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Conserved domains on  [gi|1615997038|ref|NP_001356612|]
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ankyrin repeat domain-containing protein 53 isoform c [Homo sapiens]

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
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];
66-278 4.32e-31

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 121.60  E-value: 4.32e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615997038  66 AIDQTAIGSYYQLFAAAV-GNVEWLRFCLNQSLREIPTDDKGFTAIHFAAQWGKLACLQVLVEeYKFPVDLLTNNSQTPL 144
Cdd:COG0666    79 DINAKDDGGNTLLHAAARnGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLE-AGADVNAQDNDGNTPL 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615997038 145 HLVIHRDNTTValpcIYYLLEKGADLNAQTCNGSTPLHLAARDGLLDCVKVLVQSGANVHAQDAMGYKPIDFCKIWNHRA 224
Cdd:COG0666   158 HLAAANGNLEI----VKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLE 233

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1615997038 225 CARFLKDAMWKKDKKDFAREMTKMKMFKSQLTLMEHNYLIEYQKEHKILREAAI 278
Cdd:COG0666   234 IVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
66-278 4.32e-31

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 121.60  E-value: 4.32e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615997038  66 AIDQTAIGSYYQLFAAAV-GNVEWLRFCLNQSLREIPTDDKGFTAIHFAAQWGKLACLQVLVEeYKFPVDLLTNNSQTPL 144
Cdd:COG0666    79 DINAKDDGGNTLLHAAARnGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLE-AGADVNAQDNDGNTPL 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615997038 145 HLVIHRDNTTValpcIYYLLEKGADLNAQTCNGSTPLHLAARDGLLDCVKVLVQSGANVHAQDAMGYKPIDFCKIWNHRA 224
Cdd:COG0666   158 HLAAANGNLEI----VKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLE 233

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1615997038 225 CARFLKDAMWKKDKKDFAREMTKMKMFKSQLTLMEHNYLIEYQKEHKILREAAI 278
Cdd:COG0666   234 IVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
Ank_2 pfam12796
Ankyrin repeats (3 copies);
144-240 5.56e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 64.75  E-value: 5.56e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615997038 144 LHLVIHRDNttvaLPCIYYLLEKGADLNAQTCNGSTPLHLAARDGLLDCVKVLVQSgANVHAQDaMGYKPIDFCKIWNHR 223
Cdd:pfam12796   1 LHLAAKNGN----LELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHL 74

                          90
                  ....*....|....*..
gi 1615997038 224 ACARFLKDAMWKKDKKD 240
Cdd:pfam12796  75 EIVKLLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 103-224 1.11e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 60.36  E-value: 1.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615997038 103 DDKGFTAIHFAAQWGKLACLQVLVEeYKFPVDLLTNNSQTPLHLVIHRDNTTValpcIYYLLEKGADLNAQTCNGSTPLH 182
Cdd:PHA02874  121 DAELKTFLHYAIKKGDLESIKMLFE-YGADVNIEDDNGCYPIHIAIKHNFFDI----IKLLLEKGAYANVKDNNGESPLH 195

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1615997038 183 LAARDGLLDCVKVLVQSGANVHAQDAMGYKPIDFCKIWNHRA 224
Cdd:PHA02874  196 NAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSA 237
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 106-210 3.64e-07

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 52.71  E-value: 3.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615997038 106 GFTAIHFAAQWGKLACLQVLVEEykfpVDLLTNN--------SQTPLHLVIHRDNTTValpcIYYLLEKGAD-LNAQTCN 176
Cdd:cd22192    51 GETALHVAALYDNLEAAVVLMEA----APELVNEpmtsdlyqGETALHIAVVNQNLNL----VRELIARGADvVSPRATG 122

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1615997038 177 -------------GSTPLHLAARDGLLDCVKVLVQSGANVHAQDAMG 210
Cdd:cd22192   123 tffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLG 169
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 176-205 1.51e-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: 44.50  E-value: 1.51e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 1615997038  176 NGSTPLHLAARDGLLDCVKVLVQSGANVHA 205
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 141-210 2.00e-06

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 50.46  E-value: 2.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615997038 141 QTPLHLVIHRDNttvaLPCIYYLLEKGADLNAqTCNGS---------------TPLHLAARDGLLDCVKVLVQSGANVHA 205
Cdd:TIGR00870 129 ITALHLAAHRQN----YEIVKLLLERGASVPA-RACGDffvksqgvdsfyhgeSPLNAAACLGSPSIVALLSEDPADILT 203


                  ....*
gi 1615997038 206 QDAMG 210
Cdd:TIGR00870 204 ADSLG 208
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
66-278 4.32e-31

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 121.60  E-value: 4.32e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615997038  66 AIDQTAIGSYYQLFAAAV-GNVEWLRFCLNQSLREIPTDDKGFTAIHFAAQWGKLACLQVLVEeYKFPVDLLTNNSQTPL 144
Cdd:COG0666    79 DINAKDDGGNTLLHAAARnGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLE-AGADVNAQDNDGNTPL 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615997038 145 HLVIHRDNTTValpcIYYLLEKGADLNAQTCNGSTPLHLAARDGLLDCVKVLVQSGANVHAQDAMGYKPIDFCKIWNHRA 224
Cdd:COG0666   158 HLAAANGNLEI----VKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLE 233

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1615997038 225 CARFLKDAMWKKDKKDFAREMTKMKMFKSQLTLMEHNYLIEYQKEHKILREAAI 278
Cdd:COG0666   234 IVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
78-232 1.82e-26

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 108.89  E-value: 1.82e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615997038  78 LFAAAVGNVEWLRFCLNQSLREIPTDDKGFTAIHFAAQWGKLACLQVLVEeYKFPVDLLTNNSQTPLHLVIHRDNTTVAL 157
Cdd:COG0666    59 LAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLE-AGADVNARDKDGETPLHLAAYNGNLEIVK 137

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1615997038 158 pciyYLLEKGADLNAQTCNGSTPLHLAARDGLLDCVKVLVQSGANVHAQDAMGYKPIDFCKIWNHRACARFLKDA 232
Cdd:COG0666   138 ----LLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA 208
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
78-246 1.15e-21

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 95.02  E-value: 1.15e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615997038  78 LFAAAVGNVEWLRFCLNQSLREIPTDDKGFTAIHFAAQWGKLACLQVLVEeYKFPVDLLTNNSQTPLHLVIHRDNTTVAL 157
Cdd:COG0666   125 HLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLE-AGADVNARDNDGETPLHLAAENGHLEIVK 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615997038 158 pciyYLLEKGADLNAQTCNGSTPLHLAARDGLLDCVKVLVQSGANVHAQDAMGYKPIDFCKIWNHRACARFLKDAMWKKD 237
Cdd:COG0666   204 ----LLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLA 279


                  ....*....
gi 1615997038 238 KKDFAREMT 246
Cdd:COG0666   280 AALLDLLTL 288
Ank_2 pfam12796
Ankyrin repeats (3 copies);
144-240 5.56e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 64.75  E-value: 5.56e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615997038 144 LHLVIHRDNttvaLPCIYYLLEKGADLNAQTCNGSTPLHLAARDGLLDCVKVLVQSgANVHAQDaMGYKPIDFCKIWNHR 223
Cdd:pfam12796   1 LHLAAKNGN----LELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHL 74

                          90
                  ....*....|....*..
gi 1615997038 224 ACARFLKDAMWKKDKKD 240
Cdd:pfam12796  75 EIVKLLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
103-232 4.15e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 63.82  E-value: 4.15e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615997038 103 DDKGFTAIHFAAQWGKLACLQVLVEEYKFPVDLLTNNSQTPLHLVIHRDNTTVAlpcIYYLLEKGADLNAQTCNGSTPLH 182
Cdd:COG0666    16 LLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLV---ALLLLAAGADINAKDDGGNTLLH 92

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1615997038 183 LAARDGLLDCVKVLVQSGANVHAQDAMGYKPIDFCKIWNHRACARFLKDA 232
Cdd:COG0666    93 AAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA 142
Ank_2 pfam12796
Ankyrin repeats (3 copies);
79-207 1.97e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 57.43  E-value: 1.97e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615997038  79 FAAAVGNVEWLRFCLNQSLREIPTDDKGFTAIHFAAQWGKLACLQVLVEEykfpvdlltnnsqtplhlvihrdnttvalp 158
Cdd:pfam12796   3 LAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH------------------------------ 52

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1615997038 159 ciyyllekgADLNAQtCNGSTPLHLAARDGLLDCVKVLVQSGANVHAQD 207
Cdd:pfam12796  53 ---------ADVNLK-DNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 103-224 1.11e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 60.36  E-value: 1.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615997038 103 DDKGFTAIHFAAQWGKLACLQVLVEeYKFPVDLLTNNSQTPLHLVIHRDNTTValpcIYYLLEKGADLNAQTCNGSTPLH 182
Cdd:PHA02874  121 DAELKTFLHYAIKKGDLESIKMLFE-YGADVNIEDDNGCYPIHIAIKHNFFDI----IKLLLEKGAYANVKDNNGESPLH 195

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1615997038 183 LAARDGLLDCVKVLVQSGANVHAQDAMGYKPIDFCKIWNHRA 224
Cdd:PHA02874  196 NAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSA 237
PHA03095 PHA03095
ankyrin-like protein; Provisional
 142-217 8.32e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 57.73  E-value: 8.32e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1615997038 142 TPLHLVIHRDNTTVAlPCIYYLLEKGADLNAQTCNGSTPLHLAARDG-LLDCVKVLVQSGANVHAQDAMGYKPIDFC 217
Cdd:PHA03095   49 TPLHLYLHYSSEKVK-DIVRLLLEAGADVNAPERCGFTPLHLYLYNAtTLDVIKLLIKAGADVNAKDKVGRTPLHVY 124
PHA03095 PHA03095
ankyrin-like protein; Provisional
 133-251 1.18e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 57.34  E-value: 1.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615997038 133 VDLLTNNSQTPLHLVIHRDNTtvaLPCIYYLLEKGADLNAQTCNGSTPLHLAARdGL---LDCVKVLVQSGANVHAQDAM 209
Cdd:PHA03095   76 VNAPERCGFTPLHLYLYNATT---LDVIKLLIKAGADVNAKDKVGRTPLHVYLS-GFninPKVIRLLLRKGADVNALDLY 151

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1615997038 210 GYKPIDfCKIWNHRACARFLKdAMWKKDKKDFAREMTKMKMF 251
Cdd:PHA03095  152 GMTPLA-VLLKSRNANVELLR-LLIDAGADVYAVDDRFRSLL 191
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 124-214 5.13e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 55.45  E-value: 5.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615997038 124 VLVEEYKFPVDLLTNNSQTPLHLVIHRDNTTVALPciyYLLEKGADLNAQTCNGSTPLHLAARDGL-LDCVKVLVQSGAN 202
Cdd:PHA02876  257 LLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLVP---KLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGAD 333

                          90
                  ....*....|..
gi 1615997038 203 VHAQDAMGYKPI 214
Cdd:PHA02876  334 VNAADRLYITPL 345
Ank_5 pfam13857
Ankyrin repeats (many copies);
163-217 7.14e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.88  E-value: 7.14e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1615997038 163 LLEKG-ADLNAQTCNGSTPLHLAARDGLLDCVKVLVQSGANVHAQDAMGYKPIDFC 217
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 176-207 7.73e-08

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: 48.44  E-value: 7.73e-08
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1615997038 176 NGSTPLHLAA-RDGLLDCVKVLVQSGANVHAQD 207
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 102-275 1.38e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 53.90  E-value: 1.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615997038 102 TDDKGFTAIHFAAQwgKLACLQVLVE---EYKFPVDLLTNNSQTPLHLV---IHRDNTTV-----------ALPCIYYLL 164
Cdd:PHA03100  102 PDNNGITPLLYAIS--KKSNSYSIVEyllDNGANVNIKNSDGENLLHLYlesNKIDLKILkllidkgvdinAKNRVNYLL 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615997038 165 EKGADLNAQTCNGSTPLHLAARDGLLDCVKVLVQSGANVHAQDAMGYKPIdfckiwnHRACARFLKD------------- 231
Cdd:PHA03100  180 SYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPL-------HIAILNNNKEifklllnngpsik 252

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1615997038 232 -----AMWKKDKKDFARemTKMKMFKSQLTLMEHNYLIEYqKEHKILRE 275
Cdd:PHA03100  253 tiietLLYFKDKDLNTI--TKIKMLKKSIMYMFLLDPGFY-KNRKLIEN 298
Ank_4 pfam13637
Ankyrin repeats (many copies);
177-229 1.50e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.04  E-value: 1.50e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1615997038 177 GSTPLHLAARDGLLDCVKVLVQSGANVHAQDAMGYKPIDFCKIWNHRACARFL 229
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 133-231 1.74e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 53.43  E-value: 1.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615997038 133 VDLLTNNSQTPLHLVIHRDNttvaLPCIYYLLEKGADLNAQTCNGSTPLHLAARDGLLDCVKVLVQSGANVHAQDAMGYK 212
Cdd:PHA02874  117 VNIKDAELKTFLHYAIKKGD----LESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGES 192

                          90
                  ....*....|....*....
gi 1615997038 213 PIDFCKIWNHRACARFLKD 231
Cdd:PHA02874  193 PLHNAAEYGDYACIKLLID 211
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 110-232 2.49e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 53.07  E-value: 2.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615997038 110 IHFAAQWGKLACLQVLVEEYKFPVDLLTNNSQTPLHLVIHRDNttvaLPCIYYLLEKGADLNAQTCNGSTPLHLAARDGL 189
Cdd:PHA02875   72 LHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKK----LDIMKLLIARGADPDIPNTDKFSPLHLAVMMGD 147

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1615997038 190 LDCVKVLVQSGANVHAQDAMGYKPIDFCKIWNHRACARFLKDA 232
Cdd:PHA02875  148 IKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDS 190
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 106-210 3.64e-07

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 52.71  E-value: 3.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615997038 106 GFTAIHFAAQWGKLACLQVLVEEykfpVDLLTNN--------SQTPLHLVIHRDNTTValpcIYYLLEKGAD-LNAQTCN 176
Cdd:cd22192    51 GETALHVAALYDNLEAAVVLMEA----APELVNEpmtsdlyqGETALHIAVVNQNLNL----VRELIARGADvVSPRATG 122

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1615997038 177 -------------GSTPLHLAARDGLLDCVKVLVQSGANVHAQDAMG 210
Cdd:cd22192   123 tffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLG 169
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 103-215 4.29e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 52.27  E-value: 4.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615997038 103 DDKGFTAIHFAAQWGKLACLQVLVEEYKFpVDLLTNNSQTPLHLVIHRDNTTVALpciyylLEKGADLNAQTCNGSTPLH 182
Cdd:PHA02874  187 DNNGESPLHNAAEYGDYACIKLLIDHGNH-IMNKCKNGFTPLHNAIIHNRSAIEL------LINNASINDQDIDGSTPLH 259

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1615997038 183 LAARDGL-LDCVKVLVQSGANVHAQDAMGYKPID 215
Cdd:PHA02874  260 HAINPPCdIDIIDILLYHKADISIKDNKGENPID 293
Ank_5 pfam13857
Ankyrin repeats (many copies);
125-184 1.04e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.80  E-value: 1.04e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615997038 125 LVEEYKFPVDLLTNNSQTPLHLVIHRDNTTVALpciyYLLEKGADLNAQTCNGSTPLHLA 184
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVR----VLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 176-205 1.51e-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: 44.50  E-value: 1.51e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 1615997038  176 NGSTPLHLAARDGLLDCVKVLVQSGANVHA 205
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 141-210 2.00e-06

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 50.46  E-value: 2.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615997038 141 QTPLHLVIHRDNttvaLPCIYYLLEKGADLNAqTCNGS---------------TPLHLAARDGLLDCVKVLVQSGANVHA 205
Cdd:TIGR00870 129 ITALHLAAHRQN----YEIVKLLLERGASVPA-RACGDffvksqgvdsfyhgeSPLNAAACLGSPSIVALLSEDPADILT 203


                  ....*
gi 1615997038 206 QDAMG 210
Cdd:TIGR00870 204 ADSLG 208
Ank_4 pfam13637
Ankyrin repeats (many copies);
142-197 3.27e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.19  E-value: 3.27e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1615997038 142 TPLHLVIHRDNttvaLPCIYYLLEKGADLNAQTCNGSTPLHLAARDGLLDCVKVLV 197
Cdd:pfam13637   3 TALHAAAASGH----LELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 83-210 3.75e-06

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: 49.49  E-value: 3.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615997038  83 VGNVEWLRFCLNQSLREIPTddKGFTAIHFAA---QWGKLACLQVLVEEYKFPVDL--LTNNS--------QTPLHLVIH 149
Cdd:cd21882     5 LGLLECLRWYLTDSAYQRGA--TGKTCLHKAAlnlNDGVNEAIMLLLEAAPDSGNPkeLVNAPctdefyqgQTALHIAIE 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1615997038 150 RDNttvaLPCIYYLLEKGADLNAQTCN-------------GSTPLHLAARDGLLDCVKVLVQSG---ANVHAQDAMG 210
Cdd:cd21882    83 NRN----LNLVRLLVENGADVSARATGrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGaqpAALEAQDSLG 155
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 103-221 7.13e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 48.52  E-value: 7.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615997038 103 DDKGFTAIHFAAQWGKLACLQVLVEEYKFPVDLLTNNSQTPLHLVIHRDNTTvalPCIYYLLEKGADLNAQTCNGSTPLH 182
Cdd:PHA02876  270 DDCKNTPLHHASQAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYDT---ENIRTLIMLGADVNAADRLYITPLH 346

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1615997038 183 LAAR-DGLLDCVKVLVQSGANVHAQDAMGYKPIDFCKIWN 221
Cdd:PHA02876  347 QASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRN 386
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 100-206 7.48e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 48.34  E-value: 7.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615997038 100 IPTDDKGFTAIHFAAQwGKLACLQVLVEEYKFPVDLLTNNSQTPLHLVI-HRDNttvalPCIYYLLEKGADLNAQTCNGS 178
Cdd:PHA02878  162 MKDRHKGNTALHYATE-NKDQRLTELLLSYGANVNIPDKTNNSPLHHAVkHYNK-----PIVHILLENGASTDARDKCGN 235

                          90       100
                  ....*....|....*....|....*....
gi 1615997038 179 TPLHLAARDGL-LDCVKVLVQSGANVHAQ 206
Cdd:PHA02878  236 TPLHISVGYCKdYDILKLLLEHGVDVNAK 264
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 105-203 8.10e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 48.06  E-value: 8.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615997038 105 KGFTAIHFAAQWGKLACLQVLVEeYKFPVDLLTNNSQTPLHL-VIHRDNTTVALpciyyLLEKGADLNAQTCNGSTPLHL 183
Cdd:PHA02875  101 DGMTPLHLATILKKLDIMKLLIA-RGADPDIPNTDKFSPLHLaVMMGDIKGIEL-----LIDHKACLDIEDCCGCTPLII 174

                          90       100
                  ....*....|....*....|
gi 1615997038 184 AARDGLLDCVKVLVQSGANV 203
Cdd:PHA02875  175 AMAKGDIAICKMLLDSGANI 194
PHA03095 PHA03095
ankyrin-like protein; Provisional
 106-208 8.47e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 48.10  E-value: 8.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615997038 106 GFTAIHFAAQWG-KLACLQVLVEeYKFPVDLLTNNSQTPLHlvIHRDNTTVALPCIYYLLEKGADLNAQTCNGSTPLH-- 182
Cdd:PHA03095   83 GFTPLHLYLYNAtTLDVIKLLIK-AGADVNAKDKVGRTPLH--VYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAvl 159

                          90       100
                  ....*....|....*....|....*.
gi 1615997038 183 LAARDGLLDCVKVLVQSGANVHAQDA 208
Cdd:PHA03095  160 LKSRNANVELLRLLIDAGADVYAVDD 185
PHA03095 PHA03095
ankyrin-like protein; Provisional
 85-230 8.85e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 48.10  E-value: 8.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615997038  85 NVEWLRFCLNQSLREIPTDDKGFTAIHFAAQWGKL--ACLQVLVEEYKFP--VDLLTNnsqTPLHLVihRDNTTVALPCI 160
Cdd:PHA03095  166 NVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPraRIVRELIRAGCDPaaTDMLGN---TPLHSM--ATGSSCKRSLV 240

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1615997038 161 YYLLEKGADLNAQTCNGSTPLHLAA---RDGLLDCvkvLVQSGANVHAQDAMGYKPIDF----CkiwNHRACARFLK 230
Cdd:PHA03095  241 LPLLIAGISINARNRYGQTPLHYAAvfnNPRACRR---LIALGADINAVSSDGNTPLSLmvrnN---NGRAVRAALA 311
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 163-210 9.04e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 48.33  E-value: 9.04e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1615997038 163 LLEKGADLNAQTCNGSTPLHLAARDGLLDCVKVLVQSGANVHAQDAMG 210
Cdd:PLN03192  544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANG 591
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 108-214 1.16e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 48.14  E-value: 1.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615997038 108 TAIHFAAQWGKLACLQVLVEeYKFPVDLLTNNSQTPLHLVIHRDNTTVAlpcIYYLLEKGADLNAQTCNGSTPLHLAARD 187
Cdd:PHA02876  377 TPIHYAAVRNNVVIINTLLD-YGADIEALSQKIGTALHFALCGTNPYMS---VKTLIDRGANVNSKNKDLSTPLHYACKK 452

                          90       100
                  ....*....|....*....|....*...
gi 1615997038 188 GL-LDCVKVLVQSGANVHAQDAMGYKPI 214
Cdd:PHA02876  453 NCkLDVIEMLLDNGADVNAINIQNQYPL 480
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 163-215 1.32e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.97  E-value: 1.32e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1615997038 163 LLEKGADLNAQTCNGSTPLHLAARDGLLDCVKVLVQSGANVHAQDAMGYKPID 215
Cdd:PTZ00322  101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLE 153
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 141-210 1.84e-05

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. 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.


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 47.49  E-value: 1.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615997038 141 QTPLHLVIHRDNTTValpcIYYLLEKGADLNAQTCN--------------GSTPLHLAARDGLLDCVKVLVQ---SGANV 203
Cdd:cd22196    95 QTALHIAIERRNMHL----VELLVQNGADVHARASGeffkkkkggpgfyfGELPLSLAACTNQLDIVKFLLEnphSPADI 170


                  ....*..
gi 1615997038 204 HAQDAMG 210
Cdd:cd22196   171 SARDSMG 177
Ank_4 pfam13637
Ankyrin repeats (many copies);
108-164 2.13e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.88  E-value: 2.13e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1615997038 108 TAIHFAAQWGKLACLQVLVeEYKFPVDLLTNNSQTPLHLVIHRDNttvaLPCIYYLL 164
Cdd:pfam13637   3 TALHAAAASGHLELLRLLL-EKGADINAVDGNGETALHFAASNGN----VEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
78-126 4.37e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.11  E-value: 4.37e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1615997038  78 LFAAAV-GNVEWLRFCLNQSLREIPTDDKGFTAIHFAAQWGKLACLQVLV 126
Cdd:pfam13637   5 LHAAAAsGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 120-228 7.31e-05

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 45.46  E-value: 7.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615997038 120 ACLQVLVEEYKFPVDLLTNnsqtpLHLVIHRDNTTVALPciyyllekgadlNAQTCN----GSTPLHLAARDGLLDCVKV 195
Cdd:TIGR00870  84 TLLHAISLEYVDAVEAILL-----HLLAAFRKSGPLELA------------NDQYTSeftpGITALHLAAHRQNYEIVKL 146

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1615997038 196 LVQSGANVHAQdAMGykpiDFCKIWNHRACARF 228
Cdd:TIGR00870 147 LLERGASVPAR-ACG----DFFVKSQGVDSFYH 174
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 141-210 1.10e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong 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: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 44.79  E-value: 1.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615997038 141 QTPLHLVIHRDNTTvalpCIYYLLEKGADLNAQTCN--------------GSTPLHLAARDGLLDCVKVLVQSG---ANV 203
Cdd:cd22193    77 QTALHIAIERRQGD----IVALLVENGADVHAHAKGrffqpkyqgegfyfGELPLSLAACTNQPDIVQYLLENEhqpADI 152


                  ....*..
gi 1615997038 204 HAQDAMG 210
Cdd:cd22193   153 EAQDSRG 159
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 137-214 1.63e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 43.89  E-value: 1.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615997038 137 TNNSQTPLH-LVIHRDNTTVALPCIYYLLEKGADLNAQTCNGSTPLHLAA--RDGLLDCVKVLVQSGANVHAQDAMGYKP 213
Cdd:PHA03100   65 TKNNSTPLHyLSNIKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENL 144


                  .
gi 1615997038 214 I 214
Cdd:PHA03100  145 L 145
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 176-205 2.27e-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: 38.39  E-value: 2.27e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1615997038 176 NGSTPLHLAARDGLLDCVKVLVQSGANVHA 205
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 138-214 3.44e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 42.95  E-value: 3.44e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1615997038 138 NNSQTPLHLVIHRDNTTVAlpciYYLLEKGADLNAQTCNGSTPLHLAARDGLLDCVKVLVQSGANVHAQDAMGYKPI 214
Cdd:PHA02878  166 HKGNTALHYATENKDQRLT----ELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPL 238
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 142-214 7.72e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 41.79  E-value: 7.72e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1615997038 142 TPLHLVIHRdntTVALPCIYYLLEKGADLNAQ-TCNGSTPLHLAARDGllDCVKVLVQSGANVHAQDAMGYKPI 214
Cdd:PHA02878  236 TPLHISVGY---CKDYDILKLLLEHGVDVNAKsYILGLTALHSSIKSE--RKLKLLLEYGADINSLNSYKLTPL 304
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 159-206 9.82e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely related to TRPV1, sharing high sequence identity (>50%), but TRPV2 shows a higher temperature threshold and sensitivity for activation than TRPV1. TRPV2 can be stimulated by ligands or lipids, and is involved in osmosensation and mechanosensation. TRPV2 is expressed in both neuronal and non-neuronal tissues, and it has been implicated in diverse physiological and pathophysiological processes, including cardiac-structure maintenance, innate immunity, and cancer. TRPV2 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 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.


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 41.76  E-value: 9.82e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1615997038 159 CIYYLLEKGAD-------LNAQTCN----GSTPLHLAARDGLLDCVKVLVQSGANVHAQ 206
Cdd:cd22197    65 CIMPLLEIDKDsgnpkplVNAQCTDeyyrGHSALHIAIEKRSLQCVKLLVENGADVHAR 123
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 121-210 1.01e-03

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 41.67  E-value: 1.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615997038 121 CLQVLV------EEYKfpvdlltnnSQTPLHLVIHRDNTTValpcIYYLLEKGADLNAQTCN--------------GSTP 180
Cdd:cd22194   125 ILDRFInaeyteEAYE---------GQTALNIAIERRQGDI----VKLLIAKGADVNAHAKGvffnpkykhegfyfGETP 191

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1615997038 181 LHLAARDGLLDCVKVLVQSGA-NVHAQDAMG 210
Cdd:cd22194   192 LALAACTNQPEIVQLLMEKEStDITSQDSRG 222
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 123-217 1.91e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 40.42  E-value: 1.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615997038 123 QVLVEEYKFPVdlltnnsqTPLHLVIHRDNTTValpcIYYLLEKGADLNAQTCNGSTPLHLAARDGL-----LDCVKVLV 197
Cdd:PHA03100   26 DLNDYSYKKPV--------LPLYLAKEARNIDV----VKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLL 93

                          90       100
                  ....*....|....*....|
gi 1615997038 198 QSGANVHAQDAMGYKPIDFC 217
Cdd:PHA03100   94 EYGANVNAPDNNGITPLLYA 113
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 151-214 2.25e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 40.33  E-value: 2.25e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1615997038 151 DNTTVALPC-----IYYLLEKGADLNAQTCNGSTPLHLAARDGLLDCVKVLVQSGANVHAQDAMGYKPI 214
Cdd:PHA02874   93 DTSILPIPCiekdmIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPI 161
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 117-210 2.31e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely related to TRPV1, sharing high sequence identity (>50%), but TRPV2 shows a higher temperature threshold and sensitivity for activation than TRPV1. TRPV2 can be stimulated by ligands or lipids, and is involved in osmosensation and mechanosensation. TRPV2 is expressed in both neuronal and non-neuronal tissues, and it has been implicated in diverse physiological and pathophysiological processes, including cardiac-structure maintenance, innate immunity, and cancer. TRPV2 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 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.


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 40.61  E-value: 2.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615997038 117 GKLACLQVLVEE------YKFPVDLLTNNS----QTPLHLVIHRDNttvaLPCIYYLLEKGADLNAQTCN---------- 176
Cdd:cd22197    61 GVNACIMPLLEIdkdsgnPKPLVNAQCTDEyyrgHSALHIAIEKRS----LQCVKLLVENGADVHARACGrffqkkqgtc 136

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1615997038 177 ---GSTPLHLAARDGLLDCVKVLVQSG---ANVHAQDAMG 210
Cdd:cd22197   137 fyfGELPLSLAACTKQWDVVNYLLENPhqpASLQAQDSLG 176
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 78-229 3.07e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 40.24  E-value: 3.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615997038  78 LFAAAVGNVEWLRFCLNQSLREIPTDDKGFTAIHFAAQWGKLACLQVLVeEYKFPVDLLTNNSQTPLHLVIHRDNTTval 157
Cdd:PLN03192  530 LTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLL-KHACNVHIRDANGNTALWNAISAKHHK--- 605

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1615997038 158 pcIYYLLEKGADLNAQTCNGSTpLHLAARDGLLDCVKVLVQSGANVHAQDAMGYKPIDFCKIWNHRACARFL 229
Cdd:PLN03192  606 --IFRILYHFASISDPHAAGDL-LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLL 674
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 141-174 4.00e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 34.96  E-value: 4.00e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1615997038 141 QTPLHLVIHRDNttvALPCIYYLLEKGADLNAQT 174
Cdd:pfam00023   3 NTPLHLAAGRRG---NLEIVKLLLSKGADVNARD 33
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 141-216 4.51e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 39.50  E-value: 4.51e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1615997038 141 QTPLHLVIHRDNTTVALpciyYLLEKGADLNAQTCNGSTPLHLAARDGLLDCVKVLVQSGANVHAQDAMGyKPIDF 216
Cdd:PTZ00322  116 RTPLHIACANGHVQVVR----VLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGANA-KPDSF 186
PHA02741 PHA02741
hypothetical protein; Provisional
 141-219 7.65e-03

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 37.33  E-value: 7.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615997038 141 QTPLHLVIHRDNTTVALPCIYYLLEKGADLNAQ-TCNGSTPLHLAARDGLLDCVKVLV-QSGANVHAQDAMGYKPIDFCK 218
Cdd:PHA02741   61 QMCIHIAAEKHEAQLAAEIIDHLIELGADINAQeMLEGDTALHLAAHRRDHDLAEWLCcQPGIDLHFCNADNKSPFELAI 140


                  .
gi 1615997038 219 I 219
Cdd:PHA02741  141 D 141
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 163-204 8.94e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 38.89  E-value: 8.94e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1615997038 163 LLEKGADLNAQTCNGSTPLHLAARDGLLDCVKVLVQSGANVH 204
Cdd:PHA02876  164 LLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVN 205
Ank_5 pfam13857
Ankyrin repeats (many copies);
102-147 9.93e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 34.63  E-value: 9.93e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1615997038 102 TDDKGFTAIHFAAQWGKLACLQVLVeEYKFPVDLLTNNSQTPLHLV 147
Cdd:pfam13857  12 LDGEGYTPLHVAAKYGALEIVRVLL-AYGVDLNLKDEEGLTALDLA 56
 
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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