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Conserved domains on  [gi|380495489|emb|CCF32354|]
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hypothetical protein CH063_04758 [Colletotrichum higginsianum]

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];
47-167 1.08e-17

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 78.84  E-value: 1.08e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380495489  47 AKDEGKSTCLHMAAGNGHIDIVKALIaaldarpadEKKAYVDAANEFGNTGLHWACLGGHLEVVKVLMAHGASPAAANDK 126
Cdd:COG0666  148 AQDNDGNTPLHLAAANGNLEIVKLLL---------EAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDND 218

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 380495489 127 DQIPLDSALFNGKREVADWFLAQSETMEGGNREDGLSGAAA 167
Cdd:COG0666  219 GKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLA 259
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
47-167 1.08e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 78.84  E-value: 1.08e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380495489  47 AKDEGKSTCLHMAAGNGHIDIVKALIaaldarpadEKKAYVDAANEFGNTGLHWACLGGHLEVVKVLMAHGASPAAANDK 126
Cdd:COG0666  148 AQDNDGNTPLHLAAANGNLEIVKLLL---------EAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDND 218

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 380495489 127 DQIPLDSALFNGKREVADWFLAQSETMEGGNREDGLSGAAA 167
Cdd:COG0666  219 GKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLA 259
Ank_2 pfam12796
Ankyrin repeats (3 copies);
56-147 1.54e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 63.21  E-value: 1.54e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380495489   56 LHMAAGNGHIDIVKALIaaldarpadEKKAYVDAANEFGNTGLHWACLGGHLEVVKVLMAHGAspAAANDKDQIPLDSAL 135
Cdd:pfam12796   1 LHLAAKNGNLELVKLLL---------ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAA 69

                          90
                  ....*....|..
gi 380495489  136 FNGKREVADWFL 147
Cdd:pfam12796  70 RSGHLEIVKLLL 81
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 21-170 5.94e-11

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 60.68  E-value: 5.94e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380495489  21 ELAELQETLKTLSERENASVGEVITAAKDEG-KSTCLHMAAgnghIDIVKaLIAALDA---RPADEKKAYVDAANEFGNT 96
Cdd:PTZ00322  43 EIARIDTHLEALEATENKDATPDHNLTTEEViDPVVAHMLT----VELCQ-LAASGDAvgaRILLTGGADPNCRDYDGRT 117

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 380495489  97 GLHWACLGGHLEVVKVLMAHGASPAAANDKDQIPLDSALFNGKREVADWFLAQS-ETMEGGNRE--DGLSGAAAGVE 170
Cdd:PTZ00322 118 PLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSqCHFELGANAkpDSFTGKPPSLE 194
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 94-120 2.72e-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: 39.49  E-value: 2.72e-05
                           10        20
                   ....*....|....*....|....*..
gi 380495489    94 GNTGLHWACLGGHLEVVKVLMAHGASP 120
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADI 28
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 40-122 4.48e-04

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: 40.38  E-value: 4.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380495489  40 VGEVITAAKDEGKsTCLHMAAGNGHIDIVKALIaaldARPADEKKAYV---------DAANEFGNTGLHWACLGGHLEVV 110
Cdd:cd22192   78 VNEPMTSDLYQGE-TALHIAVVNQNLNLVRELI----ARGADVVSPRAtgtffrpgpKNLIYYGEHPLSFAACVGNEEIV 152

                         90
                 ....*....|..
gi 380495489 111 KVLMAHGASPAA 122
Cdd:cd22192  153 RLLIEHGADIRA 164
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 13-124 5.58e-04

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: 40.06  E-value: 5.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380495489   13 LIYLSRAGELAELQETLKTLSERenASVGEvitaakdegksTCLHmAAGNGHIDIVKALIAALDARPADEKK---AYVDA 89
Cdd:TIGR00870  56 LFVAAIENENLELTELLLNLSCR--GAVGD-----------TLLH-AISLEYVDAVEAILLHLLAAFRKSGPlelANDQY 121

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 380495489   90 ANEF--GNTGLHWACLGGHLEVVKVLMAHGAS-PAAAN 124
Cdd:TIGR00870 122 TSEFtpGITALHLAAHRQNYEIVKLLLERGASvPARAC 159
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
47-167 1.08e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 78.84  E-value: 1.08e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380495489  47 AKDEGKSTCLHMAAGNGHIDIVKALIaaldarpadEKKAYVDAANEFGNTGLHWACLGGHLEVVKVLMAHGASPAAANDK 126
Cdd:COG0666  148 AQDNDGNTPLHLAAANGNLEIVKLLL---------EAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDND 218

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 380495489 127 DQIPLDSALFNGKREVADWFLAQSETMEGGNREDGLSGAAA 167
Cdd:COG0666  219 GKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLA 259
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
47-149 1.50e-16

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 75.76  E-value: 1.50e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380495489  47 AKDEGKSTCLHMAAGNGHIDIVKALIaaldarpadEKKAYVDAANEFGNTGLHWACLGGHLEVVKVLMAHGASPAAANDK 126
Cdd:COG0666  115 ARDKDGETPLHLAAYNGNLEIVKLLL---------EAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDND 185

                         90       100
                 ....*....|....*....|...
gi 380495489 127 DQIPLDSALFNGKREVADWFLAQ 149
Cdd:COG0666  186 GETPLHLAAENGHLEIVKLLLEA 208
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
41-149 1.28e-14

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 70.37  E-value: 1.28e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380495489  41 GEVITAAKDEGKSTCLHMAAGNGHIDIVKALIaaldarpadEKKAYVDAANEFGNTGLHWACLGGHLEVVKVLMAHGASP 120
Cdd:COG0666   76 AGADINAKDDGGNTLLHAAARNGDLEIVKLLL---------EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADV 146

                         90       100
                 ....*....|....*....|....*....
gi 380495489 121 AAANDKDQIPLDSALFNGKREVADWFLAQ 149
Cdd:COG0666  147 NAQDNDGNTPLHLAAANGNLEIVKLLLEA 175
Ank_2 pfam12796
Ankyrin repeats (3 copies);
56-147 1.54e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 63.21  E-value: 1.54e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380495489   56 LHMAAGNGHIDIVKALIaaldarpadEKKAYVDAANEFGNTGLHWACLGGHLEVVKVLMAHGAspAAANDKDQIPLDSAL 135
Cdd:pfam12796   1 LHLAAKNGNLELVKLLL---------ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAA 69

                          90
                  ....*....|..
gi 380495489  136 FNGKREVADWFL 147
Cdd:pfam12796  70 RSGHLEIVKLLL 81
Ank_2 pfam12796
Ankyrin repeats (3 copies);
48-127 7.64e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 58.97  E-value: 7.64e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380495489   48 KDEGKSTCLHMAAGNGHIDIVKALIAALDARPADEkkayvdaanefGNTGLHWACLGGHLEVVKVLMAHGASPaaaNDKD 127
Cdd:pfam12796  26 QDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN-----------GRTALHYAARSGHLEIVKLLLEKGADI---NVKD 91
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 21-170 5.94e-11

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 60.68  E-value: 5.94e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380495489  21 ELAELQETLKTLSERENASVGEVITAAKDEG-KSTCLHMAAgnghIDIVKaLIAALDA---RPADEKKAYVDAANEFGNT 96
Cdd:PTZ00322  43 EIARIDTHLEALEATENKDATPDHNLTTEEViDPVVAHMLT----VELCQ-LAASGDAvgaRILLTGGADPNCRDYDGRT 117

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 380495489  97 GLHWACLGGHLEVVKVLMAHGASPAAANDKDQIPLDSALFNGKREVADWFLAQS-ETMEGGNRE--DGLSGAAAGVE 170
Cdd:PTZ00322 118 PLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSqCHFELGANAkpDSFTGKPPSLE 194
Ank_4 pfam13637
Ankyrin repeats (many copies);
53-113 3.99e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.05  E-value: 3.99e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 380495489   53 STCLHMAAGNGHIDIVKALIaaldarpadEKKAYVDAANEFGNTGLHWACLGGHLEVVKVL 113
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLL---------EKGADINAVDGNGETALHFAASNGNVEVLKLL 53
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
47-148 9.59e-10

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 56.50  E-value: 9.59e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380495489  47 AKDEGKSTCLHMAAGNGHIDIVKALIaaldarpadEKKAYVDAANEFGNTGLHWACLGGHLEVVKVLMAHGASPAAANDK 126
Cdd:COG0666  181 ARDNDGETPLHLAAENGHLEIVKLLL---------EAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKD 251

                         90       100
                 ....*....|....*....|..
gi 380495489 127 DQIPLDSALFNGKREVADWFLA 148
Cdd:COG0666  252 GLTALLLAAAAGAALIVKLLLL 273
Ank_4 pfam13637
Ankyrin repeats (many copies);
94-147 4.20e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.35  E-value: 4.20e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 380495489   94 GNTGLHWACLGGHLEVVKVLMAHGASPAAANDKDQIPLDSALFNGKREVADWFL 147
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-148 7.45e-08

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 51.11  E-value: 7.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380495489   1 MAPKLSEEEIDDLIYLSRAGELAELQETLKTLSERENASVGEVITAAKDEGKSTCLHMAAGNGHIDIVKALIAAldarpa 80
Cdd:COG0666    3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAA------ 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 380495489  81 dekKAYVDAANEFGNTGLHWACLGGHLEVVKVLMAHGASPAAANDKDQIPLDSALFNGKREVADWFLA 148
Cdd:COG0666   77 ---GADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLE 141
Ank_5 pfam13857
Ankyrin repeats (many copies);
75-134 1.36e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.18  E-value: 1.36e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 380495489   75 LDARPADekkayVDAANEFGNTGLHWACLGGHLEVVKVLMAHGASPAAANDKDQIPLDSA 134
Cdd:pfam13857   2 LEHGPID-----LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 47-119 1.65e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 44.27  E-value: 1.65e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 380495489  47 AKDEGKSTCLHMAAGNGHIDIVKALIaaldarpadEKKAYVDAANEFGNTGLHWACLGGHLEVVKVLMAHGAS 119
Cdd:PHA03100 187 IKDVYGFTPLHYAVYNNNPEFVKYLL---------DLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
PHA03095 PHA03095
ankyrin-like protein; Provisional
 47-132 1.98e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 44.25  E-value: 1.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380495489  47 AKDEGKSTCLHMAAGNGH-IDIVKALIaaldarpadEKKAYVDAANEFGNTGLHwACLGG---HLEVVKVLMAHGASPAA 122
Cdd:PHA03095  78 APERCGFTPLHLYLYNATtLDVIKLLI---------KAGADVNAKDKVGRTPLH-VYLSGfniNPKVIRLLLRKGADVNA 147

                         90
                 ....*....|
gi 380495489 123 ANDKDQIPLD 132
Cdd:PHA03095 148 LDLYGMTPLA 157
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 94-120 2.72e-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: 39.49  E-value: 2.72e-05
                           10        20
                   ....*....|....*....|....*..
gi 380495489    94 GNTGLHWACLGGHLEVVKVLMAHGASP 120
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADI 28
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 93-122 1.11e-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: 38.01  E-value: 1.11e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 380495489   93 FGNTGLHWACLGGHLEVVKVLMAHGASPAA 122
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 94-125 1.22e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.04  E-value: 1.22e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 380495489   94 GNTGLHWACL-GGHLEVVKVLMAHGASPAAAND 125
Cdd:pfam00023   2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 40-122 4.48e-04

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: 40.38  E-value: 4.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380495489  40 VGEVITAAKDEGKsTCLHMAAGNGHIDIVKALIaaldARPADEKKAYV---------DAANEFGNTGLHWACLGGHLEVV 110
Cdd:cd22192   78 VNEPMTSDLYQGE-TALHIAVVNQNLNLVRELI----ARGADVVSPRAtgtffrpgpKNLIYYGEHPLSFAACVGNEEIV 152

                         90
                 ....*....|..
gi 380495489 111 KVLMAHGASPAA 122
Cdd:cd22192  153 RLLIEHGADIRA 164
Ank_2 pfam12796
Ankyrin repeats (3 copies);
98-149 5.08e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 37.79  E-value: 5.08e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 380495489   98 LHWACLGGHLEVVKVLMAHGASPAAANDKDQIPLDSALFNGKREVADWFLAQ 149
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH 52
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 13-124 5.58e-04

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: 40.06  E-value: 5.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380495489   13 LIYLSRAGELAELQETLKTLSERenASVGEvitaakdegksTCLHmAAGNGHIDIVKALIAALDARPADEKK---AYVDA 89
Cdd:TIGR00870  56 LFVAAIENENLELTELLLNLSCR--GAVGD-----------TLLH-AISLEYVDAVEAILLHLLAAFRKSGPlelANDQY 121

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 380495489   90 ANEF--GNTGLHWACLGGHLEVVKVLMAHGAS-PAAAN 124
Cdd:TIGR00870 122 TSEFtpGITALHLAAHRQNYEIVKLLLERGASvPARAC 159
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 21-123 5.74e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 39.86  E-value: 5.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380495489  21 ELAELQETLK---TLSERENASVGEvitaakdegksTCLHMAAGNGHIDIVKALIAALD-ARPADEKKAYVDAA--NEF- 93
Cdd:cd21882    3 ELLGLLECLRwylTDSAYQRGATGK-----------TCLHKAALNLNDGVNEAIMLLLEaAPDSGNPKELVNAPctDEFy 71

                         90       100       110
                 ....*....|....*....|....*....|.
gi 380495489  94 -GNTGLHWACLGGHLEVVKVLMAHGASPAAA 123
Cdd:cd21882   72 qGQTALHIAIENRNLNLVRLLVENGADVSAR 102
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 48-142 6.07e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 39.56  E-value: 6.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380495489  48 KDEGKSTCLHMAAGNGHIDIVKALIaaldarpadEKKAYVDAANEFGNTGLHWACLGGHLEVVKVLMAHGASPAAANDKD 127
Cdd:PHA02874 153 EDDNGCYPIHIAIKHNFFDIIKLLL---------EKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNG 223

                         90
                 ....*....|....*
gi 380495489 128 QIPLDSALFNGKREV 142
Cdd:PHA02874 224 FTPLHNAIIHNRSAI 238
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 54-135 7.84e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 39.66  E-value: 7.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380495489  54 TCLHMA-AGNGHIDIVKALIaaldarpadEKKAYVDAANEFGNTGLHWACLGG-HLEVVKVLMAHGASPAAANDKDQIPL 131
Cdd:PHA02876 410 TALHFAlCGTNPYMSVKTLI---------DRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPL 480


                 ....
gi 380495489 132 DSAL 135
Cdd:PHA02876 481 LIAL 484
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 56-137 8.19e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 39.26  E-value: 8.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380495489  56 LHMAAGNGHID--IVKALIaaldarpadEKKAYVDAAN----------------EFGNTGLHWACLGGHLEVVKVLMAHG 117
Cdd:PHA03100 145 LHLYLESNKIDlkILKLLI---------DKGVDINAKNrvnyllsygvpinikdVYGFTPLHYAVYNNNPEFVKYLLDLG 215

                         90       100
                 ....*....|....*....|
gi 380495489 118 ASPAAANDKDQIPLDSALFN 137
Cdd:PHA03100 216 ANPNLVNKYGDTPLHIAILN 235
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 49-135 1.68e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 38.32  E-value: 1.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380495489  49 DEGKSTCLHMAAGNGHIDIVKALIaaldarpadEKKAYVDAANEFGNTGLHWA---CLggHLEVVKVLMAHGASpaaAND 125
Cdd:PHA02878 198 DKTNNSPLHHAVKHYNKPIVHILL---------ENGASTDARDKCGNTPLHISvgyCK--DYDILKLLLEHGVD---VNA 263

                         90
                 ....*....|....
gi 380495489 126 KDQI----PLDSAL 135
Cdd:PHA02878 264 KSYIlgltALHSSI 277
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 54-72 1.82e-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: 34.49  E-value: 1.82e-03
                           10
                   ....*....|....*....
gi 380495489    54 TCLHMAAGNGHIDIVKALI 72
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLL 22
PHA03095 PHA03095
ankyrin-like protein; Provisional
 35-149 2.27e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 38.08  E-value: 2.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380495489  35 RENASVGeVITAAKDEGKSTCLHMAAGNG---HIDIVKALIAALDarpadekkayVDAANEFGNTGLHWACLGGHLEVVK 111
Cdd:PHA03095 206 RELIRAG-CDPAATDMLGNTPLHSMATGSsckRSLVLPLLIAGIS----------INARNRYGQTPLHYAAVFNNPRACR 274

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 380495489 112 VLMAHGASPAAANDKDQIPLDSALFNGKREVADWFLAQ 149
Cdd:PHA03095 275 RLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAK 312
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 54-72 9.94e-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.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 32.61  E-value: 9.94e-03
                          10
                  ....*....|....*....
gi 380495489   54 TCLHMAAGNGHIDIVKALI 72
Cdd:pfam13606   4 TPLHLAARNGRLEIVKLLL 22
 
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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