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Conserved domains on  [gi|19112288|ref|NP_595496|]
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MBF transcription factor complex subunit Res1 [Schizosaccharomyces pombe]

Protein Classification

MBP1 family protein( domain architecture ID 13697906)

MBP1 family protein similar to Saccharomyces cerevisiae transcription factor MBP1 that binds to MCB elements (Mlu I cell cycle box) found in the promoter of most DNA synthesis genes

CATH:  1.25.40.20|3.10.260.10
Gene Ontology:  GO:0005515|GO:0043565|GO:0003700
PubMed:  17176038|15152081
SCOP:  4000366|4001103

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
227-397 6.00e-17

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 81.92  E-value: 6.00e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112288 227 WDVNAGIDEDGHTALHWAAAMGNLEMMHALLQAGANVVAVNYLQQTSLMRCVmftMNYDLqtfEVVSELLQSAICMN--D 304
Cdd:COG0666  77 GADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAA---YNGNL---EIVKLLLEAGADVNaqD 150

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112288 305 SFGQTVFHhialLASSKSKMEAARYymdiLLQNltatqSVDVaaqiiNLQDDHGDTALLICARNGAKKCARLLLSFYASS 384
Cdd:COG0666 151 NDGNTPLH----LAAANGNLEIVKL----LLEA-----GADV-----NARDNDGETPLHLAAENGHLEIVKLLLEAGADV 212

                       170
                ....*....|...
gi 19112288 385 SIPNNQGQYPTDF 397
Cdd:COG0666 213 NAKDNDGKTALDL 225
KilA-N pfam04383
KilA-N domain; The amino-terminal module of the D6R/N1R proteins defines a novel, conserved ...
 26-102 2.41e-07

KilA-N domain; The amino-terminal module of the D6R/N1R proteins defines a novel, conserved DNA-binding domain (the KilA-N domain) that is found in a wide range of proteins of large bacterial and eukaryotic DNA viruses. The KilA-N domain family also includes the previously defined APSES domain. The KilA-N and APSES domains may also share a common fold with the nucleic acid-binding modules of the LAGLIDADG nucleases and the amino-terminal domains of the tRNA endonuclease.


:

Pssm-ID: 367917  Cd Length: 107  Bit Score: 49.24  E-value: 2.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112288    26 LMKRCHDNWLNATQILKIAELDKPRRTRILEKFAQKGLHEKIQGGC---------------GKYQGTWVPSERAVELAHE 90
Cdd:pfam04383   9 IIRRDKDGYINATKLCKAAGEKTKRFRNWLRLESTKELIEELEEENnipkiitiigrkgkgGRLQGTYVHPDLALAIASW 88

                          90
                  ....*....|....*...
gi 19112288    91 ------YNVFDLIQPLIE 102
Cdd:pfam04383  89 ispefaLKVSKIIDEYKS 106
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
227-397 6.00e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 81.92  E-value: 6.00e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112288 227 WDVNAGIDEDGHTALHWAAAMGNLEMMHALLQAGANVVAVNYLQQTSLMRCVmftMNYDLqtfEVVSELLQSAICMN--D 304
Cdd:COG0666  77 GADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAA---YNGNL---EIVKLLLEAGADVNaqD 150

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112288 305 SFGQTVFHhialLASSKSKMEAARYymdiLLQNltatqSVDVaaqiiNLQDDHGDTALLICARNGAKKCARLLLSFYASS 384
Cdd:COG0666 151 NDGNTPLH----LAAANGNLEIVKL----LLEA-----GADV-----NARDNDGETPLHLAAENGHLEIVKLLLEAGADV 212

                       170
                ....*....|...
gi 19112288 385 SIPNNQGQYPTDF 397
Cdd:COG0666 213 NAKDNDGKTALDL 225
KilA-N pfam04383
KilA-N domain; The amino-terminal module of the D6R/N1R proteins defines a novel, conserved ...
 26-102 2.41e-07

KilA-N domain; The amino-terminal module of the D6R/N1R proteins defines a novel, conserved DNA-binding domain (the KilA-N domain) that is found in a wide range of proteins of large bacterial and eukaryotic DNA viruses. The KilA-N domain family also includes the previously defined APSES domain. The KilA-N and APSES domains may also share a common fold with the nucleic acid-binding modules of the LAGLIDADG nucleases and the amino-terminal domains of the tRNA endonuclease.


Pssm-ID: 367917  Cd Length: 107  Bit Score: 49.24  E-value: 2.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112288    26 LMKRCHDNWLNATQILKIAELDKPRRTRILEKFAQKGLHEKIQGGC---------------GKYQGTWVPSERAVELAHE 90
Cdd:pfam04383   9 IIRRDKDGYINATKLCKAAGEKTKRFRNWLRLESTKELIEELEEENnipkiitiigrkgkgGRLQGTYVHPDLALAIASW 88

                          90
                  ....*....|....*...
gi 19112288    91 ------YNVFDLIQPLIE 102
Cdd:pfam04383  89 ispefaLKVSKIIDEYKS 106
Ank_2 pfam12796
Ankyrin repeats (3 copies);
241-329 2.87e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 45.88  E-value: 2.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112288   241 LHWAAAMGNLEMMHALLQAGANVVAVNYLQQTSLMRCVMFtmnydlQTFEVVSELLQSAICMNDSFGQTVFHHiallASS 320
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKN------GHLEIVKLLLEHADVNLKDNGRTALHY----AAR 70


                  ....*....
gi 19112288   321 KSKMEAARY 329
Cdd:pfam12796  71 SGHLEIVKL 79
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 236-263 5.39e-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: 43.35  E-value: 5.39e-06
                           10        20
                   ....*....|....*....|....*...
gi 19112288    236 DGHTALHWAAAMGNLEMMHALLQAGANV 263
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
PHA03095 PHA03095
ankyrin-like protein; Provisional
 228-394 1.73e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 41.16  E-value: 1.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112288  228 DVNAGiDEDGHTALHwaAAMGNLE----MMHALLQAGANVVAVNYLQQTSLMRCVMFTmNYDLqtfEVVsELLQSAICM- 302
Cdd:PHA03095 109 DVNAK-DKVGRTPLH--VYLSGFNinpkVIRLLLRKGADVNALDLYGMTPLAVLLKSR-NANV---ELL-RLLIDAGADv 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112288  303 --NDSFGQTVFHHIAllasskskmEAARYYMDILLQNLTAtqSVDVAAqiinlQDDHGDTALLICARNGAkkCARLLLSF 380
Cdd:PHA03095 181 yaVDDRFRSLLHHHL---------QSFKPRARIVRELIRA--GCDPAA-----TDMLGNTPLHSMATGSS--CKRSLVLP 242

                        170
                 ....*....|....*...
gi 19112288  381 Y----ASSSIPNNQGQYP 394
Cdd:PHA03095 243 LliagISINARNRYGQTP 260
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 237-378 8.49e-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: 39.29  E-value: 8.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112288   237 GHTALHWAAAMGNLEMMHALLQAGANVVAV---NYLQQTSLMRCVMFT---MNYD--LQTFEVVSELLQ--SAICMNDSF 306
Cdd:TIGR00870 128 GITALHLAAHRQNYEIVKLLLERGASVPARacgDFFVKSQGVDSFYHGespLNAAacLGSPSIVALLSEdpADILTADSL 207

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19112288   307 GQTVFHHIALLASSKSKMEAARYYM-DILLQNLTATQSVDVAAQIINLQddhGDTALLICARNGAKKCARLLL 378
Cdd:TIGR00870 208 GNTLLHLLVMENEFKAEYEELSCQMyNFALSLLDKLRDSKELEVILNHQ---GLTPLKLAAKEGRIVLFRLKL 277
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
227-397 6.00e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 81.92  E-value: 6.00e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112288 227 WDVNAGIDEDGHTALHWAAAMGNLEMMHALLQAGANVVAVNYLQQTSLMRCVmftMNYDLqtfEVVSELLQSAICMN--D 304
Cdd:COG0666  77 GADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAA---YNGNL---EIVKLLLEAGADVNaqD 150

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112288 305 SFGQTVFHhialLASSKSKMEAARYymdiLLQNltatqSVDVaaqiiNLQDDHGDTALLICARNGAKKCARLLLSFYASS 384
Cdd:COG0666 151 NDGNTPLH----LAAANGNLEIVKL----LLEA-----GADV-----NARDNDGETPLHLAAENGHLEIVKLLLEAGADV 212

                       170
                ....*....|...
gi 19112288 385 SIPNNQGQYPTDF 397
Cdd:COG0666 213 NAKDNDGKTALDL 225
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
228-426 1.04e-15

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 78.07  E-value: 1.04e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112288 228 DVNAgIDEDGHTALHWAAAMGNLEMMHALLQAGANVVAVNYLQQTSLMRCVmftMNYDLqtfEVVSELLQSAICMN--DS 305
Cdd:COG0666 112 DVNA-RDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA---ANGNL---EIVKLLLEAGADVNarDN 184

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112288 306 FGQTVFHhialLASSKSKMEAARYymdiLLQNltatqSVDVaaqiiNLQDDHGDTALLICARNGAKKCARLLLSFYASSS 385
Cdd:COG0666 185 DGETPLH----LAAENGHLEIVKL----LLEA-----GADV-----NAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN 246

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 19112288 386 IPNNQGQYPTDFLSSKDMSFPENDDSPLNSKIEDNLIDNLK 426
Cdd:COG0666 247 AKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
KilA-N pfam04383
KilA-N domain; The amino-terminal module of the D6R/N1R proteins defines a novel, conserved ...
 26-102 2.41e-07

KilA-N domain; The amino-terminal module of the D6R/N1R proteins defines a novel, conserved DNA-binding domain (the KilA-N domain) that is found in a wide range of proteins of large bacterial and eukaryotic DNA viruses. The KilA-N domain family also includes the previously defined APSES domain. The KilA-N and APSES domains may also share a common fold with the nucleic acid-binding modules of the LAGLIDADG nucleases and the amino-terminal domains of the tRNA endonuclease.


Pssm-ID: 367917  Cd Length: 107  Bit Score: 49.24  E-value: 2.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112288    26 LMKRCHDNWLNATQILKIAELDKPRRTRILEKFAQKGLHEKIQGGC---------------GKYQGTWVPSERAVELAHE 90
Cdd:pfam04383   9 IIRRDKDGYINATKLCKAAGEKTKRFRNWLRLESTKELIEELEEENnipkiitiigrkgkgGRLQGTYVHPDLALAIASW 88

                          90
                  ....*....|....*...
gi 19112288    91 ------YNVFDLIQPLIE 102
Cdd:pfam04383  89 ispefaLKVSKIIDEYKS 106
Ank_2 pfam12796
Ankyrin repeats (3 copies);
241-329 2.87e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 45.88  E-value: 2.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112288   241 LHWAAAMGNLEMMHALLQAGANVVAVNYLQQTSLMRCVMFtmnydlQTFEVVSELLQSAICMNDSFGQTVFHHiallASS 320
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKN------GHLEIVKLLLEHADVNLKDNGRTALHY----AAR 70


                  ....*....
gi 19112288   321 KSKMEAARY 329
Cdd:pfam12796  71 SGHLEIVKL 79
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 236-267 2.99e-06

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 44.20  E-value: 2.99e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 19112288   236 DGHTALHWAAAM-GNLEMMHALLQAGANVVAVN 267
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 236-263 5.39e-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: 43.35  E-value: 5.39e-06
                           10        20
                   ....*....|....*....|....*...
gi 19112288    236 DGHTALHWAAAMGNLEMMHALLQAGANV 263
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
Ank_4 pfam13637
Ankyrin repeats (many copies);
237-280 5.50e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.80  E-value: 5.50e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 19112288   237 GHTALHWAAAMGNLEMMHALLQAGANVVAVNYLQQTSLMRCVMF 280
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASN 44
Ank_2 pfam12796
Ankyrin repeats (3 copies);
229-267 3.14e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 42.80  E-value: 3.14e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 19112288   229 VNAGIDEDGHTALHWAAAMGNLEMMHALLQAGANVVAVN 267
Cdd:pfam12796  53 ADVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 236-263 7.05e-05

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 39.93  E-value: 7.05e-05
                          10        20
                  ....*....|....*....|....*...
gi 19112288   236 DGHTALHWAAAMGNLEMMHALLQAGANV 263
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADI 28
Ank_2 pfam12796
Ankyrin repeats (3 copies);
234-303 2.20e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 40.48  E-value: 2.20e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112288   234 DEDGHTALHWAAAMGNLEMMHALLQAGAnvVAVNYLQQTSLMRCVMftMNYdlqtFEVVSELLQSAICMN 303
Cdd:pfam12796  27 DKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAAR--SGH----LEIVKLLLEKGADIN 88
PHA03095 PHA03095
ankyrin-like protein; Provisional
 228-394 1.73e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 41.16  E-value: 1.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112288  228 DVNAGiDEDGHTALHwaAAMGNLE----MMHALLQAGANVVAVNYLQQTSLMRCVMFTmNYDLqtfEVVsELLQSAICM- 302
Cdd:PHA03095 109 DVNAK-DKVGRTPLH--VYLSGFNinpkVIRLLLRKGADVNALDLYGMTPLAVLLKSR-NANV---ELL-RLLIDAGADv 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112288  303 --NDSFGQTVFHHIAllasskskmEAARYYMDILLQNLTAtqSVDVAAqiinlQDDHGDTALLICARNGAkkCARLLLSF 380
Cdd:PHA03095 181 yaVDDRFRSLLHHHL---------QSFKPRARIVRELIRA--GCDPAA-----TDMLGNTPLHSMATGSS--CKRSLVLP 242

                        170
                 ....*....|....*...
gi 19112288  381 Y----ASSSIPNNQGQYP 394
Cdd:PHA03095 243 LliagISINARNRYGQTP 260
Ank_4 pfam13637
Ankyrin repeats (many copies);
227-257 8.48e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 34.94  E-value: 8.48e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 19112288   227 WDVNAgIDEDGHTALHWAAAMGNLEMMHALL 257
Cdd:pfam13637  25 ADINA-VDGNGETALHFAASNGNVEVLKLLL 54
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 237-378 8.49e-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: 39.29  E-value: 8.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112288   237 GHTALHWAAAMGNLEMMHALLQAGANVVAV---NYLQQTSLMRCVMFT---MNYD--LQTFEVVSELLQ--SAICMNDSF 306
Cdd:TIGR00870 128 GITALHLAAHRQNYEIVKLLLERGASVPARacgDFFVKSQGVDSFYHGespLNAAacLGSPSIVALLSEdpADILTADSL 207

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19112288   307 GQTVFHHIALLASSKSKMEAARYYM-DILLQNLTATQSVDVAAQIINLQddhGDTALLICARNGAKKCARLLL 378
Cdd:TIGR00870 208 GNTLLHLLVMENEFKAEYEELSCQMyNFALSLLDKLRDSKELEVILNHQ---GLTPLKLAAKEGRIVLFRLKL 277
 
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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