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Conserved domains on  [gi|2217376309|ref|XP_047279001|]
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KN motif and ankyrin repeat domain-containing protein 1 isoform X1 [Homo sapiens]

Protein Classification

KN_motif domain-containing protein( domain architecture ID 13778393)

KN_motif domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1155-1323 3.03e-40

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 150.87  E-value: 3.03e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376309 1155 INLADGNGNTALHYSVSHSNFEIVKLLLDADVcNVDHQNKAGYTPIMLAALAaveaeKDMRIVEELFGCG-DVNAKASQa 1233
Cdd:COG0666     80 INAKDDGGNTLLHAAARNGDLEIVKLLLEAGA-DVNARDKDGETPLHLAAYN-----GNLEIVKLLLEAGaDVNAQDND- 152

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376309 1234 GQTALMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQpGCNGHLEDNDGSTALSIALEAGH 1313
Cdd:COG0666    153 GNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA-GADVNAKDNDGKTALDLAAENGN 231

                          170
                   ....*....|
gi 2217376309 1314 KDIAVLLYAH 1323
Cdd:COG0666    232 LEIVKLLLEA 241
KN_motif pfam12075
KN motif; This small motif is found at the N-terminus of Kank proteins and has been called the ...
 30-68 1.43e-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: 80.09  E-value: 1.43e-18
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2217376309   30 PYFVETPYGYQLDLDFLKYVDDIQKGNTIKRLNIQKRRK 68
Cdd:pfam12075    1 PYSVETPYGFHLDLDFLKYVEDIESGQTIRRARVQRRPR 39
YhaN super family cl34808
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
269-496 2.76e-04

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


The actual alignment was detected with superfamily member COG4717:

Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.14  E-value: 2.76e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376309  269 IALKRLKELEEQVRTIPVLQVKISVLQEEKRQLVSQLKNQRAasQINVCGVRKRSYSA--GNASQLEQLSRARRSGGELY 346
Cdd:COG4717     68 LNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEA--ELEELREELEKLEKllQLLPLYQELEALEAELAELP 145

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376309  347 IDYEeeemetveQSTQRIKEFRQLTADMQALEQKIQdsscEASSELREngECRSVAVGAEENMNDIVvyhrgsrscKDAa 426
Cdd:COG4717    146 ERLE--------ELEERLEELRELEEELEELEAELA----ELQEELEE--LLEQLSLATEEELQDLA---------EEL- 201

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376309  427 vgtlvemrncgvsvtEAMLGVMTEADKEIELQQQTIESLKEKIYRLEVQLRETTHDREMTKLKQELQAAG 496
Cdd:COG4717    202 ---------------EELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAA 256
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1155-1323 3.03e-40

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 150.87  E-value: 3.03e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376309 1155 INLADGNGNTALHYSVSHSNFEIVKLLLDADVcNVDHQNKAGYTPIMLAALAaveaeKDMRIVEELFGCG-DVNAKASQa 1233
Cdd:COG0666     80 INAKDDGGNTLLHAAARNGDLEIVKLLLEAGA-DVNARDKDGETPLHLAAYN-----GNLEIVKLLLEAGaDVNAQDND- 152

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376309 1234 GQTALMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQpGCNGHLEDNDGSTALSIALEAGH 1313
Cdd:COG0666    153 GNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA-GADVNAKDNDGKTALDLAAENGN 231

                          170
                   ....*....|
gi 2217376309 1314 KDIAVLLYAH 1323
Cdd:COG0666    232 LEIVKLLLEA 241
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1238-1323 1.41e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 93.26  E-value: 1.41e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376309 1238 LMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQPGCNghlEDNDGSTALSIALEAGHKDIA 1317
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN---LKDNGRTALHYAARSGHLEIV 77


                   ....*.
gi 2217376309 1318 VLLYAH 1323
Cdd:pfam12796   78 KLLLEK 83
KN_motif pfam12075
KN motif; This small motif is found at the N-terminus of Kank proteins and has been called the ...
 30-68 1.43e-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: 80.09  E-value: 1.43e-18
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2217376309   30 PYFVETPYGYQLDLDFLKYVDDIQKGNTIKRLNIQKRRK 68
Cdd:pfam12075    1 PYSVETPYGFHLDLDFLKYVEDIESGQTIRRARVQRRPR 39
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 1144-1325 1.73e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 71.23  E-value: 1.73e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376309 1144 EAISPDVLRYVINL-ADGNGN-----TALHY-----SVSHSNFEIVKLLLDADVcNVDHQNKAGYTPIMLAALAAVEAEK 1212
Cdd:PHA03100    44 EARNIDVVKILLDNgADINSStknnsTPLHYlsnikYNLTDVKEIVKLLLEYGA-NVNAPDNNGITPLLYAISKKSNSYS 122

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376309 1213 dmrIVEELFGCG-DVNAKASQaGQTALMLAVSHGRIDM------------------VKGLLACGADVNIQDDEGSTALMC 1273
Cdd:PHA03100   123 ---IVEYLLDNGaNVNIKNSD-GENLLHLYLESNKIDLkilkllidkgvdinaknrVNYLLSYGVPINIKDVYGFTPLHY 198

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2217376309 1274 ASEHGHVEIVKLLLAQpGCNGHLEDNDGSTALSIALEAGHKDI-AVLLYAHVN 1325
Cdd:PHA03100   199 AVYNNNPEFVKYLLDL-GANPNLVNKYGDTPLHIAILNNNKEIfKLLLNNGPS 250
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 1162-1321 1.99e-06

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: 52.32  E-value: 1.99e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376309 1162 GNTALHYSVSHSNFEIVKLLLDADvcnvdhqnkagytPIMLaalaaveaekDMRIVEELFgcgdvnakasqAGQTALMLA 1241
Cdd:cd22192     51 GETALHVAALYDNLEAAVVLMEAA-------------PELV----------NEPMTSDLY-----------QGETALHIA 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376309 1242 VSHGRIDMVKGLLACGADVNIQDDEGS------TALMCASEH--------GHVEIVKLLLaQPGCNGHLEDNDGSTALSI 1307
Cdd:cd22192     97 VVNQNLNLVRELIARGADVVSPRATGTffrpgpKNLIYYGEHplsfaacvGNEEIVRLLI-EHGADIRAQDSLGNTVLHI 175

                          170
                   ....*....|....
gi 2217376309 1308 ALEAGHKDIAVLLY 1321
Cdd:cd22192    176 LVLQPNKTFACQMY 189
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 1234-1262 4.52e-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: 4.52e-05
                            10        20
                    ....*....|....*....|....*....
gi 2217376309  1234 GQTALMLAVSHGRIDMVKGLLACGADVNI 1262
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
269-496 2.76e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.14  E-value: 2.76e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376309  269 IALKRLKELEEQVRTIPVLQVKISVLQEEKRQLVSQLKNQRAasQINVCGVRKRSYSA--GNASQLEQLSRARRSGGELY 346
Cdd:COG4717     68 LNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEA--ELEELREELEKLEKllQLLPLYQELEALEAELAELP 145

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376309  347 IDYEeeemetveQSTQRIKEFRQLTADMQALEQKIQdsscEASSELREngECRSVAVGAEENMNDIVvyhrgsrscKDAa 426
Cdd:COG4717    146 ERLE--------ELEERLEELRELEEELEELEAELA----ELQEELEE--LLEQLSLATEEELQDLA---------EEL- 201

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376309  427 vgtlvemrncgvsvtEAMLGVMTEADKEIELQQQTIESLKEKIYRLEVQLRETTHDREMTKLKQELQAAG 496
Cdd:COG4717    202 ---------------EELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAA 256
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 265-495 5.66e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.20  E-value: 5.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376309  265 EQMAIALKRLKELEEQVRTIPVLQVKISVLQEEKRQLVSQLKNQ--RAASQINVCGVRKRSYSAGNASQLEQLS--RARR 340
Cdd:TIGR02168  691 EKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDlaRLEAEVEQLEERIAQLSKELTELEAEIEelEERL 770

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376309  341 SGGELYIDYEEEEMETVEQSTQRIK-EFRQLTADMQALEQKIQDSSCEASSELRENGECRSVAVGAEENMNDIvvyHRGS 419
Cdd:TIGR02168  771 EEAEEELAEAEAEIEELEAQIEQLKeELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDL---EEQI 847

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217376309  420 RSCKDAAVGTLVEMRNCGVSVTEAMLGVmTEADKEIELQQQTIESLKEKIYRLEVQLREttHDREMTKLKQELQAA 495
Cdd:TIGR02168  848 EELSEDIESLAAEIEELEELIEELESEL-EALLNERASLEEALALLRSELEELSEELRE--LESKRSELRRELEEL 920
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1155-1323 3.03e-40

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 150.87  E-value: 3.03e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376309 1155 INLADGNGNTALHYSVSHSNFEIVKLLLDADVcNVDHQNKAGYTPIMLAALAaveaeKDMRIVEELFGCG-DVNAKASQa 1233
Cdd:COG0666     80 INAKDDGGNTLLHAAARNGDLEIVKLLLEAGA-DVNARDKDGETPLHLAAYN-----GNLEIVKLLLEAGaDVNAQDND- 152

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376309 1234 GQTALMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQpGCNGHLEDNDGSTALSIALEAGH 1313
Cdd:COG0666    153 GNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA-GADVNAKDNDGKTALDLAAENGN 231

                          170
                   ....*....|
gi 2217376309 1314 KDIAVLLYAH 1323
Cdd:COG0666    232 LEIVKLLLEA 241
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1155-1320 3.69e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 136.24  E-value: 3.69e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376309 1155 INLADGNGNTALHYSVSHSNFEIVKLLLDADVcNVDHQNKAGYTPIMLAALAaveaeKDMRIVEELFGCG-DVNAKaSQA 1233
Cdd:COG0666    113 VNARDKDGETPLHLAAYNGNLEIVKLLLEAGA-DVNAQDNDGNTPLHLAAAN-----GNLEIVKLLLEAGaDVNAR-DND 185

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376309 1234 GQTALMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQpGCNGHLEDNDGSTALSIALEAGH 1313
Cdd:COG0666    186 GETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA-GADLNAKDKDGLTALLLAAAAGA 264


                   ....*..
gi 2217376309 1314 KDIAVLL 1320
Cdd:COG0666    265 ALIVKLL 271
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1140-1323 1.85e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 131.23  E-value: 1.85e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376309 1140 IAAFEAISPDVLRYVINLADGNGNTALHYSVSHSNFEIVKLLLDADVcNVDHQNKAGYTPIMLAALAaveaeKDMRIVEE 1219
Cdd:COG0666     32 LLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGA-DINAKDDGGNTLLHAAARN-----GDLEIVKL 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376309 1220 LFGCG-DVNAKASQaGQTALMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQpGCNGHLED 1298
Cdd:COG0666    106 LLEAGaDVNARDKD-GETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEA-GADVNARD 183

                          170       180
                   ....*....|....*....|....*
gi 2217376309 1299 NDGSTALSIALEAGHKDIAVLLYAH 1323
Cdd:COG0666    184 NDGETPLHLAAENGHLEIVKLLLEA 208
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1144-1335 3.40e-25

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 107.35  E-value: 3.40e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376309 1144 EAISPDVLRYVINLADGNGNTALHYSVSHSNFEIVKLLLDADVCNVDHQNKAGYTPIMLAALAAveaeKDMRIVEELFGC 1223
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALA----GDLLVALLLLAA 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376309 1224 GDVNAKASQAGQTALMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQpGCNGHLEDNDGST 1303
Cdd:COG0666     77 GADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA-GADVNAQDNDGNT 155

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 2217376309 1304 ALSIALEAGHKDIAVLL---YAHVNfAKAQSPGTP 1335
Cdd:COG0666    156 PLHLAAANGNLEIVKLLleaGADVN-ARDNDGETP 189
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1238-1323 1.41e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 93.26  E-value: 1.41e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376309 1238 LMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQPGCNghlEDNDGSTALSIALEAGHKDIA 1317
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN---LKDNGRTALHYAARSGHLEIV 77


                   ....*.
gi 2217376309 1318 VLLYAH 1323
Cdd:pfam12796   78 KLLLEK 83
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1155-1288 2.10e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 99.26  E-value: 2.10e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376309 1155 INLADGNGNTALHYSVSHSNFEIVKLLLDADVcNVDHQNKAGYTPIMLAALAaveaeKDMRIVEELFGCG-DVNAKaSQA 1233
Cdd:COG0666    146 VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGA-DVNARDNDGETPLHLAAEN-----GHLEIVKLLLEAGaDVNAK-DND 218

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2217376309 1234 GQTALMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLA 1288
Cdd:COG0666    219 GKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLL 273
KN_motif pfam12075
KN motif; This small motif is found at the N-terminus of Kank proteins and has been called the ...
 30-68 1.43e-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: 80.09  E-value: 1.43e-18
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2217376309   30 PYFVETPYGYQLDLDFLKYVDDIQKGNTIKRLNIQKRRK 68
Cdd:pfam12075    1 PYSVETPYGFHLDLDFLKYVEDIESGQTIRRARVQRRPR 39
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1166-1264 9.63e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 73.61  E-value: 9.63e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376309 1166 LHYSVSHSNFEIVKLLLDADvCNVDHQNKAGYTPIMLAALAaveaeKDMRIVEELFGCGDVNAKASqaGQTALMLAVSHG 1245
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENG-ADANLQDKNGRTALHLAAKN-----GHLEIVKLLLEHADVNLKDN--GRTALHYAARSG 72

                           90
                   ....*....|....*....
gi 2217376309 1246 RIDMVKGLLACGADVNIQD 1264
Cdd:pfam12796   73 HLEIVKLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 1144-1325 1.73e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 71.23  E-value: 1.73e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376309 1144 EAISPDVLRYVINL-ADGNGN-----TALHY-----SVSHSNFEIVKLLLDADVcNVDHQNKAGYTPIMLAALAAVEAEK 1212
Cdd:PHA03100    44 EARNIDVVKILLDNgADINSStknnsTPLHYlsnikYNLTDVKEIVKLLLEYGA-NVNAPDNNGITPLLYAISKKSNSYS 122

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376309 1213 dmrIVEELFGCG-DVNAKASQaGQTALMLAVSHGRIDM------------------VKGLLACGADVNIQDDEGSTALMC 1273
Cdd:PHA03100   123 ---IVEYLLDNGaNVNIKNSD-GENLLHLYLESNKIDLkilkllidkgvdinaknrVNYLLSYGVPINIKDVYGFTPLHY 198

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2217376309 1274 ASEHGHVEIVKLLLAQpGCNGHLEDNDGSTALSIALEAGHKDI-AVLLYAHVN 1325
Cdd:PHA03100   199 AVYNNNPEFVKYLLDL-GANPNLVNKYGDTPLHIAILNNNKEIfKLLLNNGPS 250
Ank_4 pfam13637
Ankyrin repeats (many copies);
1236-1287 1.86e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 60.37  E-value: 1.86e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2217376309 1236 TALMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLL 1287
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 1138-1319 3.47e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 63.89  E-value: 3.47e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376309 1138 DYIAAFEAISPDVLRYVI------NLADGNGNTALHYSVSHSN---FEIVKLLLDADVcNVDHQNKAGYTPIMLAALAAV 1208
Cdd:PHA03095    17 DYLLNASNVTVEEVRRLLaagadvNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGA-DVNAPERCGFTPLHLYLYNAT 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376309 1209 EAekdmRIVEELFGCG-DVNAKaSQAGQTALMLAVSHGRID--MVKGLLACGADVNIQDDEGSTALMC--ASEHGHVEIV 1283
Cdd:PHA03095    96 TL----DVIKLLIKAGaDVNAK-DKVGRTPLHVYLSGFNINpkVIRLLLRKGADVNALDLYGMTPLAVllKSRNANVELL 170

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 2217376309 1284 KLLLAQpGCNGHLEDNDGSTALSIALEAGHKDIAVL 1319
Cdd:PHA03095   171 RLLIDA-GADVYAVDDRFRSLLHHHLQSFKPRARIV 205
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 1212-1334 2.08e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 62.19  E-value: 2.08e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376309 1212 KDMRIVEELFGCGDVNAKASQAGQtaLMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQpG 1291
Cdd:PLN03192   505 HDLNVGDLLGDNGGEHDDPNMASN--LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKH-A 581

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 2217376309 1292 CNGHLEDNDGSTALSIALEAGHKDIAVLLYahvNFAKAQSPGT 1334
Cdd:PLN03192   582 CNVHIRDANGNTALWNAISAKHHKIFRILY---HFASISDPHA 621
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 1176-1325 5.41e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 59.98  E-value: 5.41e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376309 1176 EIVKLLLDADVcnvdhqnKAGYTPImlaalaaVEAEKDMriVEELFGCG-DVNAKASQAgQTALMLAVSHGRIDMVKGLL 1254
Cdd:PHA02874    82 DIIKLLIDNGV-------DTSILPI-------PCIEKDM--IKTILDCGiDVNIKDAEL-KTFLHYAIKKGDLESIKMLF 144

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217376309 1255 ACGADVNIQDDEGSTALMCASEHGHVEIVKLLLaQPGCNGHLEDNDGSTALSIALEAGHKDIAVLLYAHVN 1325
Cdd:PHA02874   145 EYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLL-EKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGN 214
Ank_5 pfam13857
Ankyrin repeats (many copies);
1253-1308 5.41e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 53.50  E-value: 5.41e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2217376309 1253 LLACG-ADVNIQDDEGSTALMCASEHGHVEIVKLLLAqPGCNGHLEDNDGSTALSIA 1308
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLA-YGVDLNLKDEEGLTALDLA 56
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1271-1325 5.49e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 54.35  E-value: 5.49e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2217376309 1271 LMCASEHGHVEIVKLLLaQPGCNGHLEDNDGSTALSIALEAGHKDIAVLLYAHVN 1325
Cdd:pfam12796    1 LHLAAKNGNLELVKLLL-ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 1155-1287 1.49e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 58.74  E-value: 1.49e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376309 1155 INLADGNGNTALHYSVSHSNFEIVKLLLDaDVCNVDHQNKAGYTPImlaaLAAVEAEKDMRIVEELFGCG-DVNAKASQA 1233
Cdd:PHA02878   194 VNIPDKTNNSPLHHAVKHYNKPIVHILLE-NGASTDARDKCGNTPL----HISVGYCKDYDILKLLLEHGvDVNAKSYIL 268

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2217376309 1234 GQTALMLAVSHGRIdmVKGLLACGADVNIQDDEGSTAL-MCASEHGHVEIVKLLL 1287
Cdd:PHA02878   269 GLTALHSSIKSERK--LKLLLEYGADINSLNSYKLTPLsSAVKQYLCINIGRILI 321
Ank_5 pfam13857
Ankyrin repeats (many copies);
1225-1271 3.28e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.50  E-value: 3.28e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 2217376309 1225 DVNAKaSQAGQTALMLAVSHGRIDMVKGLLACGADVNIQDDEGSTAL 1271
Cdd:pfam13857    8 DLNRL-DGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 1250-1323 3.32e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.90  E-value: 3.32e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217376309 1250 VKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLaQPGCNGHLEDNDGSTALSIALEAGHKDIAVLLYAH 1323
Cdd:PTZ00322    98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLL-EFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 1156-1344 4.01e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 54.87  E-value: 4.01e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376309 1156 NLADGNGNTALHYSVSHSNFEIVKLLLDaDVCNVDHQNKAGYTPIMLAALAaveaeKDMRIVEELFGCgdvnAKAS--QA 1233
Cdd:PLN03192   552 DIGDSKGRTPLHIAASKGYEDCVLVLLK-HACNVHIRDANGNTALWNAISA-----KHHKIFRILYHF----ASISdpHA 621

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376309 1234 GQTALMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAqpgcNG------HLEDNDGSTALSI 1307
Cdd:PLN03192   622 AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIM----NGadvdkaNTDDDFSPTELRE 697

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 2217376309 1308 AL---EAGHKdIAVLLYAHVNFAKAQSPGTPRLGRKTSPG 1344
Cdd:PLN03192   698 LLqkrELGHS-ITIVDSVPADEPDLGRDGGSRPGRLQGTS 736
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 1161-1289 1.61e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 52.30  E-value: 1.61e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376309 1161 NGNTALHYSVSHSNFEIVKLLL----DADVCNVDHqnkagYTPImlaalAAVEAEKDMRIVEELF---GCGDVNakaSQA 1233
Cdd:PHA02875   101 DGMTPLHLATILKKLDIMKLLIargaDPDIPNTDK-----FSPL-----HLAVMMGDIKGIELLIdhkACLDIE---DCC 167

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2217376309 1234 GQTALMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMC-ASEHGHVEIVKLLLAQ 1289
Cdd:PHA02875   168 GCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCyAIENNKIDIVRLFIKR 224
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 1162-1321 1.99e-06

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: 52.32  E-value: 1.99e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376309 1162 GNTALHYSVSHSNFEIVKLLLDADvcnvdhqnkagytPIMLaalaaveaekDMRIVEELFgcgdvnakasqAGQTALMLA 1241
Cdd:cd22192     51 GETALHVAALYDNLEAAVVLMEAA-------------PELV----------NEPMTSDLY-----------QGETALHIA 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376309 1242 VSHGRIDMVKGLLACGADVNIQDDEGS------TALMCASEH--------GHVEIVKLLLaQPGCNGHLEDNDGSTALSI 1307
Cdd:cd22192     97 VVNQNLNLVRELIARGADVVSPRATGTffrpgpKNLIYYGEHplsfaacvGNEEIVRLLI-EHGADIRAQDSLGNTVLHI 175

                          170
                   ....*....|....
gi 2217376309 1308 ALEAGHKDIAVLLY 1321
Cdd:cd22192    176 LVLQPNKTFACQMY 189
Ank_4 pfam13637
Ankyrin repeats (many copies);
1267-1320 3.70e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.34  E-value: 3.70e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2217376309 1267 GSTALMCASEHGHVEIVKLLLaQPGCNGHLEDNDGSTALSIALEAGHKDIAVLL 1320
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLL-EKGADINAVDGNGETALHFAASNGNVEVLKLL 53
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 1234-1265 4.70e-06

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 44.59  E-value: 4.70e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 2217376309 1234 GQTALMLAVSH-GRIDMVKGLLACGADVNIQDD 1265
Cdd:pfam00023    2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1147-1193 1.42e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 44.72  E-value: 1.42e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2217376309 1147 SPDVLRYVINLADGN----GNTALHYSVSHSNFEIVKLLLDADvCNVDHQN 1193
Cdd:pfam12796   42 HLEIVKLLLEHADVNlkdnGRTALHYAARSGHLEIVKLLLEKG-ADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 1155-1315 1.93e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 48.81  E-value: 1.93e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376309 1155 INLADGNGNTALHYSVSHSNFEIVKLLLDADV-CNVDHQNkaGYTPImlaalAAVEAEKDMRIVEELFGCGDVNAKASQA 1233
Cdd:PHA02874   150 VNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAyANVKDNN--GESPL-----HNAAEYGDYACIKLLIDHGNHIMNKCKN 222

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376309 1234 GQTALMLAVSHGRidMVKGLLACGADVNIQDDEGSTALMCASEHG-HVEIVKLLLAQPGcNGHLEDNDGSTALSIALEAG 1312
Cdd:PHA02874   223 GFTPLHNAIIHNR--SAIELLINNASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKA-DISIKDNKGENPIDTAFKYI 299


                   ...
gi 2217376309 1313 HKD 1315
Cdd:PHA02874   300 NKD 302
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 1234-1299 3.48e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.36  E-value: 3.48e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217376309 1234 GQTALMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQPGCNGHLEDN 1299
Cdd:PTZ00322   115 GRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGAN 180
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 1166-1320 3.73e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 47.68  E-value: 3.73e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376309 1166 LHYSVSHSNFEIVKLLLDADVCNVDHQNKAGYTPImlaalAAVEAEKDMRIVEELFGCGDVNAKASQAGQTALMLAVSHG 1245
Cdd:PHA02875    72 LHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPL-----HLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMG 146

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217376309 1246 RIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQPGCNGHLEDNDGSTALSIALEAGHKDIAVLL 1320
Cdd:PHA02875   147 DIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLF 221
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 1234-1262 4.52e-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: 4.52e-05
                            10        20
                    ....*....|....*....|....*....
gi 2217376309  1234 GQTALMLAVSHGRIDMVKGLLACGADVNI 1262
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
1155-1182 5.84e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.88  E-value: 5.84e-05
                           10        20
                   ....*....|....*....|....*...
gi 2217376309 1155 INLADGNGNTALHYSVSHSNFEIVKLLL 1182
Cdd:pfam13637   27 INAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 1164-1262 6.95e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 46.91  E-value: 6.95e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376309 1164 TALHYSVSHSNFEIVKLLLDADVCnVDHQNKAGYTPIMLAALAaveaeKDMRIVEELFGCG-DVNAKASQAGQTALMLAV 1242
Cdd:PHA02875   137 SPLHLAVMMGDIKGIELLIDHKAC-LDIEDCCGCTPLIIAMAK-----GDIAICKMLLDSGaNIDYFGKNGCVAALCYAI 210

                           90       100
                   ....*....|....*....|
gi 2217376309 1243 SHGRIDMVKGLLACGADVNI 1262
Cdd:PHA02875   211 ENNKIDIVRLFIKRGADCNI 230
PHA03095 PHA03095
ankyrin-like protein; Provisional
 1146-1289 1.39e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.17  E-value: 1.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376309 1146 ISPDVLRYVINL------ADGNGNTALHY--SVSHSNFEIVKLLLDADvCNVDHQNKAGYTPIMLAALAAVEAEKDMR-- 1215
Cdd:PHA03095   165 ANVELLRLLIDAgadvyaVDDRFRSLLHHhlQSFKPRARIVRELIRAG-CDPAATDMLGNTPLHSMATGSSCKRSLVLpl 243

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217376309 1216 IVEELfgcgDVNAKaSQAGQTALMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQ 1289
Cdd:PHA03095   244 LIAGI----SINAR-NRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAK 312
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 1234-1262 2.03e-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: 2.03e-04
                           10        20
                   ....*....|....*....|....*....
gi 2217376309 1234 GQTALMLAVSHGRIDMVKGLLACGADVNI 1262
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 1161-1194 2.32e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.58  E-value: 2.32e-04
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 2217376309 1161 NGNTALHYSVSHS-NFEIVKLLLDADvCNVDHQNK 1194
Cdd:pfam00023    1 DGNTPLHLAAGRRgNLEIVKLLLSKG-ADVNARDK 34
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
269-496 2.76e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.14  E-value: 2.76e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376309  269 IALKRLKELEEQVRTIPVLQVKISVLQEEKRQLVSQLKNQRAasQINVCGVRKRSYSA--GNASQLEQLSRARRSGGELY 346
Cdd:COG4717     68 LNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEA--ELEELREELEKLEKllQLLPLYQELEALEAELAELP 145

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376309  347 IDYEeeemetveQSTQRIKEFRQLTADMQALEQKIQdsscEASSELREngECRSVAVGAEENMNDIVvyhrgsrscKDAa 426
Cdd:COG4717    146 ERLE--------ELEERLEELRELEEELEELEAELA----ELQEELEE--LLEQLSLATEEELQDLA---------EEL- 201

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376309  427 vgtlvemrncgvsvtEAMLGVMTEADKEIELQQQTIESLKEKIYRLEVQLRETTHDREMTKLKQELQAAG 496
Cdd:COG4717    202 ---------------EELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAA 256
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 1163-1308 3.27e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 44.87  E-value: 3.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376309 1163 NTALHYSvshsNFEIVKLLLdadvcnVDHQNKAGYTPIMLAALAAVEAEKDMRIVEELFGCG-DVNAKASQAGQTALMLA 1241
Cdd:PHA02878   106 KDAFNNR----NVEIFKIIL------TNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGaDINMKDRHKGNTALHYA 175

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217376309 1242 VSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLaQPGCNGHLEDNDGSTALSIA 1308
Cdd:PHA02878   176 TENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILL-ENGASTDARDKCGNTPLHIS 241
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 1234-1305 5.56e-04

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: 44.36  E-value: 5.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376309 1234 GQTALMLAVSHGRIDMVKGLLACGADVNIQ----------DDE----GSTALMCASEHGHVEIVKLLLAQPGCNGHLEDN 1299
Cdd:cd22194    141 GQTALNIAIERRQGDIVKLLIAKGADVNAHakgvffnpkyKHEgfyfGETPLALAACTNQPEIVQLLMEKESTDITSQDS 220


                   ....*.
gi 2217376309 1300 DGSTAL 1305
Cdd:cd22194    221 RGNTVL 226
Ank_5 pfam13857
Ankyrin repeats (many copies);
1155-1200 7.47e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.87  E-value: 7.47e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 2217376309 1155 INLADGNGNTALHYSVSHSNFEIVKLLLDADV-CNVdhQNKAGYTPI 1200
Cdd:pfam13857    9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVdLNL--KDEEGLTAL 53
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 1161-1186 9.58e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.95  E-value: 9.58e-04
                            10        20
                    ....*....|....*....|....*.
gi 2217376309  1161 NGNTALHYSVSHSNFEIVKLLLDADV 1186
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 1238-1323 1.06e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 43.12  E-value: 1.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376309 1238 LMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHV-----EIVKLLLaQPGCNGHLEDNDGSTALSIALEA- 1311
Cdd:PHA03100    39 LYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLL-EYGANVNAPDNNGITPLLYAISKk 117

                           90
                   ....*....|...
gi 2217376309 1312 -GHKDIAVLLYAH 1323
Cdd:PHA03100   118 sNSYSIVEYLLDN 130
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 1155-1309 1.14e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 43.03  E-value: 1.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376309 1155 INLADGNGNTALHYSVSHSNFEIVKLLLD--ADVcNVDHQNkaGYTPImlaalaaveaekdmriveelfgcgdvnakasq 1232
Cdd:PHA02874   117 VNIKDAELKTFLHYAIKKGDLESIKMLFEygADV-NIEDDN--GCYPI-------------------------------- 161

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217376309 1233 agqtalMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQpGCNGHLEDNDGSTALSIAL 1309
Cdd:PHA02874   162 ------HIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDH-GNHIMNKCKNGFTPLHNAI 231
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 1266-1287 2.21e-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: 36.80  E-value: 2.21e-03
                            10        20
                    ....*....|....*....|..
gi 2217376309  1266 EGSTALMCASEHGHVEIVKLLL 1287
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLL 22
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 1213-1287 3.35e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 41.97  E-value: 3.35e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217376309 1213 DMRIVEELFGCG-DVNAKASQAgQTALMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLL 1287
Cdd:PHA02876   157 ELLIAEMLLEGGaDVNAKDIYC-ITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAII 231
Ank_4 pfam13637
Ankyrin repeats (many copies);
1162-1200 4.22e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.87  E-value: 4.22e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2217376309 1162 GNTALHYSVSHSNFEIVKLLLDADVcNVDHQNKAGYTPI 1200
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGA-DINAVDGNGETAL 38
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 1176-1325 4.29e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 41.40  E-value: 4.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376309 1176 EIVKLLLD--ADVCNVDHQNkaGYTPImlaalAAVEAEKDMRIVEELFGCG-DVNAkASQAGQTALMLAVSHGRIDMVKG 1252
Cdd:PHA02878   148 EITKLLLSygADINMKDRHK--GNTAL-----HYATENKDQRLTELLLSYGaNVNI-PDKTNNSPLHHAVKHYNKPIVHI 219

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217376309 1253 LLACGADVNIQDDEGSTALMCASEH-GHVEIVKLLLAQPGCNGHLEDNDGSTALSIALEAGHKDIAVLLY-AHVN 1325
Cdd:PHA02878   220 LLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYILGLTALHSSIKSERKLKLLLEYgADIN 294
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 265-495 5.66e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.20  E-value: 5.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376309  265 EQMAIALKRLKELEEQVRTIPVLQVKISVLQEEKRQLVSQLKNQ--RAASQINVCGVRKRSYSAGNASQLEQLS--RARR 340
Cdd:TIGR02168  691 EKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDlaRLEAEVEQLEERIAQLSKELTELEAEIEelEERL 770

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376309  341 SGGELYIDYEEEEMETVEQSTQRIK-EFRQLTADMQALEQKIQDSSCEASSELRENGECRSVAVGAEENMNDIvvyHRGS 419
Cdd:TIGR02168  771 EEAEEELAEAEAEIEELEAQIEQLKeELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDL---EEQI 847

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217376309  420 RSCKDAAVGTLVEMRNCGVSVTEAMLGVmTEADKEIELQQQTIESLKEKIYRLEVQLREttHDREMTKLKQELQAA 495
Cdd:TIGR02168  848 EELSEDIESLAAEIEELEELIEELESEL-EALLNERASLEEALALLRSELEELSEELRE--LESKRSELRRELEEL 920
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
265-495 5.97e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 5.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376309  265 EQMAIALKRLKELEEQVRTIPVLQVKISVLQEEKRQLVSQLKNQRAAsqinvcgVRKRSYSAGNASQLEQLSRARRSGGE 344
Cdd:COG4717     71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREE-------LEKLEKLLQLLPLYQELEALEAELAE 143

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376309  345 LYIDYeeeemetvEQSTQRIKEFRQLTADMQALEQKIQdsscEASSELREngECRSVAVGAEENMNDIVvyhrgsrscKD 424
Cdd:COG4717    144 LPERL--------EELEERLEELRELEEELEELEAELA----ELQEELEE--LLEQLSLATEEELQDLA---------EE 200

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217376309  425 AAvgtlvemrncgvsvteamlgvmtEADKEIELQQQTIESLKEKIYRLEVQLRETTHDREMTKLKQELQAA 495
Cdd:COG4717    201 LE-----------------------ELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEA 248
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 260-507 6.75e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.82  E-value: 6.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376309  260 LQHIREQMAIALKRLKELEEQVRTIpvlQVKISVLQEEKRQLVSQLKN-QRAASQINVCGVRKRSYSAGNASQLEQLSRA 338
Cdd:TIGR02169  697 LRRIENRLDELSQELSDASRKIGEI---EKEIEQLEQEEEKLKERLEElEEDLSSLEQEIENVKSELKELEARIEELEED 773

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376309  339 ----RRSGGELYIDYEEEEMETVEQSTQRIKEFRQ-LTADMQALEQKIQDSSCEASSelrengecrsvavgAEENMNDIV 413
Cdd:TIGR02169  774 lhklEEALNDLEARLSHSRIPEIQAELSKLEEEVSrIEARLREIEQKLNRLTLEKEY--------------LEKEIQELQ 839

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376309  414 VYhrgSRSCKD--AAVGTLVEMRNCGVSVTEAMLgvmteadKEIELQQQTIES----LKEKIYRLEVQLRETthDREMTK 487
Cdd:TIGR02169  840 EQ---RIDLKEqiKSIEKEIENLNGKKEELEEEL-------EELEAALRDLESrlgdLKKERDELEAQLREL--ERKIEE 907

                          250       260
                   ....*....|....*....|
gi 2217376309  488 LKQELQAAGSRKKVDKATMA 507
Cdd:TIGR02169  908 LEAQIEKKRKRLSELKAKLE 927
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 1266-1299 7.32e-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: 35.34  E-value: 7.32e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 2217376309 1266 EGSTALMCASEH-GHVEIVKLLLaQPGCNGHLEDN 1299
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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