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Conserved domains on  [gi|219555688|ref|NP_001137222|]
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notch-regulated ankyrin repeat-containing protein [Rattus norvegicus]

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];
21-106 1.85e-18

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 78.07  E-value: 1.85e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219555688  21 AVRKGNTQELQSLLQNmtncEFNVNSFGPEGQTALHQSVIDGNLELVKLLVKFGADIRLANRDGWSALHIAAFGGHQDIV 100
Cdd:COG0666  127 AAYNGNLEIVKLLLEA----GADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIV 202


                 ....*.
gi 219555688 101 LYLITK 106
Cdd:COG0666  203 KLLLEA 208
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
21-106 1.85e-18

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 78.07  E-value: 1.85e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219555688  21 AVRKGNTQELQSLLQNmtncEFNVNSFGPEGQTALHQSVIDGNLELVKLLVKFGADIRLANRDGWSALHIAAFGGHQDIV 100
Cdd:COG0666  127 AAYNGNLEIVKLLLEA----GADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIV 202


                 ....*.
gi 219555688 101 LYLITK 106
Cdd:COG0666  203 KLLLEA 208
Ank_2 pfam12796
Ankyrin repeats (3 copies);
21-106 3.00e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.53  E-value: 3.00e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219555688   21 AVRKGNTQELQSLLqnmtNCEFNVNSFGPEGQTALHQSVIDGNLELVKLLVKFgADIRLANrDGWSALHIAAFGGHQDIV 100
Cdd:pfam12796   4 AAKNGNLELVKLLL----ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIV 77


                  ....*.
gi 219555688  101 LYLITK 106
Cdd:pfam12796  78 KLLLEK 83
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 1-104 2.40e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 50.37  E-value: 2.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219555688   1 MSQAELSTCSAPQTQRIFQEAVRKGNTQELQSLLQNMTnceFNVNSFGPEGQTALHQSVIDGNLELVKLLVKFGADIRLA 80
Cdd:PHA02875  55 MKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGK---FADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIP 131

                         90       100
                 ....*....|....*....|....
gi 219555688  81 NRDGWSALHIAAFGGHQDIVLYLI 104
Cdd:PHA02875 132 NTDKFSPLHLAVMMGDIKGIELLI 155
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 13-114 1.57e-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: 45.00  E-value: 1.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219555688  13 QTQRIFQ----EAVRKGNTQELQSLLQNMTnceFNVNSFGPEGQTALHQSVIDGNLELVKLLVKfgADIRLANR------ 82
Cdd:cd22192   12 QQKRISEspllLAAKENDVQAIKKLLKCPS---CDLFQRGALGETALHVAALYDNLEAAVVLME--AAPELVNEpmtsdl 86

                         90       100       110
                 ....*....|....*....|....*....|...
gi 219555688  83 -DGWSALHIAAFGGHQDIVLYLITKAKYAASGR 114
Cdd:cd22192   87 yQGETALHIAVVNQNLNLVRELIARGADVVSPR 119
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 50-77 5.42e-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: 37.57  E-value: 5.42e-05
                           10        20
                   ....*....|....*....|....*...
gi 219555688    50 EGQTALHQSVIDGNLELVKLLVKFGADI 77
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 50-77 1.78e-03

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: 36.21  E-value: 1.78e-03
                          10        20
                  ....*....|....*....|....*...
gi 219555688   50 EGQTALHQSVIDGNLELVKLLVKFGADI 77
Cdd:TIGR00870 127 PGITALHLAAHRQNYEIVKLLLERGASV 154
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
21-106 1.85e-18

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 78.07  E-value: 1.85e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219555688  21 AVRKGNTQELQSLLQNmtncEFNVNSFGPEGQTALHQSVIDGNLELVKLLVKFGADIRLANRDGWSALHIAAFGGHQDIV 100
Cdd:COG0666  127 AAYNGNLEIVKLLLEA----GADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIV 202


                 ....*.
gi 219555688 101 LYLITK 106
Cdd:COG0666  203 KLLLEA 208
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
18-104 3.10e-18

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 77.30  E-value: 3.10e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219555688  18 FQEAVRKGNTQELQSLLQNmtncEFNVNSFGPEGQTALHQSVIDGNLELVKLLVKFGADIRLANRDGWSALHIAAFGGHQ 97
Cdd:COG0666   91 LHAAARNGDLEIVKLLLEA----GADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166


                 ....*..
gi 219555688  98 DIVLYLI 104
Cdd:COG0666  167 EIVKLLL 173
Ank_2 pfam12796
Ankyrin repeats (3 copies);
21-106 3.00e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.53  E-value: 3.00e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219555688   21 AVRKGNTQELQSLLqnmtNCEFNVNSFGPEGQTALHQSVIDGNLELVKLLVKFgADIRLANrDGWSALHIAAFGGHQDIV 100
Cdd:pfam12796   4 AAKNGNLELVKLLL----ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIV 77


                  ....*.
gi 219555688  101 LYLITK 106
Cdd:pfam12796  78 KLLLEK 83
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
21-108 1.37e-15

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 70.37  E-value: 1.37e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219555688  21 AVRKGNTQELQSLLQNmtncEFNVNSFGPEGQTALHQSVIDGNLELVKLLVKFGADIRLANRDGWSALHIAAFGGHQDIV 100
Cdd:COG0666  160 AAANGNLEIVKLLLEA----GADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIV 235


                 ....*...
gi 219555688 101 LYLITKAK 108
Cdd:COG0666  236 KLLLEAGA 243
Ank_2 pfam12796
Ankyrin repeats (3 copies);
55-107 3.08e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 62.83  E-value: 3.08e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 219555688   55 LHQSVIDGNLELVKLLVKFGADIRLANRDGWSALHIAAFGGHQDIVLYLITKA 107
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA 53
Ank_4 pfam13637
Ankyrin repeats (many copies);
53-104 1.02e-13

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 60.37  E-value: 1.02e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 219555688   53 TALHQSVIDGNLELVKLLVKFGADIRLANRDGWSALHIAAFGGHQDIVLYLI 104
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
43-104 2.54e-13

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 64.20  E-value: 2.54e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 219555688  43 NVNSFGPEGQTALHQSVIDGNLELVKLLVKFGADIRLANRDGWSALHIAAFGGHQDIVLYLI 104
Cdd:COG0666   79 DINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLL 140
Ank_5 pfam13857
Ankyrin repeats (many copies);
39-91 3.48e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.88  E-value: 3.48e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 219555688   39 NCEFNVNSFGPEGQTALHQSVIDGNLELVKLLVKFGADIRLANRDGWSALHIA 91
Cdd:pfam13857   4 HGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 1-104 2.40e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 50.37  E-value: 2.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219555688   1 MSQAELSTCSAPQTQRIFQEAVRKGNTQELQSLLQNMTnceFNVNSFGPEGQTALHQSVIDGNLELVKLLVKFGADIRLA 80
Cdd:PHA02875  55 MKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGK---FADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIP 131

                         90       100
                 ....*....|....*....|....
gi 219555688  81 NRDGWSALHIAAFGGHQDIVLYLI 104
Cdd:PHA02875 132 NTDKFSPLHLAVMMGDIKGIELLI 155
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 33-110 3.77e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 49.58  E-value: 3.77e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 219555688  33 LLQNMTNCEFNVNSFGPEGQTALHQSVIDGNLELVKLLVKFGADIRLANRDGWSALHIAAFGGHQDIVLYLITKAKYA 110
Cdd:PHA02874 106 MIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYA 183
Ank_2 pfam12796
Ankyrin repeats (3 copies);
21-81 9.58e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 43.57  E-value: 9.58e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 219555688   21 AVRKGNTQELQSLLQNMtncefNVNSFGpEGQTALHQSVIDGNLELVKLLVKFGADIRLAN 81
Cdd:pfam12796  37 AAKNGHLEIVKLLLEHA-----DVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 45-103 1.42e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 45.27  E-value: 1.42e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 219555688  45 NSFGPEGQTALHQSVIDGNLELVKLLVKFGADIRLANRDGWSALHIAAFGGHQDIVLYL 103
Cdd:PTZ00322 109 NCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 13-114 1.57e-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: 45.00  E-value: 1.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219555688  13 QTQRIFQ----EAVRKGNTQELQSLLQNMTnceFNVNSFGPEGQTALHQSVIDGNLELVKLLVKfgADIRLANR------ 82
Cdd:cd22192   12 QQKRISEspllLAAKENDVQAIKKLLKCPS---CDLFQRGALGETALHVAALYDNLEAAVVLME--AAPELVNEpmtsdl 86

                         90       100       110
                 ....*....|....*....|....*....|...
gi 219555688  83 -DGWSALHIAAFGGHQDIVLYLITKAKYAASGR 114
Cdd:cd22192   87 yQGETALHIAVVNQNLNLVRELIARGADVVSPR 119
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 50-104 3.42e-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: 44.23  E-value: 3.42e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 219555688  50 EGQTALHQSVIDGNLELVKLLVKFGADIRLA---------NRD-----GWSALHIAAFGGHQDIVLYLI 104
Cdd:cd22192   88 QGETALHIAVVNQNLNLVRELIARGADVVSPratgtffrpGPKnliyyGEHPLSFAACVGNEEIVRLLI 156
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
21-108 6.17e-06

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 43.40  E-value: 6.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219555688  21 AVRKGNTQELQSLLQNmtncEFNVNSFGPEGQTALHQSVIDGNLELVKLLVKFGADIRLANRDGWSALHIAAFGGHQDIV 100
Cdd:COG0666  193 AAENGHLEIVKLLLEA----GADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIV 268


                 ....*...
gi 219555688 101 LYLITKAK 108
Cdd:COG0666  269 KLLLLALL 276
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 51-104 8.05e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 43.12  E-value: 8.05e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 219555688  51 GQTALHQSVIDGNLELVKLLVKFGADIRLANRDGWSALHIAAFGGHQDIVLYLI 104
Cdd:PHA03100 192 GFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLL 245
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 50-78 1.56e-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: 38.78  E-value: 1.56e-05
                          10        20
                  ....*....|....*....|....*....
gi 219555688   50 EGQTALHQSVIDGNLELVKLLVKFGADIR 78
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 50-104 3.05e-05

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: 41.40  E-value: 3.05e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 219555688  50 EGQTALHQSVIDGNLELVKLLVKFGADIRL-ANRD------------GWSALHIAAFGGHQDIVLYLI 104
Cdd:cd21882   72 QGQTALHIAIENRNLNLVRLLVENGADVSArATGRffrkspgnlfyfGELPLSLAACTNQEEIVRLLL 139
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 50-77 5.42e-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: 37.57  E-value: 5.42e-05
                           10        20
                   ....*....|....*....|....*...
gi 219555688    50 EGQTALHQSVIDGNLELVKLLVKFGADI 77
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
43-104 1.33e-04

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 39.55  E-value: 1.33e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 219555688  43 NVNSFGPEGQTALHQSVIDGNLELVKLLVKFGADIRLANRDGWSALHIAAFGGHQDIVLYLI 104
Cdd:COG0666   46 ALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLL 107
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 50-82 1.86e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.11  E-value: 1.86e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 219555688   50 EGQTALHQSVID-GNLELVKLLVKFGADIRLANR 82
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 14-112 2.10e-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: 39.07  E-value: 2.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219555688  14 TQRIFQEAVRKGNTQELqsllqnmTNCEFNvNSFgPEGQTALHQSVIDGNLELVKLLVKFGADIRL--------ANRD-- 83
Cdd:cd22197   66 IMPLLEIDKDSGNPKPL-------VNAQCT-DEY-YRGHSALHIAIEKRSLQCVKLLVENGADVHAracgrffqKKQGtc 136

                         90       100       110
                 ....*....|....*....|....*....|..
gi 219555688  84 ---GWSALHIAAFGGHQDIVLYLITKAKYAAS 112
Cdd:cd22197  137 fyfGELPLSLAACTKQWDVVNYLLENPHQPAS 168
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 62-105 2.23e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 39.08  E-value: 2.23e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 219555688  62 GNLELVKLLVKFGADIRLANRDGWSALHIAAFGGHQDIVLYLIT 105
Cdd:PLN03192 633 NDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIM 676
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 4-106 6.95e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 37.55  E-value: 6.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219555688   4 AELSTCSAPQTQRIFQEAVRKGNTQELQSLLQNMTNCEFNVNSFgpEGQTALHQSVIDGnlELVKLLVKFGADIRLANRD 83
Cdd:PHA02878  91 RSINKCSVFYTLVAIKDAFNNRNVEIFKIILTNRYKNIQTIDLV--YIDKKSKDDIIEA--EITKLLLSYGADINMKDRH 166

                         90       100
                 ....*....|....*....|....
gi 219555688  84 -GWSALHIAAFGGHQDIVLYLITK 106
Cdd:PHA02878 167 kGNTALHYATENKDQRLTELLLSY 190
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 14-111 9.10e-04

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: 37.09  E-value: 9.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219555688  14 TQRIFQEAVRKGNTqelqslLQNMTNCEFNVNSFgpEGQTALHQSVIDGNLELVKLLVKFGADIRLA----------NRD 83
Cdd:cd22196   65 TISLLLDIAEKTGN------LKEFVNAAYTDSYY--KGQTALHIAIERRNMHLVELLVQNGADVHARasgeffkkkkGGP 136

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 219555688  84 GWS----ALHIAAFGGHQDIVLYLI----TKAKYAA 111
Cdd:cd22196  137 GFYfgelPLSLAACTNQLDIVKFLLenphSPADISA 172
PHA03095 PHA03095
ankyrin-like protein; Provisional
 51-106 1.30e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 36.54  E-value: 1.30e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 219555688  51 GQTALHQSVIDGN-LELVKLLVKFGADIRLANRDGWSALHI--AAFGGHQDIVLYLITK 106
Cdd:PHA03095  83 GFTPLHLYLYNATtLDVIKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRK 141
Ank_4 pfam13637
Ankyrin repeats (many copies);
21-71 1.52e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 34.17  E-value: 1.52e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 219555688   21 AVRKGNTQELQSLLQNmtncEFNVNSFGPEGQTALHQSVIDGNLELVKLLV 71
Cdd:pfam13637   8 AAASGHLELLRLLLEK----GADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 62-107 1.56e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 36.77  E-value: 1.56e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 219555688  62 GNLELVKLLVKFGADIRLANRDGWSALHIAAFGGHQDIVLYLITKA 107
Cdd:PLN03192 536 GNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHA 581
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 50-114 1.66e-03

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: 36.31  E-value: 1.66e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 219555688  50 EGQTALHQSVIDGNLELVKLLVKFGADIRLANRD--------------GWSALHIAAFGGHQDIVLYLITKAKYAASGR 114
Cdd:cd22193   75 EGQTALHIAIERRQGDIVALLVENGADVHAHAKGrffqpkyqgegfyfGELPLSLAACTNQPDIVQYLLENEHQPADIE 153
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 50-77 1.78e-03

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: 36.21  E-value: 1.78e-03
                          10        20
                  ....*....|....*....|....*...
gi 219555688   50 EGQTALHQSVIDGNLELVKLLVKFGADI 77
Cdd:TIGR00870 127 PGITALHLAAHRQNYEIVKLLLERGASV 154
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 43-106 2.84e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 35.80  E-value: 2.84e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 219555688  43 NVNSFGPEGQTALHQSVID--GNLELVKLLVKFGADIRLANRDGWSALHIAAFGGHQD--IVLYLITK 106
Cdd:PHA03100  98 NVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIDK 165
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 25-104 2.87e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 35.71  E-value: 2.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219555688  25 GNTQELQSLLQNMTNCefnVNSFGPEGQTALHQSVIDGNLELVKLLVKFGADIRLANRDGWSALHIAAFGGHQDIVLYLI 104
Cdd:PHA02874  12 GDIEAIEKIIKNKGNC---INISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLI 88
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 20-83 3.09e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 35.61  E-value: 3.09e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 219555688  20 EAVRKGNTQELQSLLQNmtncEFNVNSFGPEGQTALHQSVIDGNLELVKLLVKFGADIRLANRD 83
Cdd:PLN03192 628 TAAKRNDLTAMKELLKQ----GLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTD 687
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 83-106 3.11e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 32.94  E-value: 3.11e-03
                           10        20
                   ....*....|....*....|....
gi 219555688    83 DGWSALHIAAFGGHQDIVLYLITK 106
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDK 24
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 58-108 3.55e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 35.41  E-value: 3.55e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 219555688  58 SVIDGNLELVKLLVKFGADIRLANRDGWSALHIAAFG--GHQDIVLYLITKAK 108
Cdd:PHA03100  80 YNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGA 132
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 43-106 5.54e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 35.03  E-value: 5.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219555688  43 NVNSFGPEGQTALHQSV--IDGNLELVKLLVK----------------FGADIRLANRDGWSALHIAAFGGHQDIVLYLI 104
Cdd:PHA03100 133 NVNIKNSDGENLLHLYLesNKIDLKILKLLIDkgvdinaknrvnyllsYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLL 212


                 ..
gi 219555688 105 TK 106
Cdd:PHA03100 213 DL 214
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 34-77 6.21e-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: 34.73  E-value: 6.21e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 219555688  34 LQNMTNCEFNVNSFgpEGQTALHQSVIDGNLELVKLLVKFGADI 77
Cdd:cd22194  126 LDRFINAEYTEEAY--EGQTALNIAIERRQGDIVKLLIAKGADV 167
 
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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