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Conserved domains on  [gi|1082599630|gb|OFZ30003|]
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hypothetical protein A2437_00915 [Bacteroidetes bacterium RIFOXYC2_FULL_40_12]

Protein Classification

nitrilase family protein( domain architecture ID 10166093)

nitrilase family protein is a member of a large superfamily and predicted to act as a carbon-nitrogen hydrolase

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Xc-1258_like cd07575
Xanthomonas campestris XC1258 and related proteins, members of the nitrilase superfamily ...
4-255 7.64e-156

Xanthomonas campestris XC1258 and related proteins, members of the nitrilase superfamily (putative class 13 nitrilases); Uncharacterized subgroup belonging to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup either represents a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. XC1258 is a homotetramer.


:

Pssm-ID: 143599  Cd Length: 252  Bit Score: 433.50  E-value: 7.64e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630   4 LKVAFIQTDLAWENPSANIKTSDRWVDQV-GTADVIVLPEMFNTGFTMNVASMAQSNSGQTIQWMKNKSLENNTSIMGSL 82
Cdd:cd07575     1 LKIALIQTDLVWEDPEANLAHFEEKIEQLkEKTDLIVLPEMFTTGFSMNAEALAEPMNGPTLQWMKAQAKKKGAAITGSL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630  83 IVRDEEKYYNRFVMAYPCADIRWYDKRHLFRMGGEHENFSAGNHQRVFKYFGWRIKPLICYDLRFPVWSRNRNNYDLLIY 162
Cdd:cd07575    81 IIKEGGKYYNRLYFVTPDGEVYHYDKRHLFRMAGEHKVYTAGNERVIVEYKGWKILLQVCYDLRFPVWSRNTNDYDLLLY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630 163 VANWPAPRREVWKTLLKARAIENQCYVIGVNRVGTDGMGITYAGDSMIIDFKGQVISELPEGEqGIGTATLSMSELRIFR 242
Cdd:cd07575   161 VANWPAPRRAAWDTLLKARAIENQAYVIGVNRVGTDGNGLEYSGDSAVIDPLGEPLAEAEEDE-GVLTATLDKEALQEFR 239
                         250
                  ....*....|...
gi 1082599630 243 EKFPVHLDADDFE 255
Cdd:cd07575   240 EKFPFLKDADSFT 252
 
Name Accession Description Interval E-value
Xc-1258_like cd07575
Xanthomonas campestris XC1258 and related proteins, members of the nitrilase superfamily ...
4-255 7.64e-156

Xanthomonas campestris XC1258 and related proteins, members of the nitrilase superfamily (putative class 13 nitrilases); Uncharacterized subgroup belonging to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup either represents a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. XC1258 is a homotetramer.


Pssm-ID: 143599  Cd Length: 252  Bit Score: 433.50  E-value: 7.64e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630   4 LKVAFIQTDLAWENPSANIKTSDRWVDQV-GTADVIVLPEMFNTGFTMNVASMAQSNSGQTIQWMKNKSLENNTSIMGSL 82
Cdd:cd07575     1 LKIALIQTDLVWEDPEANLAHFEEKIEQLkEKTDLIVLPEMFTTGFSMNAEALAEPMNGPTLQWMKAQAKKKGAAITGSL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630  83 IVRDEEKYYNRFVMAYPCADIRWYDKRHLFRMGGEHENFSAGNHQRVFKYFGWRIKPLICYDLRFPVWSRNRNNYDLLIY 162
Cdd:cd07575    81 IIKEGGKYYNRLYFVTPDGEVYHYDKRHLFRMAGEHKVYTAGNERVIVEYKGWKILLQVCYDLRFPVWSRNTNDYDLLLY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630 163 VANWPAPRREVWKTLLKARAIENQCYVIGVNRVGTDGMGITYAGDSMIIDFKGQVISELPEGEqGIGTATLSMSELRIFR 242
Cdd:cd07575   161 VANWPAPRRAAWDTLLKARAIENQAYVIGVNRVGTDGNGLEYSGDSAVIDPLGEPLAEAEEDE-GVLTATLDKEALQEFR 239
                         250
                  ....*....|...
gi 1082599630 243 EKFPVHLDADDFE 255
Cdd:cd07575   240 EKFPFLKDADSFT 252
PRK10438 PRK10438
C-N hydrolase family amidase; Provisional
1-254 5.37e-107

C-N hydrolase family amidase; Provisional


Pssm-ID: 182461  Cd Length: 256  Bit Score: 309.75  E-value: 5.37e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630   1 MENLKVAFIQTDLAWENPSANIKTSDRWVDQVGTADVIVLPEMFNTGFTMNVA--SMAQSnsgQTIQWMKNKSLENNTSI 78
Cdd:PRK10438    1 MSGLKITLLQQPLVWMDGPANLRHFDRQLEGITGRDVIVLPEMFTTGFAMEAAasSLPQD---DVVAWMTAKAQQTNALI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630  79 MGSLIVRDEEKYYNRFVMAYPCADIRWYDKRHLFRMGGEHENFSAGNHQRVFKYFGWRIKPLICYDLRFPVWSRNRNNYD 158
Cdd:PRK10438   78 AGSVALQTESGAVNRFLLVEPGGTVHFYDKRHLFRMADEHLHYKAGNARVIVEWRGWRILPLVCYDLRFPVWSRNRNDYD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630 159 LLIYVANWPAPRREVWKTLLKARAIENQCYVIGVNRVGTDGMGITYAGDSMIIDFKGQVISELPEGEQGIGTATLSMSEL 238
Cdd:PRK10438  158 LALYVANWPAPRSLHWQTLLTARAIENQAYVAGCNRVGSDGNGHHYRGDSRIINPQGEIIATAEPHQATRIDAELSLEAL 237
                         250
                  ....*....|....*.
gi 1082599630 239 RIFREKFPVHLDADDF 254
Cdd:PRK10438  238 QEYREKFPAWRDADEF 253
Nit2 COG0388
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];
3-254 2.25e-82

Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];


Pssm-ID: 440157 [Multi-domain]  Cd Length: 264  Bit Score: 247.47  E-value: 2.25e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630   3 NLKVAFIQTDLAWENPSANIKTSDRWVDQVGT--ADVIVLPEMFNTGFTMN---VASMAQSNSGQTIQWMKNKSLENNTS 77
Cdd:COG0388     1 TMRIALAQLNPTVGDIEANLAKIEELIREAAAqgADLVVFPELFLTGYPPEdddLLELAEPLDGPALAALAELARELGIA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630  78 IMGSLIVRDEE-KYYNRFVMAYPCADIR-WYDKRHLFRMGGEHEN--FSAGNHQRVFKYFGWRIKPLICYDLRFPVWSRN 153
Cdd:COG0388    81 VVVGLPERDEGgRLYNTALVIDPDGEILgRYRKIHLPNYGVFDEKryFTPGDELVVFDTDGGRIGVLICYDLWFPELARA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630 154 --RNNYDLLIYVANWPAPR-REVWKTLLKARAIENQCYVIGVNRVGTDGmGITYAGDSMIIDFKGQVISELPEGEqGIGT 230
Cdd:COG0388   161 laLAGADLLLVPSASPFGRgKDHWELLLRARAIENGCYVVAANQVGGED-GLVFDGGSMIVDPDGEVLAEAGDEE-GLLV 238
                         250       260
                  ....*....|....*....|....
gi 1082599630 231 ATLSMSELRIFREKFPVHLDADDF 254
Cdd:COG0388   239 ADIDLDRLREARRRFPVLRDRRPD 262
CN_hydrolase pfam00795
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ...
5-242 6.78e-36

Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. The family includes: Nitrilase EC:3.5.5.1, Aliphatic amidase EC:3.5.1.4, Biotidinase EC:3.5.1.12, Beta-ureidopropionase EC:3.5.1.6. Nitrilase-related proteins generally have a conserved E-K-C catalytic triad, and are multimeric alpha-beta-beta-alpha sandwich proteins.


Pssm-ID: 425873 [Multi-domain]  Cd Length: 257  Bit Score: 128.24  E-value: 6.78e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630   5 KVAFIQTDLAWENPSANIKTSDRWVDQV--GTADVIVLPEMFNTGFtMNVASM---AQSNSGQTIQWMKNKSLENNTSIM 79
Cdd:pfam00795   1 RVALVQLPQGFWDLEANLQKALELIEEAarYGADLIVLPELFITGY-PCWAHFleaAEVGDGETLAGLAALARKNGIAIV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630  80 GSLIVRDEE--KYYNRFVMAYPCADIRW-YDKRHLFRMGG-----EHENFSAGNHQRVFKYFGWRIKPLICYDLRFPVWS 151
Cdd:pfam00795  80 IGLIERWLTggRLYNTAVLLDPDGKLVGkYRKLHLFPEPRppgfrERVLFEPGDGGTVFDTPLGKIGAAICYEIRFPELL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630 152 R--NRNNYDLLIYVAN----WPAPRREVWKTLLKARAIENQCYVIGVNRVGTDGMGITYAGDSMIIDFKGQVISELPEGE 225
Cdd:pfam00795 160 RalALKGAEILINPSArapfPGSLGPPQWLLLARARALENGCFVIAANQVGGEEDAPWPYGHSMIIDPDGRILAGAGEWE 239
                         250
                  ....*....|....*..
gi 1082599630 226 QGIGTATLSMSELRIFR 242
Cdd:pfam00795 240 EGVLIADIDLALVRAWR 256
de_GSH_amidase NF033621
deaminated glutathione amidase;
35-247 9.55e-18

deaminated glutathione amidase;


Pssm-ID: 468114  Cd Length: 260  Bit Score: 79.94  E-value: 9.55e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630  35 ADVIVLPEMF----NTGFTMNVASmAQSNSGQTIQWMKNKSLENNTSIMGSLIVRDEE-KYYNRFVMAYPCADIRWYDKR 109
Cdd:NF033621   32 ADLLVLPEAVlardDTDPDLSVKS-AQPLDGPFLTQLLAESRGNDLTTVLTVHVPSGDgRAWNTLVALRDGEIIAQYRKL 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630 110 HL---FRMGgEHENFSAGNhqrvfkyfgwRIKPLI-----------CYDLRFPVWSRNR--NNYDLLIYVANW-PAPRRE 172
Cdd:NF033621  111 HLydaFSMQ-ESRRVDAGN----------EIPPLVevagmkvglmtCYDLRFPELARRLalDGADVLVLPAAWvRGPLKE 179
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1082599630 173 V-WKTLLKARAIENQCYVIGVNRVGTDGMgityaGDSMIIDFKGQVISELPEGEQGIgTATLSMSELRIFREKFPV 247
Cdd:NF033621  180 HhWETLLAARALENTCYMVAVGECGNRNI-----GQSMVVDPLGVTIAAAAEAPALI-FAELDPERIAHAREQLPV 249
lnt TIGR00546
apolipoprotein N-acyltransferase; This enzyme transfers the acyl group to lipoproteins in the ...
2-217 1.29e-09

apolipoprotein N-acyltransferase; This enzyme transfers the acyl group to lipoproteins in the lgt/lsp/lnt system which is found broadly in bacteria but not in archaea. This model represents one component of the "lipoprotein lgt/lsp/lnt system" genome property. [Protein fate, Protein modification and repair]


Pssm-ID: 273129 [Multi-domain]  Cd Length: 391  Bit Score: 57.75  E-value: 1.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630   2 ENLKVAFIQT----DLAW--ENPSANIK--TSDRwVDQVGTADVIVLPEmfnTGFTMNVASMAQSNSgqtiQWMKNKSLE 73
Cdd:TIGR00546 158 PTLNVALVQPnipqDLKFdsEGLEAILEilTSLT-KQAVEKPDLVVWPE---TAFPFDLENSPQKLA----DRLKLLVLS 229
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630  74 NNTSIMGSLIVRDEE---KYYNRFVMAYPCADIRW-YDKRHL------------------FRMGGEHENFSAGNHQRVFK 131
Cdd:TIGR00546 230 KGIPILIGAPDAVPGgpyHYYNSAYLVDPGGEVVQrYDKVKLvpfgeyiplgflfkwlskLFFLLSQEDFSRGPGPQVLK 309
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630 132 YFGWRIKPLICYDLRFPVWSRN--RNNYDLLIYVAN--WPAPRREVWK--TLLKARAIENQCYVIgvnRVGTdgmgityA 205
Cdd:TIGR00546 310 LPGGKIAPLICYESIFPDLVRAsaRQGAELLVNLTNdaWFGDSSGPWQhfALARFRAIENGRPLV---RATN-------T 379
                         250
                  ....*....|..
gi 1082599630 206 GDSMIIDFKGQV 217
Cdd:TIGR00546 380 GISAVIDPRGRT 391
 
Name Accession Description Interval E-value
Xc-1258_like cd07575
Xanthomonas campestris XC1258 and related proteins, members of the nitrilase superfamily ...
4-255 7.64e-156

Xanthomonas campestris XC1258 and related proteins, members of the nitrilase superfamily (putative class 13 nitrilases); Uncharacterized subgroup belonging to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup either represents a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. XC1258 is a homotetramer.


Pssm-ID: 143599  Cd Length: 252  Bit Score: 433.50  E-value: 7.64e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630   4 LKVAFIQTDLAWENPSANIKTSDRWVDQV-GTADVIVLPEMFNTGFTMNVASMAQSNSGQTIQWMKNKSLENNTSIMGSL 82
Cdd:cd07575     1 LKIALIQTDLVWEDPEANLAHFEEKIEQLkEKTDLIVLPEMFTTGFSMNAEALAEPMNGPTLQWMKAQAKKKGAAITGSL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630  83 IVRDEEKYYNRFVMAYPCADIRWYDKRHLFRMGGEHENFSAGNHQRVFKYFGWRIKPLICYDLRFPVWSRNRNNYDLLIY 162
Cdd:cd07575    81 IIKEGGKYYNRLYFVTPDGEVYHYDKRHLFRMAGEHKVYTAGNERVIVEYKGWKILLQVCYDLRFPVWSRNTNDYDLLLY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630 163 VANWPAPRREVWKTLLKARAIENQCYVIGVNRVGTDGMGITYAGDSMIIDFKGQVISELPEGEqGIGTATLSMSELRIFR 242
Cdd:cd07575   161 VANWPAPRRAAWDTLLKARAIENQAYVIGVNRVGTDGNGLEYSGDSAVIDPLGEPLAEAEEDE-GVLTATLDKEALQEFR 239
                         250
                  ....*....|...
gi 1082599630 243 EKFPVHLDADDFE 255
Cdd:cd07575   240 EKFPFLKDADSFT 252
PRK10438 PRK10438
C-N hydrolase family amidase; Provisional
1-254 5.37e-107

C-N hydrolase family amidase; Provisional


Pssm-ID: 182461  Cd Length: 256  Bit Score: 309.75  E-value: 5.37e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630   1 MENLKVAFIQTDLAWENPSANIKTSDRWVDQVGTADVIVLPEMFNTGFTMNVA--SMAQSnsgQTIQWMKNKSLENNTSI 78
Cdd:PRK10438    1 MSGLKITLLQQPLVWMDGPANLRHFDRQLEGITGRDVIVLPEMFTTGFAMEAAasSLPQD---DVVAWMTAKAQQTNALI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630  79 MGSLIVRDEEKYYNRFVMAYPCADIRWYDKRHLFRMGGEHENFSAGNHQRVFKYFGWRIKPLICYDLRFPVWSRNRNNYD 158
Cdd:PRK10438   78 AGSVALQTESGAVNRFLLVEPGGTVHFYDKRHLFRMADEHLHYKAGNARVIVEWRGWRILPLVCYDLRFPVWSRNRNDYD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630 159 LLIYVANWPAPRREVWKTLLKARAIENQCYVIGVNRVGTDGMGITYAGDSMIIDFKGQVISELPEGEQGIGTATLSMSEL 238
Cdd:PRK10438  158 LALYVANWPAPRSLHWQTLLTARAIENQAYVAGCNRVGSDGNGHHYRGDSRIINPQGEIIATAEPHQATRIDAELSLEAL 237
                         250
                  ....*....|....*.
gi 1082599630 239 RIFREKFPVHLDADDF 254
Cdd:PRK10438  238 QEYREKFPAWRDADEF 253
nitrilase_5 cd07583
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
5-250 1.31e-89

Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). Class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup represents either a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer.


Pssm-ID: 143607  Cd Length: 253  Bit Score: 265.56  E-value: 1.31e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630   5 KVAFIQTDLAWENPSANIKTSDRWVDQV--GTADVIVLPEMFNTGFTMNV-ASMAQSNSGQTIQWMKNKSLENNTSIM-G 80
Cdd:cd07583     1 KIALIQLDIVWGDPEANIERVESLIEEAaaAGADLIVLPEMWNTGYFLDDlYELADEDGGETVSFLSELAKKHGVNIVaG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630  81 SLIVRDEEKYYNRFVMAYPCADIRW-YDKRHLFRMGGEHENFSAGNHQRVFKYFGWRIKPLICYDLRFPVWSRN--RNNY 157
Cdd:cd07583    81 SVAEKEGGKLYNTAYVIDPDGELIAtYRKIHLFGLMGEDKYLTAGDELEVFELDGGKVGLFICYDLRFPELFRKlaLEGA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630 158 DLLIYVANWPAPRREVWKTLLKARAIENQCYVIGVNRVGTDGmGITYAGDSMIIDFKGQVISELPEGEQGIgTATLSMSE 237
Cdd:cd07583   161 EILFVPAEWPAARIEHWRTLLRARAIENQAFVVACNRVGTDG-GNEFGGHSMVIDPWGEVLAEAGEEEEIL-TAEIDLEE 238
                         250
                  ....*....|...
gi 1082599630 238 LRIFREKFPVHLD 250
Cdd:cd07583   239 VAEVRKKIPVFKD 251
Nit2 COG0388
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];
3-254 2.25e-82

Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];


Pssm-ID: 440157 [Multi-domain]  Cd Length: 264  Bit Score: 247.47  E-value: 2.25e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630   3 NLKVAFIQTDLAWENPSANIKTSDRWVDQVGT--ADVIVLPEMFNTGFTMN---VASMAQSNSGQTIQWMKNKSLENNTS 77
Cdd:COG0388     1 TMRIALAQLNPTVGDIEANLAKIEELIREAAAqgADLVVFPELFLTGYPPEdddLLELAEPLDGPALAALAELARELGIA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630  78 IMGSLIVRDEE-KYYNRFVMAYPCADIR-WYDKRHLFRMGGEHEN--FSAGNHQRVFKYFGWRIKPLICYDLRFPVWSRN 153
Cdd:COG0388    81 VVVGLPERDEGgRLYNTALVIDPDGEILgRYRKIHLPNYGVFDEKryFTPGDELVVFDTDGGRIGVLICYDLWFPELARA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630 154 --RNNYDLLIYVANWPAPR-REVWKTLLKARAIENQCYVIGVNRVGTDGmGITYAGDSMIIDFKGQVISELPEGEqGIGT 230
Cdd:COG0388   161 laLAGADLLLVPSASPFGRgKDHWELLLRARAIENGCYVVAANQVGGED-GLVFDGGSMIVDPDGEVLAEAGDEE-GLLV 238
                         250       260
                  ....*....|....*....|....
gi 1082599630 231 ATLSMSELRIFREKFPVHLDADDF 254
Cdd:COG0388   239 ADIDLDRLREARRRFPVLRDRRPD 262
nitrilase cd07197
Nitrilase superfamily, including nitrile- or amide-hydrolyzing enzymes and amide-condensing ...
6-250 2.85e-68

Nitrilase superfamily, including nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes; This superfamily (also known as the C-N hydrolase superfamily) contains hydrolases that break carbon-nitrogen bonds; it includes nitrilases, cyanide dihydratases, aliphatic amidases, N-terminal amidases, beta-ureidopropionases, biotinidases, pantotheinase, N-carbamyl-D-amino acid amidohydrolases, the glutaminase domain of glutamine-dependent NAD+ synthetase, apolipoprotein N-acyltransferases, and N-carbamoylputrescine amidohydrolases, among others. These enzymes depend on a Glu-Lys-Cys catalytic triad, and work through a thiol acylenzyme intermediate. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. These oligomers include dimers, tetramers, hexamers, octamers, tetradecamers, octadecamers, as well as variable length helical arrangements and homo-oligomeric spirals. These proteins have roles in vitamin and co-enzyme metabolism, in detoxifying small molecules, in the synthesis of signaling molecules, and in the post-translational modification of proteins. They are used industrially, as biocatalysts in the fine chemical and pharmaceutical industry, in cyanide remediation, and in the treatment of toxic effluent. This superfamily has been classified previously in the literature, based on global and structure-based sequence analysis, into thirteen different enzyme classes (referred to as 1-13). This hierarchy includes those thirteen classes and a few additional subfamilies. A putative distant relative, the plasmid-borne TraB family, has not been included in the hierarchy.


Pssm-ID: 143587 [Multi-domain]  Cd Length: 253  Bit Score: 211.41  E-value: 2.85e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630   6 VAFIQTDLAWENPSANIKTSDRWVDQVGT--ADVIVLPEMFNTGF----TMNVASMAQSNSGQTIQWMKNKSLENNTSIM 79
Cdd:cd07197     1 IAAVQLAPKIGDVEANLAKALRLIKEAAEqgADLIVLPELFLTGYsfesAKEDLDLAEELDGPTLEALAELAKELGIYIV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630  80 GSLIVRDEEKYYNRFVMAYPCADIR-WYDKRHLFRMGgEHENFSAGNHQRVFKYFGWRIKPLICYDLRFPVWSR--NRNN 156
Cdd:cd07197    81 AGIAEKDGDKLYNTAVVIDPDGEIIgKYRKIHLFDFG-ERRYFSPGDEFPVFDTPGGKIGLLICYDLRFPELARelALKG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630 157 YDLLIYVANWPAPRREVWKTLLKARAIENQCYVIGVNRVGTDGmGITYAGDSMIIDFKGQVISELPEGEqGIGTATLSMS 236
Cdd:cd07197   160 ADIILVPAAWPTARREHWELLLRARAIENGVYVVAANRVGEEG-GLEFAGGSMIVDPDGEVLAEASEEE-GILVAELDLD 237
                         250
                  ....*....|....
gi 1082599630 237 ELRIFREKFPVHLD 250
Cdd:cd07197   238 ELREARKRWSYLRD 251
nit cd07572
Nit1, Nit 2, and related proteins, and the Nit1-like domain of NitFhit (class 10 nitrilases); ...
5-247 8.34e-39

Nit1, Nit 2, and related proteins, and the Nit1-like domain of NitFhit (class 10 nitrilases); This subgroup includes mammalian Nit1 and Nit2, the Nit1-like domain of the invertebrate NitFhit, and various uncharacterized bacterial and archaeal Nit-like proteins. Nit1 and Nit2 are candidate tumor suppressor proteins. In NitFhit, the Nit1-like domain is encoded as a fusion protein with the non-homologous tumor suppressor, fragile histidine triad (Fhit). Mammalian Nit1 and Fhit may affect distinct signal pathways, and both may participate in DNA damage-induced apoptosis. Nit1 is a negative regulator in T cells. Overexpression of Nit2 in HeLa cells leads to a suppression of cell growth through cell cycle arrest in G2. These Nit proteins and the Nit1-like domain of NitFhit belong to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to class 10.


Pssm-ID: 143596  Cd Length: 265  Bit Score: 136.02  E-value: 8.34e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630   5 KVAFIQTDLAwENPSANIKTSDRWVDQVGT--ADVIVLPEMFNTgFTMN----VASMAQSNSGQTIQWMKNKSLENN-TS 77
Cdd:cd07572     1 RVALIQMTST-ADKEANLARAKELIEEAAAqgAKLVVLPECFNY-PGGTdafkLALAEEEGDGPTLQALSELAKEHGiWL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630  78 IMGSLIVRDEE--KYYNR-FVMAyPCADI--RwYDKRHLFRM---GG----EHENFSAGNHQRVFKYFGWRIKPLICYDL 145
Cdd:cd07572    79 VGGSIPERDDDdgKVYNTsLVFD-PDGELvaR-YRKIHLFDVdvpGGisyrESDTLTPGDEVVVVDTPFGKIGLGICYDL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630 146 RFPVWSR--NRNNYDLLIYVA--NW---PAPrrevWKTLLKARAIENQCYVIGVNRVGTDGMG-ITYaGDSMIIDFKGQV 217
Cdd:cd07572   157 RFPELARalARQGADILTVPAafTMttgPAH----WELLLRARAIENQCYVVAAAQAGDHEAGrETY-GHSMIVDPWGEV 231
                         250       260       270
                  ....*....|....*....|....*....|
gi 1082599630 218 ISELPEGEqGIGTATLSMSELRIFREKFPV 247
Cdd:cd07572   232 LAEAGEGE-GVVVAEIDLDRLEEVRRQIPV 260
nitrilase_3 cd07581
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
16-247 3.23e-37

Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). Class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup represents either a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer.


Pssm-ID: 143605  Cd Length: 255  Bit Score: 131.54  E-value: 3.23e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630  16 ENPSANIKTSDRWVDQVGT--ADVIVLPE--MFNTGFT-MNVASMAQSNSGQTIQWMKNKSLENNTSIMGSLIVR-DEEK 89
Cdd:cd07581    10 GDKEENLEKVRRLLAEAAAagADLVVFPEytMARFGDGlDDYARVAEPLDGPFVSALARLARELGITVVAGMFEPaGDGR 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630  90 YYNRFVMAYPC-ADIRWYDKRHLFRMGG--EHENFSAGN--HQRVFKYFGWRIKPLICYDLRFPVWSRN--RNNYDLLIY 162
Cdd:cd07581    90 VYNTLVVVGPDgEIIAVYRKIHLYDAFGfrESDTVAPGDelPPVVFVVGGVKVGLATCYDLRFPELARAlaLAGADVIVV 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630 163 VANW-PAPRREV-WKTLLKARAIENQCYVIGVNRVGTdgmgiTYAGDSMIIDFKGQVISELPEGEqGIGTATLSMSELRI 240
Cdd:cd07581   170 PAAWvAGPGKEEhWETLLRARALENTVYVAAAGQAGP-----RGIGRSMVVDPLGVVLADLGERE-GLLVADIDPERVEE 243

                  ....*..
gi 1082599630 241 FREKFPV 247
Cdd:cd07581   244 AREALPV 250
Ph0642_like cd07577
Pyrococcus horikoshii Ph0642 and related proteins, members of the nitrilase superfamily ...
5-246 2.23e-36

Pyrococcus horikoshii Ph0642 and related proteins, members of the nitrilase superfamily (putative class 13 nitrilases); Uncharacterized subgroup of the nitrilase superfamily. This superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. Pyrococcus horikoshii Ph0642 is a hypothetical protein belonging to this subgroup. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). This subgroup was classified as belonging to class 13, which represents proteins that at the time were difficult to place in a distinct similarity group. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer.


Pssm-ID: 143601  Cd Length: 259  Bit Score: 129.73  E-value: 2.23e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630   5 KVAFIQTDLAWENPSANIKTSDRWVDQVgTADVIVLPEMFNTGFTMN----VASMAQS-NSGQTIQWMKNKSLENNTSIM 79
Cdd:cd07577     1 KVGYVQFNPKFGEVEKNLKKVESLIKGV-EADLIVLPELFNTGYAFTskeeVASLAESiPDGPTTRFLQELARETGAYIV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630  80 GSLIVRDEEKYYNRFVMAYPCADIRWYDKRHLFrmggEHEN--FSAGNHQ-RVFKYFGWRIKPLICYDLRFPVWSRN--R 154
Cdd:cd07577    80 AGLPERDGDKFYNSAVVVGPEGYIGIYRKTHLF----YEEKlfFEPGDTGfRVFDIGDIRIGVMICFDWYFPEAARTlaL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630 155 NNYDLLIYVANWPAPrreVWKTLLKARAIENQCYVIGVNRVGTD---GMGITYAGDSMIIDFKGQVISELPEGEQGIGTA 231
Cdd:cd07577   156 KGADIIAHPANLVLP---YCPKAMPIRALENRVFTITANRIGTEergGETLRFIGKSQITSPKGEVLARAPEDGEEVLVA 232
                         250       260
                  ....*....|....*....|....
gi 1082599630 232 TLSMSELR---------IFREKFP 246
Cdd:cd07577   233 EIDPRLARdkrineendIFKDRRP 256
CN_hydrolase pfam00795
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ...
5-242 6.78e-36

Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. The family includes: Nitrilase EC:3.5.5.1, Aliphatic amidase EC:3.5.1.4, Biotidinase EC:3.5.1.12, Beta-ureidopropionase EC:3.5.1.6. Nitrilase-related proteins generally have a conserved E-K-C catalytic triad, and are multimeric alpha-beta-beta-alpha sandwich proteins.


Pssm-ID: 425873 [Multi-domain]  Cd Length: 257  Bit Score: 128.24  E-value: 6.78e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630   5 KVAFIQTDLAWENPSANIKTSDRWVDQV--GTADVIVLPEMFNTGFtMNVASM---AQSNSGQTIQWMKNKSLENNTSIM 79
Cdd:pfam00795   1 RVALVQLPQGFWDLEANLQKALELIEEAarYGADLIVLPELFITGY-PCWAHFleaAEVGDGETLAGLAALARKNGIAIV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630  80 GSLIVRDEE--KYYNRFVMAYPCADIRW-YDKRHLFRMGG-----EHENFSAGNHQRVFKYFGWRIKPLICYDLRFPVWS 151
Cdd:pfam00795  80 IGLIERWLTggRLYNTAVLLDPDGKLVGkYRKLHLFPEPRppgfrERVLFEPGDGGTVFDTPLGKIGAAICYEIRFPELL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630 152 R--NRNNYDLLIYVAN----WPAPRREVWKTLLKARAIENQCYVIGVNRVGTDGMGITYAGDSMIIDFKGQVISELPEGE 225
Cdd:pfam00795 160 RalALKGAEILINPSArapfPGSLGPPQWLLLARARALENGCFVIAANQVGGEEDAPWPYGHSMIIDPDGRILAGAGEWE 239
                         250
                  ....*....|....*..
gi 1082599630 226 QGIGTATLSMSELRIFR 242
Cdd:pfam00795 240 EGVLIADIDLALVRAWR 256
R-amidase_like cd07576
Pseudomonas sp. MCI3434 R-amidase and related proteins (putative class 13 nitrilases); ...
5-250 7.88e-34

Pseudomonas sp. MCI3434 R-amidase and related proteins (putative class 13 nitrilases); Pseudomonas sp. MCI3434 R-amidase hydrolyzes (R,S)-piperazine-2-tert-butylcarboxamide to form (R)-piperazine-2-carboxylic acid. It does so with strict R-stereoselectively. Its preferred substrates are carboxamide compounds which have the amino or imino group connected to their beta- or gamma-carbon. This subgroup belongs to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), class 13 represents proteins that at the time were difficult to place in a distinct similarity group. It has been suggested that this subgroup represents a new class. Members of the nitrilase superfamily generally form homomeric complexes, the basic building block of which is a homodimer. Native R-amidase however appears to be a monomer.


Pssm-ID: 143600  Cd Length: 254  Bit Score: 122.69  E-value: 7.88e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630   5 KVAFIQTDLAWENPSANIktsdRWVDQVGT------ADVIVLPEMFNTGFTM--NVASMAQSNSGQTIQWMKNKSLENNT 76
Cdd:cd07576     1 RLALYQGPARDGDVAANL----ARLDEAAAraaaagADLLVFPELFLTGYNIgdAVARLAEPADGPALQALRAIARRHGI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630  77 SIMGSLIVRDEEKYYNRFVMAYPCADIRW-YDKRHLFrmGG-EHENFSAGNHQRVFKYFGWRIKPLICYDLRFPVWSRN- 153
Cdd:cd07576    77 AIVVGYPERAGGAVYNAAVLIDEDGTVLAnYRKTHLF--GDsERAAFTPGDRFPVVELRGLRVGLLICYDVEFPELVRAl 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630 154 -RNNYDLLIyV--ANwPAPRREVWKTLLKARAIENQCYVIGVNRVGTDGmGITYAGDSMIIDFKGQVISELPEGEqGIGT 230
Cdd:cd07576   155 aLAGADLVL-VptAL-MEPYGFVARTLVPARAFENQIFVAYANRCGAED-GLTYVGLSSIAGPDGTVLARAGRGE-ALLV 230
                         250       260
                  ....*....|....*....|
gi 1082599630 231 ATLSMSELRIFREKFPvHLD 250
Cdd:cd07576   231 ADLDPAALAAARRENP-YLA 249
nitrilase_6 cd07584
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
5-246 7.58e-33

Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). Class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup represents either a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer.


Pssm-ID: 143608  Cd Length: 258  Bit Score: 120.17  E-value: 7.58e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630   5 KVAFIQTDLAWENPSANIKTSDRWVDQVGT--ADVIVLPEMFNTGFTMNVAS-----MAQSNSGQTIQWMKNKSLENNTS 77
Cdd:cd07584     1 KVALIQMDSVLGDVKANLKKAAELCKEAAAegADLICFPELATTGYRPDLLGpklweLSEPIDGPTVRLFSELAKELGVY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630  78 IMGSLIVRDE--EKYYNRFVMAYPCADIRW-YDKRHLFrmGGEHENFSAGNHQRVFKY-FGwRIKPLICYDLRFPVWSR- 152
Cdd:cd07584    81 IVCGFVEKGGvpGKVYNSAVVIDPEGESLGvYRKIHLW--GLEKQYFREGEQYPVFDTpFG-KIGVMICYDMGFPEVARi 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630 153 -NRNNYDLLIYVANWPAPRREVWKTLLKARAIENQCYVIGVNRVGTDGMGITYaGDSMIIDFKGQVISELPEGEQGIGTA 231
Cdd:cd07584   158 lTLKGAEVIFCPSAWREQDADIWDINLPARALENTVFVAAVNRVGNEGDLVLF-GKSKILNPRGQVLAEASEEAEEILYA 236
                         250
                  ....*....|....*
gi 1082599630 232 TLSMSELRIFREKFP 246
Cdd:cd07584   237 EIDLDAIADYRMTLP 251
nitrilase_7 cd07585
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
17-243 5.44e-30

Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). Class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup represents either a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer.


Pssm-ID: 143609  Cd Length: 261  Bit Score: 112.79  E-value: 5.44e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630  17 NPSANIKTSDRWVDQVGT--ADVIVLPEMFNTGFTMNVAS--MAQSNSGQTIQWMKNKSLENNTSIMGSLIVRDEEKYYN 92
Cdd:cd07585    13 DKARNLAVIARWTRKAAAqgAELVCFPEMCITGYTHVRALsrEAEVPDGPSTQALSDLARRYGLTILAGLIEKAGDRPYN 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630  93 RFVMAYPCADIRWYDKRHLFRMggEHENFSAGNHQRVFKYFGWRIKPLICYDLRFPVWSRnrnNYDLL---IYVA----- 164
Cdd:cd07585    93 TYLVCLPDGLVHRYRKLHLFRR--EHPYIAAGDEYPVFATPGVRFGILICYDNHFPENVR---ATALLgaeILFAphatp 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630 165 -NWPAPRREVWKTLLKARAIENQCYVIGVNRVGTDGmGITYAGDSMIIDFKGQVISELPEGEQGIGTATLSMSELRIFRE 243
Cdd:cd07585   168 gTTSPKGREWWMRWLPARAYDNGVFVAACNGVGRDG-GEVFPGGAMILDPYGRVLAETTSGGDGMVVADLDLDLINTVRG 246
nitrilase_8 cd07586
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
5-252 1.18e-24

Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). Class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup represents either a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer.


Pssm-ID: 143610  Cd Length: 269  Bit Score: 98.90  E-value: 1.18e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630   5 KVAFIQTDLAWENPSANIKTSDRWVDQV--GTADVIVLPEMFNTGFTM--NVASMAQSNSGQTIQWMKNKSlENNTSIMG 80
Cdd:cd07586     1 RVAIAQIDPVLGDVEENLEKHLEIIETAreRGADLVVFPELSLTGYNLgdLVYEVAMHADDPRLQALAEAS-GGICVVFG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630  81 SLIVRDEEKYYNrfVMAYPC--ADIRWYDKRHLFRMGG--EHENFSAGNHQRVFKYFGWRIKPLICYDLRFP--VWSRNR 154
Cdd:cd07586    80 FVEEGRDGRFYN--SAAYLEdgRVVHVHRKVYLPTYGLfeEGRYFAPGSHLRAFDTRFGRAGVLICEDAWHPslPYLLAL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630 155 NNYDLLIYVANwpAPRR---------EVWKTLLKARAIENQCYVIGVNRVGTDGmGITYAGDSMIIDFKGQVISELPEGE 225
Cdd:cd07586   158 DGADVIFIPAN--SPARgvggdfdneENWETLLKFYAMMNGVYVVFANRVGVED-GVYFWGGSRVVDPDGEVVAEAPLFE 234
                         250       260
                  ....*....|....*....|....*..
gi 1082599630 226 QGIGTATLSMSELRIFREKFPVHLDAD 252
Cdd:cd07586   235 EDLLVAELDRSAIRRARFFSPTFRDED 261
nitrilase_2 cd07580
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
5-239 6.55e-22

Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). Class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup represents either a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer.


Pssm-ID: 143604  Cd Length: 268  Bit Score: 91.64  E-value: 6.55e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630   5 KVAFIQTDLAWENPSANIKTSDRWVDQV--GTADVIVLPEMFNTGFTMN-----VASMAQSNSGQTIQWMKNKSLENNTS 77
Cdd:cd07580     1 RVACVQFDPRVGDLDANLARSIELIREAadAGANLVVLPELANTGYVFEsrdeaFALAEEVPDGASTRAWAELAAELGLY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630  78 IMGSLIVRDEEKYYNRFVMAYPCADIRWYDKRHLFrmGGEHENFSAGNHQ-RVFKY-FGwRIKPLICYDLRFPVWSRN-- 153
Cdd:cd07580    81 IVAGFAERDGDRLYNSAVLVGPDGVIGTYRKAHLW--NEEKLLFEPGDLGlPVFDTpFG-RIGVAICYDGWFPETFRLla 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630 154 RNNYDLLIYVANW-PAPR-----REVWKTLLKARAIENQCYVIGVNRVGTDgMGITYAGDSMIIDFKGQVISEL-PEGEQ 226
Cdd:cd07580   158 LQGADIVCVPTNWvPMPRppeggPPMANILAMAAAHSNGLFIACADRVGTE-RGQPFIGQSLIVGPDGWPLAGPaSGDEE 236
                         250
                  ....*....|...
gi 1082599630 227 GIGTATLSMSELR 239
Cdd:cd07580   237 EILLADIDLTAAR 249
nitrilase_Rim1_like cd07574
Uncharacterized subgroup of the nitrilase superfamily; some members of this subgroup have an ...
4-252 1.23e-19

Uncharacterized subgroup of the nitrilase superfamily; some members of this subgroup have an N-terminal RimI domain (class 12 nitrilases); Some members of this subgroup are implicated in post-translational modification, as they contain an N-terminal GCN5-related N-acetyltransferase (GNAT) protein RimI family domain. The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to class 12. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer.


Pssm-ID: 143598  Cd Length: 280  Bit Score: 85.72  E-value: 1.23e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630   4 LKVAFIQTDLAW-ENPSANIKTSDRWVDQVGT--ADVIVLPEMFNTGFtMNVASMAQSNSGQTIQW-----------MKN 69
Cdd:cd07574     1 VRVAAAQYPLRRyASFEEFAAKVEYWVAEAAGygADLLVFPEYFTMEL-LSLLPEAIDGLDEAIRAlaaltpdyvalFSE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630  70 KSLENNTSIM-GSLIVRDEEKYYNRFVMAYPCADIRWYDKRHLFRMGGEHENFSAGNHQRVFKYFGWRIKPLICYDLRFP 148
Cdd:cd07574    80 LARKYGINIIaGSMPVREDGRLYNRAYLFGPDGTIGHQDKLHMTPFEREEWGISGGDKLKVFDTDLGKIGILICYDSEFP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630 149 VWSR-----------------NRNNYDLLIYVAnwpaprrevwktllKARAIENQCYVIGVNRVG----TDGMGITYAGd 207
Cdd:cd07574   160 ELARalaeagadlllvpsctdTRAGYWRVRIGA--------------QARALENQCYVVQSGTVGnapwSPAVDVNYGQ- 224
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1082599630 208 SMII---DF----KGqVISELPEGEQGIGTATLSMSELRIFREKFPVHLDAD 252
Cdd:cd07574   225 AAVYtpcDFgfpeDG-ILAEGEPNTEGWLIADLDLEALRRLREEGSVRNLRD 275
PLN02798 PLN02798
nitrilase
86-247 1.30e-18

nitrilase


Pssm-ID: 215428  Cd Length: 286  Bit Score: 82.87  E-value: 1.30e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630  86 DEEKYYNRFVMAYPCADIR-WYDKRHLFRM---GG----EHENFSAGNHQRVFKYFGWRIKPLICYDLRFP-VWSRNRNN 156
Cdd:PLN02798   99 DDSHLYNTHVLIDDSGEIRsSYRKIHLFDVdvpGGpvlkESSFTAPGKTIVAVDSPVGRLGLTVCYDLRFPeLYQQLRFE 178
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630 157 YDLLIYVAnwPAPRREV-----WKTLLKARAIENQCYVIGVNRVGTDGMGITYAGDSMIIDFKGQVISELPEGEQ-GIGT 230
Cdd:PLN02798  179 HGAQVLLV--PSAFTKPtgeahWEVLLRARAIETQCYVIAAAQAGKHNEKRESYGHALIIDPWGTVVARLPDRLStGIAV 256
                         170
                  ....*....|....*..
gi 1082599630 231 ATLSMSELRIFREKFPV 247
Cdd:PLN02798  257 ADIDLSLLDSVRTKMPI 273
CPA cd07573
N-carbamoylputrescine amidohydrolase (CPA) (class 11 nitrilases); CPA (EC 3.5.1.53, also known ...
4-247 6.95e-18

N-carbamoylputrescine amidohydrolase (CPA) (class 11 nitrilases); CPA (EC 3.5.1.53, also known as N-carbamoylputrescine amidase and carbamoylputrescine hydrolase) converts N-carbamoylputrescine to putrescine, a step in polyamine biosynthesis in plants and bacteria. This subgroup includes Arabidopsis thaliana CPA, also known as nitrilase-like 1 (NLP1), and Pseudomonas aeruginosa AguB. This subgroup belongs to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to class 11. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer; P. aeruginosa AugB is a homohexamer, Arabidopsis thaliana NLP1 is a homooctomer.


Pssm-ID: 143597  Cd Length: 284  Bit Score: 80.68  E-value: 6.95e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630   4 LKVAFIQTDLAWeNPSANIKTSDRWVDQV---GtADVIVLPEMFNTGF---TMNVAS---MAQSNSGQTIQWMKNKSLEN 74
Cdd:cd07573     1 VTVALVQMACSE-DPEANLAKAEELVREAaaqG-AQIVCLQELFETPYfcqEEDEDYfdlAEPPIPGPTTARFQALAKEL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630  75 NTSIMGSLIVRDEEK-YYNRFVMAYpcAD---IRWYDKRHLFRMGGEHEN--FSAGN-HQRVFKYFGWRIKPLICYDLRF 147
Cdd:cd07573    79 GVVIPVSLFEKRGNGlYYNSAVVID--ADgslLGVYRKMHIPDDPGYYEKfyFTPGDtGFKVFDTRYGRIGVLICWDQWF 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630 148 PVWSRNR--NNYDLLIY---------VANWPAPRREVWKTLLKARAIENQCYVIGVNRVGT---DGMGITYAGDSMIIDF 213
Cdd:cd07573   157 PEAARLMalQGAEILFYptaigsepqEPPEGLDQRDAWQRVQRGHAIANGVPVAAVNRVGVegdPGSGITFYGSSFIADP 236
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1082599630 214 KGQVISELPEGEQGIGTATLSMSELRIFREKFPV 247
Cdd:cd07573   237 FGEILAQASRDEEEILVAEFDLDEIEEVRRAWPF 270
de_GSH_amidase NF033621
deaminated glutathione amidase;
35-247 9.55e-18

deaminated glutathione amidase;


Pssm-ID: 468114  Cd Length: 260  Bit Score: 79.94  E-value: 9.55e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630  35 ADVIVLPEMF----NTGFTMNVASmAQSNSGQTIQWMKNKSLENNTSIMGSLIVRDEE-KYYNRFVMAYPCADIRWYDKR 109
Cdd:NF033621   32 ADLLVLPEAVlardDTDPDLSVKS-AQPLDGPFLTQLLAESRGNDLTTVLTVHVPSGDgRAWNTLVALRDGEIIAQYRKL 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630 110 HL---FRMGgEHENFSAGNhqrvfkyfgwRIKPLI-----------CYDLRFPVWSRNR--NNYDLLIYVANW-PAPRRE 172
Cdd:NF033621  111 HLydaFSMQ-ESRRVDAGN----------EIPPLVevagmkvglmtCYDLRFPELARRLalDGADVLVLPAAWvRGPLKE 179
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1082599630 173 V-WKTLLKARAIENQCYVIGVNRVGTDGMgityaGDSMIIDFKGQVISELPEGEQGIgTATLSMSELRIFREKFPV 247
Cdd:NF033621  180 HhWETLLAARALENTCYMVAVGECGNRNI-----GQSMVVDPLGVTIAAAAEAPALI-FAELDPERIAHAREQLPV 249
Lnt COG0815
Apolipoprotein N-acyltransferase [Cell wall/membrane/envelope biogenesis];
2-233 2.11e-16

Apolipoprotein N-acyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440577 [Multi-domain]  Cd Length: 472  Bit Score: 77.96  E-value: 2.11e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630   2 ENLKVAFIQTDLA----WeNPSANIKTSDRWVDQV-----GTADVIVLPEmfntgftmNVASMAQSNSGQTIQWMKNKSL 72
Cdd:COG0815   193 EPLRVALVQGNIPqdlkW-DPEQRREILDRYLDLTreladDGPDLVVWPE--------TALPFLLDEDPDALARLAAAAR 263
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630  73 ENNTS-IMGSLIVRDEE-KYYNRFVMAYPCADIR-WYDKRHL--FrmgGEH------------------ENFSAGNHQRV 129
Cdd:COG0815   264 EAGAPlLTGAPRRDGGGgRYYNSALLLDPDGGILgRYDKHHLvpF---GEYvplrdllrplipfldlplGDFSPGTGPPV 340
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630 130 FKYFGWRIKPLICYDLRFP--VWSRNRNNYDLLIYVAN--W----PAPR------RevwktllkARAIENQCYVIgvnRV 195
Cdd:COG0815   341 LDLGGVRVGPLICYESIFPelVRDAVRAGADLLVNITNdaWfgdsIGPYqhlaiaR--------LRAIETGRPVV---RA 409
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1082599630 196 GTDGMgityagdSMIIDFKGQVISELPEGEQGIGTATL 233
Cdd:COG0815   410 TNTGI-------SAVIDPDGRVLARLPLFTRGVLVAEV 440
ALP_N-acyl_transferase cd07571
Apolipoprotein N-acyl transferase (class 9 nitrilases); ALP N-acyl transferase (Lnt), is an ...
4-233 5.64e-15

Apolipoprotein N-acyl transferase (class 9 nitrilases); ALP N-acyl transferase (Lnt), is an essential membrane-bound enzyme in gram-negative bacteria, which catalyzes the N-acylation of apolipoproteins, the final step in lipoprotein maturation. This is a reverse amidase (i.e. condensation) reaction. This subgroup belongs to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to class 9.


Pssm-ID: 143595  Cd Length: 270  Bit Score: 72.63  E-value: 5.64e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630   4 LKVAFIQTDLA---WENPSANIKTSDRWVDQVGTA-----DVIVLPEmfntgftmNVASMAQSNSGQTIQWMKNKSLENN 75
Cdd:cd07571     1 LRVALVQGNIPqdeKWDPEQRQATLDRYLDLTRELadekpDLVVWPE--------TALPFDLQRDPDALARLARAARAVG 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630  76 TSIMGSLIVRDEE--KYYNRFVMAYPCADIR-WYDKRHLFrMGGEH------------------ENFSAGNHQRVFKY-F 133
Cdd:cd07571    73 APLLTGAPRREPGggRYYNSALLLDPGGGILgRYDKHHLV-PFGEYvplrdllrflgllfdlpmGDFSPGTGPQPLLLgG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630 134 GWRIKPLICYDLRFP--VWSRNRNNYDLLIYVAN--W----PAPRREVWKTLLkaRAIENQCYVIgvnRVGTDGMgitya 205
Cdd:cd07571   152 GVRVGPLICYESIFPelVRDAVRQGADLLVNITNdaWfgdsAGPYQHLAMARL--RAIETGRPLV---RAANTGI----- 221
                         250       260
                  ....*....|....*....|....*...
gi 1082599630 206 gdSMIIDFKGQVISELPEGEQGIGTATL 233
Cdd:cd07571   222 --SAVIDPDGRIVARLPLFEAGVLVAEV 247
aliphatic_amidase cd07565
aliphatic amidases (class 2 nitrilases); Aliphatic amidases catalyze the hydrolysis of ...
134-243 2.06e-14

aliphatic amidases (class 2 nitrilases); Aliphatic amidases catalyze the hydrolysis of short-chain aliphatic amides to form ammonia and the corresponding organic acid. This group includes Pseudomonas aeruginosa (Pa) AmiE, the amidase from Geobacillus pallidus RAPc8 (RAPc8 amidase), and Helicobacter pylori (Hp) AmiE and AmiF. PaAimE and HpAmiE hydrolyze various very short aliphatic amides, including propionamide, acetamide and acrylamide. HpAmiF is a formamidase which specifically hydrolyzes formamide. These proteins belong to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to class 2. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. HpAmiE , HpAmiF, and RAPc8 amidase, and PaAimE appear to be homohexameric enzymes, trimer of dimers.


Pssm-ID: 143589  Cd Length: 291  Bit Score: 71.16  E-value: 2.06e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630 134 GWRIKPLICYDLRFPVWSRN--RNNYDLLIYVANWPAPRREVWKTLLKARAIENQCYVIGVNRVGTDGMgITYAGDSMII 211
Cdd:cd07565   145 GSKIALIICHDGMYPEIAREcaYKGAELIIRIQGYMYPAKDQWIITNKANAWCNLMYTASVNLAGFDGV-FSYFGESMIV 223
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1082599630 212 DFKGQVISELPEGEQGIGTATLSMSELRIFRE 243
Cdd:cd07565   224 NFDGRTLGEGGREPDEIVTAELSPSLVRDARK 255
nitrilase_4 cd07582
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
38-248 9.08e-14

Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). Class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup represents either a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer.


Pssm-ID: 143606  Cd Length: 294  Bit Score: 69.29  E-value: 9.08e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630  38 IVLPEMFNTGFTMN-------VASMAQSNSGQTIQWMKNKSLENNTSIMGSLIVRDEE---KYYNRFVMAYPCADI--RW 105
Cdd:cd07582    46 VVLPEYALQGFPMGeprevwqFDKAAIDIPGPETEALGEKAKELNVYIAANAYERDPDfpgLYFNTAFIIDPSGEIilRY 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630 106 YDKRHLFRMGGE--HENfsagnHQRVFKYFGW--------------RIKPLICYDLRFPVWSR--NRNNYDLLIY-VANW 166
Cdd:cd07582   126 RKMNSLAAEGSPspHDV-----WDEYIEVYGYgldalfpvadteigNLGCLACEEGLYPEVARglAMNGAEVLLRsSSEV 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630 167 PAPRREVWKTLLKARAIENQCYVIGVNR---VGTDGMGITYAGDSMIIDFKGQVISELPEG-EQGIGTATLSMSELRIFR 242
Cdd:cd07582   201 PSVELDPWEIANRARALENLAYVVSANSggiYGSPYPADSFGGGSMIVDYKGRVLAEAGYGpGSMVAGAEIDIEALRRAR 280

                  ....*.
gi 1082599630 243 EKFPVH 248
Cdd:cd07582   281 ARPGMH 286
lnt PRK00302
apolipoprotein N-acyltransferase; Reviewed
2-233 1.89e-13

apolipoprotein N-acyltransferase; Reviewed


Pssm-ID: 234721 [Multi-domain]  Cd Length: 505  Bit Score: 69.52  E-value: 1.89e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630   2 ENLKVAFIQ----TDLAWeNPSANIKTSDRWVD----QVGTADVIVLPEmfntgftmnVA--SMAQSNSGQTIQWMKNKS 71
Cdd:PRK00302  218 PALKVALVQgnipQSLKW-DPAGLEATLQKYLDlsrpALGPADLIIWPE---------TAipFLLEDLPQAFLKALDDLA 287
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630  72 LENNTS-IMGslIVRDEEK-----YYNRFVMAYPCADIRWYDKRHL------------FR---------MGGehenFSAG 124
Cdd:PRK00302  288 REKGSAlITG--APRAENKqgrydYYNSIYVLGPYGILNRYDKHHLvpfgeyvpleslLRplapffnlpMGD----FSRG 361
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630 125 NH-QRVFKYFGWRIKPLICYDLRFP--VWSRNRNNYDLLIYVAN--W----PAPrrevWKTLLKA--RAIENQCYVIgvn 193
Cdd:PRK00302  362 PYvQPPLLAKGLKLAPLICYEIIFPeeVRANVRQGADLLLNISNdaWfgdsIGP----YQHFQMArmRALELGRPLI--- 434
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1082599630 194 RVGTDGMgityagdSMIIDFKGQVISELPEGEQGIGTATL 233
Cdd:PRK00302  435 RATNTGI-------TAVIDPLGRIIAQLPQFTEGVLDGTV 467
nitrilase_1_R1 cd07578
First nitrilase domain of an uncharacterized subgroup of the nitrilase superfamily (putative ...
32-246 9.87e-11

First nitrilase domain of an uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); Members of this subgroup have two nitrilase domains. This is the first of those two domains. The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). Class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup represents either a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer.


Pssm-ID: 143602  Cd Length: 258  Bit Score: 60.24  E-value: 9.87e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630  32 VGTADVIVLPEMFNTGFT----MNVASMAQSNSGQTIQWMKNKSLENNTSIMGSLIVRDEEK--YYNRFVMAYPCADIRW 105
Cdd:cd07578    31 RAGARLIVTPEMATTGYCwydrAEIAPFVEPIPGPTTARFAELAREHDCYIVVGLPEVDSRSgiYYNSAVLIGPSGVIGR 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630 106 YDKRHLFRmgGEHENFSAGN-HQRVFKYFGWRIKPLICYDLRFPVWSR--NRNNYDLLIYVANW-----PAPrreVWKtl 177
Cdd:cd07578   111 HRKTHPYI--SEPKWAADGDlGHQVFDTEIGRIALLICMDIHFFETARllALGGADVICHISNWlaertPAP---YWI-- 183
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1082599630 178 lkARAIENQCYVIGVNRVGTDgMGITYAGDSMIIDFKGQVISELPEGEqGIGTATLSMSELRifREKFP 246
Cdd:cd07578   184 --NRAFENGCYLIESNRWGLE-RGVQFSGGSCIIEPDGTIQASIDSGD-GVALGEIDLDRAR--HRQFP 246
nitrilases_CHs cd07564
Nitrilases, cyanide hydratase (CH)s, and similar proteins (class 1 nitrilases); Nitrilases ...
161-247 5.55e-10

Nitrilases, cyanide hydratase (CH)s, and similar proteins (class 1 nitrilases); Nitrilases (nitrile aminohydrolases, EC:3.5.5.1) hydrolyze nitriles (RCN) to ammonia and the corresponding carboxylic acid. Most nitrilases prefer aromatic nitriles, some prefer arylacetonitriles and others aliphatic nitriles. This group includes the nitrilase cyanide dihydratase (CDH), which hydrolyzes inorganic cyanide (HCN) to produce formate. It also includes cyanide hydratase (CH), which hydrolyzes HCN to formamide. This group includes four Arabidopsis thaliana nitrilases (Ath)NIT1-4. AthNIT1-3 have a strong substrate preference for phenylpropionitrile (PPN) and other nitriles which may originate from the breakdown of glucosinolates. The product of PPN hydrolysis, phenylacetic acid has auxin activity. AthNIT1-3 can also convert indoacetonitrile to indole-3-acetic acid (IAA, auxin), but with a lower affinity and velocity. From their expression patterns, it has been speculated that NIT3 may produce IAA during the early stages of germination, and that NIT3 may produce IAA during embryo development and maturation. AthNIT4 has a strong substrate specificity for the nitrile, beta-cyano-L-alanine (Ala(CN)), an intermediate of cyanide detoxification. AthNIT4 has both a nitrilase activity and a nitrile hydratase (NHase) activity, which generate aspartic acid and asparagine respectively from Ala(CN). NHase catalyzes the hydration of nitriles to their corresponding amides. This subgroup belongs to a larger nitrilase superfamily comprised of belong to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to class 1.


Pssm-ID: 143588  Cd Length: 297  Bit Score: 58.65  E-value: 5.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630 161 IYVANWPAPR-----REVWKTLLKARAIENQCYVIGVNRVGTDGM--------------GITYAGDSMIIDFKGQVISEL 221
Cdd:cd07564   176 IHVAPWPDFSpyylsREAWLAASRHYALEGRCFVLSACQVVTEEDipadceddeeadplEVLGGGGSAIVGPDGEVLAGP 255
                          90       100
                  ....*....|....*....|....*.
gi 1082599630 222 PEGEQGIGTATLSMSELRIFREKFPV 247
Cdd:cd07564   256 LPDEEGILYADIDLDDIVEAKLDFDP 281
lnt TIGR00546
apolipoprotein N-acyltransferase; This enzyme transfers the acyl group to lipoproteins in the ...
2-217 1.29e-09

apolipoprotein N-acyltransferase; This enzyme transfers the acyl group to lipoproteins in the lgt/lsp/lnt system which is found broadly in bacteria but not in archaea. This model represents one component of the "lipoprotein lgt/lsp/lnt system" genome property. [Protein fate, Protein modification and repair]


Pssm-ID: 273129 [Multi-domain]  Cd Length: 391  Bit Score: 57.75  E-value: 1.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630   2 ENLKVAFIQT----DLAW--ENPSANIK--TSDRwVDQVGTADVIVLPEmfnTGFTMNVASMAQSNSgqtiQWMKNKSLE 73
Cdd:TIGR00546 158 PTLNVALVQPnipqDLKFdsEGLEAILEilTSLT-KQAVEKPDLVVWPE---TAFPFDLENSPQKLA----DRLKLLVLS 229
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630  74 NNTSIMGSLIVRDEE---KYYNRFVMAYPCADIRW-YDKRHL------------------FRMGGEHENFSAGNHQRVFK 131
Cdd:TIGR00546 230 KGIPILIGAPDAVPGgpyHYYNSAYLVDPGGEVVQrYDKVKLvpfgeyiplgflfkwlskLFFLLSQEDFSRGPGPQVLK 309
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630 132 YFGWRIKPLICYDLRFPVWSRN--RNNYDLLIYVAN--WPAPRREVWK--TLLKARAIENQCYVIgvnRVGTdgmgityA 205
Cdd:TIGR00546 310 LPGGKIAPLICYESIFPDLVRAsaRQGAELLVNLTNdaWFGDSSGPWQhfALARFRAIENGRPLV---RATN-------T 379
                         250
                  ....*....|..
gi 1082599630 206 GDSMIIDFKGQV 217
Cdd:TIGR00546 380 GISAVIDPRGRT 391
amiE PRK13286
aliphatic amidase;
134-242 3.20e-09

aliphatic amidase;


Pssm-ID: 237335  Cd Length: 345  Bit Score: 56.67  E-value: 3.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630 134 GWRIKPLICYDLRFP-VWsRN--RNNYDLLIYVANWPAPRREVWKTLLKARAIENQCYVIGVNRVGTDGMgITYAGDSMI 210
Cdd:PRK13286  158 GLKISLIICDDGNYPeIW-RDcaMKGAELIVRCQGYMYPAKEQQVLVAKAMAWANNCYVAVANAAGFDGV-YSYFGHSAI 235
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1082599630 211 IDFKGQVISELPEGEQGIGTATLSMSELRIFR 242
Cdd:PRK13286  236 IGFDGRTLGECGEEEMGIQYAQLSVSQIRDAR 267
GAT_Gln-NAD-synth cd07570
Glutamine aminotransferase (GAT, glutaminase) domain of glutamine-dependent NAD synthetases ...
35-254 2.76e-08

Glutamine aminotransferase (GAT, glutaminase) domain of glutamine-dependent NAD synthetases (class 7 and 8 nitrilases); Glutamine-dependent NAD synthetases are bifunctional enzymes, which have an N-terminal GAT domain and a C-terminal NAD+ synthetase domain. The GAT domain is a glutaminase (EC 3.5.1.2) which hydrolyses L-glutamine to L-glutamate and ammonia. The ammonia is used by the NAD+ synthetase domain in the ATP-dependent amidation of nicotinic acid adenine dinucleotide. Glutamine aminotransferases are categorized depending on their active site residues into different unrelated classes. This class of GAT domain belongs to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to classes 7 and 8. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. Mycobacterium tuberculosis glutamine-dependent NAD+ synthetase forms a homooctamer.


Pssm-ID: 143594 [Multi-domain]  Cd Length: 261  Bit Score: 53.24  E-value: 2.76e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630  35 ADVIVLPEMFNTGFT-----MNVASMAQSNsgQTIQWMKNKSLENN-TSIMGsLIVRDEEKYYNrfvMAYPCAD---IRW 105
Cdd:cd07570    33 ADLVVFPELSLTGYPpedllLRPDFLEAAE--EALEELAAATADLDiAVVVG-LPLRHDGKLYN---AAAVLQNgkiLGV 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630 106 YDKRHL-----FRmggEHENFSAGNHQRVFKYFGWRIKPLICYDLRFP-VWSRN--RNNYDLLI------YVANWPAPRR 171
Cdd:cd07570   107 VPKQLLpnygvFD---EKRYFTPGDKPDVLFFKGLRIGVEICEDLWVPdPPSAElaLAGADLILnlsaspFHLGKQDYRR 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630 172 EvwktLLKARAIENQCYVIGVNRVG--TDgmgITYAGDSMIIDFKGQVISELPEGEqgIGTATLSMSELRIFREKFPVHL 249
Cdd:cd07570   184 E----LVSSRSARTGLPYVYVNQVGgqDD---LVFDGGSFIADNDGELLAEAPRFE--EDLADVDLDRLRSERRRNSSFL 254

                  ....*
gi 1082599630 250 DADDF 254
Cdd:cd07570   255 DEEAE 259
PLN02747 PLN02747
N-carbamolyputrescine amidase
19-246 7.28e-07

N-carbamolyputrescine amidase


Pssm-ID: 215398  Cd Length: 296  Bit Score: 49.38  E-value: 7.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630  19 SANIKTSDRWVDQVGT--ADVIVLPEMFNTGFTMNVASM-----AQSNSGQ-TIQWMKNKSLENNTSIMGSLIVRDEEKY 90
Cdd:PLN02747   21 AANVDKAERLVREAHAkgANIILIQELFEGYYFCQAQREdffqrAKPYEGHpTIARMQKLAKELGVVIPVSFFEEANNAH 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630  91 YNRF-VMAYPCADIRWYDKRHLFRMGGEHENF--SAGNHQ-RVFKYFGWRIKPLICYDLRFPVWSRNR--NNYDLLIY-V 163
Cdd:PLN02747  101 YNSIaIIDADGTDLGLYRKSHIPDGPGYQEKFyfNPGDTGfKVFDTKFAKIGVAICWDQWFPEAARAMvlQGAEVLLYpT 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630 164 ANWPAPR------REVWKTLLKARAIENQCYVIGVNRVGTD-------GMGITYAGDSMIIDFKGQVISELPEGEQGIGT 230
Cdd:PLN02747  181 AIGSEPQdpgldsRDHWKRVMQGHAGANLVPLVASNRIGTEiletehgPSKITFYGGSFIAGPTGEIVAEADDKAEAVLV 260
                         250       260
                  ....*....|....*....|...
gi 1082599630 231 ATLSMSELR-------IFREKFP 246
Cdd:PLN02747  261 AEFDLDQIKskraswgVFRDRRP 283
amiF PRK13287
formamidase; Provisional
134-233 3.29e-06

formamidase; Provisional


Pssm-ID: 183950  Cd Length: 333  Bit Score: 47.38  E-value: 3.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630 134 GWRIKPLICYDLRFPVWSRN--RNNYDLLIYVANWPAPRREVWKTLLKARAIENQCYVIGVNRVGTDGMgITYAGDSMII 211
Cdd:PRK13287  157 GSKLAVCICHDGMFPEMAREaaYKGANVMIRISGYSTQVREQWILTNRSNAWQNLMYTASVNLAGYDGV-FYYFGEGQVC 235
                          90       100
                  ....*....|....*....|..
gi 1082599630 212 DFKGQVISELPEGEQGIGTATL 233
Cdd:PRK13287  236 NFDGTTLVQGHRNPWEIVTAEV 257
ML_beta-AS_like cd07568
mammalian-like beta-alanine synthase (beta-AS) and similar proteins (class 5 nitrilases); This ...
61-250 3.92e-06

mammalian-like beta-alanine synthase (beta-AS) and similar proteins (class 5 nitrilases); This family includes mammalian-like beta-AS (EC 3.5.1.6, also known as beta-ureidopropionase or N-carbamoyl-beta-alanine amidohydrolase). This enzyme catalyzes the third and final step in the catabolic pyrimidine catabolic pathway responsible for the degradation of uracil and thymine, the hydrolysis of N-carbamyl-beta-alanine and N-carbamyl-beta-aminoisobutyrate to the beta-amino acids, beta-alanine and beta-aminoisobutyrate respectively. This family belongs to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to class 5. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. Beta-ASs from this subgroup are found in various oligomeric states, dimer (human), hexamer (calf liver), decamer (Arabidopsis and Zea mays), and in the case of Drosophila melanogaster beta-AS, as a homooctamer assembled as a left-handed helical turn, with the possibility of higher order oligomers formed by adding dimers at either end. Rat beta-AS changes its oligomeric state (hexamer, trimer, dodecamer) in response to allosteric effectors. Eukaryotic Saccharomyces kluyveri beta-AS belongs to a different superfamily.


Pssm-ID: 143592  Cd Length: 287  Bit Score: 47.11  E-value: 3.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630  61 GQTIQWMKNKSLENNTSIMGSLIVRD-EEKYYNRFVMAYpcADIRW---YDKRHLFRMGGEHEN--FSAGNH-QRVFKYF 133
Cdd:cd07568    76 GPTTKRFAALAKEYNMVLILPIYEKEqGGTLYNTAAVID--ADGTYlgkYRKNHIPHVGGFWEKfyFRPGNLgYPVFDTA 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630 134 GWRIKPLICYDLRFPVWSR--NRNNYDLliyVANWPAPRR----EVWKTLLKARAIENQCYVIGVNRVGTD---GMGITY 204
Cdd:cd07568   154 FGKIGVYICYDRHFPEGWRalGLNGAEI---VFNPSATVAglseYLWKLEQPAAAVANGYFVGAINRVGTEapwNIGEFY 230
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1082599630 205 aGDSMIIDFKGQVISELPEGEQGIGTATLSMSELRIFREKFPVHLD 250
Cdd:cd07568   231 -GSSYFVDPRGQFVASASRDKDELLVAELDLDLIREVRDTWQFYRD 275
PRK13981 PRK13981
NAD synthetase; Provisional
35-230 1.33e-05

NAD synthetase; Provisional


Pssm-ID: 237577 [Multi-domain]  Cd Length: 540  Bit Score: 45.92  E-value: 1.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630  35 ADVIVLPEMFNTGF-----TMNVASMAQSNsgQTIQWMKNKSLENNTSIMGSlIVRDEEKYYNrfvmAYPCAD----IRW 105
Cdd:PRK13981   34 ADLLLFPELFLSGYppedlLLRPAFLAACE--AALERLAAATAGGPAVLVGH-PWREGGKLYN----AAALLDggevLAT 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630 106 YDKRHL-----FrmgGEHENFSAGNHQRVFKYFGWRIKPLICYDLRFP-VWSRNRNN-YDLLI------YVANWPAPRRE 172
Cdd:PRK13981  107 YRKQDLpnygvF---DEKRYFAPGPEPGVVELKGVRIGVPICEDIWNPePAETLAEAgAELLLvpnaspYHRGKPDLREA 183
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1082599630 173 VwktlLKARAIENQCYVIGVNRVGtdgmG---ITYAGDSMIIDFKGQVISELPEGEQGIGT 230
Cdd:PRK13981  184 V----LRARVRETGLPLVYLNQVG----GqdeLVFDGASFVLNADGELAARLPAFEEQIAV 236
nitrilase_1_R2 cd07579
Second nitrilase domain of an uncharacterized subgroup of the nitrilase superfamily (putative ...
19-238 2.36e-04

Second nitrilase domain of an uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); Members of this subgroup have two nitrilase domains. This is the second of those two domains. The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). Class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup represents either a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer.


Pssm-ID: 143603  Cd Length: 279  Bit Score: 41.77  E-value: 2.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630  19 SANIKTSDRWVDQV--GTADVIVLPEMFNTGFTmNVASMAQSNSGQTIQWMKNKSLENNTSIMGSLIVRDEEKYYNRFVM 96
Cdd:cd07579    14 AGNLATIDRLAAEAkaTGAELVVFPELALTGLD-DPASEAESDTGPAVSALRRLARRLRLYLVAGFAEADGDGLYNSAVL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630  97 AYPCADIRWYDKRHLfrMGGEHENFSAGNHQRVFKYFGWRIKPLICYDLRFPVWSR--NRNNYDLLIYVA---------- 164
Cdd:cd07579    93 VGPEGLVGTYRKTHL--IEPERSWATPGDTWPVYDLPLGRVGLLIGHDALFPEAGRvlALRGCDLLACPAaiaipfvgah 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599630 165 -------NWPAPRRE---VWKtLLKARAIENQCYVIGVN-----RVGTDGMGItYAGDSMIidFKGQviSELPEGEQGIG 229
Cdd:cd07579   171 agtsvpqPYPIPTGAdptHWH-LARVRAGENNVYFAFANvpdpaRGYTGWSGV-FGPDTFA--FPRQ--EAAIGDEEGIA 244

                  ....*....
gi 1082599630 230 TATLSMSEL 238
Cdd:cd07579   245 WALIDTSNL 253
 
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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