NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|568978554|ref|XP_006515411|]
View 

60 kDa lysophospholipase isoform X2 [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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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) ...
 1-243 3.64e-100

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: 302.66  E-value: 3.64e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978554   1 MAFAASVLSFMLENLQKPVVLTGAQVPIHALWSDGRENLLGALLMAGQYVIPEVCLFFQNQLFRGNRTTKVDARRFAAFC 80
Cdd:PRK09461  94 MAYTASALSFMLENLGKPVIVTGSQIPLAELRSDGQTNLLNALYVAANYPINEVTLFFNNKLFRGNRTTKAHADGFDAFA 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978554  81 SPNLPPLATVGADVTINRELVRKACGKShLVVHSSMEPDVGLLRLYPGIPASLVRTFLQPPLKGVVMETFGSGNGPTKPD 160
Cdd:PRK09461 174 SPNLPPLLEAGIHIRRLNTPPAPHGEGE-LIVHPITPQPIGVVTIYPGISAEVVRNFLRQPVKALILRSYGVGNAPQNPA 252

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978554 161 LLQELRVAAEQGLIIVNCTHCLQGAVT-SDYASGMAMAGAGIVSGFDMTSEAALAKLSYVLGQPgLSLNDRKKLLAKDLR 239
Cdd:PRK09461 253 LLQELKEASERGIVVVNLTQCMSGKVNmGGYATGNALAHAGVISGADMTVEAALTKLHYLLSQE-LSTEEIRQAMQQNLR 331


                 ....
gi 568978554 240 GEMT 243
Cdd:PRK09461 332 GELT 335
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
294-433 1.20e-22

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 97.33  E-value: 1.20e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978554 294 DTLQAFVELDRDLNLKDYSGQTPLHVAARRGHAAVVTMLLQRGADVDARNEDGQSPLLLAVRGRHQSVIGLLRAAGARLS 373
Cdd:COG0666  101 EIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVN 180

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978554 374 PQELEDvGTELCRLASRGDSEGLRAWWQAGADLGQPDYDGHCALQVAEAAGNADVVALLQ 433
Cdd:COG0666  181 ARDNDG-ETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239
 
Name Accession Description Interval E-value
ansA PRK09461
cytoplasmic asparaginase I; Provisional
 1-243 3.64e-100

cytoplasmic asparaginase I; Provisional


Pssm-ID: 181876 [Multi-domain]  Cd Length: 335  Bit Score: 302.66  E-value: 3.64e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978554   1 MAFAASVLSFMLENLQKPVVLTGAQVPIHALWSDGRENLLGALLMAGQYVIPEVCLFFQNQLFRGNRTTKVDARRFAAFC 80
Cdd:PRK09461  94 MAYTASALSFMLENLGKPVIVTGSQIPLAELRSDGQTNLLNALYVAANYPINEVTLFFNNKLFRGNRTTKAHADGFDAFA 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978554  81 SPNLPPLATVGADVTINRELVRKACGKShLVVHSSMEPDVGLLRLYPGIPASLVRTFLQPPLKGVVMETFGSGNGPTKPD 160
Cdd:PRK09461 174 SPNLPPLLEAGIHIRRLNTPPAPHGEGE-LIVHPITPQPIGVVTIYPGISAEVVRNFLRQPVKALILRSYGVGNAPQNPA 252

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978554 161 LLQELRVAAEQGLIIVNCTHCLQGAVT-SDYASGMAMAGAGIVSGFDMTSEAALAKLSYVLGQPgLSLNDRKKLLAKDLR 239
Cdd:PRK09461 253 LLQELKEASERGIVVVNLTQCMSGKVNmGGYATGNALAHAGVISGADMTVEAALTKLHYLLSQE-LSTEEIRQAMQQNLR 331


                 ....
gi 568978554 240 GEMT 243
Cdd:PRK09461 332 GELT 335
Asparaginase smart00870
Asparaginase, found in various plant, animal and bacterial cells; Asparaginase catalyses the ...
 1-231 6.64e-79

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: 247.43  E-value: 6.64e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978554     1 MAFAASVLSFMLENLQKPVVLTGAQVPIHALWSDGRENLLGALLMAGQY--VIPEVCLFFQNQLFRGNRTTKVDARRFAA 78
Cdd:smart00870  90 LEETAYFLSLTLDSLDKPVVLTGAMRPATALSSDGPANLLDAVRVAASPeaRGRGVLVVFNDEIHRARRVTKTHTSRVDA 169

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978554    79 FCSPNLPPLATVGADVTINRELVRKACGKS---HLVVHSSMEPDVGLLRLYPGIPASLVRTFLQPPLKGVVMETFGSGNG 155
Cdd:smart00870 170 FQSPNFGPLGYVDEGGVVYYTRPTRRHTKRspfLLDLKDALLPKVAIVKAYPGMDAELLDALLDSGAKGLVLEGTGAGNV 249

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568978554   156 PtkPDLLQELRVAAEQGLIIVNCTHCLQGAVT-SDYASGMAMAGAGIVSGFDMTSEAALAKLSYVLGQpGLSLNDRK 231
Cdd:smart00870 250 P--PDLLEALKEALERGIPVVRTSRCLSGRVDpGYYATGRDLAKAGVISAGDLTPEKARIKLMLALGK-GLDPEEIR 323
AnsA COG0252
L-asparaginase/archaeal Glu-tRNAGln amidotransferase subunit D [Translation, ribosomal ...
 1-236 1.05e-78

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: 246.97  E-value: 1.05e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978554   1 MAFAASVLSFMLEnLQKPVVLTGAQVPIHALWSDGRENLLGALLMA--GQYVIPEVCLFFQNQLFRGNRTTKVDARRFAA 78
Cdd:COG0252   93 LEETAYALSLMLD-LPKPVVLTGAQRPADAPSSDGPANLLDAVRVAasPEARGRGVLVVFNDEIHRARRVTKTHTSRVDA 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978554  79 FCSPNLPPLATVGAD-VTINRELVRKacGKSHLVVHSSMEPDVGLLRLYPGIPASLVRTFLQPPLKGVVMETFGSGNGPt 157
Cdd:COG0252  172 FQSPNYGPLGEVDEGrVRFYRRPPRR--PESELDLAPALLPRVAILKLYPGMDPALLDALLAAGVKGIVLEGTGAGNVP- 248

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568978554 158 kPDLLQELRVAAEQGLIIVNCTHCLQGAVTSDYASGMAMAGAGIVSGFDMTSEAALAKLSYVLGQpGLSLNDRKKLLAK 236
Cdd:COG0252  249 -PALLPALKRAIERGVPVVVTSRCPEGRVNGVYGGGRDLAEAGVISGGDLTPEKARIKLMLALGQ-GLDPEEIRRLFET 325
L-asparaginase_I cd08963
Type I (cytosolic) bacterial L-asparaginase; Asparaginases (amidohydrolases, E.C. 3.5.1.1) are ...
 1-223 7.72e-74

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: 234.40  E-value: 7.72e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978554   1 MAFAASVLSFMLENLQKPVVLTGAQVPIHALWSDGRENLLGALLMAGQYVIPEVCLFFQNQLFRGNRTTKVDARRFAAFC 80
Cdd:cd08963   87 MAYTAAALSFLLQNLPKPVVLTGSQLPLGEPGSDARRNLRDALRAASSGSIRGVYVAFNGKLIRGTRARKVRTTSFDAFE 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978554  81 SPNLPPLATVGADVTINRELVRKACGKSHLvvHSSMEPDVGLLRLYPGIPASLVRTFLQPPLKGVVMETFGSGNGPTKPD 160
Cdd:cd08963  167 SINYPLLAEIGAGGLTLERLLQYEPLPSLF--YPDLDPNVFLLKLIPGLLPAILDALLEKYPRGLILEGFGAGNIPYDGD 244

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568978554 161 LLQELRVAAEQGLIIVNCTHCLQGAV-TSDYASGMAMAGAGIVSGFDMTSEAALAKLSYVLGQP 223
Cdd:cd08963  245 LLAALEEATARGKPVVVTTQCPYGGSdLSVYAVGQALLEAGVIPGGDMTTEAAVAKLMWLLGQT 308
Asparaginase pfam00710
Asparaginase, N-terminal; This is the N-terminal domain of this enzyme.
 1-99 9.02e-42

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


Pssm-ID: 459913 [Multi-domain]  Cd Length: 188  Bit Score: 146.53  E-value: 9.02e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978554    1 MAFAASVLSFMLENLQKPVVLTGAQVPIHALWSDGRENLLGALLMAGQY--VIPEVCLFFQNQLFRGNRTTKVDARRFAA 78
Cdd:pfam00710  87 LEETASALSFMLKNLGKPVVLTGSQRPSDEPSSDGPMNLLAALRVAASPaaRGPGVLVVFNDKLHRARRVTKTHTSSLDA 166

                          90       100
                  ....*....|....*....|..
gi 568978554   79 FCSPNLPPLATV-GADVTINRE 99
Cdd:pfam00710 167 FDSPNFGPLGEVdGGQVELYRE 188
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
294-433 1.20e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 97.33  E-value: 1.20e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978554 294 DTLQAFVELDRDLNLKDYSGQTPLHVAARRGHAAVVTMLLQRGADVDARNEDGQSPLLLAVRGRHQSVIGLLRAAGARLS 373
Cdd:COG0666  101 EIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVN 180

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978554 374 PQELEDvGTELCRLASRGDSEGLRAWWQAGADLGQPDYDGHCALQVAEAAGNADVVALLQ 433
Cdd:COG0666  181 ARDNDG-ETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 255-432 3.94e-18

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 87.23  E-value: 3.94e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978554 255 MLGCRVAWLLSMNGSQEADTMKDVLLPGLALAAAHAGDLDTLQAfvELDRDLNlkDYSGQTPLHVAARRGHAAVVTMLLQ 334
Cdd:PLN03192 504 LHDLNVGDLLGDNGGEHDDPNMASNLLTVASTGNAALLEELLKA--KLDPDIG--DSKGRTPLHIAASKGYEDCVLVLLK 579

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978554 335 RGADVDARNEDGQSPLLLAVRGRHQSVIGLLRAAGARLSPQELEDVgteLCRLASRGDSEGLRAWWQAGADLGQPDYDGH 414
Cdd:PLN03192 580 HACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAGDL---LCTAAKRNDLTAMKELLKQGLNVDSEDHQGA 656

                        170
                 ....*....|....*...
gi 568978554 415 CALQVAEAAGNADVVALL 432
Cdd:PLN03192 657 TALQVAMAEDHVDMVRLL 674
Ank_2 pfam12796
Ankyrin repeats (3 copies);
294-372 3.79e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 56.28  E-value: 3.79e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568978554  294 DTLQAFVELDRDLNLKDYSGQTPLHVAARRGHAAVVTMLLQRgADVDARNeDGQSPLLLAVRGRHQSVIGLLRAAGARL 372
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 ...
 313-341 2.86e-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: 2.86e-06
                           10        20
                   ....*....|....*....|....*....
gi 568978554   313 GQTPLHVAARRGHAAVVTMLLQRGADVDA 341
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 294-342 3.13e-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: 3.13e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978554 294 DTLQAFVEL-DRDLNLKD----------YSGQTPLHVAARRGHAAVVTMLLQRGADVDAR 342
Cdd:cd22196   64 DTISLLLDIaEKTGNLKEfvnaaytdsyYKGQTALHIAIERRNMHLVELLVQNGADVHAR 123
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 311-342 3.28e-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: 3.28e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 568978554  311 YSGQTPLHVAARRGHAAVVTMLLQRGADVDAR 342
Cdd:TIGR00870 126 TPGITALHLAAHRQNYEIVKLLLERGASVPAR 157
 
Name Accession Description Interval E-value
ansA PRK09461
cytoplasmic asparaginase I; Provisional
 1-243 3.64e-100

cytoplasmic asparaginase I; Provisional


Pssm-ID: 181876 [Multi-domain]  Cd Length: 335  Bit Score: 302.66  E-value: 3.64e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978554   1 MAFAASVLSFMLENLQKPVVLTGAQVPIHALWSDGRENLLGALLMAGQYVIPEVCLFFQNQLFRGNRTTKVDARRFAAFC 80
Cdd:PRK09461  94 MAYTASALSFMLENLGKPVIVTGSQIPLAELRSDGQTNLLNALYVAANYPINEVTLFFNNKLFRGNRTTKAHADGFDAFA 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978554  81 SPNLPPLATVGADVTINRELVRKACGKShLVVHSSMEPDVGLLRLYPGIPASLVRTFLQPPLKGVVMETFGSGNGPTKPD 160
Cdd:PRK09461 174 SPNLPPLLEAGIHIRRLNTPPAPHGEGE-LIVHPITPQPIGVVTIYPGISAEVVRNFLRQPVKALILRSYGVGNAPQNPA 252

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978554 161 LLQELRVAAEQGLIIVNCTHCLQGAVT-SDYASGMAMAGAGIVSGFDMTSEAALAKLSYVLGQPgLSLNDRKKLLAKDLR 239
Cdd:PRK09461 253 LLQELKEASERGIVVVNLTQCMSGKVNmGGYATGNALAHAGVISGADMTVEAALTKLHYLLSQE-LSTEEIRQAMQQNLR 331


                 ....
gi 568978554 240 GEMT 243
Cdd:PRK09461 332 GELT 335
Asparaginase smart00870
Asparaginase, found in various plant, animal and bacterial cells; Asparaginase catalyses the ...
 1-231 6.64e-79

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: 247.43  E-value: 6.64e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978554     1 MAFAASVLSFMLENLQKPVVLTGAQVPIHALWSDGRENLLGALLMAGQY--VIPEVCLFFQNQLFRGNRTTKVDARRFAA 78
Cdd:smart00870  90 LEETAYFLSLTLDSLDKPVVLTGAMRPATALSSDGPANLLDAVRVAASPeaRGRGVLVVFNDEIHRARRVTKTHTSRVDA 169

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978554    79 FCSPNLPPLATVGADVTINRELVRKACGKS---HLVVHSSMEPDVGLLRLYPGIPASLVRTFLQPPLKGVVMETFGSGNG 155
Cdd:smart00870 170 FQSPNFGPLGYVDEGGVVYYTRPTRRHTKRspfLLDLKDALLPKVAIVKAYPGMDAELLDALLDSGAKGLVLEGTGAGNV 249

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568978554   156 PtkPDLLQELRVAAEQGLIIVNCTHCLQGAVT-SDYASGMAMAGAGIVSGFDMTSEAALAKLSYVLGQpGLSLNDRK 231
Cdd:smart00870 250 P--PDLLEALKEALERGIPVVRTSRCLSGRVDpGYYATGRDLAKAGVISAGDLTPEKARIKLMLALGK-GLDPEEIR 323
AnsA COG0252
L-asparaginase/archaeal Glu-tRNAGln amidotransferase subunit D [Translation, ribosomal ...
 1-236 1.05e-78

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: 246.97  E-value: 1.05e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978554   1 MAFAASVLSFMLEnLQKPVVLTGAQVPIHALWSDGRENLLGALLMA--GQYVIPEVCLFFQNQLFRGNRTTKVDARRFAA 78
Cdd:COG0252   93 LEETAYALSLMLD-LPKPVVLTGAQRPADAPSSDGPANLLDAVRVAasPEARGRGVLVVFNDEIHRARRVTKTHTSRVDA 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978554  79 FCSPNLPPLATVGAD-VTINRELVRKacGKSHLVVHSSMEPDVGLLRLYPGIPASLVRTFLQPPLKGVVMETFGSGNGPt 157
Cdd:COG0252  172 FQSPNYGPLGEVDEGrVRFYRRPPRR--PESELDLAPALLPRVAILKLYPGMDPALLDALLAAGVKGIVLEGTGAGNVP- 248

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568978554 158 kPDLLQELRVAAEQGLIIVNCTHCLQGAVTSDYASGMAMAGAGIVSGFDMTSEAALAKLSYVLGQpGLSLNDRKKLLAK 236
Cdd:COG0252  249 -PALLPALKRAIERGVPVVVTSRCPEGRVNGVYGGGRDLAEAGVISGGDLTPEKARIKLMLALGQ-GLDPEEIRRLFET 325
L-asparaginase_I cd08963
Type I (cytosolic) bacterial L-asparaginase; Asparaginases (amidohydrolases, E.C. 3.5.1.1) are ...
 1-223 7.72e-74

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: 234.40  E-value: 7.72e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978554   1 MAFAASVLSFMLENLQKPVVLTGAQVPIHALWSDGRENLLGALLMAGQYVIPEVCLFFQNQLFRGNRTTKVDARRFAAFC 80
Cdd:cd08963   87 MAYTAAALSFLLQNLPKPVVLTGSQLPLGEPGSDARRNLRDALRAASSGSIRGVYVAFNGKLIRGTRARKVRTTSFDAFE 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978554  81 SPNLPPLATVGADVTINRELVRKACGKSHLvvHSSMEPDVGLLRLYPGIPASLVRTFLQPPLKGVVMETFGSGNGPTKPD 160
Cdd:cd08963  167 SINYPLLAEIGAGGLTLERLLQYEPLPSLF--YPDLDPNVFLLKLIPGLLPAILDALLEKYPRGLILEGFGAGNIPYDGD 244

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568978554 161 LLQELRVAAEQGLIIVNCTHCLQGAV-TSDYASGMAMAGAGIVSGFDMTSEAALAKLSYVLGQP 223
Cdd:cd08963  245 LLAALEEATARGKPVVVTTQCPYGGSdLSVYAVGQALLEAGVIPGGDMTTEAAVAKLMWLLGQT 308
Asparaginase pfam00710
Asparaginase, N-terminal; This is the N-terminal domain of this enzyme.
 1-99 9.02e-42

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


Pssm-ID: 459913 [Multi-domain]  Cd Length: 188  Bit Score: 146.53  E-value: 9.02e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978554    1 MAFAASVLSFMLENLQKPVVLTGAQVPIHALWSDGRENLLGALLMAGQY--VIPEVCLFFQNQLFRGNRTTKVDARRFAA 78
Cdd:pfam00710  87 LEETASALSFMLKNLGKPVVLTGSQRPSDEPSSDGPMNLLAALRVAASPaaRGPGVLVVFNDKLHRARRVTKTHTSSLDA 166

                          90       100
                  ....*....|....*....|..
gi 568978554   79 FCSPNLPPLATV-GADVTINRE 99
Cdd:pfam00710 167 FDSPNFGPLGEVdGGQVELYRE 188
GatD cd08962
GatD subunit of archaeal Glu-tRNA amidotransferase; GatD is involved in the alternative ...
 1-222 3.40e-36

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: 137.36  E-value: 3.40e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978554   1 MAFAASVLSFMLENLQKPVVLTGAQVPIHALWSDGRENLLGALLMAGQYvIPEV------------CLffqnqLFRGNRT 68
Cdd:cd08962  160 MHYTASALSFMLETLPVPVVFVGAQRSSDRPSSDAAMNLIAAVLVAASD-IAEVvvvmhgttsddyCL-----LHRGTRV 233

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978554  69 TKVDARRFAAFCSPNLPPLATV---GADVTINRELVRKacGKSHLVVHSSMEPDVGLLRLYPGIPASLVRTFLQPPLKGV 145
Cdd:cd08962  234 RKMHTSRRDAFQSINDEPLAKVdppGKIEKLSKDYRKR--GDEELELNDKLEEKVALIKFYPGMDPEIIDFYVDKGYKGI 311

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568978554 146 VMEtfGSGNGPTKPDLLQELRVAAEQGLIIVNCTHCLQGAVTSD-YASGMAMAGAGIVSGFDMTSEAALAKLSYVLGQ 222
Cdd:cd08962  312 VIE--GTGLGHVSEDLIPSIKKAIDDGIPVVMTSQCIYGRVNLNvYSTGRELLKAGVIPGEDMLPETAYVKLMWVLGN 387
PRK04183 PRK04183
Glu-tRNA(Gln) amidotransferase subunit GatD;
1-243 1.09e-34

Glu-tRNA(Gln) amidotransferase subunit GatD;


Pssm-ID: 235245 [Multi-domain]  Cd Length: 419  Bit Score: 133.82  E-value: 1.09e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978554   1 MAFAASVLSFMLeNLQKPVVLTGAQV----PIhalwSDGRENLLGALLMA----GQYVI-------PEVCLffqnqLFRG 65
Cdd:PRK04183 165 MHYTAAALSFML-KTPVPIVFVGAQRssdrPS----SDAAMNLICAVLAAtsdiAEVVVvmhgttsDDYCA-----LHRG 234

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978554  66 NRTTKVDARRFAAFCSPNLPPLATV----GADVTINRELVRKacGKSHLVVHSSMEPDVGLLRLYPGIPASLVRTFLQPP 141
Cdd:PRK04183 235 TRVRKMHTSRRDAFQSINDKPLAKVdykeGKIEFLRKDYRKR--GEKELELNDKLEEKVALIKFYPGMDPEILDFYVDKG 312

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978554 142 LKGVVMEtfGSGNGPTKPDLLQELRVAAEQGLIIVNCTHCLQGAVTSD-YASGMAMAGAGIVSGFDMTSEAALAKLSYVL 220
Cdd:PRK04183 313 YKGIVIE--GTGLGHVSTDLIPSIKRATDDGIPVVMTSQCLYGRVNMNvYSTGRDLLKAGVIPGEDMLPEVAYVKLMWVL 390

                        250       260
                 ....*....|....*....|...
gi 568978554 221 GQPGlSLNDRKKLLAKDLRGEMT 243
Cdd:PRK04183 391 GNTY-DLEEVRELMLTNLAGEIN 412
Asparaginase_C pfam17763
Glutaminase/Asparaginase C-terminal domain; This domain is found at the C-terminus of ...
 119-233 2.50e-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: 116.04  E-value: 2.50e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978554  119 DVGLLRLYPGIPASLVRTFLQPPLKGVVMETFGSGNGPtkPDLLQELRVAAEQGLIIVNCTHCLQGAVT-SDYASGMAMA 197
Cdd:pfam17763   1 RVDILYLYPGMDPELLDAALAAGAKGIVIAGFGAGNVP--SALLDALKEAVARGIPVVRSSRCGSGRVNlGYYETGRDLL 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 568978554  198 GAGIVSGFDMTSEAALAKLSYVLGQpGLSLNDRKKL 233
Cdd:pfam17763  79 EAGVISGGDLTPEKARIKLMLALGK-GLDPEEIREL 113
L-asparaginase_like cd00411
Bacterial L-asparaginases and related enzymes; Asparaginases (amidohydrolases, E.C. 3.5.1.1) ...
 2-222 1.34e-29

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: 117.61  E-value: 1.34e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978554   2 AFAASVLSFMLENlQKPVVLTGAQVPIHALWSDGRENLLGALLMA--GQYVIPEVCLFFQNQLFRGNRTTKVDARRFAAF 79
Cdd:cd00411   93 EETAYFLSLTLKN-DKPVVLVGAMRPSTAMSADGPFNLYNAVRVAkdKDSRGRGVLVVMNDKVHSGRDVSKTNTSGFDAF 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978554  80 CSPNLPPLATVGADVTI--NRELVRKACGKSHLVVHSSMEPDVGLLRLYPGIPASLVRTFLQPPLKGVVMEtfGSGNGPT 157
Cdd:cd00411  172 RSINYGPLGEIKDNKIYyqRKPARKHTDESEFDVSDIKSLPKVDIVYLYPGLSDDIYDALVDLGYKGIVLA--GTGNGSV 249

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568978554 158 KPDLLQELRVAAEQGLIIVNCTHCLQGAVTSDYASGMAMAGaGIVSGfDMTSEAALAKLSYVLGQ 222
Cdd:cd00411  250 PYDVFPVLSSASKRGVAVVRSSQVIYGGVDLNAEKVDLKAG-VIPAG-DLNPEKARVLLMWALTH 312
L-asparaginase_II cd08964
Type II (periplasmic) bacterial L-asparaginase; Asparaginases (amidohydrolases, E.C. 3.5.1.1) ...
 17-222 1.40e-25

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: 106.06  E-value: 1.40e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978554  17 KPVVLTGAQVPIHALWSDGRENLLGALLMAGQyviPE-----VCLFFQNQLFRGNRTTKVDARRFAAFCSPNLPPLATV- 90
Cdd:cd08964  106 KPVVLTGAMRPADAPSADGPANLLDAVRVAAS---PEargrgVLVVFNDEIHAARDVTKTHTTSLDAFASPGFGPLGYVd 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978554  91 GADVTINRELVRKACGKShlvVHSSMEPDVGLLRLYPGIPASLVRTFLQPPLKGVVMETFGSGNGPtkPDLLQELRVAAE 170
Cdd:cd08964  183 GGKVRFYRRPARPHTLPS---EFDDELPRVDIVYAYAGADGALLDAAVAAGAKGIVIAGFGAGNVP--PALVEALERAVA 257

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568978554 171 QGLIIVNCTHCLQGAVTSDYA--SGMAMAGAGIVSGFDMTSEAALAKLSYVLGQ 222
Cdd:cd08964  258 KGIPVVRSSRVGNGRVLPVYGygGGADLAEAGAIFAGDLSPQKARILLMLALAA 311
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
294-433 1.20e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 97.33  E-value: 1.20e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978554 294 DTLQAFVELDRDLNLKDYSGQTPLHVAARRGHAAVVTMLLQRGADVDARNEDGQSPLLLAVRGRHQSVIGLLRAAGARLS 373
Cdd:COG0666  101 EIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVN 180

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978554 374 PQELEDvGTELCRLASRGDSEGLRAWWQAGADLGQPDYDGHCALQVAEAAGNADVVALLQ 433
Cdd:COG0666  181 ARDNDG-ETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
305-433 7.05e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 95.41  E-value: 7.05e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978554 305 DLNLKDYSGQTPLHVAARRGHAAVVTMLLQRGADVDARNEDGQSPLLLAVRGRHQSVIGLLRAAGARLSPQELEDvGTEL 384
Cdd:COG0666  145 DVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDG-KTAL 223

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 568978554 385 CRLASRGDSEGLRAWWQAGADLGQPDYDGHCALQVAEAAGNADVVALLQ 433
Cdd:COG0666  224 DLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLL 272
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
227-432 2.82e-19

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 87.70  E-value: 2.82e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978554 227 LNDRKKLLAKDLRGEMTLPATDVLLQDGMLGCRVAWLLSMNGSQEADTMKDVLLPGLALAAAHAGDLDTLQAFVELDRDL 306
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978554 307 NLKDYSGQTPLHVAARRGHAAVVTMLLQRGADVDARNEDGQSPLLLAVRGRHQSVIGLLRAAGARLSPQELEDVgTELCR 386
Cdd:COG0666   81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGN-TPLHL 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 568978554 387 LASRGDSEGLRAWWQAGADLGQPDYDGHCALQVAEAAGNADVVALL 432
Cdd:COG0666  160 AAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 255-432 3.94e-18

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 87.23  E-value: 3.94e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978554 255 MLGCRVAWLLSMNGSQEADTMKDVLLPGLALAAAHAGDLDTLQAfvELDRDLNlkDYSGQTPLHVAARRGHAAVVTMLLQ 334
Cdd:PLN03192 504 LHDLNVGDLLGDNGGEHDDPNMASNLLTVASTGNAALLEELLKA--KLDPDIG--DSKGRTPLHIAASKGYEDCVLVLLK 579

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978554 335 RGADVDARNEDGQSPLLLAVRGRHQSVIGLLRAAGARLSPQELEDVgteLCRLASRGDSEGLRAWWQAGADLGQPDYDGH 414
Cdd:PLN03192 580 HACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAGDL---LCTAAKRNDLTAMKELLKQGLNVDSEDHQGA 656

                        170
                 ....*....|....*...
gi 568978554 415 CALQVAEAAGNADVVALL 432
Cdd:PLN03192 657 TALQVAMAEDHVDMVRLL 674
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 305-380 4.27e-12

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 68.00  E-value: 4.27e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978554 305 DLNLKDYSGQTPLHVAARRGHAAVVTMLLQRGADVDARNEDGQSPLLLAVRGRHQSVIGLLRA-------AGARLSPQEL 377
Cdd:PTZ00322 107 DPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRhsqchfeLGANAKPDSF 186


                 ...
gi 568978554 378 EDV 380
Cdd:PTZ00322 187 TGK 189
Ank_2 pfam12796
Ankyrin repeats (3 copies);
294-372 3.79e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 56.28  E-value: 3.79e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568978554  294 DTLQAFVELDRDLNLKDYSGQTPLHVAARRGHAAVVTMLLQRgADVDARNeDGQSPLLLAVRGRHQSVIGLLRAAGARL 372
Cdd:pfam12796  11 ELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADI 87
ansB PRK11096
L-asparaginase II; Provisional
 16-189 1.27e-09

L-asparaginase II; Provisional


Pssm-ID: 182958 [Multi-domain]  Cd Length: 347  Bit Score: 59.35  E-value: 1.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978554  16 QKPVVLTGAQVPIHALWSDGRENLLGALLMAG--QYVIPEVCLFFQNQLFRGNRTTKVDARRFAAFCSPNLPPLATV-GA 92
Cdd:PRK11096 127 DKPVVLVGAMRPSTAMSADGPLNLYNAVVTAAdkASANRGVLVAMNDTVLDGRDVTKTNTTDVQTFQSPNYGPLGYIhNG 206

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978554  93 DVTINRELVRKACGKSHL-VVHSSMEPDVGLLRLYPGIPASLVRTFLQPPLKGVVmeTFGSGNGPTKPDLLQELRVAAEQ 171
Cdd:PRK11096 207 KVDYQRTPARKHTTDTPFdVSKLNELPKVGIVYNYANASDLPAKALVDAGYDGIV--SAGVGNGNLYKTVFDTLATAAKN 284

                        170
                 ....*....|....*...
gi 568978554 172 GLIIVNCTHCLQGAVTSD 189
Cdd:PRK11096 285 GVAVVRSSRVPTGATTQD 302
Ank_5 pfam13857
Ankyrin repeats (many copies);
303-353 1.53e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 53.50  E-value: 1.53e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568978554  303 DRDLNLKDYSGQTPLHVAARRGHAAVVTMLLQRGADVDARNEDGQSPLLLA 353
Cdd:pfam13857   6 PIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
315-365 8.77e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.42  E-value: 8.77e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568978554  315 TPLHVAARRGHAAVVTMLLQRGADVDARNEDGQSPLLLAVRGRHQSVIGLL 365
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 313-344 9.81e-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: 47.67  E-value: 9.81e-08
                          10        20        30
                  ....*....|....*....|....*....|...
gi 568978554  313 GQTPLHVAA-RRGHAAVVTMLLQRGADVDARNE 344
Cdd:pfam00023   2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
Ank_2 pfam12796
Ankyrin repeats (3 copies);
317-365 1.26e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 49.34  E-value: 1.26e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 568978554  317 LHVAARRGHAAVVTMLLQRGADVDARNEDGQSPLLLAVRGRHQSVIGLL 365
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL 49
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 299-370 8.95e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 50.82  E-value: 8.95e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568978554 299 FVELDRDLNLKDYSGQTPLHVAARRGHAAVVTMLLQRGADVDARNEDGQSPLLLAVRGRHQSVIGLLRAAGA 370
Cdd:PHA03100 178 LLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
294-372 1.06e-06

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 49.95  E-value: 1.06e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568978554 294 DTLQAFVELDRDLNLKDYSGQTPLHVAARRGHAAVVTMLLQRGADVDARNEDGQSPLLLAVRGRHQSVIGLLRAAGARL 372
Cdd:COG0666  200 EIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLL 278
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 294-373 1.07e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 50.73  E-value: 1.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978554 294 DTLQAFVELDRDLNLKDYSGQTPLHVAARRGHAAVVTMLLQRGADVDARNEDGQSPLLLAVRGRHQSVIGLLRAAGARLS 373
Cdd:PHA02874 105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184
PHA03095 PHA03095
ankyrin-like protein; Provisional
 305-355 1.45e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 50.41  E-value: 1.45e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568978554 305 DLNLKDYSGQTPLHVAARRGHAAVVTMLLQRGADVDARNEDGQSPLLLAVR 355
Cdd:PHA03095 249 SINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVR 299
Ank_2 pfam12796
Ankyrin repeats (3 copies);
305-343 1.79e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 45.88  E-value: 1.79e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 568978554  305 DLNLKDYsGQTPLHVAARRGHAAVVTMLLQRGADVDARN 343
Cdd:pfam12796  54 DVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 313-341 2.86e-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: 2.86e-06
                           10        20
                   ....*....|....*....|....*....
gi 568978554   313 GQTPLHVAARRGHAAVVTMLLQRGADVDA 341
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 372-435 3.85e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.13  E-value: 3.85e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978554 372 LSPQELED------VGTELCRLASRGDSEGLRAWWQAGADLGQPDYDGHCALQVAEAAGNADVVALLQSF 435
Cdd:PTZ00322  68 LTTEEVIDpvvahmLTVELCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEF 137
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 313-434 1.30e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 47.29  E-value: 1.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978554 313 GQTPLHVAARRGHAAVVTMLLQRGADVDARNEDGQSPLLLAVRGRHQSVIGLLRAAGARLspqELEDV--GTELCRLASR 390
Cdd:PHA02875 102 GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACL---DIEDCcgCTPLIIAMAK 178

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 568978554 391 GDSEGLRAWWQAGADlgqPDYDGH--CALQVAEAAGN--ADVVALLQS 434
Cdd:PHA02875 179 GDIAICKMLLDSGAN---IDYFGKngCVAALCYAIENnkIDIVRLFIK 223
PHA03095 PHA03095
ankyrin-like protein; Provisional
 294-373 1.60e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.94  E-value: 1.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978554 294 DTLQAFVELDRDLNLKDYSGQTPLHVAAR--RGHAAVVTMLLQRGADVDARNEDGQSPLLLAVRGRHQSV--IGLLRAAG 369
Cdd:PHA03095  98 DVIKLLIKAGADVNAKDKVGRTPLHVYLSgfNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVelLRLLIDAG 177


                 ....
gi 568978554 370 ARLS 373
Cdd:PHA03095 178 ADVY 181
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 313-341 2.25e-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: 41.09  E-value: 2.25e-05
                          10        20
                  ....*....|....*....|....*....
gi 568978554  313 GQTPLHVAARRGHAAVVTMLLQRGADVDA 341
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 305-362 2.71e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.60  E-value: 2.71e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568978554 305 DLNLKDYSGQTPLHVAARRGHAAVVTMLLQRGADVDARNEDGQSPLLLAVRGRHQSVI 362
Cdd:PHA02876 170 DVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTI 227
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 294-342 3.13e-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: 3.13e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978554 294 DTLQAFVEL-DRDLNLKD----------YSGQTPLHVAARRGHAAVVTMLLQRGADVDAR 342
Cdd:cd22196   64 DTISLLLDIaEKTGNLKEfvnaaytdsyYKGQTALHIAIERRNMHLVELLVQNGADVHAR 123
Ank_4 pfam13637
Ankyrin repeats (many copies);
294-333 4.59e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 40.72  E-value: 4.59e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 568978554  294 DTLQAFVELDRDLNLKDYSGQTPLHVAARRGHAAVVTMLL 333
Cdd:pfam13637  15 ELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 306-432 5.10e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 45.34  E-value: 5.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978554 306 LNLKDYSGQTPLHVAARRGHAAVVTMLLQRGADVDARNEDGQSPLLLAVRGRHQSVIGLLRAAGARLSPQELEDVGTELC 385
Cdd:PHA02874  28 INISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSILPIPCIEKDMI 107

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568978554 386 RL----------------------ASRGDSEGLRAWWQAGADLGQPDYDGHCALQVAEAAGNADVVALL 432
Cdd:PHA02874 108 KTildcgidvnikdaelktflhyaIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLL 176
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 294-356 5.65e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.44  E-value: 5.65e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568978554 294 DTLQAFVELDRDLNLKDYSGQTPLHVAARRGHAAVVTMLLQRGADVDARNEDGQSPLLLAVRG 356
Cdd:PHA02876 356 DIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCG 418
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 295-372 6.06e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.44  E-value: 6.06e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568978554 295 TLQAFVELDRDLNLKDYSGQTPLHVAARRG-HAAVVTMLLQRGADVDARNEDGQSPLLLAVrgRHQSVIGLLRAAGARL 372
Cdd:PHA02876 424 SVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIAL--EYHGIVNILLHYGAEL 500
PHA03095 PHA03095
ankyrin-like protein; Provisional
 300-373 7.76e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 45.02  E-value: 7.76e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568978554 300 VELDRDLNLKDYSGQTPLHVAARRG--HAAVVTMLLQRGADVDARNEDGQSPLLLAVRGRHQSVIGLLRAAGARLS 373
Cdd:PHA03095 209 IRAGCDPAATDMLGNTPLHSMATGSscKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADIN 284
PHA03095 PHA03095
ankyrin-like protein; Provisional
 294-370 1.20e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 44.25  E-value: 1.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978554 294 DTLQAFVELDRDLNLKDYSGQTPLHVAARRGH-AAVVTMLLQRGADVDARNEDGQSPLLLAVRGR--HQSVIGLLRAAGA 370
Cdd:PHA03095  64 DIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAGADVNAKDKVGRTPLHVYLSGFniNPKVIRLLLRKGA 143
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 294-355 1.66e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 43.80  E-value: 1.66e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568978554 294 DTLQAFVELDRDLNLKDYSGQTPLHVAARRGHAAVVTMLLQRGADVDARNEDGQSPLLLAVR 355
Cdd:PHA02874 138 ESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAE 199
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 294-365 2.20e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 43.41  E-value: 2.20e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568978554 294 DTLQAFVELDRDLNLKDYSGQTPLHVAARRGHAAVVTMLLQRGADVDARNEDGQSPLLLAVRgRHQSVIGLL 365
Cdd:PHA02874 171 DIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII-HNRSAIELL 241
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 311-342 3.28e-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: 3.28e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 568978554  311 YSGQTPLHVAARRGHAAVVTMLLQRGADVDAR 342
Cdd:TIGR00870 126 TPGITALHLAAHRQNYEIVKLLLERGASVPAR 157
PHA02917 PHA02917
ankyrin-like protein; Provisional
 304-354 5.33e-04

ankyrin-like protein; Provisional


Pssm-ID: 165231 [Multi-domain]  Cd Length: 661  Bit Score: 42.29  E-value: 5.33e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568978554 304 RDLNLKDYSGQTPLHVAARRGHAAVVTMLLQRGADVDARNEDGQSPLLLAV 354
Cdd:PHA02917 443 KDINMIDKRGETLLHKAVRYNKQSLVSLLLESGSDVNIRSNNGYTCIAIAI 493
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 294-394 6.73e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 42.16  E-value: 6.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978554 294 DTLQAFVELDRDLNLKDYSGQTPLHVAARRGHAAVVTMLLQRGADVDARN-EDGQSPLLL--AVRGRHQSVIGLLRAAGA 370
Cdd:PLN03192 636 TAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANtDDDFSPTELreLLQKRELGHSITIVDSVP 715

                         90       100
                 ....*....|....*....|....
gi 568978554 371 RLSPQELEDVGTELCRLASRGDSE 394
Cdd:PLN03192 716 ADEPDLGRDGGSRPGRLQGTSSDN 739
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 295-353 1.04e-03

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 41.67  E-value: 1.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978554 295 TLQAFVE----LDRDLNL----KDYSGQTPLHVAARRGHAAVVTMLLQRGADVDAR----------NED----GQSPLLL 352
Cdd:cd22194  115 ILLAFAEengiLDRFINAeyteEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHakgvffnpkyKHEgfyfGETPLAL 194


                 .
gi 568978554 353 A 353
Cdd:cd22194  195 A 195
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 294-344 1.58e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 40.80  E-value: 1.58e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568978554 294 DTLQAFVELDRDLNLKDYSGQTPLHVAARRGHAAVVTMLLQRGADVDARNE 344
Cdd:PHA03100 206 EFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256
PHA02741 PHA02741
hypothetical protein; Provisional
 296-366 2.25e-03

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 38.87  E-value: 2.25e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568978554 296 LQAFVELDRDLNLKD-YSGQTPLHVAA-RRGHAAVVTMLLQRGADVDARNEDGQSPLLLAVRGRHQSVIGLLR 366
Cdd:PHA02741  80 IDHLIELGADINAQEmLEGDTALHLAAhRRDHDLAEWLCCQPGIDLHFCNADNKSPFELAIDNEDVAMMQILR 152
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 307-375 2.48e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 40.25  E-value: 2.48e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978554 307 NLKDYSGQTPLHVAARRGHAAVVTMLLQRGADVDARNEDGQSPLLLAV-RGRHQSVIGLLRAAGARLSPQ 375
Cdd:PHA02878 195 NIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVgYCKDYDILKLLLEHGVDVNAK 264
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 311-379 3.52e-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: 3.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978554 311 YSGQTPLHVAARRGHAAVVTMLLQRGADVDARNED-------------GQSPLLLAVRGRHQSVIGLLRAAGARLSPQEL 377
Cdd:cd21882   71 YQGQTALHIAIENRNLNLVRLLVENGADVSARATGrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQPAALEA 150


                 ..
gi 568978554 378 ED 379
Cdd:cd21882  151 QD 152
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 306-370 4.66e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 39.28  E-value: 4.66e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568978554 306 LNLKDYSGQTPLHVAARRGH-AAVVTMLLQRGADVDARNEDGQSPL-LLAVRGRHQSVIGLLRAAGA 370
Cdd:PHA02876 266 VNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLyLMAKNGYDTENIRTLIMLGA 332
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 311-387 5.15e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 39.47  E-value: 5.15e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568978554 311 YSGQTPLHVAARRGHAAVVTMLLQRGADVDARNEDGQSPLLLAVRGRHQSVIGLLRAAGARLSPQELED--VGTELCRL 387
Cdd:PLN03192 620 HAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDDdfSPTELREL 698
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 305-370 5.67e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 39.09  E-value: 5.67e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568978554 305 DLNLKD-YSGQTPLHVAARRGHAAVVTMLLQRGADVDARNEDGQSPLLLAVRGRHQSVIGLLRAAGA 370
Cdd:PHA02878 159 DINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA 225
PHA03095 PHA03095
ankyrin-like protein; Provisional
 294-432 8.43e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 38.47  E-value: 8.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978554 294 DTLQAFVELDRDLNLKDYSGQTPLHVAARRGH---AAVVTMLLQRGADVDARNEDGQSPLLLAVrgRHQSVIGLLR---A 367
Cdd:PHA03095  28 EEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYL--YNATTLDVIKlliK 105

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568978554 368 AGARLspQELEDVGTELCRLASRGDS---EGLRAWWQAGADLGQPDYDGHCALQVAEAAGNADV--VALL 432
Cdd:PHA03095 106 AGADV--NAKDKVGRTPLHVYLSGFNinpKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVelLRLL 173
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 294-357 8.68e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 38.32  E-value: 8.68e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568978554 294 DTLQAFVELDRDLNLKDY-SGQTPLHVAARrgHAAVVTMLLQRGADVDARNEDGQSPLLLAVRGR 357
Cdd:PHA02878 249 DILKLLLEHGVDVNAKSYiLGLTALHSSIK--SERKLKLLLEYGADINSLNSYKLTPLSSAVKQY 311
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 294-370 9.89e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 38.32  E-value: 9.89e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568978554 294 DTLQAFVELDRDLNLKDYSGQTPLHVAARR-GHAAVVTMLLQRGADVDARNE-DGQSPLLLAVRGrhQSVIGLLRAAGA 370
Cdd:PHA02878 215 PIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIKS--ERKLKLLLEYGA 291
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH