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Conserved domains on  [gi|1034587000|ref|XP_016876762|]
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60 kDa lysophospholipase isoform X10 [Homo sapiens]

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) ...
 102-389 2.31e-120

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: 359.67  E-value: 2.31e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 102 YTVLECQPLFDSSDMTIAEWVCLAQTIKRHYEQYHGFVVIHGTDTMAFAASMLSFMLENLQKTVILTGAQVPIHALWSDG 181
Cdd:PRK09461   49 FTIHEYTPLIDSSDMTPEDWQHIADDIKANYDDYDGFVILHGTDTMAYTASALSFMLENLGKPVIVTGSQIPLAELRSDG 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 182 RENLLGALLMAGQYVIPEVCLFFQNQLFRGNRATKVDARRFAAFCSPNLLPLATVGADITINRELVRKVDGKAgLVVHSS 261
Cdd:PRK09461  129 QTNLLNALYVAANYPINEVTLFFNNKLFRGNRTTKAHADGFDAFASPNLPPLLEAGIHIRRLNTPPAPHGEGE-LIVHPI 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 262 MEQDVGLLRLYPGIPAALVRAFLQPPLKGVVMETFGSGNGPTKPDLLQELRVATERGLVIVNCTHCLQGAVTTD-YAAGM 340
Cdd:PRK09461  208 TPQPIGVVTIYPGISAEVVRNFLRQPVKALILRSYGVGNAPQNPALLQELKEASERGIVVVNLTQCMSGKVNMGgYATGN 287

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1034587000 341 AMAGAGVISGFDMTSEAALAKLSYVLGQPgLSLDVRKELLTKDLRGEMT 389
Cdd:PRK09461  288 ALAHAGVISGADMTVEAALTKLHYLLSQE-LSTEEIRQAMQQNLRGELT 335
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
412-592 4.08e-28

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 114.28  E-value: 4.08e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 412 LLSLSGSQEADALRNALVPSLACAAAHAGDVEALQALVELGSDLGLVDFNGQTPLHAAARGGHTEAVTMLLQRGVDVNTR 491
Cdd:COG0666    70 ALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQ 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 492 DTDGFSPLLLAVRGRHPGVIGLLREAGASLSTQELEEaGTELCRLAYRADLEGLQVWWQAGADLGQPGYDGHSALHVAEA 571
Cdd:COG0666   150 DNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDG-ETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAE 228

                         170       180
                  ....*....|....*....|.
gi 1034587000 572 AGNLAVVAFLQSLEGAVGAQA 592
Cdd:COG0666   229 NGNLEIVKLLLEAGADLNAKD 249
 
Name Accession Description Interval E-value
ansA PRK09461
cytoplasmic asparaginase I; Provisional
 102-389 2.31e-120

cytoplasmic asparaginase I; Provisional


Pssm-ID: 181876 [Multi-domain]  Cd Length: 335  Bit Score: 359.67  E-value: 2.31e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 102 YTVLECQPLFDSSDMTIAEWVCLAQTIKRHYEQYHGFVVIHGTDTMAFAASMLSFMLENLQKTVILTGAQVPIHALWSDG 181
Cdd:PRK09461   49 FTIHEYTPLIDSSDMTPEDWQHIADDIKANYDDYDGFVILHGTDTMAYTASALSFMLENLGKPVIVTGSQIPLAELRSDG 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 182 RENLLGALLMAGQYVIPEVCLFFQNQLFRGNRATKVDARRFAAFCSPNLLPLATVGADITINRELVRKVDGKAgLVVHSS 261
Cdd:PRK09461  129 QTNLLNALYVAANYPINEVTLFFNNKLFRGNRTTKAHADGFDAFASPNLPPLLEAGIHIRRLNTPPAPHGEGE-LIVHPI 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 262 MEQDVGLLRLYPGIPAALVRAFLQPPLKGVVMETFGSGNGPTKPDLLQELRVATERGLVIVNCTHCLQGAVTTD-YAAGM 340
Cdd:PRK09461  208 TPQPIGVVTIYPGISAEVVRNFLRQPVKALILRSYGVGNAPQNPALLQELKEASERGIVVVNLTQCMSGKVNMGgYATGN 287

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1034587000 341 AMAGAGVISGFDMTSEAALAKLSYVLGQPgLSLDVRKELLTKDLRGEMT 389
Cdd:PRK09461  288 ALAHAGVISGADMTVEAALTKLHYLLSQE-LSTEEIRQAMQQNLRGELT 335
Asparaginase smart00870
Asparaginase, found in various plant, animal and bacterial cells; Asparaginase catalyses the ...
 101-377 3.96e-94

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: 291.73  E-value: 3.96e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000  101 LYTVLECQPLFDSSDMTIAEWVCLAQTIK--RHYEQYHGFVVIHGTDTMAFAASMLSFMLENLQKTVILTGAQVPIHALW 178
Cdd:smart00870  42 DDIEVEQVANIDSSNMTPEDWLKLAKRINeaLADDGYDGVVVTHGTDTLEETAYFLSLTLDSLDKPVVLTGAMRPATALS 121

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000  179 SDGRENLLGALLMAGQY--VIPEVCLFFQNQLFRGNRATKVDARRFAAFCSPNLLPLATVGADITINRELVRKVDGKAG- 255
Cdd:smart00870 122 SDGPANLLDAVRVAASPeaRGRGVLVVFNDEIHRARRVTKTHTSRVDAFQSPNFGPLGYVDEGGVVYYTRPTRRHTKRSp 201

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000  256 --LVVHSSMEQDVGLLRLYPGIPAALVRAFLQPPLKGVVMETFGSGNGPtkPDLLQELRVATERGLVIVNCTHCLQGAVT 333
Cdd:smart00870 202 flLDLKDALLPKVAIVKAYPGMDAELLDALLDSGAKGLVLEGTGAGNVP--PDLLEALKEALERGIPVVRTSRCLSGRVD 279

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1034587000  334 TD-YAAGMAMAGAGVISGFDMTSEAALAKLSYVLGQpGLSLDVRK 377
Cdd:smart00870 280 PGyYATGRDLAKAGVISAGDLTPEKARIKLMLALGK-GLDPEEIR 323
AnsA COG0252
L-asparaginase/archaeal Glu-tRNAGln amidotransferase subunit D [Translation, ribosomal ...
 112-382 1.34e-90

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: 282.79  E-value: 1.34e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 112 DSSDMTIAEWVCLAQTIKRHY-EQYHGFVVIHGTDTMAFAASMLSFMLEnLQKTVILTGAQVPIHALWSDGRENLLGALL 190
Cdd:COG0252    57 DSSNMTPADWLALARRIEEALaDDYDGVVVTHGTDTLEETAYALSLMLD-LPKPVVLTGAQRPADAPSSDGPANLLDAVR 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 191 MA--GQYVIPEVCLFFQNQLFRGNRATKVDARRFAAFCSPNLLPLATVGAD-ITINRELVRKVDGKagLVVHSSMEQDVG 267
Cdd:COG0252   136 VAasPEARGRGVLVVFNDEIHRARRVTKTHTSRVDAFQSPNYGPLGEVDEGrVRFYRRPPRRPESE--LDLAPALLPRVA 213

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 268 LLRLYPGIPAALVRAFLQPPLKGVVMETFGSGNGPtkPDLLQELRVATERGLVIVNCTHCLQGAVTTDYAAGMAMAGAGV 347
Cdd:COG0252   214 ILKLYPGMDPALLDALLAAGVKGIVLEGTGAGNVP--PALLPALKRAIERGVPVVVTSRCPEGRVNGVYGGGRDLAEAGV 291

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1034587000 348 ISGFDMTSEAALAKLSYVLGQpGLSLDVRKELLTK 382
Cdd:COG0252   292 ISGGDLTPEKARIKLMLALGQ-GLDPEEIRRLFET 325
L-asparaginase_I cd08963
Type I (cytosolic) bacterial L-asparaginase; Asparaginases (amidohydrolases, E.C. 3.5.1.1) are ...
 105-369 6.87e-88

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: 275.23  E-value: 6.87e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 105 LECQPLFDSSDMTIAEWVCLAQTIKRHYEQYHGFVVIHGTDTMAFAASMLSFMLENLQKTVILTGAQVPIHALWSDGREN 184
Cdd:cd08963    45 VEQLPNIDSSNMTPEDWLRIARAIAENYDGYDGFVITHGTDTMAYTAAALSFLLQNLPKPVVLTGSQLPLGEPGSDARRN 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 185 LLGALLMAGQYVIPEVCLFFQNQLFRGNRATKVDARRFAAFCSPNLLPLATVGADITINRELVRKVDGKAGLvvHSSMEQ 264
Cdd:cd08963   125 LRDALRAASSGSIRGVYVAFNGKLIRGTRARKVRTTSFDAFESINYPLLAEIGAGGLTLERLLQYEPLPSLF--YPDLDP 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 265 DVGLLRLYPGIPAALVRAFLQPPLKGVVMETFGSGNGPTKPDLLQELRVATERGLVIVNCTHCLQGAVTTD-YAAGMAMA 343
Cdd:cd08963   203 NVFLLKLIPGLLPAILDALLEKYPRGLILEGFGAGNIPYDGDLLAALEEATARGKPVVVTTQCPYGGSDLSvYAVGQALL 282

                         250       260
                  ....*....|....*....|....*.
gi 1034587000 344 GAGVISGFDMTSEAALAKLSYVLGQP 369
Cdd:cd08963   283 EAGVIPGGDMTTEAAVAKLMWLLGQT 308
asnASE_I TIGR00519
L-asparaginase, type I; Two related families of asparaginase are designated type I and type II ...
 109-390 5.44e-79

L-asparaginase, type I; Two related families of asparaginase are designated type I and type II according to the terminology in E. coli, which has both: L-asparaginase I is a low-affinity enzyme found in the cytoplasm, while L-asparaginase II is a high-affinity secreted enzyme synthesized with a cleavable signal sequence. This model describes L-asparaginases related to type I of E. coli. Archaeal putative asparaginases are of this type but contain an extra ~ 80 residues in a conserved N-terminal region. These archaeal homologs are included in this model.


Pssm-ID: 129610 [Multi-domain]  Cd Length: 336  Bit Score: 252.82  E-value: 5.44e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 109 PLFDSSDMTIAEWVCLAQTIKRHYEQYHGFVVIHGTDTMAFAASMLSFMLENlQKTVILTGAQVPIHALWSDGRENLLGA 188
Cdd:TIGR00519  52 MNILSENMKPEYWVEIAEAVKKEYDDYDGFVITHGTDTMAYTAAALSFMLET-PKPVVFTGAQRSSDRPSSDAALNLLCA 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 189 LLMAGQYV------IPEVCLFFQNQLFRGNRATKVDARRFAAFCSPNLLPLATVGADITINRELVRKVDGKAGLVVHSSM 262
Cdd:TIGR00519 131 VRAATEYIaevtvcMHGVTLDFNCRLHRGVKVRKAHTSRRDAFASINAPPLAEINPDGIEYLNEVYRPRGEDELEVHDRL 210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 263 EQDVGLLRLYPGIPAALVRAFLQPPLKGVVMETFGSGNGPTkpDLLQELRVATERGLVIVNCTHCLQGAVTTD-YAAGMA 341
Cdd:TIGR00519 211 EEKVALIKIYPGISPDIIRNYLSKGYKGIVIEGTGLGHAPQ--NKLQELQEASDRGVVVVMTTQCLNGRVNMNvYSTGRR 288

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1034587000 342 MAGAGVISGFDMTSEAALAKLSYVLGQPgLSLDVRKELLTKDLRGEMTP 390
Cdd:TIGR00519 289 LLQAGVIGGEDMLPEVALVKLMWLLGQY-SDPEEAKKMMSKNIAGEIEP 336
Asparaginase pfam00710
Asparaginase, N-terminal; This is the N-terminal domain of this enzyme.
 106-245 9.23e-62

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


Pssm-ID: 459913 [Multi-domain]  Cd Length: 188  Bit Score: 202.38  E-value: 9.23e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 106 ECQPLFDSSDMTIAEWVCLAQTIKRHYEQYHGFVVIHGTDTMAFAASMLSFMLENLQKTVILTGAQVPIHALWSDGRENL 185
Cdd:pfam00710  46 EQVANIDSSNMTPADWLRLARRIAEALDDYDGVVVTHGTDTLEETASALSFMLKNLGKPVVLTGSQRPSDEPSSDGPMNL 125

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034587000 186 LGALLMAGQY--VIPEVCLFFQNQLFRGNRATKVDARRFAAFCSPNLLPLATV-GADITINRE 245
Cdd:pfam00710 126 LAALRVAASPaaRGPGVLVVFNDKLHRARRVTKTHTSSLDAFDSPNFGPLGEVdGGQVELYRE 188
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
412-592 4.08e-28

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 114.28  E-value: 4.08e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 412 LLSLSGSQEADALRNALVPSLACAAAHAGDVEALQALVELGSDLGLVDFNGQTPLHAAARGGHTEAVTMLLQRGVDVNTR 491
Cdd:COG0666    70 ALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQ 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 492 DTDGFSPLLLAVRGRHPGVIGLLREAGASLSTQELEEaGTELCRLAYRADLEGLQVWWQAGADLGQPGYDGHSALHVAEA 571
Cdd:COG0666   150 DNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDG-ETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAE 228

                         170       180
                  ....*....|....*....|.
gi 1034587000 572 AGNLAVVAFLQSLEGAVGAQA 592
Cdd:COG0666   229 NGNLEIVKLLLEAGADLNAKD 249
Ank_2 pfam12796
Ankyrin repeats (3 copies);
436-524 4.99e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 76.31  E-value: 4.99e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 436 AAHAGDVEALQALVELGSDLGLVDFNGQTPLHAAARGGHTEAVTMLLQRgVDVNTRDtDGFSPLLLAVRGRHPGVIGLLR 515
Cdd:pfam12796   4 AAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKLLL 81


                  ....*....
gi 1034587000 516 EAGASLSTQ 524
Cdd:pfam12796  82 EKGADINVK 90
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 435-581 3.67e-14

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 75.67  E-value: 3.67e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 435 AAAHAGDVEALQALVELGSDLGLVDFNGQTPLHAAARGGHTEAVTMLLQRGVDVNTRDTDGFSPLLLAVRGRHPGVIGLL 514
Cdd:PLN03192  531 TVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL 610

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034587000 515 REAgASLSTQELeeAGTELCRLAYRADLEGLQVWWQAGADLGQPGYDGHSALHVAEAAGNLAVVAFL 581
Cdd:PLN03192  611 YHF-ASISDPHA--AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLL 674
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 461-489 1.12e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.19  E-value: 1.12e-05
                           10        20
                   ....*....|....*....|....*....
gi 1034587000  461 NGQTPLHAAARGGHTEAVTMLLQRGVDVN 489
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 462-537 1.55e-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: 44.69  E-value: 1.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 462 GQTPLHAAARGGHTEAVTMLLQRGVDVNTR----------DTDGF----SPLLLAVRGRHPGVIGLLREAGASLSTQelE 527
Cdd:TIGR00870 128 GITALHLAAHRQNYEIVKLLLERGASVPARacgdffvksqGVDSFyhgeSPLNAAACLGSPSIVALLSEDPADILTA--D 205

                          90
                  ....*....|
gi 1034587000 528 EAGTELCRLA 537
Cdd:TIGR00870 206 SLGNTLLHLL 215
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 436-525 1.03e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 41.92  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 436 AAHAGDVEALQALVE---------LGSDLglvdFNGQTPLHAAARGGHTEAVTMLLQRGVDVNT-RDTDGF---SPLLLA 502
Cdd:cd22192    58 AALYDNLEAAVVLMEaapelvnepMTSDL----YQGETALHIAVVNQNLNLVRELIARGADVVSpRATGTFfrpGPKNLI 133

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1034587000 503 VRGRHP----------GVIGLLREAGASLSTQE 525
Cdd:cd22192   134 YYGEHPlsfaacvgneEIVRLLIEHGADIRAQD 166
 
Name Accession Description Interval E-value
ansA PRK09461
cytoplasmic asparaginase I; Provisional
 102-389 2.31e-120

cytoplasmic asparaginase I; Provisional


Pssm-ID: 181876 [Multi-domain]  Cd Length: 335  Bit Score: 359.67  E-value: 2.31e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 102 YTVLECQPLFDSSDMTIAEWVCLAQTIKRHYEQYHGFVVIHGTDTMAFAASMLSFMLENLQKTVILTGAQVPIHALWSDG 181
Cdd:PRK09461   49 FTIHEYTPLIDSSDMTPEDWQHIADDIKANYDDYDGFVILHGTDTMAYTASALSFMLENLGKPVIVTGSQIPLAELRSDG 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 182 RENLLGALLMAGQYVIPEVCLFFQNQLFRGNRATKVDARRFAAFCSPNLLPLATVGADITINRELVRKVDGKAgLVVHSS 261
Cdd:PRK09461  129 QTNLLNALYVAANYPINEVTLFFNNKLFRGNRTTKAHADGFDAFASPNLPPLLEAGIHIRRLNTPPAPHGEGE-LIVHPI 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 262 MEQDVGLLRLYPGIPAALVRAFLQPPLKGVVMETFGSGNGPTKPDLLQELRVATERGLVIVNCTHCLQGAVTTD-YAAGM 340
Cdd:PRK09461  208 TPQPIGVVTIYPGISAEVVRNFLRQPVKALILRSYGVGNAPQNPALLQELKEASERGIVVVNLTQCMSGKVNMGgYATGN 287

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1034587000 341 AMAGAGVISGFDMTSEAALAKLSYVLGQPgLSLDVRKELLTKDLRGEMT 389
Cdd:PRK09461  288 ALAHAGVISGADMTVEAALTKLHYLLSQE-LSTEEIRQAMQQNLRGELT 335
Asparaginase smart00870
Asparaginase, found in various plant, animal and bacterial cells; Asparaginase catalyses the ...
 101-377 3.96e-94

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: 291.73  E-value: 3.96e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000  101 LYTVLECQPLFDSSDMTIAEWVCLAQTIK--RHYEQYHGFVVIHGTDTMAFAASMLSFMLENLQKTVILTGAQVPIHALW 178
Cdd:smart00870  42 DDIEVEQVANIDSSNMTPEDWLKLAKRINeaLADDGYDGVVVTHGTDTLEETAYFLSLTLDSLDKPVVLTGAMRPATALS 121

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000  179 SDGRENLLGALLMAGQY--VIPEVCLFFQNQLFRGNRATKVDARRFAAFCSPNLLPLATVGADITINRELVRKVDGKAG- 255
Cdd:smart00870 122 SDGPANLLDAVRVAASPeaRGRGVLVVFNDEIHRARRVTKTHTSRVDAFQSPNFGPLGYVDEGGVVYYTRPTRRHTKRSp 201

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000  256 --LVVHSSMEQDVGLLRLYPGIPAALVRAFLQPPLKGVVMETFGSGNGPtkPDLLQELRVATERGLVIVNCTHCLQGAVT 333
Cdd:smart00870 202 flLDLKDALLPKVAIVKAYPGMDAELLDALLDSGAKGLVLEGTGAGNVP--PDLLEALKEALERGIPVVRTSRCLSGRVD 279

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1034587000  334 TD-YAAGMAMAGAGVISGFDMTSEAALAKLSYVLGQpGLSLDVRK 377
Cdd:smart00870 280 PGyYATGRDLAKAGVISAGDLTPEKARIKLMLALGK-GLDPEEIR 323
AnsA COG0252
L-asparaginase/archaeal Glu-tRNAGln amidotransferase subunit D [Translation, ribosomal ...
 112-382 1.34e-90

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: 282.79  E-value: 1.34e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 112 DSSDMTIAEWVCLAQTIKRHY-EQYHGFVVIHGTDTMAFAASMLSFMLEnLQKTVILTGAQVPIHALWSDGRENLLGALL 190
Cdd:COG0252    57 DSSNMTPADWLALARRIEEALaDDYDGVVVTHGTDTLEETAYALSLMLD-LPKPVVLTGAQRPADAPSSDGPANLLDAVR 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 191 MA--GQYVIPEVCLFFQNQLFRGNRATKVDARRFAAFCSPNLLPLATVGAD-ITINRELVRKVDGKagLVVHSSMEQDVG 267
Cdd:COG0252   136 VAasPEARGRGVLVVFNDEIHRARRVTKTHTSRVDAFQSPNYGPLGEVDEGrVRFYRRPPRRPESE--LDLAPALLPRVA 213

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 268 LLRLYPGIPAALVRAFLQPPLKGVVMETFGSGNGPtkPDLLQELRVATERGLVIVNCTHCLQGAVTTDYAAGMAMAGAGV 347
Cdd:COG0252   214 ILKLYPGMDPALLDALLAAGVKGIVLEGTGAGNVP--PALLPALKRAIERGVPVVVTSRCPEGRVNGVYGGGRDLAEAGV 291

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1034587000 348 ISGFDMTSEAALAKLSYVLGQpGLSLDVRKELLTK 382
Cdd:COG0252   292 ISGGDLTPEKARIKLMLALGQ-GLDPEEIRRLFET 325
L-asparaginase_I cd08963
Type I (cytosolic) bacterial L-asparaginase; Asparaginases (amidohydrolases, E.C. 3.5.1.1) are ...
 105-369 6.87e-88

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: 275.23  E-value: 6.87e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 105 LECQPLFDSSDMTIAEWVCLAQTIKRHYEQYHGFVVIHGTDTMAFAASMLSFMLENLQKTVILTGAQVPIHALWSDGREN 184
Cdd:cd08963    45 VEQLPNIDSSNMTPEDWLRIARAIAENYDGYDGFVITHGTDTMAYTAAALSFLLQNLPKPVVLTGSQLPLGEPGSDARRN 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 185 LLGALLMAGQYVIPEVCLFFQNQLFRGNRATKVDARRFAAFCSPNLLPLATVGADITINRELVRKVDGKAGLvvHSSMEQ 264
Cdd:cd08963   125 LRDALRAASSGSIRGVYVAFNGKLIRGTRARKVRTTSFDAFESINYPLLAEIGAGGLTLERLLQYEPLPSLF--YPDLDP 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 265 DVGLLRLYPGIPAALVRAFLQPPLKGVVMETFGSGNGPTKPDLLQELRVATERGLVIVNCTHCLQGAVTTD-YAAGMAMA 343
Cdd:cd08963   203 NVFLLKLIPGLLPAILDALLEKYPRGLILEGFGAGNIPYDGDLLAALEEATARGKPVVVTTQCPYGGSDLSvYAVGQALL 282

                         250       260
                  ....*....|....*....|....*.
gi 1034587000 344 GAGVISGFDMTSEAALAKLSYVLGQP 369
Cdd:cd08963   283 EAGVIPGGDMTTEAAVAKLMWLLGQT 308
asnASE_I TIGR00519
L-asparaginase, type I; Two related families of asparaginase are designated type I and type II ...
 109-390 5.44e-79

L-asparaginase, type I; Two related families of asparaginase are designated type I and type II according to the terminology in E. coli, which has both: L-asparaginase I is a low-affinity enzyme found in the cytoplasm, while L-asparaginase II is a high-affinity secreted enzyme synthesized with a cleavable signal sequence. This model describes L-asparaginases related to type I of E. coli. Archaeal putative asparaginases are of this type but contain an extra ~ 80 residues in a conserved N-terminal region. These archaeal homologs are included in this model.


Pssm-ID: 129610 [Multi-domain]  Cd Length: 336  Bit Score: 252.82  E-value: 5.44e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 109 PLFDSSDMTIAEWVCLAQTIKRHYEQYHGFVVIHGTDTMAFAASMLSFMLENlQKTVILTGAQVPIHALWSDGRENLLGA 188
Cdd:TIGR00519  52 MNILSENMKPEYWVEIAEAVKKEYDDYDGFVITHGTDTMAYTAAALSFMLET-PKPVVFTGAQRSSDRPSSDAALNLLCA 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 189 LLMAGQYV------IPEVCLFFQNQLFRGNRATKVDARRFAAFCSPNLLPLATVGADITINRELVRKVDGKAGLVVHSSM 262
Cdd:TIGR00519 131 VRAATEYIaevtvcMHGVTLDFNCRLHRGVKVRKAHTSRRDAFASINAPPLAEINPDGIEYLNEVYRPRGEDELEVHDRL 210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 263 EQDVGLLRLYPGIPAALVRAFLQPPLKGVVMETFGSGNGPTkpDLLQELRVATERGLVIVNCTHCLQGAVTTD-YAAGMA 341
Cdd:TIGR00519 211 EEKVALIKIYPGISPDIIRNYLSKGYKGIVIEGTGLGHAPQ--NKLQELQEASDRGVVVVMTTQCLNGRVNMNvYSTGRR 288

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1034587000 342 MAGAGVISGFDMTSEAALAKLSYVLGQPgLSLDVRKELLTKDLRGEMTP 390
Cdd:TIGR00519 289 LLQAGVIGGEDMLPEVALVKLMWLLGQY-SDPEEAKKMMSKNIAGEIEP 336
Asparaginase pfam00710
Asparaginase, N-terminal; This is the N-terminal domain of this enzyme.
 106-245 9.23e-62

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


Pssm-ID: 459913 [Multi-domain]  Cd Length: 188  Bit Score: 202.38  E-value: 9.23e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 106 ECQPLFDSSDMTIAEWVCLAQTIKRHYEQYHGFVVIHGTDTMAFAASMLSFMLENLQKTVILTGAQVPIHALWSDGRENL 185
Cdd:pfam00710  46 EQVANIDSSNMTPADWLRLARRIAEALDDYDGVVVTHGTDTLEETASALSFMLKNLGKPVVLTGSQRPSDEPSSDGPMNL 125

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034587000 186 LGALLMAGQY--VIPEVCLFFQNQLFRGNRATKVDARRFAAFCSPNLLPLATV-GADITINRE 245
Cdd:pfam00710 126 LAALRVAASPaaRGPGVLVVFNDKLHRARRVTKTHTSSLDAFDSPNFGPLGEVdGGQVELYRE 188
gatD_arch TIGR02153
glutamyl-tRNA(Gln) amidotransferase, subunit D; This peptide is found only in the Archaea. It ...
 102-393 3.03e-46

glutamyl-tRNA(Gln) amidotransferase, subunit D; This peptide is found only in the Archaea. It is part of a heterodimer, with GatE (TIGR00134), that acts as an amidotransferase on misacylated Glu-tRNA(Gln) to produce Gln-tRNA(Gln). The analogous amidotransferase found in bacteria is the GatABC system, although GatABC homologs in the Archaea appear to act instead on Asp-tRNA(Asn). [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 274001 [Multi-domain]  Cd Length: 404  Bit Score: 167.94  E-value: 3.03e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 102 YTVLECQPLFD--SSDMTIAEWVCLAQTIKRHYEQYH-GFVVIHGTDTMAFAASMLSFMLENLQKTVILTGAQVPIHALW 178
Cdd:TIGR02153 104 IANIKARAVFNilSENMKPEYWIKIAEAVAKALKEGAdGVVVAHGTDTMAYTAAALSFMFETLPVPVVLVGAQRSSDRPS 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 179 SDGRENLLGALLMAGQyVIPEV------------CLffqnqLFRGNRATKVDARRFAAFCSPNLLPLATVGAD--ITINR 244
Cdd:TIGR02153 184 SDAALNLICAVRAATS-PIAEVtvvmhgetsdtyCL-----VHRGVKVRKMHTSRRDAFQSINDIPIAKIDPDegIEKLR 257

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 245 ELVRKvDGKAGLVVHSSMEQDVGLLRLYPGIPAALVRAFLQPPLKGVVMEtfGSGNGPTKPDLLQELRVATERGLVIVNC 324
Cdd:TIGR02153 258 IDYRR-RGEKELELDDKFEEKVALVKFYPGISPEIIEFLVDKGYKGIVIE--GTGLGHVSEDWIPSIKRATDDGVPVVMT 334

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 325 THCLQGAVTTD-YAAGMAMAGAGVISGFDMTSEAALAKLSYVLGQPGlSLDVRKELLTKDLRGEMTPPSV 393
Cdd:TIGR02153 335 SQCLYGRVNLNvYSTGRELLKAGVIPCEDMLPEVAYVKLMWVLGQTD-DLEEVRKMMRTNIAGEINERTL 403
GatD cd08962
GatD subunit of archaeal Glu-tRNA amidotransferase; GatD is involved in the alternative ...
 113-384 5.17e-44

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: 161.63  E-value: 5.17e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 113 SSDMTIAEWVCLAQTIKRHYEQ-YHGFVVIHGTDTMAFAASMLSFMLENLQKTVILTGAQVPIHALWSDGRENLLGALLM 191
Cdd:cd08962   125 SENMTPEYWVKIAEAVYKEIKEgADGVVVAHGTDTMHYTASALSFMLETLPVPVVFVGAQRSSDRPSSDAAMNLIAAVLV 204

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 192 AGQYvIPEV------------CLffqnqLFRGNRATKVDARRFAAFCSPNLLPLATV---GADITINRELVRKvdGKAGL 256
Cdd:cd08962   205 AASD-IAEVvvvmhgttsddyCL-----LHRGTRVRKMHTSRRDAFQSINDEPLAKVdppGKIEKLSKDYRKR--GDEEL 276

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 257 VVHSSMEQDVGLLRLYPGIPAALVRAFLQPPLKGVVMEtfGSGNGPTKPDLLQELRVATERGLVIVNCTHCLQGAVTTD- 335
Cdd:cd08962   277 ELNDKLEEKVALIKFYPGMDPEIIDFYVDKGYKGIVIE--GTGLGHVSEDLIPSIKKAIDDGIPVVMTSQCIYGRVNLNv 354

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1034587000 336 YAAGMAMAGAGVISGFDMTSEAALAKLSYVLGQPGlSLDVRKELLTKDL 384
Cdd:cd08962   355 YSTGRELLKAGVIPGEDMLPETAYVKLMWVLGNTD-DLEEVRKLMLTNL 402
PRK04183 PRK04183
Glu-tRNA(Gln) amidotransferase subunit GatD;
113-393 1.30e-42

Glu-tRNA(Gln) amidotransferase subunit GatD;


Pssm-ID: 235245 [Multi-domain]  Cd Length: 419  Bit Score: 158.47  E-value: 1.30e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 113 SSDMTIAEWVCLAQTIKRHYEQ-YHGFVVIHGTDTMAFAASMLSFMLeNLQKTVILTGAQ----VPIhalwSDGRENLLG 187
Cdd:PRK04183  130 SENMTPEYWVEIAEAVYEEIKNgADGVVVAHGTDTMHYTAAALSFML-KTPVPIVFVGAQrssdRPS----SDAAMNLIC 204

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 188 ALLMA----GQYVI-------PEVCLffqnqLFRGNRATKVDARRFAAFCSPNLLPLATV----GADITINRELVRKVDG 252
Cdd:PRK04183  205 AVLAAtsdiAEVVVvmhgttsDDYCA-----LHRGTRVRKMHTSRRDAFQSINDKPLAKVdykeGKIEFLRKDYRKRGEK 279

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 253 KagLVVHSSMEQDVGLLRLYPGIPAALVRAFLQPPLKGVVMEtfGSGNGPTKPDLLQELRVATERGLVIVNCTHCLQGAV 332
Cdd:PRK04183  280 E--LELNDKLEEKVALIKFYPGMDPEILDFYVDKGYKGIVIE--GTGLGHVSTDLIPSIKRATDDGIPVVMTSQCLYGRV 355

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034587000 333 TTD-YAAGMAMAGAGVISGFDMTSEAALAKLSYVLGQPGlSLDVRKELLTKDLRGEMTPPSV 393
Cdd:PRK04183  356 NMNvYSTGRDLLKAGVIPGEDMLPEVAYVKLMWVLGNTY-DLEEVRELMLTNLAGEINERSR 416
L-asparaginase_like cd00411
Bacterial L-asparaginases and related enzymes; Asparaginases (amidohydrolases, E.C. 3.5.1.1) ...
 112-368 2.08e-36

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: 138.42  E-value: 2.08e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 112 DSSDMTIAEWVCLAQTI-KRHYEQYHGFVVIHGTDTMAFAASMLSFMLENlQKTVILTGAQVPIHALWSDGRENLLGALL 190
Cdd:cd00411    56 ASEDITPDDWLKLAKEVaKLLDSDVDGIVITHGTDT*EETAYFLSLTLKN-DKPVVLVGAMRPSTAMSADGPFNLYNAVR 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 191 MA--GQYVIPEVCLFFQNQLFRGNRATKVDARRFAAFCSPNLLPLATVGADITI--NRELVRKVDGKAGLVVHSSMEQDV 266
Cdd:cd00411   135 VAkdKDSRGRGVLVVMNDKVHSGRDVSKTNTSGFDAFRSINYGPLGEIKDNKIYyqRKPARKHTDESEFDVSDIKSLPKV 214

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 267 GLLRLYPGIPAALVRAFLQPPLKGVVMEtfGSGNGPTKPDLLQELRVATERGLVIVNCTHCLQGAVTTDyaAGMAMAGAG 346
Cdd:cd00411   215 DIVYLYPGLSDDIYDALVDLGYKGIVLA--GTGNGSVPYDVFPVLSSASKRGVAVVRSSQVIYGGVDLN--AEKVDLKAG 290

                         250       260
                  ....*....|....*....|..
gi 1034587000 347 VISGFDMTSEAALAKLSYVLGQ 368
Cdd:cd00411   291 VIPAGDLNPEKARVLLMWALTH 312
L-asparaginase_II cd08964
Type II (periplasmic) bacterial L-asparaginase; Asparaginases (amidohydrolases, E.C. 3.5.1.1) ...
 112-336 5.13e-34

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: 131.86  E-value: 5.13e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 112 DSSDMTIAEWVCLAQTIKRHYEQ--YHGFVVIHGTDTM---AFAASMLsfmlENLQKTVILTGAQVPIHALWSDGRENLL 186
Cdd:cd08964    54 PSSDMTPADWLALAARVNEALADpdVDGVVVTHGTDTLeetAYFLDLT----LDSDKPVVLTGAMRPADAPSADGPANLL 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 187 GALLMAGQyviPE-----VCLFFQNQLFRGNRATKVDARRFAAFCSPNLLPLATV-GADITINRELVRKvdgKAGLVVHS 260
Cdd:cd08964   130 DAVRVAAS---PEargrgVLVVFNDEIHAARDVTKTHTTSLDAFASPGFGPLGYVdGGKVRFYRRPARP---HTLPSEFD 203

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034587000 261 SMEQDVGLLRLYPGIPAALVRAFLQPPLKGVVMETFGSGNGPtkPDLLQELRVATERGLVIVNCTHCLQGAVTTDY 336
Cdd:cd08964   204 DELPRVDIVYAYAGADGALLDAAVAAGAKGIVIAGFGAGNVP--PALVEALERAVAKGIPVVRSSRVGNGRVLPVY 277
Asparaginase_C pfam17763
Glutaminase/Asparaginase C-terminal domain; This domain is found at the C-terminus of ...
 265-379 3.44e-29

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: 111.80  E-value: 3.44e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 265 DVGLLRLYPGIPAALVRAFLQPPLKGVVMETFGSGNGPtkPDLLQELRVATERGLVIVNCTHCLQGAVTTD-YAAGMAMA 343
Cdd:pfam17763   1 RVDILYLYPGMDPELLDAALAAGAKGIVIAGFGAGNVP--SALLDALKEAVARGIPVVRSSRCGSGRVNLGyYETGRDLL 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1034587000 344 GAGVISGFDMTSEAALAKLSYVLGQpGLSLDVRKEL 379
Cdd:pfam17763  79 EAGVISGGDLTPEKARIKLMLALGK-GLDPEEIREL 113
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
412-592 4.08e-28

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 114.28  E-value: 4.08e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 412 LLSLSGSQEADALRNALVPSLACAAAHAGDVEALQALVELGSDLGLVDFNGQTPLHAAARGGHTEAVTMLLQRGVDVNTR 491
Cdd:COG0666    70 ALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQ 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 492 DTDGFSPLLLAVRGRHPGVIGLLREAGASLSTQELEEaGTELCRLAYRADLEGLQVWWQAGADLGQPGYDGHSALHVAEA 571
Cdd:COG0666   150 DNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDG-ETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAE 228

                         170       180
                  ....*....|....*....|.
gi 1034587000 572 AGNLAVVAFLQSLEGAVGAQA 592
Cdd:COG0666   229 NGNLEIVKLLLEAGADLNAKD 249
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
435-582 7.13e-28

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 113.51  E-value: 7.13e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 435 AAAHAGDVEALQALVELGSDLGLVDFNGQTPLHAAARGGHTEAVTMLLQRGVDVNTRDTDGFSPLLLAVRGRHPGVIGLL 514
Cdd:COG0666   126 LAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034587000 515 REAGASLSTQElEEAGTELCRLAYRADLEGLQVWWQAGADLGQPGYDGHSALHVAEAAGNLAVVAFLQ 582
Cdd:COG0666   206 LEAGADVNAKD-NDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLL 272
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
411-581 4.31e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 102.72  E-value: 4.31e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 411 WLLSLSGSQEADALRNALVPSLACAAAHAGDVEALQALVELGSDLGLVDFNGQTPLHAAARGGHTEAVTMLLQRGVDVNT 490
Cdd:COG0666    36 LLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNA 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 491 RDTDGFSPLLLAVRGRHPGVIGLLREAGASLSTQElEEAGTELCRLAYRADLEGLQVWWQAGADLGQPGYDGHSALHVAE 570
Cdd:COG0666   116 RDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQD-NDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAA 194

                         170
                  ....*....|.
gi 1034587000 571 AAGNLAVVAFL 581
Cdd:COG0666   195 ENGHLEIVKLL 205
Ank_2 pfam12796
Ankyrin repeats (3 copies);
436-524 4.99e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 76.31  E-value: 4.99e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 436 AAHAGDVEALQALVELGSDLGLVDFNGQTPLHAAARGGHTEAVTMLLQRgVDVNTRDtDGFSPLLLAVRGRHPGVIGLLR 515
Cdd:pfam12796   4 AAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKLLL 81


                  ....*....
gi 1034587000 516 EAGASLSTQ 524
Cdd:pfam12796  82 EKGADINVK 90
asnASE_II TIGR00520
L-asparaginase, type II; Two related families of asparaginase (L-asparagine amidohydrolase, EC ...
 112-335 1.54e-16

L-asparaginase, type II; Two related families of asparaginase (L-asparagine amidohydrolase, EC 3.5.1.1) are designated type I and type II according to the terminology in E. coli, which has both: L-asparaginase I is a low-affinity enzyme found in the cytoplasm, while L-asparaginase II is a high-affinity periplasmic enzyme synthesized with a cleavable signal sequence. This model describes L-asparaginases related to type II of E. coli. Both the cytoplasmic and the cell wall asparaginases of Saccharomyces cerevisiae belong to this set. Members of this set from Acinetobacter glutaminasificans and Pseudomonas fluorescens are described as having both glutaminase and asparaginase activitities. All members are homotetrameric. [Energy metabolism, Amino acids and amines]


Pssm-ID: 273115 [Multi-domain]  Cd Length: 349  Bit Score: 81.35  E-value: 1.54e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 112 DSSDMTIAEWVCLAQTIKRHYE--QYHGFVVIHGTDTMAFAASMLSFMLeNLQKTVILTGAQVPIHALWSDGRENLLGAL 189
Cdd:TIGR00520  81 GSQDMNEEVLLKLAKGINELLAsdDYDGIVITHGTDTLEETAYFLDLTV-KSDKPVVIVGAMRPATSVSADGPMNLYNAV 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 190 LMAGQyviPE-----VCLFFQNQLFRGNRATKVDARRFAAFCSPNLLPLATV-GADITINRELVRK--VDGKAGLVVHSS 261
Cdd:TIGR00520 160 SVAAN---PKsagrgVLVVLNDRIASGRYVTKTNTTSLDTFKSRNQGYLGYIhNGKIDYYYPPVRKhtCDTPFSVSNLDE 236

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034587000 262 MEQDVGLLRLYPGIPAALVRAFLQPPLKGVVMEtfGSGNGPTKPDLLQELRVATERGLVIVNCTHCLQGAVTTD 335
Cdd:TIGR00520 237 PLPKVDIIYAYQNAPPLIVNAVLDAGAKGIVLA--GVGNGSLSAAGLKVNETAAKLGVPIVRSSRVGDGMVTPD 308
ansB PRK11096
L-asparaginase II; Provisional
 113-335 2.33e-16

L-asparaginase II; Provisional


Pssm-ID: 182958 [Multi-domain]  Cd Length: 347  Bit Score: 80.92  E-value: 2.33e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 113 SSDMTIAEWVCLAQTIKRHYEQYHGFVVIHGTDTMAFAASMLSfMLENLQKTVILTGAQVPIHALWSDGRENLLGALLMA 192
Cdd:PRK11096   79 SQDMNDEVWLTLAKKINTDCDKTDGFVITHGTDTMEETAYFLD-LTVKCDKPVVLVGAMRPSTAMSADGPLNLYNAVVTA 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 193 G--QYVIPEVCLFFQNQLFRGNRATKVDARRFAAFCSPNLLPLATV-GADITINRELVRKVDGKAGLVVhSSMEQ--DVG 267
Cdd:PRK11096  158 AdkASANRGVLVAMNDTVLDGRDVTKTNTTDVQTFQSPNYGPLGYIhNGKVDYQRTPARKHTTDTPFDV-SKLNElpKVG 236

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034587000 268 LLRLYPGIPAALVRAFLQPPLKGVVmeTFGSGNGPTKPDLLQELRVATERGLVIVNCTHCLQGAVTTD 335
Cdd:PRK11096  237 IVYNYANASDLPAKALVDAGYDGIV--SAGVGNGNLYKTVFDTLATAAKNGVAVVRSSRVPTGATTQD 302
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
421-581 2.12e-15

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 76.92  E-value: 2.12e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 421 ADALRNALVPSLACAAAHAGDVEALQALVELGSDLGLVDFNGQTPLHAAARGGHTEAVTMLLQRGVDVNTRDTDGFSPLL 500
Cdd:COG0666    13 AALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLH 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 501 LAVRGRHPGVIGLLREAGASLSTQElEEAGTELCRLAYRADLEGLQVWWQAGADLGQPGYDGHSALHVAEAAGNLAVVAF 580
Cdd:COG0666    93 AAARNGDLEIVKLLLEAGADVNARD-KDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKL 171


                  .
gi 1034587000 581 L 581
Cdd:COG0666   172 L 172
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 435-581 3.67e-14

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 75.67  E-value: 3.67e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 435 AAAHAGDVEALQALVELGSDLGLVDFNGQTPLHAAARGGHTEAVTMLLQRGVDVNTRDTDGFSPLLLAVRGRHPGVIGLL 514
Cdd:PLN03192  531 TVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL 610

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034587000 515 REAgASLSTQELeeAGTELCRLAYRADLEGLQVWWQAGADLGQPGYDGHSALHVAEAAGNLAVVAFL 581
Cdd:PLN03192  611 YHF-ASISDPHA--AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLL 674
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
435-519 5.64e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 63.82  E-value: 5.64e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 435 AAAHAGDVEALQALVELGSDLGLVDFNGQTPLHAAARGGHTEAVTMLLQRGVDVNTRDTDGFSPLLLAVRGRHPGVIGLL 514
Cdd:COG0666   192 LAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLL 271


                  ....*
gi 1034587000 515 REAGA 519
Cdd:COG0666   272 LLALL 276
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 434-514 2.76e-10

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 63.38  E-value: 2.76e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 434 CAAAHAGDVEALQALVELGSDLGLVDFNGQTPLHAAARGGHTEAVTMLLQRGVDVNTRDTDGFSPLLLAVRGRHPGVIGL 513
Cdd:PTZ00322   87 CQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                  .
gi 1034587000 514 L 514
Cdd:PTZ00322  167 L 167
Ank_2 pfam12796
Ankyrin repeats (3 copies);
435-492 4.61e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 56.66  E-value: 4.61e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034587000 435 AAAHAGDVEALQALVELGSdlGLVDFNGQTPLHAAARGGHTEAVTMLLQRGVDVNTRD 492
Cdd:pfam12796  36 LAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
Ank_4 pfam13637
Ankyrin repeats (many copies);
431-482 5.88e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.97  E-value: 5.88e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1034587000 431 SLACAAAHAGDVEALQALVELGSDLGLVDFNGQTPLHAAARGGHTEAVTMLL 482
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
464-514 5.12e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.28  E-value: 5.12e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1034587000 464 TPLHAAARGGHTEAVTMLLQRGVDVNTRDTDGFSPLLLAVRGRHPGVIGLL 514
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
Ank_2 pfam12796
Ankyrin repeats (3 copies);
466-581 7.28e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 53.20  E-value: 7.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 466 LHAAARGGHTEAVTMLLQRGVDVNTRDTDGFSPLLLAVRGRHPGVIGLLreagaslstqeLEEAGTELCrlayradlegl 545
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL-----------LEHADVNLK----------- 58

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1034587000 546 qvwwqagadlgqpgYDGHSALHVAEAAGNLAVVAFL 581
Cdd:pfam12796  59 --------------DNGRTALHYAARSGHLEIVKLL 80
PHA03095 PHA03095
ankyrin-like protein; Provisional
 441-521 1.93e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 56.96  E-value: 1.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 441 DVEALQALVELGSDLGLVDFNGQTPLHAAARGGHTEAVT-MLLQRGVDVNTRDTDGFSPLLLAVRGR--HPGVIGLLREA 517
Cdd:PHA03095   62 VKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDVIkLLIKAGADVNAKDKVGRTPLHVYLSGFniNPKVIRLLLRK 141


                  ....
gi 1034587000 518 GASL 521
Cdd:PHA03095  142 GADV 145
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 409-523 1.35e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 54.29  E-value: 1.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 409 VSWLLSLSGSQEADALRNALVPSLACAAAHAGDVEALQALVELGSDLGLVDFNGQTPLHAAARGGHTE------------ 476
Cdd:PHA03100   88 IVKLLLEYGANVNAPDNNGITPLLYAISKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDlkilkllidkgv 167

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1034587000 477 ------AVTMLLQRGVDVNTRDTDGFSPLLLAVRGRHPGVIGLLREAGASLST 523
Cdd:PHA03100  168 dinaknRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNL 220
Ank_5 pfam13857
Ankyrin repeats (many copies);
448-502 2.25e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.73  E-value: 2.25e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034587000 448 LVELGS-DLGLVDFNGQTPLHAAARGGHTEAVTMLLQRGVDVNTRDTDGFSPLLLA 502
Cdd:pfam13857   1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA03095 PHA03095
ankyrin-like protein; Provisional
 432-523 2.26e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 53.49  E-value: 2.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 432 LACAAAHAGDVEALQALVELGSDLGLVDFNGQTPLHAAARGG--HTEAVTMLLQRGVDVNTRDTDGFSPL--LLAVRGRH 507
Cdd:PHA03095   87 LHLYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVYLSGFniNPKVIRLLLRKGADVNALDLYGMTPLavLLKSRNAN 166

                          90
                  ....*....|....*.
gi 1034587000 508 PGVIGLLREAGASLST 523
Cdd:PHA03095  167 VELLRLLIDAGADVYA 182
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 448-523 2.32e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 53.52  E-value: 2.32e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034587000 448 LVELGSDLGLVDFNGQTPLHAAARGGHTEAVTMLLQRGVDVNTRDTDGFSPLLLAVRGRHPGVIGLLREAGASLST 523
Cdd:PHA03100  178 LLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 461-492 2.91e-07

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: 46.90  E-value: 2.91e-07
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1034587000 461 NGQTPLHAAA-RGGHTEAVTMLLQRGVDVNTRD 492
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 424-504 1.23e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 51.12  E-value: 1.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 424 LRNALVPSLACAAAHAGDVEALQALVELGSDLGLVDFNGQTPLHAAARGGHTEAVTMLLQRGVDVNTRDTDGFSPLLLAV 503
Cdd:PHA02874  119 IKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAA 198


                  .
gi 1034587000 504 R 504
Cdd:PHA02874  199 E 199
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 443-525 1.52e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 50.73  E-value: 1.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 443 EALQALVELGSDLGLVDFNGQTPLHAAARGGHTEAVTMLLQRGVDVNTRDTDGFSPLLLAVRGRHPGVIGLLREAGASLS 522
Cdd:PHA02874  105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184


                  ...
gi 1034587000 523 TQE 525
Cdd:PHA02874  185 VKD 187
PHA03095 PHA03095
ankyrin-like protein; Provisional
 448-504 1.62e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 50.79  E-value: 1.62e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034587000 448 LVELGSDLGLVDFNGQTPLHAAARGGHTEAVTMLLQRGVDVNTRDTDGFSPLLLAVR 504
Cdd:PHA03095  243 LLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVR 299
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 436-536 4.11e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 49.60  E-value: 4.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 436 AAHAGDVEALQALVELGSDLGLVDF-NGQTPLHAAARGGHTEAVTMLLQRGVDVNTRDTDGFSPLLLAVRGRHPGVIGLL 514
Cdd:PHA02875   75 AVEEGDVKAVEELLDLGKFADDVFYkDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELL 154

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1034587000 515 REAGASLSTQE----------LEEAGTELCRL 536
Cdd:PHA02875  155 IDHKACLDIEDccgctpliiaMAKGDIAICKM 186
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 432-501 4.79e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 49.87  E-value: 4.79e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034587000 432 LACAAAHAGDVEALQALVELGSDLGLVDFNGQTPLHAAARGGHTEAVTMLLQRGVDVNTRDT-DGFSPLLL 501
Cdd:PLN03192  625 LLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTdDDFSPTEL 695
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 461-489 1.12e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.19  E-value: 1.12e-05
                           10        20
                   ....*....|....*....|....*....
gi 1034587000  461 NGQTPLHAAARGGHTEAVTMLLQRGVDVN 489
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
PHA03095 PHA03095
ankyrin-like protein; Provisional
 445-522 1.69e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 47.71  E-value: 1.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 445 LQALVELGSDLGLVDFNGQTPLHAAARGGHTEAVTM--LLQRGVDVNTRDTDGFSPLLLAVRGRHPGVIGLLREAGASLS 522
Cdd:PHA03095  205 VRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADIN 284
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 461-490 1.74e-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: 41.86  E-value: 1.74e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 1034587000 461 NGQTPLHAAARGGHTEAVTMLLQRGVDVNT 490
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 441-569 3.78e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 46.41  E-value: 3.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 441 DVEALQALVELGSDLGLVDFN-GQTPLHAAARGGHTEAVTMLLQRGVDVNTRDTDGFSPLLLAVRGRHPGVIGLLREAGA 519
Cdd:PHA02878  146 EAEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA 225

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1034587000 520 slSTQELEEAGTELCRLA--YRADLEGLQVWWQAGADLGQPGY-DGHSALHVA 569
Cdd:PHA02878  226 --STDARDKCGNTPLHISvgYCKDYDILKLLLEHGVDVNAKSYiLGLTALHSS 276
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 446-576 3.83e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.60  E-value: 3.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 446 QALVELGSDLGLVDFNGQTPLHAAARGGHTEAVTMLLQRGVDVNTRDTDGFSPLLLAVRGRHPGVIGLLREAGASLSTQE 525
Cdd:PHA02876  162 EMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKND 241

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1034587000 526 LeeagtELCRLAYRADLEGLQVWWQAGADLGQPGYDGHSALHVAEAAGNLA 576
Cdd:PHA02876  242 L-----SLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLS 287
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 448-574 6.94e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.82  E-value: 6.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 448 LVELGSDLGLVDFNGQTPLHAAARGGH-TEAVTMLLQRGVDVNTRDTDGFSPLLLA-VRGRHPGVIGLLREAGASLSTQE 525
Cdd:PHA02876  293 LLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQAsTLDRNKDIVITLLELGANVNARD 372

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1034587000 526 LEEAgTELCRLAYRADLEGLQVWWQAGADLGQPGYDGHSALHVAEAAGN 574
Cdd:PHA02876  373 YCDK-TPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTN 420
PHA03095 PHA03095
ankyrin-like protein; Provisional
 441-521 8.06e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 45.40  E-value: 8.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 441 DVEALQALVELGSDLGLVDFNGQTPLHAAARGGH---TEAVTMLLQRGVDVNTRDTDGFSPLLLAVR-GRHPGVIGLLRE 516
Cdd:PHA03095   26 TVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYnATTLDVIKLLIK 105


                  ....*
gi 1034587000 517 AGASL 521
Cdd:PHA03095  106 AGADV 110
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 462-537 1.55e-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: 44.69  E-value: 1.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 462 GQTPLHAAARGGHTEAVTMLLQRGVDVNTR----------DTDGF----SPLLLAVRGRHPGVIGLLREAGASLSTQelE 527
Cdd:TIGR00870 128 GITALHLAAHRQNYEIVKLLLERGASVPARacgdffvksqGVDSFyhgeSPLNAAACLGSPSIVALLSEDPADILTA--D 205

                          90
                  ....*....|
gi 1034587000 528 EAGTELCRLA 537
Cdd:TIGR00870 206 SLGNTLLHLL 215
PHA02741 PHA02741
hypothetical protein; Provisional
 442-520 2.39e-04

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 42.34  E-value: 2.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 442 VEALQALVELGSDL-GLVDFNGQTPLHAAA-RGGHTEAVTMLLQRGVDVNTRDTDGFSPLLLAVRGRHPGVIGLLREAGA 519
Cdd:PHA02741   77 AEIIDHLIELGADInAQEMLEGDTALHLAAhRRDHDLAEWLCCQPGIDLHFCNADNKSPFELAIDNEDVAMMQILREIVA 156


                  .
gi 1034587000 520 S 520
Cdd:PHA02741  157 T 157
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 436-581 4.00e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 43.03  E-value: 4.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 436 AAHAGDVEALQALVELGSDLGLVDFNGQTPLHAAARGGHTEAVTMLLQRGVD-----------------------VNTRD 492
Cdd:PHA02874   42 AIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDtsilpipciekdmiktildcgidVNIKD 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 493 TDGFSPLLLAVRGRHPGVIGLLREAGASLSTQELEeaGTELCRLAYRAD-LEGLQVWWQAGADLGQPGYDGHSALHVAEA 571
Cdd:PHA02874  122 AELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDN--GCYPIHIAIKHNfFDIIKLLLEKGAYANVKDNNGESPLHNAAE 199

                         170
                  ....*....|
gi 1034587000 572 AGNLAVVAFL 581
Cdd:PHA02874  200 YGDYACIKLL 209
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 438-581 4.68e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 43.03  E-value: 4.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 438 HAGDVEALQALVEL-GSDLGLVDFNGQTPLHAAARGGHTEAVTMLLQRGVDVNTRDTDGFSPLLLAVRGRHPGVIGLLRE 516
Cdd:PHA02874   10 YSGDIEAIEKIIKNkGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLID 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 517 AGASLSTQELEEAGTELCR-------------------LAY---RADLEGLQVWWQAGADLGQPGYDGHSALHVAEAAGN 574
Cdd:PHA02874   90 NGVDTSILPIPCIEKDMIKtildcgidvnikdaelktfLHYaikKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNF 169


                  ....*..
gi 1034587000 575 LAVVAFL 581
Cdd:PHA02874  170 FDIIKLL 176
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 443-503 5.42e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 42.64  E-value: 5.42e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034587000 443 EALQALVELGSDLGLVDFNGQTPLHAAARGGHTEAVTMLLQRGVDVNTRDTDGFSPLLLAV 503
Cdd:PHA02874  171 DIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI 231
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 532-581 7.45e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.58  E-value: 7.45e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1034587000 532 ELCRLAYRADLEGLQVWWQAGADLGQPGYDGHSALHVAEAAGNLAVVAFL 581
Cdd:PTZ00322   85 ELCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVL 134
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 436-525 1.03e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 41.92  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 436 AAHAGDVEALQALVE---------LGSDLglvdFNGQTPLHAAARGGHTEAVTMLLQRGVDVNT-RDTDGF---SPLLLA 502
Cdd:cd22192    58 AALYDNLEAAVVLMEaapelvnepMTSDL----YQGETALHIAVVNQNLNLVRELIARGADVVSpRATGTFfrpGPKNLI 133

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1034587000 503 VRGRHP----------GVIGLLREAGASLSTQE 525
Cdd:cd22192   134 YYGEHPlsfaacvgneEIVRLLIEHGADIRAQD 166
PHA02917 PHA02917
ankyrin-like protein; Provisional
 454-503 1.13e-03

ankyrin-like protein; Provisional


Pssm-ID: 165231 [Multi-domain]  Cd Length: 661  Bit Score: 41.91  E-value: 1.13e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1034587000 454 DLGLVDFNGQTPLHAAARGGHTEAVTMLLQRGVDVNTRDTDGFSPLLLAV 503
Cdd:PHA02917  444 DINMIDKRGETLLHKAVRYNKQSLVSLLLESGSDVNIRSNNGYTCIAIAI 493
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 436-490 1.16e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 41.57  E-value: 1.16e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1034587000 436 AAHAGDVEALQALVELGSDLGLVDFNGQTPLHAAARGGHTEAVTMLLQRGVDVNT 490
Cdd:PHA03100  199 AVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 436-521 5.87e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 39.66  E-value: 5.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 436 AAHAGDVEALQALVELGSDLGLVDFNGQTPLHAAAR-GGHTEAVTMLLQRGVDVNTRDTDGFSPLLLAVRGRHPGVIGLL 514
Cdd:PHA02876  315 AKNGYDTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTL 394


                  ....*..
gi 1034587000 515 REAGASL 521
Cdd:PHA02876  395 LDYGADI 401
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 436-520 6.53e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 39.20  E-value: 6.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 436 AAHAGDVEALQALVELGSDLGLVDFNGQTPLHAAARGGHTEAVTMLLQRGVDVNTRDTDGFSPLLLAVRGRHPGVIGLLR 515
Cdd:PHA02875  109 ATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLL 188


                  ....*
gi 1034587000 516 EAGAS 520
Cdd:PHA02875  189 DSGAN 193
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 470-541 7.00e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 39.50  E-value: 7.00e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034587000 470 ARGGHTEAVTMLLQRGVDVNTRDTDGFSPLLLAVRGRHPGVIGLLREAGASLSTqeLEEAGTELCRLAYRAD 541
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTL--LDKDGKTPLELAEENG 159
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 420-521 8.27e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 39.28  E-value: 8.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587000 420 EADALRNALVPSLACAAAHAGDVEALQALVELGSDLGLVDFNGQTPLHAAARGG-HTEAVTMLLQRGVDVNTRDTDGFSP 498
Cdd:PHA02876  400 DIEALSQKIGTALHFALCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYP 479

                          90       100
                  ....*....|....*....|...
gi 1034587000 499 LLLAVrGRHpGVIGLLREAGASL 521
Cdd:PHA02876  480 LLIAL-EYH-GIVNILLHYGAEL 500
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 441-504 9.91e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 38.89  E-value: 9.91e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034587000 441 DVEALQALVELGSDLGLVDFNGQTPLHAAARGGH-TEAVTMLLQRGVDVNTRDTDGFSPLLLAVR 504
Cdd:PHA02876  252 DLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYLMAK 316
 
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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