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Conserved domains on  [gi|568978556|ref|XP_006515412|]
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60 kDa lysophospholipase isoform X3 [Mus musculus]

Protein Classification

L-asparaginase family protein( domain architecture ID 13049359)

L-asparaginase family protein containing ankyrin (ANK) repeats, may catalyze the deamination of asparagine to yield aspartic acid and ammonium

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
L-asparaginase_like super family cl00216
Bacterial L-asparaginases and related enzymes; Asparaginases (amidohydrolases, E.C. 3.5.1.1) ...
 2-199 2.07e-72

Bacterial L-asparaginases and related enzymes; Asparaginases (amidohydrolases, E.C. 3.5.1.1) are dimeric or tetrameric enzymes that catalyze the hydrolysis of asparagine to aspartic acid and ammonia. In bacteria, there are two classes of amidohydrolases, one highly specific for asparagine and localized to the periplasm (type II L-asparaginase), and a second (asparaginase- glutaminase) present in the cytosol (type I L-asparaginase) that hydrolyzes both asparagine and glutamine with similar specificities and has a lower affinity for its substrate. Bacterial L-asparaginases (type II) are potent antileukemic agents and have been used in the treatment of acute lymphoblastic leukemia (ALL). A conserved threonine residue is thought to supply the nucleophile hydroxy-group that attacks the amide bond. Many bacterial L-asparaginases have both L-asparagine and L-glutamine hydrolysis activities, to a different degree, and some of them are annotated as asparaginase/glutaminase. This wider family also includes a subunit of an archaeal Glu-tRNA amidotransferase.


The actual alignment was detected with superfamily member PRK09461:

Pssm-ID: 469665 [Multi-domain]  Cd Length: 335  Bit Score: 229.86  E-value: 2.07e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978556   2 AGQYVIPEVCLFFQNQLFRGNRTTKVDARRFAAFCSPNLPPLATVGADVTINRELVRKACGKShLVVHSSMEPDVGLLRL 81
Cdd:PRK09461 139 AANYPINEVTLFFNNKLFRGNRTTKAHADGFDAFASPNLPPLLEAGIHIRRLNTPPAPHGEGE-LIVHPITPQPIGVVTI 217

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978556  82 YPGIPASLVRTFLQPPLKGVVMETFGSGNGPTKPDLLQELRVAAEQGLIIVNCTHCLQGAVT-SDYASGMAMAGAGIVSG 160
Cdd:PRK09461 218 YPGISAEVVRNFLRQPVKALILRSYGVGNAPQNPALLQELKEASERGIVVVNLTQCMSGKVNmGGYATGNALAHAGVISG 297

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 568978556 161 FDMTSEAALAKLSYVLGQPgLSLNDRKKLLAKDLRGEMT 199
Cdd:PRK09461 298 ADMTVEAALTKLHYLLSQE-LSTEEIRQAMQQNLRGELT 335
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
250-389 2.61e-23

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 98.87  E-value: 2.61e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978556 250 DTLQAFVELDRDLNLKDYSGQTPLHVAARRGHAAVVTMLLQRGADVDARNEDGQSPLLLAVRGRHQSVIGLLRAAGARLS 329
Cdd:COG0666  101 EIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVN 180

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978556 330 PQELEDvGTELCRLASRGDSEGLRAWWQAGADLGQPDYDGHCALQVAEAAGNADVVALLQ 389
Cdd:COG0666  181 ARDNDG-ETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239
 
Name Accession Description Interval E-value
ansA PRK09461
cytoplasmic asparaginase I; Provisional
 2-199 2.07e-72

cytoplasmic asparaginase I; Provisional


Pssm-ID: 181876 [Multi-domain]  Cd Length: 335  Bit Score: 229.86  E-value: 2.07e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978556   2 AGQYVIPEVCLFFQNQLFRGNRTTKVDARRFAAFCSPNLPPLATVGADVTINRELVRKACGKShLVVHSSMEPDVGLLRL 81
Cdd:PRK09461 139 AANYPINEVTLFFNNKLFRGNRTTKAHADGFDAFASPNLPPLLEAGIHIRRLNTPPAPHGEGE-LIVHPITPQPIGVVTI 217

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978556  82 YPGIPASLVRTFLQPPLKGVVMETFGSGNGPTKPDLLQELRVAAEQGLIIVNCTHCLQGAVT-SDYASGMAMAGAGIVSG 160
Cdd:PRK09461 218 YPGISAEVVRNFLRQPVKALILRSYGVGNAPQNPALLQELKEASERGIVVVNLTQCMSGKVNmGGYATGNALAHAGVISG 297

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 568978556 161 FDMTSEAALAKLSYVLGQPgLSLNDRKKLLAKDLRGEMT 199
Cdd:PRK09461 298 ADMTVEAALTKLHYLLSQE-LSTEEIRQAMQQNLRGELT 335
AnsA COG0252
L-asparaginase/archaeal Glu-tRNAGln amidotransferase subunit D [Translation, ribosomal ...
 2-192 1.13e-57

L-asparaginase/archaeal Glu-tRNAGln amidotransferase subunit D [Translation, ribosomal structure and biogenesis, Amino acid transport and metabolism];


Pssm-ID: 440022 [Multi-domain]  Cd Length: 325  Bit Score: 191.50  E-value: 1.13e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978556   2 AGQYVIPEVCLFFQNQLFRGNRTTKVDARRFAAFCSPNLPPLATVGAD-VTINRELVRKacGKSHLVVHSSMEPDVGLLR 80
Cdd:COG0252  139 SPEARGRGVLVVFNDEIHRARRVTKTHTSRVDAFQSPNYGPLGEVDEGrVRFYRRPPRR--PESELDLAPALLPRVAILK 216

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978556  81 LYPGIPASLVRTFLQPPLKGVVMETFGSGNGPtkPDLLQELRVAAEQGLIIVNCTHCLQGAVTSDYASGMAMAGAGIVSG 160
Cdd:COG0252  217 LYPGMDPALLDALLAAGVKGIVLEGTGAGNVP--PALLPALKRAIERGVPVVVTSRCPEGRVNGVYGGGRDLAEAGVISG 294

                        170       180       190
                 ....*....|....*....|....*....|..
gi 568978556 161 FDMTSEAALAKLSYVLGQpGLSLNDRKKLLAK 192
Cdd:COG0252  295 GDLTPEKARIKLMLALGQ-GLDPEEIRRLFET 325
Asparaginase smart00870
Asparaginase, found in various plant, animal and bacterial cells; Asparaginase catalyses the ...
 2-187 1.12e-53

Asparaginase, found in various plant, animal and bacterial cells; Asparaginase catalyses the deamination of asparagine to yield aspartic acid and an ammonium ion, resulting in a depletion of free circulatory asparagine in plasma. The enzyme is effective in the treatment of human malignant lymphomas, which have a diminished capacity to produce asparagine synthetase: in order to survive, such cells absorb asparagine from blood plasma..- if Asn levels have been depleted by injection of asparaginase, the lymphoma cells die.


Pssm-ID: 214873 [Multi-domain]  Cd Length: 323  Bit Score: 180.79  E-value: 1.12e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978556     2 AGQYVIPEVCLFFQNQLFRGNRTTKVDARRFAAFCSPNLPPLATVGADVTINRELVRKACGKS---HLVVHSSMEPDVGL 78
Cdd:smart00870 137 SPEARGRGVLVVFNDEIHRARRVTKTHTSRVDAFQSPNFGPLGYVDEGGVVYYTRPTRRHTKRspfLLDLKDALLPKVAI 216

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978556    79 LRLYPGIPASLVRTFLQPPLKGVVMETFGSGNGPtkPDLLQELRVAAEQGLIIVNCTHCLQGAVT-SDYASGMAMAGAGI 157
Cdd:smart00870 217 VKAYPGMDAELLDALLDSGAKGLVLEGTGAGNVP--PDLLEALKEALERGIPVVRTSRCLSGRVDpGYYATGRDLAKAGV 294

                          170       180       190
                   ....*....|....*....|....*....|
gi 568978556   158 VSGFDMTSEAALAKLSYVLGQpGLSLNDRK 187
Cdd:smart00870 295 ISAGDLTPEKARIKLMLALGK-GLDPEEIR 323
L-asparaginase_I cd08963
Type I (cytosolic) bacterial L-asparaginase; Asparaginases (amidohydrolases, E.C. 3.5.1.1) are ...
 1-179 1.06e-48

Type I (cytosolic) bacterial L-asparaginase; Asparaginases (amidohydrolases, E.C. 3.5.1.1) are enzymes that catalyze the hydrolysis of asparagine to aspartic acid and ammonia. In bacteria, there are two classes of amidohydrolases. This model represents type I L-asparaginases, which are highly specific for asparagine and localized in the cytosol. Type I L-asparaginase acts as a dimer. A conserved threonine residue is thought to supply the nucleophile hydroxy-group that attacks the amide bond. Many bacterial L-asparaginases have both L-asparagine and L-glutamine hydrolysis activities, to a different degree, and some of them are annotated as asparaginase/glutaminase. One example of an enzyme with no L-glutaminase activity is the type I L-asparaginase from Wolinella succinogenes.


Pssm-ID: 199207 [Multi-domain]  Cd Length: 316  Bit Score: 167.76  E-value: 1.06e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978556   1 MAGQYVIPEVCLFFQNQLFRGNRTTKVDARRFAAFCSPNLPPLATVGADVTINRELVRKACGKSHLvvHSSMEPDVGLLR 80
Cdd:cd08963  131 AASSGSIRGVYVAFNGKLIRGTRARKVRTTSFDAFESINYPLLAEIGAGGLTLERLLQYEPLPSLF--YPDLDPNVFLLK 208

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978556  81 LYPGIPASLVRTFLQPPLKGVVMETFGSGNGPTKPDLLQELRVAAEQGLIIVNCTHCLQGAV-TSDYASGMAMAGAGIVS 159
Cdd:cd08963  209 LIPGLLPAILDALLEKYPRGLILEGFGAGNIPYDGDLLAALEEATARGKPVVVTTQCPYGGSdLSVYAVGQALLEAGVIP 288

                        170       180
                 ....*....|....*....|
gi 568978556 160 GFDMTSEAALAKLSYVLGQP 179
Cdd:cd08963  289 GGDMTTEAAVAKLMWLLGQT 308
Asparaginase_C pfam17763
Glutaminase/Asparaginase C-terminal domain; This domain is found at the C-terminus of ...
 75-189 1.09e-31

Glutaminase/Asparaginase C-terminal domain; This domain is found at the C-terminus of asparaginase enzymes.


Pssm-ID: 465490 [Multi-domain]  Cd Length: 114  Bit Score: 116.43  E-value: 1.09e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978556   75 DVGLLRLYPGIPASLVRTFLQPPLKGVVMETFGSGNGPtkPDLLQELRVAAEQGLIIVNCTHCLQGAVT-SDYASGMAMA 153
Cdd:pfam17763   1 RVDILYLYPGMDPELLDAALAAGAKGIVIAGFGAGNVP--SALLDALKEAVARGIPVVRSSRCGSGRVNlGYYETGRDLL 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 568978556  154 GAGIVSGFDMTSEAALAKLSYVLGQpGLSLNDRKKL 189
Cdd:pfam17763  79 EAGVISGGDLTPEKARIKLMLALGK-GLDPEEIREL 113
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
250-389 2.61e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 98.87  E-value: 2.61e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978556 250 DTLQAFVELDRDLNLKDYSGQTPLHVAARRGHAAVVTMLLQRGADVDARNEDGQSPLLLAVRGRHQSVIGLLRAAGARLS 329
Cdd:COG0666  101 EIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVN 180

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978556 330 PQELEDvGTELCRLASRGDSEGLRAWWQAGADLGQPDYDGHCALQVAEAAGNADVVALLQ 389
Cdd:COG0666  181 ARDNDG-ETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 211-388 2.70e-18

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 87.23  E-value: 2.70e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978556 211 MLGCRVAWLLSMNGSQEADTMKDVLLPGLALAAAHAGDLDTLQAfvELDRDLNlkDYSGQTPLHVAARRGHAAVVTMLLQ 290
Cdd:PLN03192 504 LHDLNVGDLLGDNGGEHDDPNMASNLLTVASTGNAALLEELLKA--KLDPDIG--DSKGRTPLHIAASKGYEDCVLVLLK 579

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978556 291 RGADVDARNEDGQSPLLLAVRGRHQSVIGLLRAAGARLSPQELEDVgteLCRLASRGDSEGLRAWWQAGADLGQPDYDGH 370
Cdd:PLN03192 580 HACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAGDL---LCTAAKRNDLTAMKELLKQGLNVDSEDHQGA 656

                        170
                 ....*....|....*...
gi 568978556 371 CALQVAEAAGNADVVALL 388
Cdd:PLN03192 657 TALQVAMAEDHVDMVRLL 674
Ank_2 pfam12796
Ankyrin repeats (3 copies);
250-328 2.23e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 57.05  E-value: 2.23e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568978556  250 DTLQAFVELDRDLNLKDYSGQTPLHVAARRGHAAVVTMLLQRgADVDARNeDGQSPLLLAVRGRHQSVIGLLRAAGARL 328
Cdd:pfam12796  11 ELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADI 87
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 269-297 2.00e-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: 43.73  E-value: 2.00e-06
                           10        20
                   ....*....|....*....|....*....
gi 568978556   269 GQTPLHVAARRGHAAVVTMLLQRGADVDA 297
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 250-298 2.62e-05

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 46.34  E-value: 2.62e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978556 250 DTLQAFVEL-DRDLNLKD----------YSGQTPLHVAARRGHAAVVTMLLQRGADVDAR 298
Cdd:cd22196   64 DTISLLLDIaEKTGNLKEfvnaaytdsyYKGQTALHIAIERRNMHLVELLVQNGADVHAR 123
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 267-298 2.78e-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: 43.15  E-value: 2.78e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 568978556  267 YSGQTPLHVAARRGHAAVVTMLLQRGADVDAR 298
Cdd:TIGR00870 126 TPGITALHLAAHRQNYEIVKLLLERGASVPAR 157
 
Name Accession Description Interval E-value
ansA PRK09461
cytoplasmic asparaginase I; Provisional
 2-199 2.07e-72

cytoplasmic asparaginase I; Provisional


Pssm-ID: 181876 [Multi-domain]  Cd Length: 335  Bit Score: 229.86  E-value: 2.07e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978556   2 AGQYVIPEVCLFFQNQLFRGNRTTKVDARRFAAFCSPNLPPLATVGADVTINRELVRKACGKShLVVHSSMEPDVGLLRL 81
Cdd:PRK09461 139 AANYPINEVTLFFNNKLFRGNRTTKAHADGFDAFASPNLPPLLEAGIHIRRLNTPPAPHGEGE-LIVHPITPQPIGVVTI 217

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978556  82 YPGIPASLVRTFLQPPLKGVVMETFGSGNGPTKPDLLQELRVAAEQGLIIVNCTHCLQGAVT-SDYASGMAMAGAGIVSG 160
Cdd:PRK09461 218 YPGISAEVVRNFLRQPVKALILRSYGVGNAPQNPALLQELKEASERGIVVVNLTQCMSGKVNmGGYATGNALAHAGVISG 297

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 568978556 161 FDMTSEAALAKLSYVLGQPgLSLNDRKKLLAKDLRGEMT 199
Cdd:PRK09461 298 ADMTVEAALTKLHYLLSQE-LSTEEIRQAMQQNLRGELT 335
AnsA COG0252
L-asparaginase/archaeal Glu-tRNAGln amidotransferase subunit D [Translation, ribosomal ...
 2-192 1.13e-57

L-asparaginase/archaeal Glu-tRNAGln amidotransferase subunit D [Translation, ribosomal structure and biogenesis, Amino acid transport and metabolism];


Pssm-ID: 440022 [Multi-domain]  Cd Length: 325  Bit Score: 191.50  E-value: 1.13e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978556   2 AGQYVIPEVCLFFQNQLFRGNRTTKVDARRFAAFCSPNLPPLATVGAD-VTINRELVRKacGKSHLVVHSSMEPDVGLLR 80
Cdd:COG0252  139 SPEARGRGVLVVFNDEIHRARRVTKTHTSRVDAFQSPNYGPLGEVDEGrVRFYRRPPRR--PESELDLAPALLPRVAILK 216

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978556  81 LYPGIPASLVRTFLQPPLKGVVMETFGSGNGPtkPDLLQELRVAAEQGLIIVNCTHCLQGAVTSDYASGMAMAGAGIVSG 160
Cdd:COG0252  217 LYPGMDPALLDALLAAGVKGIVLEGTGAGNVP--PALLPALKRAIERGVPVVVTSRCPEGRVNGVYGGGRDLAEAGVISG 294

                        170       180       190
                 ....*....|....*....|....*....|..
gi 568978556 161 FDMTSEAALAKLSYVLGQpGLSLNDRKKLLAK 192
Cdd:COG0252  295 GDLTPEKARIKLMLALGQ-GLDPEEIRRLFET 325
Asparaginase smart00870
Asparaginase, found in various plant, animal and bacterial cells; Asparaginase catalyses the ...
 2-187 1.12e-53

Asparaginase, found in various plant, animal and bacterial cells; Asparaginase catalyses the deamination of asparagine to yield aspartic acid and an ammonium ion, resulting in a depletion of free circulatory asparagine in plasma. The enzyme is effective in the treatment of human malignant lymphomas, which have a diminished capacity to produce asparagine synthetase: in order to survive, such cells absorb asparagine from blood plasma..- if Asn levels have been depleted by injection of asparaginase, the lymphoma cells die.


Pssm-ID: 214873 [Multi-domain]  Cd Length: 323  Bit Score: 180.79  E-value: 1.12e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978556     2 AGQYVIPEVCLFFQNQLFRGNRTTKVDARRFAAFCSPNLPPLATVGADVTINRELVRKACGKS---HLVVHSSMEPDVGL 78
Cdd:smart00870 137 SPEARGRGVLVVFNDEIHRARRVTKTHTSRVDAFQSPNFGPLGYVDEGGVVYYTRPTRRHTKRspfLLDLKDALLPKVAI 216

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978556    79 LRLYPGIPASLVRTFLQPPLKGVVMETFGSGNGPtkPDLLQELRVAAEQGLIIVNCTHCLQGAVT-SDYASGMAMAGAGI 157
Cdd:smart00870 217 VKAYPGMDAELLDALLDSGAKGLVLEGTGAGNVP--PDLLEALKEALERGIPVVRTSRCLSGRVDpGYYATGRDLAKAGV 294

                          170       180       190
                   ....*....|....*....|....*....|
gi 568978556   158 VSGFDMTSEAALAKLSYVLGQpGLSLNDRK 187
Cdd:smart00870 295 ISAGDLTPEKARIKLMLALGK-GLDPEEIR 323
L-asparaginase_I cd08963
Type I (cytosolic) bacterial L-asparaginase; Asparaginases (amidohydrolases, E.C. 3.5.1.1) are ...
 1-179 1.06e-48

Type I (cytosolic) bacterial L-asparaginase; Asparaginases (amidohydrolases, E.C. 3.5.1.1) are enzymes that catalyze the hydrolysis of asparagine to aspartic acid and ammonia. In bacteria, there are two classes of amidohydrolases. This model represents type I L-asparaginases, which are highly specific for asparagine and localized in the cytosol. Type I L-asparaginase acts as a dimer. A conserved threonine residue is thought to supply the nucleophile hydroxy-group that attacks the amide bond. Many bacterial L-asparaginases have both L-asparagine and L-glutamine hydrolysis activities, to a different degree, and some of them are annotated as asparaginase/glutaminase. One example of an enzyme with no L-glutaminase activity is the type I L-asparaginase from Wolinella succinogenes.


Pssm-ID: 199207 [Multi-domain]  Cd Length: 316  Bit Score: 167.76  E-value: 1.06e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978556   1 MAGQYVIPEVCLFFQNQLFRGNRTTKVDARRFAAFCSPNLPPLATVGADVTINRELVRKACGKSHLvvHSSMEPDVGLLR 80
Cdd:cd08963  131 AASSGSIRGVYVAFNGKLIRGTRARKVRTTSFDAFESINYPLLAEIGAGGLTLERLLQYEPLPSLF--YPDLDPNVFLLK 208

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978556  81 LYPGIPASLVRTFLQPPLKGVVMETFGSGNGPTKPDLLQELRVAAEQGLIIVNCTHCLQGAV-TSDYASGMAMAGAGIVS 159
Cdd:cd08963  209 LIPGLLPAILDALLEKYPRGLILEGFGAGNIPYDGDLLAALEEATARGKPVVVTTQCPYGGSdLSVYAVGQALLEAGVIP 288

                        170       180
                 ....*....|....*....|
gi 568978556 160 GFDMTSEAALAKLSYVLGQP 179
Cdd:cd08963  289 GGDMTTEAAVAKLMWLLGQT 308
Asparaginase_C pfam17763
Glutaminase/Asparaginase C-terminal domain; This domain is found at the C-terminus of ...
 75-189 1.09e-31

Glutaminase/Asparaginase C-terminal domain; This domain is found at the C-terminus of asparaginase enzymes.


Pssm-ID: 465490 [Multi-domain]  Cd Length: 114  Bit Score: 116.43  E-value: 1.09e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978556   75 DVGLLRLYPGIPASLVRTFLQPPLKGVVMETFGSGNGPtkPDLLQELRVAAEQGLIIVNCTHCLQGAVT-SDYASGMAMA 153
Cdd:pfam17763   1 RVDILYLYPGMDPELLDAALAAGAKGIVIAGFGAGNVP--SALLDALKEAVARGIPVVRSSRCGSGRVNlGYYETGRDLL 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 568978556  154 GAGIVSGFDMTSEAALAKLSYVLGQpGLSLNDRKKL 189
Cdd:pfam17763  79 EAGVISGGDLTPEKARIKLMLALGK-GLDPEEIREL 113
PRK04183 PRK04183
Glu-tRNA(Gln) amidotransferase subunit GatD;
20-199 1.55e-24

Glu-tRNA(Gln) amidotransferase subunit GatD;


Pssm-ID: 235245 [Multi-domain]  Cd Length: 419  Bit Score: 104.16  E-value: 1.55e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978556  20 RGNRTTKVDARRFAAFCSPNLPPLATV----GADVTINRELVRKacGKSHLVVHSSMEPDVGLLRLYPGIPASLVRTFLQ 95
Cdd:PRK04183 233 RGTRVRKMHTSRRDAFQSINDKPLAKVdykeGKIEFLRKDYRKR--GEKELELNDKLEEKVALIKFYPGMDPEILDFYVD 310

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978556  96 PPLKGVVMEtfGSGNGPTKPDLLQELRVAAEQGLIIVNCTHCLQGAVTSD-YASGMAMAGAGIVSGFDMTSEAALAKLSY 174
Cdd:PRK04183 311 KGYKGIVIE--GTGLGHVSTDLIPSIKRATDDGIPVVMTSQCLYGRVNMNvYSTGRDLLKAGVIPGEDMLPEVAYVKLMW 388

                        170       180
                 ....*....|....*....|....*
gi 568978556 175 VLGQPGlSLNDRKKLLAKDLRGEMT 199
Cdd:PRK04183 389 VLGNTY-DLEEVRELMLTNLAGEIN 412
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
250-389 2.61e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 98.87  E-value: 2.61e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978556 250 DTLQAFVELDRDLNLKDYSGQTPLHVAARRGHAAVVTMLLQRGADVDARNEDGQSPLLLAVRGRHQSVIGLLRAAGARLS 329
Cdd:COG0666  101 EIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVN 180

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978556 330 PQELEDvGTELCRLASRGDSEGLRAWWQAGADLGQPDYDGHCALQVAEAAGNADVVALLQ 389
Cdd:COG0666  181 ARDNDG-ETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239
GatD cd08962
GatD subunit of archaeal Glu-tRNA amidotransferase; GatD is involved in the alternative ...
 20-178 1.25e-22

GatD subunit of archaeal Glu-tRNA amidotransferase; GatD is involved in the alternative synthesis of Gln-tRNA(Gln) in archaea via the transamidation of incorrectly charged Glu-tRNA(Gln). GatD is active as a dimer, and it provides the amino group required for this reaction. GatD is related to bacterial L-asparaginases (amidohydrolases), which catalyze the hydrolysis of asparagine to aspartic acid and ammonia. This CD spans both the L-asparaginase_like domain and an N-terminal supplementary domain.


Pssm-ID: 199206 [Multi-domain]  Cd Length: 402  Bit Score: 98.46  E-value: 1.25e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978556  20 RGNRTTKVDARRFAAFCSPNLPPLATV---GADVTINRELVRKacGKSHLVVHSSMEPDVGLLRLYPGIPASLVRTFLQP 96
Cdd:cd08962  229 RGTRVRKMHTSRRDAFQSINDEPLAKVdppGKIEKLSKDYRKR--GDEELELNDKLEEKVALIKFYPGMDPEIIDFYVDK 306

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978556  97 PLKGVVMEtfGSGNGPTKPDLLQELRVAAEQGLIIVNCTHCLQGAVTSD-YASGMAMAGAGIVSGFDMTSEAALAKLSYV 175
Cdd:cd08962  307 GYKGIVIE--GTGLGHVSEDLIPSIKKAIDDGIPVVMTSQCIYGRVNLNvYSTGRELLKAGVIPGEDMLPETAYVKLMWV 384


                 ...
gi 568978556 176 LGQ 178
Cdd:cd08962  385 LGN 387
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
261-389 1.47e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 96.56  E-value: 1.47e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978556 261 DLNLKDYSGQTPLHVAARRGHAAVVTMLLQRGADVDARNEDGQSPLLLAVRGRHQSVIGLLRAAGARLSPQELEDvGTEL 340
Cdd:COG0666  145 DVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDG-KTAL 223

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 568978556 341 CRLASRGDSEGLRAWWQAGADLGQPDYDGHCALQVAEAAGNADVVALLQ 389
Cdd:COG0666  224 DLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLL 272
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
183-388 7.70e-20

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 88.86  E-value: 7.70e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978556 183 LNDRKKLLAKDLRGEMTLPATDVLLQDGMLGCRVAWLLSMNGSQEADTMKDVLLPGLALAAAHAGDLDTLQAFVELDRDL 262
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978556 263 NLKDYSGQTPLHVAARRGHAAVVTMLLQRGADVDARNEDGQSPLLLAVRGRHQSVIGLLRAAGARLSPQELEDVgTELCR 342
Cdd:COG0666   81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGN-TPLHL 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 568978556 343 LASRGDSEGLRAWWQAGADLGQPDYDGHCALQVAEAAGNADVVALL 388
Cdd:COG0666  160 AAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205
L-asparaginase_like cd00411
Bacterial L-asparaginases and related enzymes; Asparaginases (amidohydrolases, E.C. 3.5.1.1) ...
 3-178 1.78e-18

Bacterial L-asparaginases and related enzymes; Asparaginases (amidohydrolases, E.C. 3.5.1.1) are dimeric or tetrameric enzymes that catalyze the hydrolysis of asparagine to aspartic acid and ammonia. In bacteria, there are two classes of amidohydrolases, one highly specific for asparagine and localized to the periplasm (type II L-asparaginase), and a second (asparaginase- glutaminase) present in the cytosol (type I L-asparaginase) that hydrolyzes both asparagine and glutamine with similar specificities and has a lower affinity for its substrate. Bacterial L-asparaginases (type II) are potent antileukemic agents and have been used in the treatment of acute lymphoblastic leukemia (ALL). A conserved threonine residue is thought to supply the nucleophile hydroxy-group that attacks the amide bond. Many bacterial L-asparaginases have both L-asparagine and L-glutamine hydrolysis activities, to a different degree, and some of them are annotated as asparaginase/glutaminase. This wider family also includes a subunit of an archaeal Glu-tRNA amidotransferase.


Pssm-ID: 199205 [Multi-domain]  Cd Length: 320  Bit Score: 85.64  E-value: 1.78e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978556   3 GQYVIPEVCLFFQNQLFRGNRTTKVDARRFAAFCSPNLPPLATVGADVTI--NRELVRKACGKSHLVVHSSMEPDVGLLR 80
Cdd:cd00411  139 KDSRGRGVLVVMNDKVHSGRDVSKTNTSGFDAFRSINYGPLGEIKDNKIYyqRKPARKHTDESEFDVSDIKSLPKVDIVY 218

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978556  81 LYPGIPASLVRTFLQPPLKGVVMEtfGSGNGPTKPDLLQELRVAAEQGLIIVNCTHCLQGAVTSDYASGMAMAGaGIVSG 160
Cdd:cd00411  219 LYPGLSDDIYDALVDLGYKGIVLA--GTGNGSVPYDVFPVLSSASKRGVAVVRSSQVIYGGVDLNAEKVDLKAG-VIPAG 295

                        170
                 ....*....|....*...
gi 568978556 161 fDMTSEAALAKLSYVLGQ 178
Cdd:cd00411  296 -DLNPEKARVLLMWALTH 312
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 211-388 2.70e-18

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 87.23  E-value: 2.70e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978556 211 MLGCRVAWLLSMNGSQEADTMKDVLLPGLALAAAHAGDLDTLQAfvELDRDLNlkDYSGQTPLHVAARRGHAAVVTMLLQ 290
Cdd:PLN03192 504 LHDLNVGDLLGDNGGEHDDPNMASNLLTVASTGNAALLEELLKA--KLDPDIG--DSKGRTPLHIAASKGYEDCVLVLLK 579

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978556 291 RGADVDARNEDGQSPLLLAVRGRHQSVIGLLRAAGARLSPQELEDVgteLCRLASRGDSEGLRAWWQAGADLGQPDYDGH 370
Cdd:PLN03192 580 HACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAGDL---LCTAAKRNDLTAMKELLKQGLNVDSEDHQGA 656

                        170
                 ....*....|....*...
gi 568978556 371 CALQVAEAAGNADVVALL 388
Cdd:PLN03192 657 TALQVAMAEDHVDMVRLL 674
L-asparaginase_II cd08964
Type II (periplasmic) bacterial L-asparaginase; Asparaginases (amidohydrolases, E.C. 3.5.1.1) ...
 14-178 1.20e-16

Type II (periplasmic) bacterial L-asparaginase; Asparaginases (amidohydrolases, E.C. 3.5.1.1) are enzymes that catalyze the hydrolysis of asparagine to aspartic acid and ammonia. In bacteria, there are two classes of amidohydrolases. This model represents type II L-asparaginases, which tend to be highly specific for asparagine and localized to the periplasm. They are potent antileukemic agents and have been used in the treatment of acute lymphoblastic leukemia (ALL), but not without severe side effects. Tumor cells appear to have a heightened dependence on exogenous L-aspartate, and depleting their surroundings of L-aspartate may starve cancerous ALL cells. Type II L-asparaginase acts as a tetramer, which is actually a dimer of two tightly bound dimers. A conserved threonine residue is thought to supply the nucleophile hydroxy-group that attacks the amide bond. Many bacterial L-asparaginases have both L-asparagine and L-glutamine hydrolysis activities, to a different degree, and some of them are annotated as asparaginase/glutaminase.


Pssm-ID: 199208 [Multi-domain]  Cd Length: 319  Bit Score: 80.25  E-value: 1.20e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978556  14 FQNQLFRGNRTTKVDARRFAAFCSPNLPPLATV-GADVTINRELVRKACGKShlvVHSSMEPDVGLLRLYPGIPASLVRT 92
Cdd:cd08964  149 FNDEIHAARDVTKTHTTSLDAFASPGFGPLGYVdGGKVRFYRRPARPHTLPS---EFDDELPRVDIVYAYAGADGALLDA 225

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978556  93 FLQPPLKGVVMETFGSGNGPtkPDLLQELRVAAEQGLIIVNCTHCLQGAVTSDYA--SGMAMAGAGIVSGFDMTSEAALA 170
Cdd:cd08964  226 AVAAGAKGIVIAGFGAGNVP--PALVEALERAVAKGIPVVRSSRVGNGRVLPVYGygGGADLAEAGAIFAGDLSPQKARI 303


                 ....*...
gi 568978556 171 KLSYVLGQ 178
Cdd:cd08964  304 LLMLALAA 311
Asparaginase pfam00710
Asparaginase, N-terminal; This is the N-terminal domain of this enzyme.
 1-55 1.35e-14

Asparaginase, N-terminal; This is the N-terminal domain of this enzyme.


Pssm-ID: 459913 [Multi-domain]  Cd Length: 188  Bit Score: 71.80  E-value: 1.35e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568978556    1 MAGQY--VIPEVCLFFQNQLFRGNRTTKVDARRFAAFCSPNLPPLATV-GADVTINRE 55
Cdd:pfam00710 131 VAASPaaRGPGVLVVFNDKLHRARRVTKTHTSSLDAFDSPNFGPLGEVdGGQVELYRE 188
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 261-336 3.84e-12

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 68.00  E-value: 3.84e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978556 261 DLNLKDYSGQTPLHVAARRGHAAVVTMLLQRGADVDARNEDGQSPLLLAVRGRHQSVIGLLRA-------AGARLSPQEL 333
Cdd:PTZ00322 107 DPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRhsqchfeLGANAKPDSF 186


                 ...
gi 568978556 334 EDV 336
Cdd:PTZ00322 187 TGK 189
Ank_2 pfam12796
Ankyrin repeats (3 copies);
250-328 2.23e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 57.05  E-value: 2.23e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568978556  250 DTLQAFVELDRDLNLKDYSGQTPLHVAARRGHAAVVTMLLQRgADVDARNeDGQSPLLLAVRGRHQSVIGLLRAAGARL 328
Cdd:pfam12796  11 ELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADI 87
Ank_5 pfam13857
Ankyrin repeats (many copies);
259-309 1.01e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 53.89  E-value: 1.01e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568978556  259 DRDLNLKDYSGQTPLHVAARRGHAAVVTMLLQRGADVDARNEDGQSPLLLA 309
Cdd:pfam13857   6 PIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
271-321 5.38e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.81  E-value: 5.38e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568978556  271 TPLHVAARRGHAAVVTMLLQRGADVDARNEDGQSPLLLAVRGRHQSVIGLL 321
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 269-300 7.21e-08

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 48.05  E-value: 7.21e-08
                          10        20        30
                  ....*....|....*....|....*....|...
gi 568978556  269 GQTPLHVAA-RRGHAAVVTMLLQRGADVDARNE 300
Cdd:pfam00023   2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
Ank_2 pfam12796
Ankyrin repeats (3 copies);
273-321 8.20e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 49.73  E-value: 8.20e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 568978556  273 LHVAARRGHAAVVTMLLQRGADVDARNEDGQSPLLLAVRGRHQSVIGLL 321
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL 49
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
250-328 5.53e-07

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 50.72  E-value: 5.53e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568978556 250 DTLQAFVELDRDLNLKDYSGQTPLHVAARRGHAAVVTMLLQRGADVDARNEDGQSPLLLAVRGRHQSVIGLLRAAGARL 328
Cdd:COG0666  200 EIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLL 278
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 255-326 7.44e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 50.82  E-value: 7.44e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568978556 255 FVELDRDLNLKDYSGQTPLHVAARRGHAAVVTMLLQRGADVDARNEDGQSPLLLAVRGRHQSVIGLLRAAGA 326
Cdd:PHA03100 178 LLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 250-329 8.87e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 50.73  E-value: 8.87e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978556 250 DTLQAFVELDRDLNLKDYSGQTPLHVAARRGHAAVVTMLLQRGADVDARNEDGQSPLLLAVRGRHQSVIGLLRAAGARLS 329
Cdd:PHA02874 105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184
PHA03095 PHA03095
ankyrin-like protein; Provisional
 261-311 1.14e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 50.41  E-value: 1.14e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568978556 261 DLNLKDYSGQTPLHVAARRGHAAVVTMLLQRGADVDARNEDGQSPLLLAVR 311
Cdd:PHA03095 249 SINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVR 299
Ank_2 pfam12796
Ankyrin repeats (3 copies);
261-299 1.17e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 46.26  E-value: 1.17e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 568978556  261 DLNLKDYsGQTPLHVAARRGHAAVVTMLLQRGADVDARN 299
Cdd:pfam12796  54 DVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 269-297 2.00e-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: 43.73  E-value: 2.00e-06
                           10        20
                   ....*....|....*....|....*....
gi 568978556   269 GQTPLHVAARRGHAAVVTMLLQRGADVDA 297
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 328-391 3.58e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.13  E-value: 3.58e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978556 328 LSPQELED------VGTELCRLASRGDSEGLRAWWQAGADLGQPDYDGHCALQVAEAAGNADVVALLQSF 391
Cdd:PTZ00322  68 LTTEEVIDpvvahmLTVELCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEF 137
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 269-390 1.09e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 47.29  E-value: 1.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978556 269 GQTPLHVAARRGHAAVVTMLLQRGADVDARNEDGQSPLLLAVRGRHQSVIGLLRAAGARLspqELEDV--GTELCRLASR 346
Cdd:PHA02875 102 GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACL---DIEDCcgCTPLIIAMAK 178

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 568978556 347 GDSEGLRAWWQAGADlgqPDYDGH--CALQVAEAAGN--ADVVALLQS 390
Cdd:PHA02875 179 GDIAICKMLLDSGAN---IDYFGKngCVAALCYAIENnkIDIVRLFIK 223
PHA03095 PHA03095
ankyrin-like protein; Provisional
 250-329 1.23e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 47.33  E-value: 1.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978556 250 DTLQAFVELDRDLNLKDYSGQTPLHVAAR--RGHAAVVTMLLQRGADVDARNEDGQSPLLLAVRGRHQSV--IGLLRAAG 325
Cdd:PHA03095  98 DVIKLLIKAGADVNAKDKVGRTPLHVYLSgfNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVelLRLLIDAG 177


                 ....
gi 568978556 326 ARLS 329
Cdd:PHA03095 178 ADVY 181
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 269-297 1.47e-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: 41.47  E-value: 1.47e-05
                          10        20
                  ....*....|....*....|....*....
gi 568978556  269 GQTPLHVAARRGHAAVVTMLLQRGADVDA 297
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 261-318 2.27e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.60  E-value: 2.27e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568978556 261 DLNLKDYSGQTPLHVAARRGHAAVVTMLLQRGADVDARNEDGQSPLLLAVRGRHQSVI 318
Cdd:PHA02876 170 DVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTI 227
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 250-298 2.62e-05

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 46.34  E-value: 2.62e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978556 250 DTLQAFVEL-DRDLNLKD----------YSGQTPLHVAARRGHAAVVTMLLQRGADVDAR 298
Cdd:cd22196   64 DTISLLLDIaEKTGNLKEfvnaaytdsyYKGQTALHIAIERRNMHLVELLVQNGADVHAR 123
Ank_4 pfam13637
Ankyrin repeats (many copies);
250-289 3.01e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.11  E-value: 3.01e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 568978556  250 DTLQAFVELDRDLNLKDYSGQTPLHVAARRGHAAVVTMLL 289
Cdd:pfam13637  15 ELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 262-388 4.31e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 45.34  E-value: 4.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978556 262 LNLKDYSGQTPLHVAARRGHAAVVTMLLQRGADVDARNEDGQSPLLLAVRGRHQSVIGLLRAAGARLSPQELEDVGTELC 341
Cdd:PHA02874  28 INISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSILPIPCIEKDMI 107

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568978556 342 RL----------------------ASRGDSEGLRAWWQAGADLGQPDYDGHCALQVAEAAGNADVVALL 388
Cdd:PHA02874 108 KTildcgidvnikdaelktflhyaIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLL 176
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 250-312 4.75e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.44  E-value: 4.75e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568978556 250 DTLQAFVELDRDLNLKDYSGQTPLHVAARRGHAAVVTMLLQRGADVDARNEDGQSPLLLAVRG 312
Cdd:PHA02876 356 DIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCG 418
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 251-328 5.10e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.44  E-value: 5.10e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568978556 251 TLQAFVELDRDLNLKDYSGQTPLHVAARRG-HAAVVTMLLQRGADVDARNEDGQSPLLLAVrgRHQSVIGLLRAAGARL 328
Cdd:PHA02876 424 SVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIAL--EYHGIVNILLHYGAEL 500
PHA03095 PHA03095
ankyrin-like protein; Provisional
 256-329 6.05e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 45.02  E-value: 6.05e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568978556 256 VELDRDLNLKDYSGQTPLHVAARRG--HAAVVTMLLQRGADVDARNEDGQSPLLLAVRGRHQSVIGLLRAAGARLS 329
Cdd:PHA03095 209 IRAGCDPAATDMLGNTPLHSMATGSscKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADIN 284
PHA03095 PHA03095
ankyrin-like protein; Provisional
 250-326 9.72e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 44.25  E-value: 9.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978556 250 DTLQAFVELDRDLNLKDYSGQTPLHVAARRGH-AAVVTMLLQRGADVDARNEDGQSPLLLAVRGR--HQSVIGLLRAAGA 326
Cdd:PHA03095  64 DIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAGADVNAKDKVGRTPLHVYLSGFniNPKVIRLLLRKGA 143
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 250-311 1.41e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 43.80  E-value: 1.41e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568978556 250 DTLQAFVELDRDLNLKDYSGQTPLHVAARRGHAAVVTMLLQRGADVDARNEDGQSPLLLAVR 311
Cdd:PHA02874 138 ESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAE 199
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 250-321 1.87e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 43.41  E-value: 1.87e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568978556 250 DTLQAFVELDRDLNLKDYSGQTPLHVAARRGHAAVVTMLLQRGADVDARNEDGQSPLLLAVRgRHQSVIGLL 321
Cdd:PHA02874 171 DIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII-HNRSAIELL 241
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 267-298 2.78e-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: 43.15  E-value: 2.78e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 568978556  267 YSGQTPLHVAARRGHAAVVTMLLQRGADVDAR 298
Cdd:TIGR00870 126 TPGITALHLAAHRQNYEIVKLLLERGASVPAR 157
PHA02917 PHA02917
ankyrin-like protein; Provisional
 260-310 4.52e-04

ankyrin-like protein; Provisional


Pssm-ID: 165231 [Multi-domain]  Cd Length: 661  Bit Score: 42.29  E-value: 4.52e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568978556 260 RDLNLKDYSGQTPLHVAARRGHAAVVTMLLQRGADVDARNEDGQSPLLLAV 310
Cdd:PHA02917 443 KDINMIDKRGETLLHKAVRYNKQSLVSLLLESGSDVNIRSNNGYTCIAIAI 493
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 250-350 5.70e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 42.16  E-value: 5.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978556 250 DTLQAFVELDRDLNLKDYSGQTPLHVAARRGHAAVVTMLLQRGADVDARN-EDGQSPLLL--AVRGRHQSVIGLLRAAGA 326
Cdd:PLN03192 636 TAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANtDDDFSPTELreLLQKRELGHSITIVDSVP 715

                         90       100
                 ....*....|....*....|....
gi 568978556 327 RLSPQELEDVGTELCRLASRGDSE 350
Cdd:PLN03192 716 ADEPDLGRDGGSRPGRLQGTSSDN 739
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 251-309 8.83e-04

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 41.67  E-value: 8.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978556 251 TLQAFVE----LDRDLNL----KDYSGQTPLHVAARRGHAAVVTMLLQRGADVDAR----------NED----GQSPLLL 308
Cdd:cd22194  115 ILLAFAEengiLDRFINAeyteEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHakgvffnpkyKHEgfyfGETPLAL 194


                 .
gi 568978556 309 A 309
Cdd:cd22194  195 A 195
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 250-300 1.35e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 40.80  E-value: 1.35e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568978556 250 DTLQAFVELDRDLNLKDYSGQTPLHVAARRGHAAVVTMLLQRGADVDARNE 300
Cdd:PHA03100 206 EFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256
PHA02741 PHA02741
hypothetical protein; Provisional
 252-322 1.97e-03

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 38.87  E-value: 1.97e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568978556 252 LQAFVELDRDLNLKD-YSGQTPLHVAA-RRGHAAVVTMLLQRGADVDARNEDGQSPLLLAVRGRHQSVIGLLR 322
Cdd:PHA02741  80 IDHLIELGADINAQEmLEGDTALHLAAhRRDHDLAEWLCCQPGIDLHFCNADNKSPFELAIDNEDVAMMQILR 152
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 263-331 2.12e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 40.25  E-value: 2.12e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978556 263 NLKDYSGQTPLHVAARRGHAAVVTMLLQRGADVDARNEDGQSPLLLAV-RGRHQSVIGLLRAAGARLSPQ 331
Cdd:PHA02878 195 NIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVgYCKDYDILKLLLEHGVDVNAK 264
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 267-335 2.42e-03

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 39.86  E-value: 2.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978556 267 YSGQTPLHVAARRGHAAVVTMLLQRGADVDARNED-------------GQSPLLLAVRGRHQSVIGLLRAAGARLSPQEL 333
Cdd:cd21882   71 YQGQTALHIAIENRNLNLVRLLVENGADVSARATGrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQPAALEA 150


                 ..
gi 568978556 334 ED 335
Cdd:cd21882  151 QD 152
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 262-326 3.99e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 39.28  E-value: 3.99e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568978556 262 LNLKDYSGQTPLHVAARRGH-AAVVTMLLQRGADVDARNEDGQSPL-LLAVRGRHQSVIGLLRAAGA 326
Cdd:PHA02876 266 VNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLyLMAKNGYDTENIRTLIMLGA 332
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 267-343 4.48e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 39.47  E-value: 4.48e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568978556 267 YSGQTPLHVAARRGHAAVVTMLLQRGADVDARNEDGQSPLLLAVRGRHQSVIGLLRAAGARLSPQELED--VGTELCRL 343
Cdd:PLN03192 620 HAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDDdfSPTELREL 698
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 261-326 4.86e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 39.09  E-value: 4.86e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568978556 261 DLNLKD-YSGQTPLHVAARRGHAAVVTMLLQRGADVDARNEDGQSPLLLAVRGRHQSVIGLLRAAGA 326
Cdd:PHA02878 159 DINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA 225
PHA03095 PHA03095
ankyrin-like protein; Provisional
 250-388 7.05e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 38.47  E-value: 7.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978556 250 DTLQAFVELDRDLNLKDYSGQTPLHVAARRGH---AAVVTMLLQRGADVDARNEDGQSPLLLAVrgRHQSVIGLLR---A 323
Cdd:PHA03095  28 EEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYL--YNATTLDVIKlliK 105

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978556 324 AGARLspQELEDVGTELCRLASRGDS---EGLRAWWQAGADLGQPDYDGHCALQVAEAAGNADV--VALL 388
Cdd:PHA03095 106 AGADV--NAKDKVGRTPLHVYLSGFNinpKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVelLRLL 173
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 250-313 7.45e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 38.32  E-value: 7.45e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568978556 250 DTLQAFVELDRDLNLKDY-SGQTPLHVAARrgHAAVVTMLLQRGADVDARNEDGQSPLLLAVRGR 313
Cdd:PHA02878 249 DILKLLLEHGVDVNAKSYiLGLTALHSSIK--SERKLKLLLEYGADINSLNSYKLTPLSSAVKQY 311
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 250-326 8.50e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 38.32  E-value: 8.50e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568978556 250 DTLQAFVELDRDLNLKDYSGQTPLHVAARR-GHAAVVTMLLQRGADVDARNE-DGQSPLLLAVRGrhQSVIGLLRAAGA 326
Cdd:PHA02878 215 PIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIKS--ERKLKLLLEYGA 291
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 252-327 8.85e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 36.78  E-value: 8.85e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568978556 252 LQAFVELDRDLNLKD-YSGQTPLHVAARRGHAAVVTMLLQR-GADVDARNEDGQSPLLLAVRGRHQSVIGLLRAAGAR 327
Cdd:PHA02736  74 LKLLMEWGADINGKErVFGNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVACERHDAKMMNILRAKGAQ 151
 
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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