVDGNGETALHFAAS 43
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 606-766 1.36e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 41.90  E-value: 1.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507632  606 NGNTALHYSVSHGNLAISSLLLDTGVcDVNHQNRAGYSALMLAA----------LTSVGQ-----------------EEE 658
Cdd:PHA02875   1 MDQVALCDAILFGELDIARRLLDIGI-NPNFEIYDGISPIKLAMkfrdseaiklLMKHGAipdvkypdieselhdavEEG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507632  659 DMAVAQRLFSMGD-VNAKASQTGQTALMLAISHGHQDMVAALLECGADVNVQDADGATALMCASEYGRLDTVQLLLAQPG 737
Cdd:PHA02875  80 DVKAVEELLDLGKfADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKA 159

                        170       180
                 ....*....|....*....|....*....
gi 13507632  738 CdLTILDNEGTSALAIALEAEQDEVAALL 766
Cdd:PHA02875 160 C-LDIEDCCGCTPLIIAMAKGDIAICKML 187
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 606-639 1.47e-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: 1.47e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 13507632   606 NGNTALHYSVSH-GNLAISSLLLDTGvCDVNHQNR 639
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKG-ADVNARDK 34
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
121-359 1.50e-03

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 41.92  E-value: 1.50e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507632 121 RSLSRNPrvehtlletSRRLEQAQARERALSPARAVTRSPRGSG--RSSPAPNPALASPGPAQLQLVREQMAAALRRLRE 198
Cdd:COG0515 245 RALAKDP---------EERYQSAAELAAALRAVLRSLAAAAAAAaaAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 315

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507632 199 LEDQARALPELQEQVRALRAEKARLLAGRVQPEQEVEIEARPDKLAQLRRLTERLATSDRGVRSRASPRAEDPDGLAARR 278
Cdd:COG0515 316 AAAAAAAPAAAAAAAAAAAALAAAAAAAAAAAAAALLAAAAALAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAA 395

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507632 279 SEGALQVLDPGSRTPDGEPRTRETGTEVVPETREVDAQAVPETGEAGVEVVPETVEVDTWVTEELLGLPEAAERELELLR 358
Cdd:COG0515 396 AAAALAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAAAARLLAAAAAAAAAAAAAPLLAALLAAAALAAAAA 475


                .
gi 13507632 359 T 359
Cdd:COG0515 476 A 476
Ank_4 pfam13637
Ankyrin repeats (many copies);
600-627 1.81e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.87  E-value: 1.81e-03
                          10        20
                  ....*....|....*....|....*...
gi 13507632   600 VNLADGNGNTALHYSVSHGNLAISSLLL 627
Cdd:pfam13637  27 INAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 680-761 2.00e-03

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 41.67  E-value: 2.00e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507632 680 GQTALMLAISHGHQDMVAALLECGADVNVQDAD--------------GATALMCASEYGRLDTVQLLLAQPGCDLTILDN 745
Cdd:cd22194 141 GQTALNIAIERRQGDIVKLLIAKGADVNAHAKGvffnpkykhegfyfGETPLALAACTNQPEIVQLLMEKESTDITSQDS 220

                        90
                ....*....|....*..
gi 13507632 746 EGTSAL-AIALEAEQDE 761
Cdd:cd22194 221 RGNTVLhALVTVAEDSK 237
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
129-315 2.37e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.44  E-value: 2.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507632  129 VEH--TLLETSRRLEQAQARERALSPARAVTRSpRGSGRSSPAPNPALASPGPAQ-----LQLVREQMAAALRRLRELED 201
Cdd:COG4913  231 VEHfdDLERAHEALEDAREQIELLEPIRELAER-YAAARERLAELEYLRAALRLWfaqrrLELLEAELEELRAELARLEA 309

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507632  202 QARALP----ELQEQVRALRAEKARLLAGRVQPEQEvEIEARPDKLAQLRRLTERLatsDRGVRSRASPRAEDPDGLAAR 277
Cdd:COG4913  310 ELERLEarldALREELDELEAQIRGNGGDRLEQLER-EIERLERELEERERRRARL---EALLAALGLPLPASAEEFAAL 385

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 13507632  278 RSEGALQVLDPGSRTPDGEPRTRETGTEVVPETREVDA 315
Cdd:COG4913  386 RAEAAALLEALEEELEALEEALAEAEAALRDLRRELRE 423
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 606-635 2.64e-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: 2.64e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 13507632    606 NGNTALHYSVSHGNLAISSLLLDTGVcDVN 635
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGA-DIN 29
PHA03095 PHA03095
ankyrin-like protein; Provisional
 635-755 5.23e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 40.01  E-value: 5.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507632  635 NHQNRAGYSALMLAALTSvgqEEEDMAVAQRLFSMG-DVNAKASqTGQTALMLAISHGHQ---DMVAALLECGADVNVQD 710
Cdd:PHA03095   5 ESVDIIMEAALYDYLLNA---SNVTVEEVRRLLAAGaDVNFRGE-YGKTPLHLYLHYSSEkvkDIVRLLLEAGADVNAPE 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 13507632  711 ADGATALMCASEYG-RLDTVQLLLaQPGCDLTILDNEGTSALAIAL 755
Cdd:PHA03095  81 RCGFTPLHLYLYNAtTLDVIKLLI-KAGADVNAKDKVGRTPLHVYL 125
HpnN TIGR03480
hopanoid biosynthesis associated RND transporter like protein HpnN; The genomes containing ...
 187-286 6.60e-03

hopanoid biosynthesis associated RND transporter like protein HpnN; The genomes containing members of this family share the machinery for the biosynthesis of hopanoid lipids. Furthermore, the genes of this family are usually located proximal to other components of this biological process. The proteins appear to be related to the RND family of export proteins, particularly the hydrophobe/amphiphile efflux-3 (HAE3) family represented by TIGR00921.


Pssm-ID: 274598 [Multi-domain]  Cd Length: 862  Bit Score: 39.98  E-value: 6.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507632   187 EQMAAALRRLRELeDQARAL----PELQEQVRALRAEKARLLAGRVQPEQEVEIEARPDKLAQLRRLTERLAtsdrgvrs 262
Cdd:TIGR03480 514 RALTERLEALPEV-DQVVTLpdfvPDDQEAKLALIADLALVLGPTLNPGEADPAPSAEEVAAALRRLAARLR-------- 584

                          90       100
                  ....*....|....*....|....
gi 13507632   263 RASPRAEDPDGLAARRSEGALQVL 286
Cdd:TIGR03480 585 AAAAKSQDPDAAAAGRLAASLDRL 608
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 699-766 6.82e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 40.05  E-value: 6.82e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13507632  699 LLECGADVNVQDADGATALMCASEYGRLDTVQLLLAQpGCDLTILDNEGTSALAIALEAEQ-DEVAALL 766
Cdd:PHA02876 164 LLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSY-GADVNIIALDDLSVLECAVDSKNiDTIKAII 231
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
130-258 9.76e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.37  E-value: 9.76e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507632 130 EHTLLETSRRLEQAQARERALSPARAVTRSPRGsgrsspapnpalASPGPAQLQLVREQMAAALRRLRELEDQARALPEL 209
Cdd:COG4717  94 QEELEELEEELEELEAELEELREELEKLEKLLQ------------LLPLYQELEALEAELAELPERLEELEERLEELREL 161

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 13507632 210 QEQVRALRAEKARLLAGRVQPEQEVEIEAR---PDKLAQLRRLTERLATSDR 258
Cdd:COG4717 162 EEELEELEAELAELQEELEELLEQLSLATEeelQDLAEELEELQQRLAELEE 213
 
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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