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Conserved domains on  [gi|2221814844|ref|NP_001391512|]
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KN motif and ankyrin repeat domains 1 isoform 5 [Mus musculus]

Protein Classification

ankyrin repeat domain-containing protein( domain architecture ID 11430360)

ankyrin repeat (ANK) domain-containing protein mediate specific protein-protein interactions without necessarily recognizing specific primary sequences which allows for one ankyrin repeat domain to recognize and bind to a variety of intracellular substrates and may be involved in a wide array of functions

CATH:  1.25.40.20
Gene Ontology:  GO:0005515
SCOP:  4000366

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
990-1179 2.80e-34

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 133.54  E-value: 2.80e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221814844  990 IAAFEAVSPDVLRYII------NMADGNGNTALHYSVSHSNFQIVKLLLDADVcNVDHQNKAGYTPIMLAALAaveaeKD 1063
Cdd:COG0666     92 HAAARNGDLEIVKLLLeagadvNARDKDGETPLHLAAYNGNLEIVKLLLEAGA-DVNAQDNDGNTPLHLAAAN-----GN 165
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221814844 1064 MQVVEELFSCG-DVNAKaSQAGQTALMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQpGC 1142
Cdd:COG0666    166 LEIVKLLLEAGaDVNAR-DNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA-GA 243
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 2221814844 1143 NGHLEDNDGSTALSIALEAGHKDIAVLLYAHLNFSKA 1179
Cdd:COG0666    244 DLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAA 280
YhaN super family cl34808
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
111-342 3.81e-03

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: 41.29  E-value: 3.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221814844  111 IALKRLKELEEQVRTIPVLQVKISVLQEEKRQLASQLKSQRASSQNEACGVRKRSYSAGNASQLELLARARRgggELyid 190
Cdd:COG4717     68 LNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEA---EL--- 141
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221814844  191 yeEEEMESVEQSTQRIQEFRQLTADMQALERKIQDSSCEVASELRENGQcpsrecksvavgsdenmndvvVYHRDLRPCK 270
Cdd:COG4717    142 --AELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSL---------------------ATEEELQDLA 198
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2221814844  271 DTavgtvtetrnvgisvteamlgvITEADKEIELQQQTIEALKEKIYRLEVQLKETTHDREMTKLKQELQAA 342
Cdd:COG4717    199 EE----------------------LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEA 248
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
990-1179 2.80e-34

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 133.54  E-value: 2.80e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221814844  990 IAAFEAVSPDVLRYII------NMADGNGNTALHYSVSHSNFQIVKLLLDADVcNVDHQNKAGYTPIMLAALAaveaeKD 1063
Cdd:COG0666     92 HAAARNGDLEIVKLLLeagadvNARDKDGETPLHLAAYNGNLEIVKLLLEAGA-DVNAQDNDGNTPLHLAAAN-----GN 165
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221814844 1064 MQVVEELFSCG-DVNAKaSQAGQTALMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQpGC 1142
Cdd:COG0666    166 LEIVKLLLEAGaDVNAR-DNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA-GA 243
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 2221814844 1143 NGHLEDNDGSTALSIALEAGHKDIAVLLYAHLNFSKA 1179
Cdd:COG0666    244 DLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAA 280
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1088-1173 1.25e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 93.26  E-value: 1.25e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221814844 1088 LMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQPGCNghlEDNDGSTALSIALEAGHKDIA 1167
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN---LKDNGRTALHYAARSGHLEIV 77

                   ....*.
gi 2221814844 1168 VLLYAH 1173
Cdd:pfam12796   78 KLLLEK 83
PHA03100 PHA03100
ankyrin repeat protein; Provisional
1005-1175 1.11e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 71.62  E-value: 1.11e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221814844 1005 INMADGNGNTALHYSVSHS--NFQIVKLLLDADvCNVDHQNKAGYTPImlaALAAVEAEKDMQVVEELFSCG-DVNAKas 1081
Cdd:PHA03100    99 VNAPDNNGITPLLYAISKKsnSYSIVEYLLDNG-ANVNIKNSDGENLL---HLYLESNKIDLKILKLLIDKGvDINAK-- 172
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221814844 1082 qagqtalmlavshgriDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQpGCNGHLEDNDGSTALSIALEA 1161
Cdd:PHA03100   173 ----------------NRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDL-GANPNLVNKYGDTPLHIAILN 235
                          170
                   ....*....|....*
gi 2221814844 1162 GHKDI-AVLLYAHLN 1175
Cdd:PHA03100   236 NNKEIfKLLLNNGPS 250
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
1012-1171 4.55e-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: 50.78  E-value: 4.55e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221814844 1012 GNTALHYSVSHSNFQIVKLLLDADvcnvdhqnkagytPIMLaalaaveaekDMQVVEELFscgdvnakasqAGQTALMLA 1091
Cdd:cd22192     51 GETALHVAALYDNLEAAVVLMEAA-------------PELV----------NEPMTSDLY-----------QGETALHIA 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221814844 1092 VSHGRIDMVKGLLACGADVNIQDDEGS------TALMCASEH--------GHVEIVKLLLaQPGCNGHLEDNDGSTALSI 1157
Cdd:cd22192     97 VVNQNLNLVRELIARGADVVSPRATGTffrpgpKNLIYYGEHplsfaacvGNEEIVRLLI-EHGADIRAQDSLGNTVLHI 175
                          170
                   ....*....|....
gi 2221814844 1158 ALEAGHKDIAVLLY 1171
Cdd:cd22192    176 LVLQPNKTFACQMY 189
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
1084-1112 4.03e-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: 4.03e-05
                            10        20
                    ....*....|....*....|....*....
gi 2221814844  1084 GQTALMLAVSHGRIDMVKGLLACGADVNI 1112
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
111-342 3.81e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.29  E-value: 3.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221814844  111 IALKRLKELEEQVRTIPVLQVKISVLQEEKRQLASQLKSQRASSQNEACGVRKRSYSAGNASQLELLARARRgggELyid 190
Cdd:COG4717     68 LNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEA---EL--- 141
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221814844  191 yeEEEMESVEQSTQRIQEFRQLTADMQALERKIQDSSCEVASELRENGQcpsrecksvavgsdenmndvvVYHRDLRPCK 270
Cdd:COG4717    142 --AELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSL---------------------ATEEELQDLA 198
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2221814844  271 DTavgtvtetrnvgisvteamlgvITEADKEIELQQQTIEALKEKIYRLEVQLKETTHDREMTKLKQELQAA 342
Cdd:COG4717    199 EE----------------------LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEA 248
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
990-1179 2.80e-34

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 133.54  E-value: 2.80e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221814844  990 IAAFEAVSPDVLRYII------NMADGNGNTALHYSVSHSNFQIVKLLLDADVcNVDHQNKAGYTPIMLAALAaveaeKD 1063
Cdd:COG0666     92 HAAARNGDLEIVKLLLeagadvNARDKDGETPLHLAAYNGNLEIVKLLLEAGA-DVNAQDNDGNTPLHLAAAN-----GN 165
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221814844 1064 MQVVEELFSCG-DVNAKaSQAGQTALMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQpGC 1142
Cdd:COG0666    166 LEIVKLLLEAGaDVNAR-DNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA-GA 243
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 2221814844 1143 NGHLEDNDGSTALSIALEAGHKDIAVLLYAHLNFSKA 1179
Cdd:COG0666    244 DLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAA 280
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
990-1173 8.22e-34

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 132.39  E-value: 8.22e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221814844  990 IAAFEAVSPDVLRYIINMADGNGNTALHYSVSHSNFQIVKLLLDADVcNVDHQNKAGYTPIMLAALAaveaeKDMQVVEE 1069
Cdd:COG0666     32 LLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGA-DINAKDDGGNTLLHAAARN-----GDLEIVKL 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221814844 1070 LFSCG-DVNAKASQaGQTALMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQpGCNGHLED 1148
Cdd:COG0666    106 LLEAGaDVNARDKD-GETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEA-GADVNARD 183
                          170       180
                   ....*....|....*....|....*
gi 2221814844 1149 NDGSTALSIALEAGHKDIAVLLYAH 1173
Cdd:COG0666    184 NDGETPLHLAAENGHLEIVKLLLEA 208
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
999-1173 5.41e-25

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 106.58  E-value: 5.41e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221814844  999 DVLRYIINMADGNGNTALHYSVSHSNFQIVKLLLDADVCNVDHQNKAGYTPIMLAALAAveaeKDMQVVEELFSCGDVNA 1078
Cdd:COG0666      6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALA----GDLLVALLLLAAGADIN 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221814844 1079 KASQAGQTALMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQpGCNGHLEDNDGSTALSIA 1158
Cdd:COG0666     82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA-GADVNAQDNDGNTPLHLA 160
                          170
                   ....*....|....*
gi 2221814844 1159 LEAGHKDIAVLLYAH 1173
Cdd:COG0666    161 AANGNLEIVKLLLEA 175
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1088-1173 1.25e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 93.26  E-value: 1.25e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221814844 1088 LMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQPGCNghlEDNDGSTALSIALEAGHKDIA 1167
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN---LKDNGRTALHYAARSGHLEIV 77

                   ....*.
gi 2221814844 1168 VLLYAH 1173
Cdd:pfam12796   78 KLLLEK 83
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1016-1114 7.02e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 74.00  E-value: 7.02e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221814844 1016 LHYSVSHSNFQIVKLLLDADvCNVDHQNKAGYTPIMLAALAaveaeKDMQVVEELFSCGDVNAKASqaGQTALMLAVSHG 1095
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENG-ADANLQDKNGRTALHLAAKN-----GHLEIVKLLLEHADVNLKDN--GRTALHYAARSG 72
                           90
                   ....*....|....*....
gi 2221814844 1096 RIDMVKGLLACGADVNIQD 1114
Cdd:pfam12796   73 HLEIVKLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
1005-1175 1.11e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 71.62  E-value: 1.11e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221814844 1005 INMADGNGNTALHYSVSHS--NFQIVKLLLDADvCNVDHQNKAGYTPImlaALAAVEAEKDMQVVEELFSCG-DVNAKas 1081
Cdd:PHA03100    99 VNAPDNNGITPLLYAISKKsnSYSIVEYLLDNG-ANVNIKNSDGENLL---HLYLESNKIDLKILKLLIDKGvDINAK-- 172
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221814844 1082 qagqtalmlavshgriDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQpGCNGHLEDNDGSTALSIALEA 1161
Cdd:PHA03100   173 ----------------NRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDL-GANPNLVNKYGDTPLHIAILN 235
                          170
                   ....*....|....*
gi 2221814844 1162 GHKDI-AVLLYAHLN 1175
Cdd:PHA03100   236 NNKEIfKLLLNNGPS 250
Ank_4 pfam13637
Ankyrin repeats (many copies);
1086-1137 1.65e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 60.37  E-value: 1.65e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2221814844 1086 TALMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLL 1137
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
988-1169 2.16e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 64.66  E-value: 2.16e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221814844  988 DYIAAFEAVSPDVLRYIINM-ADGN-----GNTALHYSVSHSNFQ---IVKLLLDADVcNVDHQNKAGYTPIMLAALAAV 1058
Cdd:PHA03095    17 DYLLNASNVTVEEVRRLLAAgADVNfrgeyGKTPLHLYLHYSSEKvkdIVRLLLEAGA-DVNAPERCGFTPLHLYLYNAT 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221814844 1059 EAEkdmqVVEELFSCG-DVNAKaSQAGQTALMLAVSHGRID--MVKGLLACGADVNIQDDEGSTALMC--ASEHGHVEIV 1133
Cdd:PHA03095    96 TLD----VIKLLIKAGaDVNAK-DKVGRTPLHVYLSGFNINpkVIRLLLRKGADVNALDLYGMTPLAVllKSRNANVELL 170
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 2221814844 1134 KLLLAQpGCNGHLEDNDGSTALSIALEAGHKDIAVL 1169
Cdd:PHA03095   171 RLLIDA-GADVYAVDDRFRSLLHHHLQSFKPRARIV 205
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
1062-1182 2.60e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 61.81  E-value: 2.60e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221814844 1062 KDMQVVEELFSCGDVNAKASQAGQtaLMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQpG 1141
Cdd:PLN03192   505 HDLNVGDLLGDNGGEHDDPNMASN--LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKH-A 581
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 2221814844 1142 CNGHLEDNDGSTALSIALEAGHKDIAVLLYahlNFSKAQSP 1182
Cdd:PLN03192   582 CNVHIRDANGNTALWNAISAKHHKIFRILY---HFASISDP 619
PHA02874 PHA02874
ankyrin repeat protein; Provisional
1062-1175 4.38e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 60.36  E-value: 4.38e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221814844 1062 KDMqvVEELFSCG-DVNAKASQAgQTALMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLaQP 1140
Cdd:PHA02874   104 KDM--IKTILDCGiDVNIKDAEL-KTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLL-EK 179
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2221814844 1141 GCNGHLEDNDGSTALSIALEAGHKDIAVLLYAHLN 1175
Cdd:PHA02874   180 GAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGN 214
Ank_5 pfam13857
Ankyrin repeats (many copies);
1103-1158 4.81e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 53.50  E-value: 4.81e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2221814844 1103 LLACG-ADVNIQDDEGSTALMCASEHGHVEIVKLLLAqPGCNGHLEDNDGSTALSIA 1158
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLA-YGVDLNLKDEEGLTALDLA 56
PHA02878 PHA02878
ankyrin repeat protein; Provisional
999-1137 7.19e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 59.51  E-value: 7.19e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221814844  999 DVLRYII------NMADGNGNTALHYSVSHSNFQIVKLLLDaDVCNVDHQNKAGYTPImlaaLAAVEAEKDMQVVEELFS 1072
Cdd:PHA02878   182 RLTELLLsyganvNIPDKTNNSPLHHAVKHYNKPIVHILLE-NGASTDARDKCGNTPL----HISVGYCKDYDILKLLLE 256
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2221814844 1073 CG-DVNAKASQAGQTALMLAVSHGRIdmVKGLLACGADVNIQDDEGSTAL-MCASEHGHVEIVKLLL 1137
Cdd:PHA02878   257 HGvDVNAKSYILGLTALHSSIKSERK--LKLLLEYGADINSLNSYKLTPLsSAVKQYLCINIGRILI 321
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1121-1175 1.01e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 53.58  E-value: 1.01e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2221814844 1121 LMCASEHGHVEIVKLLLaQPGCNGHLEDNDGSTALSIALEAGHKDIAVLLYAHLN 1175
Cdd:pfam12796    1 LHLAAKNGNLELVKLLL-ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
1075-1121 2.92e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.50  E-value: 2.92e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 2221814844 1075 DVNAKaSQAGQTALMLAVSHGRIDMVKGLLACGADVNIQDDEGSTAL 1121
Cdd:pfam13857    8 DLNRL-DGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
1100-1173 3.03e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.90  E-value: 3.03e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2221814844 1100 VKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLaQPGCNGHLEDNDGSTALSIALEAGHKDIAVLLYAH 1173
Cdd:PTZ00322    98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLL-EFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
1084-1170 4.57e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 54.49  E-value: 4.57e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221814844 1084 GQTALMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLL--------------------------- 1136
Cdd:PLN03192   558 GRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILyhfasisdphaagdllctaakrndlta 637
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2221814844 1137 ---LAQPGCNGHLEDNDGSTALSIALEAGHKDIAVLL 1170
Cdd:PLN03192   638 mkeLLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLL 674
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
1006-1137 2.84e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 51.79  E-value: 2.84e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221814844 1006 NMADGNGNTALHYSVSHSNFQIVKLLLDaDVCNVDHQNKAGYTPIMLAALAaveaeKDMQVVEELFSCgdvnAKAS--QA 1083
Cdd:PLN03192   552 DIGDSKGRTPLHIAASKGYEDCVLVLLK-HACNVHIRDANGNTALWNAISA-----KHHKIFRILYHF----ASISdpHA 621
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2221814844 1084 GQTALMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLL 1137
Cdd:PLN03192   622 AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLI 675
PHA02875 PHA02875
ankyrin repeat protein; Provisional
999-1139 3.11e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 51.15  E-value: 3.11e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221814844  999 DVLRYIINMADGNGNTALHYSVSHSNFQIVKLLL----DADVCNVDHqnkagYTPImlaalAAVEAEKDMQVVEELF--- 1071
Cdd:PHA02875    89 DLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIargaDPDIPNTDK-----FSPL-----HLAVMMGDIKGIELLIdhk 158
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2221814844 1072 SCGDVNakaSQAGQTALMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMC-ASEHGHVEIVKLLLAQ 1139
Cdd:PHA02875   159 ACLDIE---DCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCyAIENNKIDIVRLFIKR 224
Ank_4 pfam13637
Ankyrin repeats (many copies);
1117-1170 3.28e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.34  E-value: 3.28e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2221814844 1117 GSTALMCASEHGHVEIVKLLLaQPGCNGHLEDNDGSTALSIALEAGHKDIAVLL 1170
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLL-EKGADINAVDGNGETALHFAASNGNVEVLKLL 53
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
1084-1115 4.44e-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: 44.20  E-value: 4.44e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 2221814844 1084 GQTALMLAVSH-GRIDMVKGLLACGADVNIQDD 1115
Cdd:pfam00023    2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
1012-1171 4.55e-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: 50.78  E-value: 4.55e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221814844 1012 GNTALHYSVSHSNFQIVKLLLDADvcnvdhqnkagytPIMLaalaaveaekDMQVVEELFscgdvnakasqAGQTALMLA 1091
Cdd:cd22192     51 GETALHVAALYDNLEAAVVLMEAA-------------PELV----------NEPMTSDLY-----------QGETALHIA 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221814844 1092 VSHGRIDMVKGLLACGADVNIQDDEGS------TALMCASEH--------GHVEIVKLLLaQPGCNGHLEDNDGSTALSI 1157
Cdd:cd22192     97 VVNQNLNLVRELIARGADVVSPRATGTffrpgpKNLIYYGEHplsfaacvGNEEIVRLLI-EHGADIRAQDSLGNTVLHI 175
                          170
                   ....*....|....
gi 2221814844 1158 ALEAGHKDIAVLLY 1171
Cdd:cd22192    176 LVLQPNKTFACQMY 189
Ank_4 pfam13637
Ankyrin repeats (many copies);
999-1032 1.21e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.80  E-value: 1.21e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 2221814844  999 DVLRYI------INMADGNGNTALHYSVSHSNFQIVKLLL 1032
Cdd:pfam13637   15 ELLRLLlekgadINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
1005-1138 1.42e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 49.19  E-value: 1.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221814844 1005 INMADGNGNTALHYSVSHSNFQIVKLLLDaDVCNVDHQNKAGYTPImlaalaAVEAEKDMQVVEELFSCGDVNAKASQaG 1084
Cdd:PHA02874   183 ANVKDNNGESPLHNAAEYGDYACIKLLID-HGNHIMNKCKNGFTPL------HNAIIHNRSAIELLINNASINDQDID-G 254
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2221814844 1085 QTALMLAVSHG-RIDMVKGLLACGADVNIQDDEGSTALMCASEH-GHVEIVKLLLA 1138
Cdd:PHA02874   255 STPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTAFKYiNKDPVIKDIIA 310
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
1084-1183 1.71e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.13  E-value: 1.71e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221814844 1084 GQTALMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQPGCNGHLEDNdgSTALSIALEAGH 1163
Cdd:PTZ00322   115 GRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGAN--AKPDSFTGKPPS 192
                           90       100
                   ....*....|....*....|
gi 2221814844 1164 KDIAVLLYAHLNFSKAQSPV 1183
Cdd:PTZ00322   193 LEDSPISSHHPDFSAVPQPM 212
PHA02875 PHA02875
ankyrin repeat protein; Provisional
1016-1170 2.28e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 48.45  E-value: 2.28e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221814844 1016 LHYSVSHSNFQIVKLLLDADVCNVDHQNKAGYTPImlaalAAVEAEKDMQVVEELFSCGDVNAKASQAGQTALMLAVSHG 1095
Cdd:PHA02875    72 LHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPL-----HLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMG 146
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2221814844 1096 RIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQPGCNGHLEDNDGSTALSIALEAGHKDIAVLL 1170
Cdd:PHA02875   147 DIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLF 221
PHA02874 PHA02874
ankyrin repeat protein; Provisional
1005-1165 2.53e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 48.04  E-value: 2.53e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221814844 1005 INMADGNGNTALHYSVSHSNFQIVKLLLDADV-CNVDHQNkaGYTPImlaalAAVEAEKDMQVVEELFSCGDVNAKASQA 1083
Cdd:PHA02874   150 VNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAyANVKDNN--GESPL-----HNAAEYGDYACIKLLIDHGNHIMNKCKN 222
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221814844 1084 GQTALMLAVSHGRidMVKGLLACGADVNIQDDEGSTALMCASEHG-HVEIVKLLLAQPGcNGHLEDNDGSTALSIALEAG 1162
Cdd:PHA02874   223 GFTPLHNAIIHNR--SAIELLINNASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKA-DISIKDNKGENPIDTAFKYI 299

                   ...
gi 2221814844 1163 HKD 1165
Cdd:PHA02874   300 NKD 302
PHA02875 PHA02875
ankyrin repeat protein; Provisional
1014-1112 2.67e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 48.06  E-value: 2.67e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221814844 1014 TALHYSVSHSNFQIVKLLLDADVCnVDHQNKAGYTPIMLAALAaveaeKDMQVVEELFSCG-DVNAKASQAGQTALMLAV 1092
Cdd:PHA02875   137 SPLHLAVMMGDIKGIELLIDHKAC-LDIEDCCGCTPLIIAMAK-----GDIAICKMLLDSGaNIDYFGKNGCVAALCYAI 210
                           90       100
                   ....*....|....*....|
gi 2221814844 1093 SHGRIDMVKGLLACGADVNI 1112
Cdd:PHA02875   211 ENNKIDIVRLFIKRGADCNI 230
PHA03095 PHA03095
ankyrin-like protein; Provisional
996-1139 4.01e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 47.71  E-value: 4.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221814844  996 VSPDVLRYIINM------ADGNGNTALHY--SVSHSNFQIVKLLLDADvCNVDHQNKAGYTPImlAALAAVEAEKDMQVV 1067
Cdd:PHA03095   165 ANVELLRLLIDAgadvyaVDDRFRSLLHHhlQSFKPRARIVRELIRAG-CDPAATDMLGNTPL--HSMATGSSCKRSLVL 241
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2221814844 1068 EELFSCGDVNAKaSQAGQTALMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQ 1139
Cdd:PHA03095   242 PLLIAGISINAR-NRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAK 312
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
1084-1112 4.03e-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: 4.03e-05
                            10        20
                    ....*....|....*....|....*....
gi 2221814844  1084 GQTALMLAVSHGRIDMVKGLLACGADVNI 1112
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
1084-1112 1.81e-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: 1.81e-04
                           10        20
                   ....*....|....*....|....*....
gi 2221814844 1084 GQTALMLAVSHGRIDMVKGLLACGADVNI 1112
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
1005-1121 2.79e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 45.24  E-value: 2.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221814844 1005 INMADGNGNTALHYSVSHSNFQIVKLLldadvcnvdHQNKAGYTP-IMLAALAAVEAEKDMQVVEELFSCG-DVNAKASQ 1082
Cdd:PLN03192   584 VHIRDANGNTALWNAISAKHHKIFRIL---------YHFASISDPhAAGDLLCTAAKRNDLTAMKELLKQGlNVDSEDHQ 654
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2221814844 1083 aGQTALMLAVSHGRIDMVKGLLACGADV---NIQDDEGSTAL 1121
Cdd:PLN03192   655 -GATALQVAMAEDHVDMVRLLIMNGADVdkaNTDDDFSPTEL 695
PHA02878 PHA02878
ankyrin repeat protein; Provisional
999-1158 4.71e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 44.10  E-value: 4.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221814844  999 DVLRYIINMADGNGNTALHYSVSHSNFQIVKLLLdadvcnVDHQNKAGYTPIMLAALAAVEAEKDMQVVEELFSCG-DVN 1077
Cdd:PHA02878    88 EMIRSINKCSVFYTLVAIKDAFNNRNVEIFKIIL------TNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGaDIN 161
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221814844 1078 AKASQAGQTALMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLaQPGCNGHLEDNDGSTALSI 1157
Cdd:PHA02878   162 MKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILL-ENGASTDARDKCGNTPLHI 240

                   .
gi 2221814844 1158 A 1158
Cdd:PHA02878   241 S 241
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
1084-1155 4.85e-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: 4.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221814844 1084 GQTALMLAVSHGRIDMVKGLLACGADVNIQ----------DDE----GSTALMCASEHGHVEIVKLLLAQPGCNGHLEDN 1149
Cdd:cd22194    141 GQTALNIAIERRQGDIVKLLIAKGADVNAHakgvffnpkyKHEgfyfGETPLALAACTNQPEIVQLLMEKESTDITSQDS 220

                   ....*.
gi 2221814844 1150 DGSTAL 1155
Cdd:cd22194    221 RGNTVL 226
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
1011-1044 5.04e-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: 38.42  E-value: 5.04e-04
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 2221814844 1011 NGNTALHYSVSHS-NFQIVKLLLDADvCNVDHQNK 1044
Cdd:pfam00023    1 DGNTPLHLAAGRRgNLEIVKLLLSKG-ADVNARDK 34
PHA03100 PHA03100
ankyrin repeat protein; Provisional
1088-1173 9.29e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 43.12  E-value: 9.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221814844 1088 LMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHV-----EIVKLLLaQPGCNGHLEDNDGSTALSIALEA- 1161
Cdd:PHA03100    39 LYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLL-EYGANVNAPDNNGITPLLYAISKk 117
                           90
                   ....*....|...
gi 2221814844 1162 -GHKDIAVLLYAH 1173
Cdd:PHA03100   118 sNSYSIVEYLLDN 130
Ank_5 pfam13857
Ankyrin repeats (many copies);
1005-1050 1.92e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.71  E-value: 1.92e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 2221814844 1005 INMADGNGNTALHYSVSHSNFQIVKLLLDADV-CNVdhQNKAGYTPI 1050
Cdd:pfam13857    9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVdLNL--KDEEGLTAL 53
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
1116-1137 1.97e-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: 1.97e-03
                            10        20
                    ....*....|....*....|..
gi 2221814844  1116 EGSTALMCASEHGHVEIVKLLL 1137
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLL 22
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
111-342 3.81e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.29  E-value: 3.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221814844  111 IALKRLKELEEQVRTIPVLQVKISVLQEEKRQLASQLKSQRASSQNEACGVRKRSYSAGNASQLELLARARRgggELyid 190
Cdd:COG4717     68 LNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEA---EL--- 141
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221814844  191 yeEEEMESVEQSTQRIQEFRQLTADMQALERKIQDSSCEVASELRENGQcpsrecksvavgsdenmndvvVYHRDLRPCK 270
Cdd:COG4717    142 --AELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSL---------------------ATEEELQDLA 198
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2221814844  271 DTavgtvtetrnvgisvteamlgvITEADKEIELQQQTIEALKEKIYRLEVQLKETTHDREMTKLKQELQAA 342
Cdd:COG4717    199 EE----------------------LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEA 248
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
1011-1036 4.07e-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: 4.07e-03
                            10        20
                    ....*....|....*....|....*.
gi 2221814844  1011 NGNTALHYSVSHSNFQIVKLLLDADV 1036
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
1116-1149 6.77e-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: 6.77e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 2221814844 1116 EGSTALMCASEH-GHVEIVKLLLaQPGCNGHLEDN 1149
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLL-SKGADVNARDK 34
PHA02878 PHA02878
ankyrin repeat protein; Provisional
1005-1171 9.49e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 39.86  E-value: 9.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221814844 1005 INMADGN-GNTALHYSVSHSNFQIVKLLLDADVcNVDHQNKAGYTPimlaalaaveaekdmqvveelfscgdvnakasqa 1083
Cdd:PHA02878   160 INMKDRHkGNTALHYATENKDQRLTELLLSYGA-NVNIPDKTNNSP---------------------------------- 204
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221814844 1084 gqtaLMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEH-GHVEIVKLLLAQPGCNGHLEDNDGSTALSIALEAG 1162
Cdd:PHA02878   205 ----LHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYILGLTALHSSIKSE 280

                   ....*....
gi 2221814844 1163 HKDIAVLLY 1171
Cdd:PHA02878   281 RKLKLLLEY 289
 
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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