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Conserved domains on  [gi|148706370|gb|EDL38317|]
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ankyrin repeat domain 12, isoform CRA_c, partial [Mus musculus]

Protein Classification

ankyrin repeat domain-containing protein( domain architecture ID 11429852)

ankyrin repeat domain-containing protein; ANK proteins 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

Gene Ontology:  GO:0005515
PubMed:  17176038

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
178-296 1.15e-39

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 144.71  E-value: 1.15e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706370 178 RQKDKINKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDD 257
Cdd:COG0666  108 EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGE 187

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 148706370 258 TPLHDSASSGHRDIVKLLLRHGGNPFQANKHGERPVDVA 296
Cdd:COG0666  188 TPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLA 226
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
178-296 1.15e-39

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 144.71  E-value: 1.15e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706370 178 RQKDKINKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDD 257
Cdd:COG0666  108 EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGE 187

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 148706370 258 TPLHDSASSGHRDIVKLLLRHGGNPFQANKHGERPVDVA 296
Cdd:COG0666  188 TPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLA 226
Ank_2 pfam12796
Ankyrin repeats (3 copies);
194-282 2.54e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 90.95  E-value: 2.54e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706370  194 LHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIaAGADVNTQGlDDDTPLHDSASSGHRDIVK 273
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARSGHLEIVK 78


                  ....*....
gi 148706370  274 LLLRHGGNP 282
Cdd:pfam12796  79 LLLEKGADI 87
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 125-281 1.34e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 81.64  E-value: 1.34e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706370 125 STPVSILFGYPLSERKQM---ALLMQMTARDNSPDSTPSHPSQATPAQKKTPSS-----SSRQKDkINKRNERGETPLHM 196
Cdd:PHA03100  69 STPLHYLSNIKYNLTDVKeivKLLLEYGANVNAPDNNGITPLLYAISKKSNSYSiveylLDNGAN-VNIKNSDGENLLHL 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706370 197 AAIRGDVK------------------QVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDT 258
Cdd:PHA03100 148 YLESNKIDlkilkllidkgvdinaknRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDT 227

                        170       180
                 ....*....|....*....|...
gi 148706370 259 PLHDSASSGHRDIVKLLLRHGGN 281
Cdd:PHA03100 228 PLHIAILNNNKEIFKLLLNNGPS 250
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 190-261 1.68e-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: 50.40  E-value: 1.68e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706370 190 GETPLHMAAIRGDVKQVKELISLGANVNV--------------KDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLD 255
Cdd:cd22192   89 GETALHIAVVNQNLNLVRELIARGADVVSpratgtffrpgpknLIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSL 168


                 ....*.
gi 148706370 256 DDTPLH 261
Cdd:cd22192  169 GNTVLH 174
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 223-250 6.61e-06

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: 42.57  E-value: 6.61e-06
                           10        20
                   ....*....|....*....|....*...
gi 148706370   223 GWTPLHEACNVGYYDVAKILIAAGADVN 250
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADIN 29
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
178-296 1.15e-39

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 144.71  E-value: 1.15e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706370 178 RQKDKINKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDD 257
Cdd:COG0666  108 EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGE 187

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 148706370 258 TPLHDSASSGHRDIVKLLLRHGGNPFQANKHGERPVDVA 296
Cdd:COG0666  188 TPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLA 226
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
179-296 3.51e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 135.47  E-value: 3.51e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706370 179 QKDKINKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDT 258
Cdd:COG0666   76 AGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNT 155

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 148706370 259 PLHDSASSGHRDIVKLLLRHGGNPFQANKHGERPVDVA 296
Cdd:COG0666  156 PLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLA 193
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
183-316 4.12e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 126.99  E-value: 4.12e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706370 183 INKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLHD 262
Cdd:COG0666  146 VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDL 225

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 148706370 263 SASSGHRDIVKLLLRHGGNPFQANKHGERPVDVAETEELELLLKREVPLSGDDE 316
Cdd:COG0666  226 AAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLA 279
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
180-296 6.42e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 98.49  E-value: 6.42e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706370 180 KDKINKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTP 259
Cdd:COG0666   44 LLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETP 123

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 148706370 260 LHDSASSGHRDIVKLLLRHGGNPFQANKHGERPVDVA 296
Cdd:COG0666  124 LHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
Ank_2 pfam12796
Ankyrin repeats (3 copies);
194-282 2.54e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 90.95  E-value: 2.54e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706370  194 LHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIaAGADVNTQGlDDDTPLHDSASSGHRDIVK 273
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARSGHLEIVK 78


                  ....*....
gi 148706370  274 LLLRHGGNP 282
Cdd:pfam12796  79 LLLEKGADI 87
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
183-291 1.80e-21

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 94.25  E-value: 1.80e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706370 183 INKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLHD 262
Cdd:COG0666  179 VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLL 258

                         90       100
                 ....*....|....*....|....*....
gi 148706370 263 SASSGHRDIVKLLLRHGGNPFQANKHGER 291
Cdd:COG0666  259 AAAAGAALIVKLLLLALLLLAAALLDLLT 287
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 125-281 1.34e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 81.64  E-value: 1.34e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706370 125 STPVSILFGYPLSERKQM---ALLMQMTARDNSPDSTPSHPSQATPAQKKTPSS-----SSRQKDkINKRNERGETPLHM 196
Cdd:PHA03100  69 STPLHYLSNIKYNLTDVKeivKLLLEYGANVNAPDNNGITPLLYAISKKSNSYSiveylLDNGAN-VNIKNSDGENLLHL 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706370 197 AAIRGDVK------------------QVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDT 258
Cdd:PHA03100 148 YLESNKIDlkilkllidkgvdinaknRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDT 227

                        170       180
                 ....*....|....*....|...
gi 148706370 259 PLHDSASSGHRDIVKLLLRHGGN 281
Cdd:PHA03100 228 PLHIAILNNNKEIFKLLLNNGPS 250
PHA03095 PHA03095
ankyrin-like protein; Provisional
 183-295 1.35e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 81.99  E-value: 1.35e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706370 183 INKRNERGETPLHM---AAIRGDVKQVKELISLGANVNVKDFAGWTPLH-EACNVGYYDVAKILIAAGADVNTQGLDDDT 258
Cdd:PHA03095  40 VNFRGEYGKTPLHLylhYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADVNAKDKVGRT 119

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 148706370 259 PLHDSASSG--HRDIVKLLLRHGGNPFQANKHGERPVDV 295
Cdd:PHA03095 120 PLHVYLSGFniNPKVIRLLLRKGADVNALDLYGMTPLAV 158
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 182-296 2.50e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 80.78  E-value: 2.50e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706370 182 KINKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLH 261
Cdd:PHA02874 116 DVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLH 195

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 148706370 262 DSASSGHRDIVKLLLRHGGNPFQANKHGERPVDVA 296
Cdd:PHA02874 196 NAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNA 230
Ank_2 pfam12796
Ankyrin repeats (3 copies);
183-252 5.77e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.84  E-value: 5.77e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706370  183 INKRNERGETPLHMAAIRGDVKQVKELISlGANVNVKDFaGWTPLHEACNVGYYDVAKILIAAGADVNTQ 252
Cdd:pfam12796  23 ANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINVK 90
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 153-281 3.43e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 75.10  E-value: 3.43e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706370 153 NSPD---STPSHPSQATPAQKK-TPSSSSRQKDkINKRNERGETPLHMAAIRG-DVKQVKELISLGANVNVKDFAGWTPL 227
Cdd:PHA02876 267 NSIDdckNTPLHHASQAPSLSRlVPKLLERGAD-VNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPL 345

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 148706370 228 HEACNVGYY-DVAKILIAAGADVNTQGLDDDTPLHDSASSGHRDIVKLLLRHGGN 281
Cdd:PHA02876 346 HQASTLDRNkDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGAD 400
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 121-289 5.05e-14

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 74.55  E-value: 5.05e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706370 121 GTKKSTPVSILFgyplserKQMALLMQMTARDNSPDSTpshpSQATPAQKKTPSSSSRQKDKINkrnergETPLHMAAIR 200
Cdd:PTZ00322  23 GSRKRRAKPISF-------ERMAAIQEEIARIDTHLEA----LEATENKDATPDHNLTTEEVID------PVVAHMLTVE 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706370 201 -------GDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLHDSASSGHRDIVK 273
Cdd:PTZ00322  86 lcqlaasGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165

                        170
                 ....*....|....*.
gi 148706370 274 LLLRHGGNPFQANKHG 289
Cdd:PTZ00322 166 LLSRHSQCHFELGANA 181
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 183-296 5.71e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 67.30  E-value: 5.71e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706370 183 INKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEAcnVGYYDVAKILIAAGADVNTQGLDDDTPLHD 262
Cdd:PHA02874 183 ANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNA--IIHNRSAIELLINNASINDQDIDGSTPLHH 260

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 148706370 263 SAS-SGHRDIVKLLLRHGGNPFQANKHGERPVDVA 296
Cdd:PHA02874 261 AINpPCDIDIIDILLYHKADISIKDNKGENPIDTA 295
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 183-279 1.08e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 66.83  E-value: 1.08e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706370 183 INKRNE-RGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLH 261
Cdd:PHA02878 160 INMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLH 239

                         90
                 ....*....|....*....
gi 148706370 262 DSASS-GHRDIVKLLLRHG 279
Cdd:PHA02878 240 ISVGYcKDYDILKLLLEHG 258
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
180-296 1.12e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 65.36  E-value: 1.12e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706370 180 KDKINKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTP 259
Cdd:COG0666   11 LLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTL 90

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 148706370 260 LHDSASSGHRDIVKLLLRHGGNPFQANKHGERPVDVA 296
Cdd:COG0666   91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLA 127
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 151-296 1.37e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 66.44  E-value: 1.37e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706370 151 RDNSPDSTPSHPSQATPAQKKTPSSSSRQKdKINKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEA 230
Cdd:PHA02878 163 KDRHKGNTALHYATENKDQRLTELLLSYGA-NVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHIS 241

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706370 231 cnVGY---YDVAKILIAAGADVNTQG-LDDDTPLHDSASSghRDIVKLLLRHGGNPFQANKHGERPVDVA 296
Cdd:PHA02878 242 --VGYckdYDILKLLLEHGVDVNAKSyILGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSA 307
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 191-278 2.39e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 65.40  E-value: 2.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706370 191 ETPLHMAAIRGDVKQVKELISLGANVN---VKDfaGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLHDSASSG 267
Cdd:PHA02875  69 ESELHDAVEEGDVKAVEELLDLGKFADdvfYKD--GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMG 146

                         90
                 ....*....|.
gi 148706370 268 HRDIVKLLLRH 278
Cdd:PHA02875 147 DIKGIELLIDH 157
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 182-251 1.28e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 63.15  E-value: 1.28e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706370 182 KINKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNT 251
Cdd:PHA03100 184 PINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
PHA03095 PHA03095
ankyrin-like protein; Provisional
 183-292 1.62e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 63.12  E-value: 1.62e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706370 183 INKRNERGETPLH--MAAIRGDVKQVKELISLGANVNVKDFAGWTPLH-----EACNVgyyDVAKILIAAGADVNTQGLD 255
Cdd:PHA03095 110 VNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAvllksRNANV---ELLRLLIDAGADVYAVDDR 186

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 148706370 256 DDTPLHDSASSGHRD--IVKLLLRHGGNPFQANKHGERP 292
Cdd:PHA03095 187 FRSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTP 225
PHA03095 PHA03095
ankyrin-like protein; Provisional
 202-281 2.07e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 62.73  E-value: 2.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706370 202 DVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKI---LIAAGADVNTQGLDDDTPLHDSASSGHR-DIVKLLLR 277
Cdd:PHA03095  26 TVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIvrlLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIK 105


                 ....
gi 148706370 278 HGGN 281
Cdd:PHA03095 106 AGAD 109
Ank_4 pfam13637
Ankyrin repeats (many copies);
192-243 3.70e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.36  E-value: 3.70e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 148706370  192 TPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILI 243
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
223-276 4.82e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.97  E-value: 4.82e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 148706370  223 GWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLHDSASSGHRDIVKLLL 276
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 202-296 6.47e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 61.05  E-value: 6.47e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706370 202 DVKQVKELISLGANVNVKD-FAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLHDSASSGHRDIVKLLLRHGG 280
Cdd:PHA02878 146 EAEITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA 225

                         90
                 ....*....|....*.
gi 148706370 281 NPFQANKHGERPVDVA 296
Cdd:PHA02878 226 STDARDKCGNTPLHIS 241
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 192-281 1.69e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 56.54  E-value: 1.69e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706370 192 TPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLHDSASSGHR-D 270
Cdd:PHA02875 137 SPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKiD 216

                         90
                 ....*....|.
gi 148706370 271 IVKLLLRHGGN 281
Cdd:PHA02875 217 IVRLFIKRGAD 227
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 123-280 3.30e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 55.84  E-value: 3.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706370 123 KKSTPVSILF--GYplsERKQMALLMQMTARDNSPDS---TPSHPSQATPAQKKTPSSSSRQKDKINKRNERGETPLHMA 197
Cdd:PHA02876 306 KGETPLYLMAknGY---DTENIRTLIMLGADVNAADRlyiTPLHQASTLDRNKDIVITLLELGANVNARDYCDKTPIHYA 382

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706370 198 AIRGDV----------------------------------KQVKELISLGANVNVKDFAGWTPLHEAC-NVGYYDVAKIL 242
Cdd:PHA02876 383 AVRNNVviintlldygadiealsqkigtalhfalcgtnpyMSVKTLIDRGANVNSKNKDLSTPLHYACkKNCKLDVIEML 462

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 148706370 243 IAAGADVNTQGLDDDTPLhdSASSGHRDIVKLLLRHGG 280
Cdd:PHA02876 463 LDNGADVNAINIQNQYPL--LIALEYHGIVNILLHYGA 498
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
182-260 4.97e-08

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 54.19  E-value: 4.97e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148706370 182 KINKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPL 260
Cdd:COG0666  211 DVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 194-257 7.01e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 54.87  E-value: 7.01e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148706370 194 LHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDD 257
Cdd:PLN03192 626 LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDDD 689
Ank_5 pfam13857
Ankyrin repeats (many copies);
183-230 8.00e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.88  E-value: 8.00e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 148706370  183 INKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEA 230
Cdd:pfam13857   9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 183-289 8.84e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 52.51  E-value: 8.84e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706370 183 INKRNERGETPLHMAAIRGDVKQ--VKELISLGANVNVKdfagwTPLHEACNVGYY---------DVAKILIAAGADVNT 251
Cdd:PHA02859  44 VNDCNDLYETPIFSCLEKDKVNVeiLKFLIENGADVNFK-----TRDNNLSALHHYlsfnknvepEILKILIDSGSSITE 118

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 148706370 252 QGLDDDTPLHDSAS--SGHRDIVKLLLRHGGNPFQANKHG 289
Cdd:PHA02859 119 EDEDGKNLLHMYMCnfNVRINVIKLLIDSGVSFLNKDFDN 158
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 189-290 1.60e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 53.72  E-value: 1.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706370 189 RGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKIL--IAAGADVNT--------------- 251
Cdd:PLN03192 557 KGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILyhFASISDPHAagdllctaakrndlt 636

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 148706370 252 -------QGLDDDTPLHDSASS-------GHRDIVKLLLRHGGNPFQANKHGE 290
Cdd:PLN03192 637 amkellkQGLNVDSEDHQGATAlqvamaeDHVDMVRLLIMNGADVDKANTDDD 689
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 192-281 1.63e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 53.52  E-value: 1.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706370 192 TPLHMA--AIRGDVkqVKELISLGANVNVKDFAGWTPLHEACNVGYY-----DVAKILIAAGADVNTQGLDDDTPLHDSA 264
Cdd:PHA03100  37 LPLYLAkeARNIDV--VKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAI 114

                         90
                 ....*....|....*....
gi 148706370 265 S--SGHRDIVKLLLRHGGN 281
Cdd:PHA03100 115 SkkSNSYSIVEYLLDNGAN 133
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 188-296 4.23e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 51.92  E-value: 4.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706370 188 ERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLHDSASSG 267
Cdd:PHA02875 100 KDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKG 179

                         90       100
                 ....*....|....*....|....*....
gi 148706370 268 HRDIVKLLLRHGGNPfqaNKHGERPvDVA 296
Cdd:PHA02875 180 DIAICKMLLDSGANI---DYFGKNG-CVA 204
Ank_5 pfam13857
Ankyrin repeats (many copies);
242-296 5.30e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.57  E-value: 5.30e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 148706370  242 LIAAG-ADVNTQGLDDDTPLHDSASSGHRDIVKLLLRHGGNPFQANKHGERPVDVA 296
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 170-281 9.92e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 51.22  E-value: 9.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706370 170 KKTPSSSSRQKDKINKRNErgetplHMAAIRGDVKQ-----VKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIA 244
Cdd:PHA02876 126 KEAISGNDIHYDKINESIE------YMKLIKERIQQdelliAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLS 199

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 148706370 245 AGADVNTQGLDDDTPLHDSASSGHRDIVKLLLRHGGN 281
Cdd:PHA02876 200 YGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSN 236
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 206-293 1.22e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 50.73  E-value: 1.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706370 206 VKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLHDSASSGHRDIVKLLLRHGGNPFQA 285
Cdd:PHA02874 107 IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVK 186


                 ....*...
gi 148706370 286 NKHGERPV 293
Cdd:PHA02874 187 DNNGESPL 194
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 189-220 1.25e-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: 44.97  E-value: 1.25e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 148706370  189 RGETPLHMAAIR-GDVKQVKELISLGANVNVKD 220
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 239-296 1.63e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.67  E-value: 1.63e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 148706370 239 AKILIAAGADVNTQGLDDDTPLHDSASSGHRDIVKLLLRHGGNPFQANKHGERPVDVA 296
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELA 155
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 190-261 1.68e-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: 50.40  E-value: 1.68e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706370 190 GETPLHMAAIRGDVKQVKELISLGANVNV--------------KDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLD 255
Cdd:cd22192   89 GETALHIAVVNQNLNLVRELIARGADVVSpratgtffrpgpknLIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSL 168


                 ....*.
gi 148706370 256 DDTPLH 261
Cdd:cd22192  169 GNTVLH 174
PHA03095 PHA03095
ankyrin-like protein; Provisional
 186-277 2.26e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 50.02  E-value: 2.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706370 186 RNERGETPLHMAAIRGDVK--QVKELISLGANVNVKDFAGWTPLHEAcnvGYYD---VAKILIAAGADVNTQGLDDDTPL 260
Cdd:PHA03095 218 TDMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYGQTPLHYA---AVFNnprACRRLIALGADINAVSSDGNTPL 294

                         90
                 ....*....|....*..
gi 148706370 261 HDSASSGHRDIVKLLLR 277
Cdd:PHA03095 295 SLMVRNNNGRAVRAALA 311
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 223-250 3.23e-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: 43.43  E-value: 3.23e-06
                          10        20
                  ....*....|....*....|....*....
gi 148706370  223 GWTPLHEAC-NVGYYDVAKILIAAGADVN 250
Cdd:pfam00023   2 GNTPLHLAAgRRGNLEIVKLLLSKGADVN 30
PHA03095 PHA03095
ankyrin-like protein; Provisional
 183-230 3.91e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 49.25  E-value: 3.91e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 148706370 183 INKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEA 230
Cdd:PHA03095 250 INARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLM 297
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 223-250 6.61e-06

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: 42.57  E-value: 6.61e-06
                           10        20
                   ....*....|....*....|....*...
gi 148706370   223 GWTPLHEACNVGYYDVAKILIAAGADVN 250
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADIN 29
PHA02798 PHA02798
ankyrin-like protein; Provisional
 203-289 6.61e-06

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 48.29  E-value: 6.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706370 203 VKQVKELISLGANVNVKDFAGWTPLheaC----NVGYY----DVAKILIAAGADVNTQGLDDDTPLHDSASSGH---RDI 271
Cdd:PHA02798  51 TDIVKLFINLGANVNGLDNEYSTPL---CtilsNIKDYkhmlDIVKILIENGADINKKNSDGETPLYCLLSNGYinnLEI 127

                         90
                 ....*....|....*...
gi 148706370 272 VKLLLRHGGNPFQANKHG 289
Cdd:PHA02798 128 LLFMIENGADTTLLDKDG 145
Ank_5 pfam13857
Ankyrin repeats (many copies);
214-261 9.13e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.10  E-value: 9.13e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 148706370  214 ANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLH 261
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 255-282 9.98e-06

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: 42.19  E-value: 9.98e-06
                           10        20
                   ....*....|....*....|....*...
gi 148706370   255 DDDTPLHDSASSGHRDIVKLLLRHGGNP 282
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 189-218 1.04e-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: 42.19  E-value: 1.04e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 148706370   189 RGETPLHMAAIRGDVKQVKELISLGANVNV 218
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA03095 PHA03095
ankyrin-like protein; Provisional
 186-282 2.47e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.56  E-value: 2.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706370 186 RNERGETPLHMAA--IRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKI--LIAAGADVNTQGLDDDTPLH 261
Cdd:PHA03095 183 VDDRFRSLLHHHLqsFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLH 262

                         90       100
                 ....*....|....*....|.
gi 148706370 262 DSASSGHRDIVKLLLRHGGNP 282
Cdd:PHA03095 263 YAAVFNNPRACRRLIALGADI 283
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 197-275 4.18e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 46.01  E-value: 4.18e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148706370 197 AAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLHDSASSGHRDIVKLL 275
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL 610
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 255-287 4.61e-05

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: 40.35  E-value: 4.61e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 148706370  255 DDDTPLHDSA-SSGHRDIVKLLLRHGGNPFQANK 287
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
Ank_2 pfam12796
Ankyrin repeats (3 copies);
181-220 6.15e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 41.64  E-value: 6.15e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 148706370  181 DKINKRN-ERGETPLHMAAIRGDVKQVKELISLGANVNVKD 220
Cdd:pfam12796  51 EHADVNLkDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 189-218 9.35e-05

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: 9.35e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 148706370  189 RGETPLHMAAIRGDVKQVKELISLGANVNV 218
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 223-251 1.00e-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: 39.16  E-value: 1.00e-04
                          10        20
                  ....*....|....*....|....*....
gi 148706370  223 GWTPLHEACNVGYYDVAKILIAAGADVNT 251
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 183-296 1.04e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 44.57  E-value: 1.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706370 183 INKRNERGETPLhMAAIR-GDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILI------------------ 243
Cdd:PHA02874  28 INISVDETTTPL-IDAIRsGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIdngvdtsilpipciekdm 106

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 148706370 244 -----AAGADVNTQGLDDDTPLHDSASSGHRDIVKLLLRHGGNPFQANKHGERPVDVA 296
Cdd:PHA02874 107 iktilDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIA 164
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 190-296 2.81e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 43.06  E-value: 2.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706370 190 GETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDD-DTPLHDSASSGH 268
Cdd:PHA02875  35 GISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYKDgMTPLHLATILKK 114

                         90       100
                 ....*....|....*....|....*...
gi 148706370 269 RDIVKLLLRHGGNPFQANKHGERPVDVA 296
Cdd:PHA02875 115 LDIMKLLIARGADPDIPNTDKFSPLHLA 142
Ank_4 pfam13637
Ankyrin repeats (many copies);
183-210 3.12e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.41  E-value: 3.12e-04
                          10        20
                  ....*....|....*....|....*...
gi 148706370  183 INKRNERGETPLHMAAIRGDVKQVKELI 210
Cdd:pfam13637  27 INAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 193-293 8.98e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 41.79  E-value: 8.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706370 193 PLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEAC------------------NVGYYDVA--------------- 239
Cdd:PHA02878  40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICkepnklgmkemirsinkcSVFYTLVAikdafnnrnveifki 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706370 240 -------------------------------KILIAAGADVNTQGLD-DDTPLHDSASSGHRDIVKLLLRHGGNPFQANK 287
Cdd:PHA02878 120 iltnrykniqtidlvyidkkskddiieaeitKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDK 199


                 ....*.
gi 148706370 288 HGERPV 293
Cdd:PHA02878 200 TNNSPL 205
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 194-279 1.53e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 40.72  E-value: 1.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706370 194 LHMAAIRGDVKQVKELISLGAN-VNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLHDSASSGHRDIV 272
Cdd:PHA02874   5 LRMCIYSGDIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDII 84


                 ....*..
gi 148706370 273 KLLLRHG 279
Cdd:PHA02874  85 KLLIDNG 91
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 219-282 5.33e-03

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 39.36  E-value: 5.33e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148706370 219 KDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDD--------------DTPLHDSASSGHRDIVKLLLRHGGNP 282
Cdd:cd22194  137 EAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGVffnpkykhegfyfgETPLALAACTNQPEIVQLLMEKESTD 214
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 191-280 5.56e-03

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: 39.23  E-value: 5.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706370 191 ETPLHMAAIRGDVKQVKELI-SLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGAD-VNTQGLDD----DTPLHDSA 264
Cdd:cd22192   18 ESPLLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNEPMTSDlyqgETALHIAV 97

                         90
                 ....*....|....*.
gi 148706370 265 SSGHRDIVKLLLRHGG 280
Cdd:cd22192   98 VNQNLNLVRELIARGA 113
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 175-282 6.46e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (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. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 39.09  E-value: 6.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706370 175 SSSRQKDKINKRNERGETPLHMAA----------------IRGDVKQVKELISlgANVNVKDFAGWTPLHEACNVGYYDV 238
Cdd:cd21882   11 LRWYLTDSAYQRGATGKTCLHKAAlnlndgvneaimllleAAPDSGNPKELVN--APCTDEFYQGQTALHIAIENRNLNL 88

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 148706370 239 AKILIAAGADVNTQGLDD-------------DTPLHDSASSGHRDIVKLLLRHGGNP 282
Cdd:cd21882   89 VRLLVENGADVSARATGRffrkspgnlfyfgELPLSLAACTNQEEIVRLLLENGAQP 145
PHA02741 PHA02741
hypothetical protein; Provisional
 183-296 7.74e-03

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 37.33  E-value: 7.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706370 183 INKRNERGETPLHMAAIRGDVKQVKELI------SLGANVNVKDFAGWTPLHEAC--NVGYY--DVAKILIAAGADVNTQ 252
Cdd:PHA02741  14 IAEKNSEGENFFHEAARCGCFDIIARFTpfirgdCHAAALNATDDAGQMCIHIAAekHEAQLaaEIIDHLIELGADINAQ 93

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 148706370 253 G-LDDDTPLHDSASSGHRDIVKLLLRHGG-NPFQANKHGERPVDVA 296
Cdd:PHA02741  94 EmLEGDTALHLAAHRRDHDLAEWLCCQPGiDLHFCNADNKSPFELA 139
 
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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