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Conserved domains on  [gi|1002231449|ref|XP_015612707|]
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protein LONG AFTER FAR-RED 3 isoform X1 [Oryza sativa Japonica Group]

Protein Classification

amidohydrolase( domain architecture ID 11446324)

metal-dependent amidohydrolase similar to Bacillus subtilis YtcJ and Arthrobacter pascens N-substituted formamide deformylase, which catalyzes the hydrolysis of N-substituted formamides

CATH:  3.20.20.140
EC:  3.5.-.-
Gene Ontology:  GO:0046872|GO:0016810
PubMed:  9144792
SCOP:  3000176

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
YtcJ COG1574
Predicted amidohydrolase YtcJ [General function prediction only];
31-569 0e+00

Predicted amidohydrolase YtcJ [General function prediction only];


:

Pssm-ID: 441182 [Multi-domain]  Cd Length: 535  Bit Score: 571.74  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002231449  31 LGEAVADMILANATIYTADPAMPFAEAMAVRAGRVLRVGGYYSVKELKGRHTMELNLSGNVVLPGFIDSHVHFIDGGLQL 110
Cdd:COG1574     3 LAAAAADLLLTNGRIYTMDPAQPVAEAVAVRDGRIVAVGSDAEVRALAGPATEVIDLGGKTVLPGFIDAHVHLLGGGLAL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002231449 111 ARVPLRGVTSKDDFINRVKEAVKDKHPGQWIFGGGWNNDFWG-GDYPTAAWLDDISPDNPVWLSRMDGHMGIANSLAMRM 189
Cdd:COG1574    83 LGVDLSGARSLDELLARLRAAAAELPPGEWILGRGWDESLWPeGRFPTRADLDAVSPDRPVVLTRVDGHAAWVNSAALEL 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002231449 190 AGINKNTNNPVGGTIMRTTEGEPTGLLVDAAMKLVFDVISEVSIHERRDALLRASRHALMRGVTTVVDVGSYfpgksekq 269
Cdd:COG1574   163 AGITADTPDPEGGEIERDADGEPTGVLREAAMDLVRAAIPPPTPEELRAALRAALRELASLGITSVHDAGLG-------- 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002231449 270 vWQDFtDIYEWAHSVETMIMRVCLFfPMPTWSRVYDLIHE--KGRMLSQWIHLGGVKAFLDGSLGSSSALFYEHYKDDPR 347
Cdd:COG1574   235 -PDDL-AAYRELAAAGELPLRVVLY-LGADDEDLEELLALglRTGYGDDRLRVGGVKLFADGSLGSRTAALLEPYADDPG 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002231449 348 SYGLQLVDMDYLLNTTLELDKSGLQIAIHAIGDKANDMLLDMYEKVVDLNGMKDHRFRIEHAQHLAPGAAKRFGKHGIIA 427
Cdd:COG1574   312 NRGLLLLDPEELRELVRAADAAGLQVAVHAIGDAAVDEVLDAYEAARAANGRRDRRHRIEHAQLVDPDDLARFAELGVIA 391

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002231449 428 SVQPDHILDDANSAGKKIGIERAERsSYSFRSLLDGGAHLAFGSDWPVSDINPLQAIRTAVSRKPVGwEVPWIPAERLSL 507
Cdd:COG1574   392 SMQPTHATSDGDWAEDRLGPERAAR-AYPFRSLLDAGAPLAFGSDAPVEPLDPLLGIYAAVTRRTPS-GRGLGPEERLTV 469

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002231449 508 DDSLKAHTISAAYACFLDHVLGSLSEGKYADFVILpstSWNEFGSDITD----HVLATYVNGKQAY 569
Cdd:COG1574   470 EEALRAYTIGAAYAAFEEDEKGSLEPGKLADFVVL---DRDPLTVPPEEikdiKVLLTVVGGRVVY 532
 
Name Accession Description Interval E-value
YtcJ COG1574
Predicted amidohydrolase YtcJ [General function prediction only];
31-569 0e+00

Predicted amidohydrolase YtcJ [General function prediction only];


Pssm-ID: 441182 [Multi-domain]  Cd Length: 535  Bit Score: 571.74  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002231449  31 LGEAVADMILANATIYTADPAMPFAEAMAVRAGRVLRVGGYYSVKELKGRHTMELNLSGNVVLPGFIDSHVHFIDGGLQL 110
Cdd:COG1574     3 LAAAAADLLLTNGRIYTMDPAQPVAEAVAVRDGRIVAVGSDAEVRALAGPATEVIDLGGKTVLPGFIDAHVHLLGGGLAL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002231449 111 ARVPLRGVTSKDDFINRVKEAVKDKHPGQWIFGGGWNNDFWG-GDYPTAAWLDDISPDNPVWLSRMDGHMGIANSLAMRM 189
Cdd:COG1574    83 LGVDLSGARSLDELLARLRAAAAELPPGEWILGRGWDESLWPeGRFPTRADLDAVSPDRPVVLTRVDGHAAWVNSAALEL 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002231449 190 AGINKNTNNPVGGTIMRTTEGEPTGLLVDAAMKLVFDVISEVSIHERRDALLRASRHALMRGVTTVVDVGSYfpgksekq 269
Cdd:COG1574   163 AGITADTPDPEGGEIERDADGEPTGVLREAAMDLVRAAIPPPTPEELRAALRAALRELASLGITSVHDAGLG-------- 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002231449 270 vWQDFtDIYEWAHSVETMIMRVCLFfPMPTWSRVYDLIHE--KGRMLSQWIHLGGVKAFLDGSLGSSSALFYEHYKDDPR 347
Cdd:COG1574   235 -PDDL-AAYRELAAAGELPLRVVLY-LGADDEDLEELLALglRTGYGDDRLRVGGVKLFADGSLGSRTAALLEPYADDPG 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002231449 348 SYGLQLVDMDYLLNTTLELDKSGLQIAIHAIGDKANDMLLDMYEKVVDLNGMKDHRFRIEHAQHLAPGAAKRFGKHGIIA 427
Cdd:COG1574   312 NRGLLLLDPEELRELVRAADAAGLQVAVHAIGDAAVDEVLDAYEAARAANGRRDRRHRIEHAQLVDPDDLARFAELGVIA 391

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002231449 428 SVQPDHILDDANSAGKKIGIERAERsSYSFRSLLDGGAHLAFGSDWPVSDINPLQAIRTAVSRKPVGwEVPWIPAERLSL 507
Cdd:COG1574   392 SMQPTHATSDGDWAEDRLGPERAAR-AYPFRSLLDAGAPLAFGSDAPVEPLDPLLGIYAAVTRRTPS-GRGLGPEERLTV 469

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002231449 508 DDSLKAHTISAAYACFLDHVLGSLSEGKYADFVILpstSWNEFGSDITD----HVLATYVNGKQAY 569
Cdd:COG1574   470 EEALRAYTIGAAYAAFEEDEKGSLEPGKLADFVVL---DRDPLTVPPEEikdiKVLLTVVGGRVVY 532
YtcJ_like cd01300
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ...
 57-541 0e+00

YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. The Arabidopsis homolog LAF3 has been identified as a factor required for phytochrome A signalling.


Pssm-ID: 238625 [Multi-domain]  Cd Length: 479  Bit Score: 560.00  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002231449  57 AMAVRAGRVLRVGGYYSVKELKGRHTMELNLSGNVVLPGFIDSHVHFIDGGLQLARVPLRGVTSKDDFINRVKEAVKDKH 136
Cdd:cd01300     1 AVAVRDGRIVAVGSDAEAKALKGPATEVIDLKGKTVLPGFIDSHSHLLLGGLSLLWLDLSGVTSKEEALARIREDAAAAP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002231449 137 PGQWIFGGGWNNDFWGGD-YPTAAWLDDISPDNPVWLSRMDGHMGIANSLAMRMAGINKNTNNPVGGTIMRTTEGEPTGL 215
Cdd:cd01300    81 PGEWILGFGWDESLLGEGrYPTRAELDAVSPDRPVLLLRRDGHSAWVNSAALRLAGITRDTPDPPGGEIVRDADGEPTGV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002231449 216 LVDAAMKLVFDVISEVSIHERRDALLRASRHALMRGVTTVVDVGSYFPGksekqvwqDFTDIYEWAHSVE-TMIMRVCLF 294
Cdd:cd01300   161 LVEAAAALVLEAVPPPTPEERRAALRAAARELASLGVTTVHDAGGGAAD--------DIEAYRRLAAAGElTLRVRVALY 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002231449 295 FPMPTWSRVYDLIHEKGRMLSQWIHLGGVKAFLDGSLGSSSALFYEHYKDDPRSYGLQLVDMDYLLNTTLELDKSGLQIA 374
Cdd:cd01300   233 VSPLAEDLLEELGARKNGAGDDRLRLGGVKLFADGSLGSRTAALSEPYLDSPGTGGLLLISPEELEELVRAADEAGLQVA 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002231449 375 IHAIGDKANDMLLDMYEKVVDLNGMKDHRFRIEHAQHLAPGAAKRFGKHGIIASVQPDHILDDANSAGKKIGIERAERSS 454
Cdd:cd01300   313 IHAIGDRAVDTVLDALEAALKDNPRADHRHRIEHAQLVSPDDIPRFAKLGVIASVQPNHLYSDGDAAEDRRLGEERAKRS 392

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002231449 455 YSFRSLLDGGAHLAFGSDWPVSDINPLQAIRTAVSRKPVGWEVPWIPAERLSLDDSLKAHTISAAYACFLDHVLGSLSEG 534
Cdd:cd01300   393 YPFRSLLDAGVPVALGSDAPVAPPDPLLGIWAAVTRKTPGGGVLGNPEERLSLEEALRAYTIGAAYAIGEEDEKGSLEPG 472


                  ....*..
gi 1002231449 535 KYADFVI 541
Cdd:cd01300   473 KLADFVV 479
Amidohydro_3 pfam07969
Amidohydrolase family;
84-569 1.60e-79

Amidohydrolase family;


Pssm-ID: 400360 [Multi-domain]  Cd Length: 464  Bit Score: 257.85  E-value: 1.60e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002231449  84 ELNLSGNVVLPGFIDSHVHFIDGGLQLARVPLRGVTSKDdfinRVKEAVKDKHPGQWIFGGGWN--NDFWGGDYPTAAWL 161
Cdd:pfam07969   2 VIDAKGRLVLPGFVDPHTHLDGGGLNLRELRLPDVLPNA----VVKGQAGRTPKGRWLVGEGWDeaQFAETRFPYALADL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002231449 162 DDISPDNPVWLSRMDGHMGIANSLAMRMAGINKNTNNPVGGTIMRTTEGE-PTGLLVDAAmklvFDVISEVSIHERRDAL 240
Cdd:pfam07969  78 DEVAPDGPVLLRALHTHAAVANSAALDLAGITKATEDPPGGEIARDANGEgLTGLLREGA----YALPPLLAREAEAAAV 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002231449 241 LRASRHALMRGVTTVVDVGSYFPGKSEKQVWQDFTDiyewahsvETMImrvclffpmptwSRVYDLIHEKGRMLSQ-WIH 319
Cdd:pfam07969 154 AAALAALPGFGITSVDGGGGNVHSLDDYEPLRELTA--------AEKL------------KELLDAPERLGLPHSIyELR 213

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002231449 320 LGGVKAFLDGSLGSSSALFYEHYKDDPRSyGLQLVDMDYLLNTTLELDKSGLQIAIHAIGDKANDMLLDMYEKVVDLNGM 399
Cdd:pfam07969 214 IGAMKLFADGVLGSRTAALTEPYFDAPGT-GWPDFEDEALAELVAAARERGLDVAIHAIGDATIDTALDAFEAVAEKLGN 292

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002231449 400 KDHRfRIEHAQHLAPGA---AKRFGKHGIIASVQPDHILDDANSAGKKIGIERAeRSSYSFRSLLDGGAHLAFGSDWPVS 476
Cdd:pfam07969 293 QGRV-RIEHAQGVVPYTysqIERVAALGGAAGVQPVFDPLWGDWLQDRLGAERA-RGLTPVKELLNAGVKVALGSDAPVG 370

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002231449 477 DINPLQAIRTAVSRKPVGW-EVPWiPAERLSLDDSLKAHTISAAYACFLDHVLGSLSEGKYADFVILPStswNEFGSD-- 553
Cdd:pfam07969 371 PFDPWPRIGAAVMRQTAGGgEVLG-PDEELSLEEALALYTSGPAKALGLEDRKGTLGVGKDADLVVLDD---DPLTVDpp 446

                         490
                  ....*....|....*...
gi 1002231449 554 --ITDHVLATYVNGKQAY 569
Cdd:pfam07969 447 aiADIRVRLTVVDGRVVY 464
PRK09228 PRK09228
guanine deaminase; Provisional
 57-103 4.29e-06

guanine deaminase; Provisional


Pssm-ID: 236419 [Multi-domain]  Cd Length: 433  Bit Score: 49.42  E-value: 4.29e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1002231449  57 AMAVRAGRVLRVGGYYSVKELKGRHTMELNLSGNVVLPGFIDSHVHF 103
Cdd:PRK09228   33 LLLVEDGRIVAAGPYAELRAQLPADAEVTDYRGKLILPGFIDTHIHY 79
guan_deamin TIGR02967
guanine deaminase; This model describes guanine deaminase, which hydrolyzes guanine to ...
 57-103 1.28e-04

guanine deaminase; This model describes guanine deaminase, which hydrolyzes guanine to xanthine and ammonia. Xanthine can then be converted to urate by xanthine dehydrogenase, and urate subsequently degraded. In some bacteria, the guanine deaminase gene is found near the xdhABC genes for xanthine dehydrogenase. Non-homologous forms of guanine deaminase also exist, as well as distantly related forms outside the scope of this model. [Purines, pyrimidines, nucleosides, and nucleotides, Other]


Pssm-ID: 132012 [Multi-domain]  Cd Length: 401  Bit Score: 44.55  E-value: 1.28e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1002231449  57 AMAVRAGRVLRVGGYYSVKELKGRHTMELNLSGNVVLPGFIDSHVHF 103
Cdd:TIGR02967   8 LLVVENGRIVAVGDYAELKETLPAGVEIDDYRGHLIMPGFIDTHIHY 54
 
Name Accession Description Interval E-value
YtcJ COG1574
Predicted amidohydrolase YtcJ [General function prediction only];
31-569 0e+00

Predicted amidohydrolase YtcJ [General function prediction only];


Pssm-ID: 441182 [Multi-domain]  Cd Length: 535  Bit Score: 571.74  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002231449  31 LGEAVADMILANATIYTADPAMPFAEAMAVRAGRVLRVGGYYSVKELKGRHTMELNLSGNVVLPGFIDSHVHFIDGGLQL 110
Cdd:COG1574     3 LAAAAADLLLTNGRIYTMDPAQPVAEAVAVRDGRIVAVGSDAEVRALAGPATEVIDLGGKTVLPGFIDAHVHLLGGGLAL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002231449 111 ARVPLRGVTSKDDFINRVKEAVKDKHPGQWIFGGGWNNDFWG-GDYPTAAWLDDISPDNPVWLSRMDGHMGIANSLAMRM 189
Cdd:COG1574    83 LGVDLSGARSLDELLARLRAAAAELPPGEWILGRGWDESLWPeGRFPTRADLDAVSPDRPVVLTRVDGHAAWVNSAALEL 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002231449 190 AGINKNTNNPVGGTIMRTTEGEPTGLLVDAAMKLVFDVISEVSIHERRDALLRASRHALMRGVTTVVDVGSYfpgksekq 269
Cdd:COG1574   163 AGITADTPDPEGGEIERDADGEPTGVLREAAMDLVRAAIPPPTPEELRAALRAALRELASLGITSVHDAGLG-------- 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002231449 270 vWQDFtDIYEWAHSVETMIMRVCLFfPMPTWSRVYDLIHE--KGRMLSQWIHLGGVKAFLDGSLGSSSALFYEHYKDDPR 347
Cdd:COG1574   235 -PDDL-AAYRELAAAGELPLRVVLY-LGADDEDLEELLALglRTGYGDDRLRVGGVKLFADGSLGSRTAALLEPYADDPG 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002231449 348 SYGLQLVDMDYLLNTTLELDKSGLQIAIHAIGDKANDMLLDMYEKVVDLNGMKDHRFRIEHAQHLAPGAAKRFGKHGIIA 427
Cdd:COG1574   312 NRGLLLLDPEELRELVRAADAAGLQVAVHAIGDAAVDEVLDAYEAARAANGRRDRRHRIEHAQLVDPDDLARFAELGVIA 391

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002231449 428 SVQPDHILDDANSAGKKIGIERAERsSYSFRSLLDGGAHLAFGSDWPVSDINPLQAIRTAVSRKPVGwEVPWIPAERLSL 507
Cdd:COG1574   392 SMQPTHATSDGDWAEDRLGPERAAR-AYPFRSLLDAGAPLAFGSDAPVEPLDPLLGIYAAVTRRTPS-GRGLGPEERLTV 469

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002231449 508 DDSLKAHTISAAYACFLDHVLGSLSEGKYADFVILpstSWNEFGSDITD----HVLATYVNGKQAY 569
Cdd:COG1574   470 EEALRAYTIGAAYAAFEEDEKGSLEPGKLADFVVL---DRDPLTVPPEEikdiKVLLTVVGGRVVY 532
YtcJ_like cd01300
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ...
 57-541 0e+00

YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. The Arabidopsis homolog LAF3 has been identified as a factor required for phytochrome A signalling.


Pssm-ID: 238625 [Multi-domain]  Cd Length: 479  Bit Score: 560.00  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002231449  57 AMAVRAGRVLRVGGYYSVKELKGRHTMELNLSGNVVLPGFIDSHVHFIDGGLQLARVPLRGVTSKDDFINRVKEAVKDKH 136
Cdd:cd01300     1 AVAVRDGRIVAVGSDAEAKALKGPATEVIDLKGKTVLPGFIDSHSHLLLGGLSLLWLDLSGVTSKEEALARIREDAAAAP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002231449 137 PGQWIFGGGWNNDFWGGD-YPTAAWLDDISPDNPVWLSRMDGHMGIANSLAMRMAGINKNTNNPVGGTIMRTTEGEPTGL 215
Cdd:cd01300    81 PGEWILGFGWDESLLGEGrYPTRAELDAVSPDRPVLLLRRDGHSAWVNSAALRLAGITRDTPDPPGGEIVRDADGEPTGV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002231449 216 LVDAAMKLVFDVISEVSIHERRDALLRASRHALMRGVTTVVDVGSYFPGksekqvwqDFTDIYEWAHSVE-TMIMRVCLF 294
Cdd:cd01300   161 LVEAAAALVLEAVPPPTPEERRAALRAAARELASLGVTTVHDAGGGAAD--------DIEAYRRLAAAGElTLRVRVALY 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002231449 295 FPMPTWSRVYDLIHEKGRMLSQWIHLGGVKAFLDGSLGSSSALFYEHYKDDPRSYGLQLVDMDYLLNTTLELDKSGLQIA 374
Cdd:cd01300   233 VSPLAEDLLEELGARKNGAGDDRLRLGGVKLFADGSLGSRTAALSEPYLDSPGTGGLLLISPEELEELVRAADEAGLQVA 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002231449 375 IHAIGDKANDMLLDMYEKVVDLNGMKDHRFRIEHAQHLAPGAAKRFGKHGIIASVQPDHILDDANSAGKKIGIERAERSS 454
Cdd:cd01300   313 IHAIGDRAVDTVLDALEAALKDNPRADHRHRIEHAQLVSPDDIPRFAKLGVIASVQPNHLYSDGDAAEDRRLGEERAKRS 392

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002231449 455 YSFRSLLDGGAHLAFGSDWPVSDINPLQAIRTAVSRKPVGWEVPWIPAERLSLDDSLKAHTISAAYACFLDHVLGSLSEG 534
Cdd:cd01300   393 YPFRSLLDAGVPVALGSDAPVAPPDPLLGIWAAVTRKTPGGGVLGNPEERLSLEEALRAYTIGAAYAIGEEDEKGSLEPG 472


                  ....*..
gi 1002231449 535 KYADFVI 541
Cdd:cd01300   473 KLADFVV 479
Amidohydro_3 pfam07969
Amidohydrolase family;
84-569 1.60e-79

Amidohydrolase family;


Pssm-ID: 400360 [Multi-domain]  Cd Length: 464  Bit Score: 257.85  E-value: 1.60e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002231449  84 ELNLSGNVVLPGFIDSHVHFIDGGLQLARVPLRGVTSKDdfinRVKEAVKDKHPGQWIFGGGWN--NDFWGGDYPTAAWL 161
Cdd:pfam07969   2 VIDAKGRLVLPGFVDPHTHLDGGGLNLRELRLPDVLPNA----VVKGQAGRTPKGRWLVGEGWDeaQFAETRFPYALADL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002231449 162 DDISPDNPVWLSRMDGHMGIANSLAMRMAGINKNTNNPVGGTIMRTTEGE-PTGLLVDAAmklvFDVISEVSIHERRDAL 240
Cdd:pfam07969  78 DEVAPDGPVLLRALHTHAAVANSAALDLAGITKATEDPPGGEIARDANGEgLTGLLREGA----YALPPLLAREAEAAAV 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002231449 241 LRASRHALMRGVTTVVDVGSYFPGKSEKQVWQDFTDiyewahsvETMImrvclffpmptwSRVYDLIHEKGRMLSQ-WIH 319
Cdd:pfam07969 154 AAALAALPGFGITSVDGGGGNVHSLDDYEPLRELTA--------AEKL------------KELLDAPERLGLPHSIyELR 213

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002231449 320 LGGVKAFLDGSLGSSSALFYEHYKDDPRSyGLQLVDMDYLLNTTLELDKSGLQIAIHAIGDKANDMLLDMYEKVVDLNGM 399
Cdd:pfam07969 214 IGAMKLFADGVLGSRTAALTEPYFDAPGT-GWPDFEDEALAELVAAARERGLDVAIHAIGDATIDTALDAFEAVAEKLGN 292

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002231449 400 KDHRfRIEHAQHLAPGA---AKRFGKHGIIASVQPDHILDDANSAGKKIGIERAeRSSYSFRSLLDGGAHLAFGSDWPVS 476
Cdd:pfam07969 293 QGRV-RIEHAQGVVPYTysqIERVAALGGAAGVQPVFDPLWGDWLQDRLGAERA-RGLTPVKELLNAGVKVALGSDAPVG 370

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002231449 477 DINPLQAIRTAVSRKPVGW-EVPWiPAERLSLDDSLKAHTISAAYACFLDHVLGSLSEGKYADFVILPStswNEFGSD-- 553
Cdd:pfam07969 371 PFDPWPRIGAAVMRQTAGGgEVLG-PDEELSLEEALALYTSGPAKALGLEDRKGTLGVGKDADLVVLDD---DPLTVDpp 446

                         490
                  ....*....|....*...
gi 1002231449 554 --ITDHVLATYVNGKQAY 569
Cdd:pfam07969 447 aiADIRVRLTVVDGRVVY 464
metallo-dependent_hydrolases cd01292
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ...
 225-521 2.00e-25

Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The family includes urease alpha, adenosine deaminase, phosphotriesterase dihydroorotases, allantoinases, hydantoinases, AMP-, adenine and cytosine deaminases, imidazolonepropionase, aryldialkylphosphatase, chlorohydrolases, formylmethanofuran dehydrogenases and others.


Pssm-ID: 238617 [Multi-domain]  Cd Length: 275  Bit Score: 105.88  E-value: 2.00e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002231449 225 FDVISEVSIHERRDALLRASRHALMRGVTTVVDVGSYFPGKSEKQVWQdftDIYEWAHSVETMIMRVCLFFPMPTWSRVY 304
Cdd:cd01292    22 LKEAEELSPEDLYEDTLRALEALLAGGVTTVVDMGSTPPPTTTKAAIE---AVAEAARASAGIRVVLGLGIPGVPAAVDE 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002231449 305 DlihekgrmlsqWIHLGGVKAFLDGSLGSSSALFYEHYKDDPrsyglqlVDMDYLLNTTLELDKSGLQIAIHAIGDKAND 384
Cdd:cd01292    99 D-----------AEALLLELLRRGLELGAVGLKLAGPYTATG-------LSDESLRRVLEEARKLGLPVVIHAGELPDPT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002231449 385 MlldMYEKVVDLNGMkDHRFRIEHAQHLAPGAAKRFGKHGIIASVQPDHILDDansagkkigiERAERSSYSFRSLLDGG 464
Cdd:cd01292   161 R---ALEDLVALLRL-GGRVVIGHVSHLDPELLELLKEAGVSLEVCPLSNYLL----------GRDGEGAEALRRLLELG 226

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1002231449 465 AHLAFGSDWPVS--DINPLQAIRTAVsrkpvgwevpWIPAERLSLDDSLKAHTISAAYA 521
Cdd:cd01292   227 IRVTLGTDGPPHplGTDLLALLRLLL----------KVLRLGLSLEEALRLATINPARA 275
SsnA COG0402
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ...
 37-569 1.17e-11

Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and metabolism, General function prediction only]; Cytosine/adenosine deaminase or related metal-dependent hydrolase is part of the Pathway/BioSystem: Pyrimidine salvage


Pssm-ID: 440171 [Multi-domain]  Cd Length: 416  Bit Score: 66.77  E-value: 1.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002231449  37 DMILANATIYTADPAMPFAE--AMAVRAGRVLRVGGYYSVKElKGRHTMELNLSGNVVLPGFIDSHVHfidgglqLARVP 114
Cdd:COG0402     1 DLLIRGAWVLTMDPAGGVLEdgAVLVEDGRIAAVGPGAELPA-RYPAAEVIDAGGKLVLPGLVNTHTH-------LPQTL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002231449 115 LRGVTSKDDFInrvkeavkdkhpgqwifggGWNNDFWggdYPTAAwlddispdnpvwlsRMDGHMgianslamrmagink 194
Cdd:COG0402    73 LRGLADDLPLL-------------------DWLEEYI---WPLEA--------------RLDPED--------------- 101

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002231449 195 ntnnpvggtimrttegeptgllVDAAMKLVFDvisevsiherrdALLRAsrhalmrGVTTVVDVGSYFPGKSEkqvwqdf 274
Cdd:COG0402   102 ----------------------VYAGALLALA------------EMLRS-------GTTTVADFYYVHPESAD------- 133

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002231449 275 tdiyEWAHSVETMIMRVCLFFPMPTWSRVYDLIHEKGRMLSQwihlggVKAFLDGSLGSSSALFYEHYKddPRSygLQLV 354
Cdd:COG0402   134 ----ALAEAAAEAGIRAVLGRGLMDRGFPDGLREDADEGLAD------SERLIERWHGAADGRIRVALA--PHA--PYTV 199

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002231449 355 DMDYLLNTTLELDKSGLQIAIH-AIGDKANDMLLDMYEK----VVDLNGMKDHRFRIEHAQHLAPGAAKRFGKHGIIASV 429
Cdd:COG0402   200 SPELLRAAAALARELGLPLHTHlAETRDEVEWVLELYGKrpveYLDELGLLGPRTLLAHCVHLTDEEIALLAETGASVAH 279

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002231449 430 QPDHILDDANsagkkiGIERAERssysfrsLLDGGAHLAFGSDWPVS--DINPLQAIRTAVSR-KPVGWEVPWIPAERLs 506
Cdd:COG0402   280 CPTSNLKLGS------GIAPVPR-------LLAAGVRVGLGTDGAASnnSLDMFEEMRLAALLqRLRGGDPTALSAREA- 345

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002231449 507 lddsLKAHTISAAYACFLDHVLGSLSEGKYADFVILPSTSWNEFGS-DITDHVL---------ATYVNGKQAY 569
Cdd:COG0402   346 ----LEMATLGGARALGLDDEIGSLEPGKRADLVVLDLDAPHLAPLhDPLSALVyaadgrdvrTVWVAGRVVV 414
HutI COG1228
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ...
 368-566 1.40e-11

Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440841 [Multi-domain]  Cd Length: 386  Bit Score: 66.52  E-value: 1.40e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002231449 368 KSGLQIAIHAIGDKANDMLLDMyekvvdlnGMKdhrfRIEHAQHLAPGAAKRFGKHGIIAsVQPDHILDDANSAGKKIGI 447
Cdd:COG1228   203 ALGLPVAAHAHQADDIRLAVEA--------GVD----SIEHGTYLDDEVADLLAEAGTVV-LVPTLSLFLALLEGAAAPV 269

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002231449 448 ERAERSSY-----SFRSLLDGGAHLAFGSDWPVSDI---NPLQAIRTAVsrkpvgwevpwipAERLSLDDSLKAHTISAA 519
Cdd:COG1228   270 AAKARKVReaalaNARRLHDAGVPVALGTDAGVGVPpgrSLHRELALAV-------------EAGLTPEEALRAATINAA 336

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1002231449 520 YACFLDHVLGSLSEGKYADFVILPSTSWnefgSDIT--DHVLATYVNGK 566
Cdd:COG1228   337 KALGLDDDVGSLEPGKLADLVLLDGDPL----EDIAylEDVRAVMKDGR 381
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
 231-566 5.03e-11

Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase superfamily. The family includes Adenine deaminase EC:3.5.4.2 that hydrolyses adenine to form hypoxanthine and ammonia. Adenine deaminases reaction is important for adenine utilization as a purine and also as a nitrogen source. This family also includes dihydroorotase and N-acetylglucosamine-6-phosphate deacetylases, EC:3.5.1.25 These enzymes catalyze the reaction N-acetyl-D-glucosamine 6-phosphate + H2O <=> D-glucosamine 6-phosphate + acetate. This family includes the catalytic domain of urease alpha subunit. Dihydroorotases (EC:3.5.2.3) are also included.


Pssm-ID: 460401 [Multi-domain]  Cd Length: 334  Bit Score: 64.45  E-value: 5.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002231449 231 VSIHERRDALLRASRHALMRGVTTVVDVGSYFPgksekqvwQDFTDIYEWAHSVeTMIMRVCLFFPMPTWSRVYDLIHEK 310
Cdd:pfam01979  23 VPPEFAYEALRLGITTMLKSGTTTVLDMGATTS--------TGIEALLEAAEEL-PLGLRFLGPGCSLDTDGELEGRKAL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002231449 311 GRMLSQwihlgGVKAFLDGSLGSSSALFYEHykdDPRSYGLqlvdmDYLLNTTLELDKSGLQIAIHAIGDKA-------- 382
Cdd:pfam01979  94 REKLKA-----GAEFIKGMADGVVFVGLAPH---GAPTFSD-----DELKAALEEAKKYGLPVAIHALETKGevedaiaa 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002231449 383 --NDMLLDMYEKVVDLNGMKD-HRFRIEHAQHLAPGAAKRFGKHGIIASVqpDHILDDansagkkigIERAERSSYSFRS 459
Cdd:pfam01979 161 fgGGIEHGTHLEVAESGGLLDiIKLILAHGVHLSPTEANLLAEHLKGAGV--AHCPFS---------NSKLRSGRIALRK 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002231449 460 LLDGGAHLAFGSDWPVSDINP--LQAIRTAVsrkpvgwEVPWIPAERLSLDDSLKAHTISAAYACFLDHVLGSLSEGKYA 537
Cdd:pfam01979 230 ALEDGVKVGLGTDGAGSGNSLnmLEELRLAL-------ELQFDPEGGLSPLEALRMATINPAKALGLDDKVGSIEVGKDA 302

                         330       340       350
                  ....*....|....*....|....*....|..
gi 1002231449 538 DFVIL---PSTSWNEFGSDITdhVLATYVNGK 566
Cdd:pfam01979 303 DLVVVdldPLAAFFGLKPDGN--VKKVIVKGK 332
Met_dep_hydrolase_C cd01309
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ...
 335-569 4.81e-09

Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.


Pssm-ID: 238634 [Multi-domain]  Cd Length: 359  Bit Score: 58.48  E-value: 4.81e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002231449 335 SALFYEHYKDDPRSYGLQLVDMDYLLNTTLELDKSGLQIAIHAigDKANDML--LDMYEKVvDLNGMKDHrfrIEHAQHL 412
Cdd:cd01309   157 KAQEYGRKYDLGKNAKKDPPERDLKLEALLPVLKGEIPVRIHA--HRADDILtaIRIAKEF-GIKITIEH---GAEGYKL 230

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002231449 413 APgaakRFGKHGIIASVQPDhilddanSAGKKIGIERAERSSYSFRSLLDGGAHLAFGSDWPVSDIN--PLQAiRTAVsr 490
Cdd:cd01309   231 AD----ELAKHGIPVIYGPT-------LTLPKKVEEVNDAIDTNAYLLKKGGVAFAISSDHPVLNIRnlNLEA-AKAV-- 296

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002231449 491 kpvgwevpwipAERLSLDDSLKAHTISAAYACFLDHVLGSLSEGKYADFVIlpstsWNEFGSDITDHVLATYVNGKQAY 569
Cdd:cd01309   297 -----------KYGLSYEEALKAITINPAKILGIEDRVGSLEPGKDADLVV-----WNGDPLEPTSKPEQVYIDGRLVY 359
Imidazolone-5PH cd01296
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ...
 59-107 1.06e-06

Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third step in the histidine degradation pathway, the hydrolysis of (S)-3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate to N-formimidoyl-L-glutamate. In bacteria, the enzyme is part of histidine utilization (hut) operon.


Pssm-ID: 238621 [Multi-domain]  Cd Length: 371  Bit Score: 51.10  E-value: 1.06e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1002231449  59 AVRAGRVLRVGGYYSVKELKGRHTMELNLSGNVVLPGFIDSHVHFIDGG 107
Cdd:cd01296     2 AIRDGRIAAVGPAASLPAPGPAAAEEIDAGGRAVTPGLVDCHTHLVFAG 50
D-HYD cd01314
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ...
 38-124 1.09e-06

D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases are a family of enzymes that catalyze the reversible hydrolytic ring opening of the amide bond in five- or six-membered cyclic diamides, like dihydropyrimidine or hydantoin. The hydrolysis of dihydropyrimidines is the second step of reductive catabolism of pyrimidines in human. The hydrolysis of 5-substituted hydantoins in microorganisms leads to enantiomerically pure N-carbamyl amino acids, which are used for the production of antibiotics, peptide hormones, pyrethroids, and pesticides. HYDs are classified depending on their stereoselectivity. This family also includes collapsin response regulators (CRMPs), cytosolic proteins involved in neuronal differentiation and axonal guidance which have strong homology to DHPases, but lack most of the active site residues.


Pssm-ID: 238639 [Multi-domain]  Cd Length: 447  Bit Score: 51.06  E-value: 1.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002231449  38 MILANATIYTADPamPFAEAMAVRAGRVLRVGGYYSVKElkgrHTMELNLSGNVVLPGFIDSHVHFidgglQLarvPLRG 117
Cdd:cd01314     1 LIIKNGTIVTADG--SFKADILIEDGKIVAIGPNLEAPG----GVEVIDATGKYVLPGGIDPHTHL-----EL---PFMG 66


                  ....*..
gi 1002231449 118 VTSKDDF 124
Cdd:cd01314    67 TVTADDF 73
AdeC COG1001
Adenine deaminase [Nucleotide transport and metabolism];
32-120 3.50e-06

Adenine deaminase [Nucleotide transport and metabolism];


Pssm-ID: 440625 [Multi-domain]  Cd Length: 559  Bit Score: 49.71  E-value: 3.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002231449  32 GEAVADMILANAT--------IYTADpampfaeaMAVRAGRVLRVGGYysvkelKGRHTMELNLSGNVVLPGFIDSHVHf 103
Cdd:COG1001     1 GREPADLVIKNGRlvnvftgeILEGD--------IAIAGGRIAGVGDY------IGEATEVIDAAGRYLVPGFIDGHVH- 65

                          90       100
                  ....*....|....*....|..
gi 1002231449 104 IDGGL----QLARVPL-RGVTS 120
Cdd:COG1001    66 IESSMvtpaEFARAVLpHGTTT 87
PRK09228 PRK09228
guanine deaminase; Provisional
 57-103 4.29e-06

guanine deaminase; Provisional


Pssm-ID: 236419 [Multi-domain]  Cd Length: 433  Bit Score: 49.42  E-value: 4.29e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1002231449  57 AMAVRAGRVLRVGGYYSVKELKGRHTMELNLSGNVVLPGFIDSHVHF 103
Cdd:PRK09228   33 LLLVEDGRIVAAGPYAELRAQLPADAEVTDYRGKLILPGFIDTHIHY 79
AllB COG0044
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ...
 39-124 6.99e-06

Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; Dihydroorotase or related cyclic amidohydrolase is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 439814 [Multi-domain]  Cd Length: 439  Bit Score: 48.55  E-value: 6.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002231449  39 ILANATIYtaDPAMPFAEAMAVRAGRVLRVGGyySVKELKGRHTmeLNLSGNVVLPGFIDSHVHFidgglqlaRVPlrGV 118
Cdd:COG0044     1 LIKNGRVV--DPGGLERADVLIEDGRIAAIGP--DLAAPEAAEV--IDATGLLVLPGLIDLHVHL--------REP--GL 64


                  ....*.
gi 1002231449 119 TSKDDF 124
Cdd:COG0044    65 EHKEDI 70
Imidazolone-5PH cd01296
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ...
 504-559 2.44e-05

Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third step in the histidine degradation pathway, the hydrolysis of (S)-3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate to N-formimidoyl-L-glutamate. In bacteria, the enzyme is part of histidine utilization (hut) operon.


Pssm-ID: 238621 [Multi-domain]  Cd Length: 371  Bit Score: 46.87  E-value: 2.44e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002231449 504 RLSLDDSLKAHTISAAYACFLDHVLGSLSEGKYADFVILPSTSWNE----FGSDITDHVL 559
Cdd:cd01296   309 RMTPEEALTAATINAAAALGLGETVGSLEVGKQADLVILDAPSYEHlayrFGVNLVEYVI 368
PRK07203 PRK07203
putative aminohydrolase SsnA;
38-126 3.70e-05

putative aminohydrolase SsnA;


Pssm-ID: 235963 [Multi-domain]  Cd Length: 442  Bit Score: 46.47  E-value: 3.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002231449  38 MILANATIYTADPAMPFAE--AMAVRAGRVLRVGGYysvKELKGRHTME--LNLSGNVVLPGFIDSHVHFIDGglqLArv 113
Cdd:PRK07203    2 LLIGNGTAITRDPAKPVIEdgAIAIEGNVIVEIGTT---DELKAKYPDAefIDAKGKLIMPGLINSHNHIYSG---LA-- 73

                          90
                  ....*....|....*..
gi 1002231449 114 plRGVTSKD----DFIN 126
Cdd:PRK07203   74 --RGMMANIppppDFIS 88
D-aminoacylase cd01297
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ...
 37-102 1.22e-04

D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of N-acyl-D-amino acids to produce the corresponding D-amino acids, which are used as intermediates in the synthesis of pesticides, bioactive peptides, and antibiotics.


Pssm-ID: 238622 [Multi-domain]  Cd Length: 415  Bit Score: 44.60  E-value: 1.22e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002231449  37 DMILANATIYTADPAMPFAEAMAVRAGRVLRVGgyySVKELKGRHtmELNLSGNVVLPGFIDSHVH 102
Cdd:cd01297     1 DLVIRNGTVVDGTGAPPFTADVGIRDGRIAAIG---PILSTSARE--VIDAAGLVVAPGFIDVHTH 61
guan_deamin TIGR02967
guanine deaminase; This model describes guanine deaminase, which hydrolyzes guanine to ...
 57-103 1.28e-04

guanine deaminase; This model describes guanine deaminase, which hydrolyzes guanine to xanthine and ammonia. Xanthine can then be converted to urate by xanthine dehydrogenase, and urate subsequently degraded. In some bacteria, the guanine deaminase gene is found near the xdhABC genes for xanthine dehydrogenase. Non-homologous forms of guanine deaminase also exist, as well as distantly related forms outside the scope of this model. [Purines, pyrimidines, nucleosides, and nucleotides, Other]


Pssm-ID: 132012 [Multi-domain]  Cd Length: 401  Bit Score: 44.55  E-value: 1.28e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1002231449  57 AMAVRAGRVLRVGGYYSVKELKGRHTMELNLSGNVVLPGFIDSHVHF 103
Cdd:TIGR02967   8 LLVVENGRIVAVGDYAELKETLPAGVEIDDYRGHLIMPGFIDTHIHY 54
NagA COG1820
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
476-566 1.44e-04

N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];


Pssm-ID: 441425 [Multi-domain]  Cd Length: 373  Bit Score: 44.32  E-value: 1.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002231449 476 SDINPLQAIRTAVSRkpVGwevpwipaerLSLDDSLKAHTISAAYACFLDHVLGSLSEGKYADFVIlpstswneFGSDIt 555
Cdd:COG1820   305 STLTMDDAVRNLVEW--TG----------LPLEEAVRMASLNPARALGLDDRKGSIAPGKDADLVV--------LDDDL- 363

                          90
                  ....*....|.
gi 1002231449 556 dHVLATYVNGK 566
Cdd:COG1820   364 -NVRATWVGGE 373
COG3964 COG3964
Predicted amidohydrolase [General function prediction only];
37-107 2.08e-04

Predicted amidohydrolase [General function prediction only];


Pssm-ID: 443164 [Multi-domain]  Cd Length: 376  Bit Score: 43.62  E-value: 2.08e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002231449  37 DMILANATIytADPAMPFAEAM--AVRAGRVLRVGGyySVKELKGRHTmeLNLSGNVVLPGFIDSHVHFIDGG 107
Cdd:COG3964     1 DLLIKGGRV--IDPANGIDGVMdiAIKDGKIAAVAK--DIDAAEAKKV--IDASGLYVTPGLIDLHTHVFPGG 67
L-HYD_ALN cd01315
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ...
 37-107 3.19e-04

L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the dihydropyrimidinase family, which catalyzes the reversible hydrolytic ring opening of dihydropyrimidines and hydantoins (five-membered cyclic diamides used in biotechnology). But L-HYDs differ by having an L-enantio specificity and by lacking activity on possible natural substrates such as dihydropyrimidines. Allantoinase catalyzes the hydrolytic cleavage of the five-member ring of allantoin (5-ureidohydantoin) to form allantoic acid.


Pssm-ID: 238640 [Multi-domain]  Cd Length: 447  Bit Score: 43.43  E-value: 3.19e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002231449  37 DMILANATIYTADPAMPfaEAMAVRAGRVLRVGGYYSVKELKgRHtmeLNLSGNVVLPGFIDSHVHFIDGG 107
Cdd:cd01315     1 DLVIKNGRVVTPDGVRE--ADIAVKGGKIAAIGPDIANTEAE-EV---IDAGGLVVMPGLIDTHVHINEPG 65
Isoaspartyl-dipeptidase cd01308
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ...
 86-120 5.10e-04

Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of the degradative pathway to eliminate proteins with beta-L-isoaspartyl peptide bonds, bonds whereby the beta-group of an aspartate forms the peptide link with the amino group of the following amino acid. Formation of this bond is a spontaneous nonenzymatic reaction in nature and can profoundly effect the function of the protein. Isoaspartyl dipeptidase is an octameric enzyme that contains a binuclear zinc center in the active site of each subunit and shows a strong preference of hydrolyzing Asp-Leu dipeptides.


Pssm-ID: 238633 [Multi-domain]  Cd Length: 387  Bit Score: 42.76  E-value: 5.10e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1002231449  86 NLSGNVVLPGFIDSHVHFIDGG-----------LQLARVPLRGVTS 120
Cdd:cd01308    46 DLHGKILVPGFIDQHVHIIGGGgeggpstrtpeVTLSDLTTAGVTT 91
NagA cd00854
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ...
 505-565 6.86e-04

N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl group of N-acetyl-glucosamine-6-phosphate (GlcNAc-6-P) to glucosamine 6-phosphate and acetate. This is the first committed step in the biosynthetic pathway to amino-sugar-nucleotides, which is needed for cell wall peptidoglycan and teichoic acid biosynthesis. Deacetylation of N-acetylglucosamine is also important in lipopolysaccharide synthesis and cell wall recycling.


Pssm-ID: 238434 [Multi-domain]  Cd Length: 374  Bit Score: 42.18  E-value: 6.86e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002231449 505 LSLDDSLKAHTISAAYACFLDHVLGSLSEGKYADFVILpstswnefgsDITDHVLATYVNG 565
Cdd:cd00854   324 CPLEEAVRMASLNPAKLLGLDDRKGSLKPGKDADLVVL----------DDDLNVKATWING 374
PRK09060 PRK09060
dihydroorotase; Validated
 37-108 9.17e-04

dihydroorotase; Validated


Pssm-ID: 181632 [Multi-domain]  Cd Length: 444  Bit Score: 41.83  E-value: 9.17e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002231449  37 DMILANATIYTADPAmpfAEA-MAVRAGRVLRVGGYYS-----VKELKGRHtmelnlsgnvVLPGFIDSHVHFIDGGL 108
Cdd:PRK09060    6 DLILKGGTVVNPDGE---GRAdIGIRDGRIAAIGDLSGasageVIDCRGLH----------VLPGVIDSQVHFREPGL 70
isoAsp_dipep TIGR01975
isoaspartyl dipeptidase IadA; The L-isoaspartyl derivative of Asp arises non-enzymatically ...
 87-120 1.00e-03

isoaspartyl dipeptidase IadA; The L-isoaspartyl derivative of Asp arises non-enzymatically over time as a form of protein damage. In this isomerization, the connectivity of the polypeptide changes to pass through the beta-carboxyl of the side chain. Much but not all of this damage can be repaired by protein-L-isoaspartate (D-aspartate) O-methyltransferase. This model describes the isoaspartyl dipeptidase IadA, apparently one of two such enzymes in E. coli, an enzyme that degrades isoaspartyl dipeptides and may unblock degradation of proteins that cannot be repaired. This model also describes closely related proteins from other species (e.g. Clostridium perfringens, Thermoanaerobacter tengcongensis) that we assume to be equivalent in function. This family shows homology to dihydroorotases. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 131030  Cd Length: 389  Bit Score: 41.69  E-value: 1.00e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1002231449  87 LSGNVVLPGFIDSHVHFIDGG-----------LQLARVPLRGVTS 120
Cdd:TIGR01975  49 LEGMIAVPGFIDQHVHIIGGGgeggpttrtpeLTLSDITKGGVTT 93
pyrC_multi TIGR00857
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ...
 57-108 1.31e-03

dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of dihydroorotase found in E. coli, this class tends to appear in a large, multifunctional complex with aspartate transcarbamoylase. Homologous domains appear in multifunctional proteins of higher eukaryotes. In some species, including Pseudomonas putida and P. aeruginosa, this protein is inactive but is required as a non-catalytic subunit of aspartate transcarbamoylase (ATCase). In these species, a second, active dihydroorotase is also present. The seed for this model does not include any example of the dihydroorotase domain of eukaryotic multidomain pyrimidine synthesis proteins. All proteins described by this model should represent active and inactive dihydroorotase per se and functionally equivalent domains of multifunctional proteins from higher eukaryotes, but exclude related proteins such as allantoinase. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273302 [Multi-domain]  Cd Length: 411  Bit Score: 41.27  E-value: 1.31e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1002231449  57 AMAVRAGRVLRVGGYYSV--KELKGRhtmelnlSGNVVLPGFIDSHVHFIDGGL 108
Cdd:TIGR00857   7 DILVEGGRIKKIGKLRIPpdAEVIDA-------KGLLVLPGFIDLHVHLRDPGE 53
PRK08323 PRK08323
phenylhydantoinase; Validated
 37-124 2.35e-03

phenylhydantoinase; Validated


Pssm-ID: 236240 [Multi-domain]  Cd Length: 459  Bit Score: 40.54  E-value: 2.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002231449  37 DMILANATIYTADpaMPFAEAMAVRAGRVLRVGgyysvkelKGRHTMELNLSGNVVLPGFIDSHVHfidggLQLarvPLR 116
Cdd:PRK08323    2 STLIKNGTVVTAD--DTYKADVLIEDGKIAAIG--------ANLGDEVIDATGKYVMPGGIDPHTH-----MEM---PFG 63


                  ....*...
gi 1002231449 117 GVTSKDDF 124
Cdd:PRK08323   64 GTVSSDDF 71
PRK02382 PRK02382
dihydroorotase; Provisional
 37-107 2.72e-03

dihydroorotase; Provisional


Pssm-ID: 179417 [Multi-domain]  Cd Length: 443  Bit Score: 40.41  E-value: 2.72e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002231449  37 DMILANATIYTADPAMPfaEAMAVRAGRVLRVGgyysvKELKGRHT-MELNLSGNVVLPGFIDSHVHFIDGG 107
Cdd:PRK02382    3 DALLKDGRVYYNNSLQP--RDVRIDGGKITAVG-----KDLDGSSSeEVIDARGMLLLPGGIDVHVHFREPG 67
PRK13404 PRK13404
dihydropyrimidinase; Provisional
 37-125 3.42e-03

dihydropyrimidinase; Provisional


Pssm-ID: 184033 [Multi-domain]  Cd Length: 477  Bit Score: 40.07  E-value: 3.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002231449  37 DMILANATIYTADPAmpFAEAMAVRAGRVLRVGgyysvkELKGRHTMELNLSGNVVLPGFIDSHVHFidgglqlARVPLR 116
Cdd:PRK13404    5 DLVIRGGTVVTATDT--FQADIGIRGGRIAALG------EGLGPGAREIDATGRLVLPGGVDSHCHI-------DQPSGD 69


                  ....*....
gi 1002231449 117 GVTSKDDFI 125
Cdd:PRK13404   70 GIMMADDFY 78
PRK09228 PRK09228
guanine deaminase; Provisional
 503-569 3.48e-03

guanine deaminase; Provisional


Pssm-ID: 236419 [Multi-domain]  Cd Length: 433  Bit Score: 40.17  E-value: 3.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002231449 503 ERLSLDDSLKAHTISAAYACFLDHVLGSLSEGKYADFVIL--PSTS----WNEFGSDITD------------HVLATYVN 564
Cdd:PRK09228  346 YRLSPFQAFYLATLGGARALGLDDRIGNLAPGKEADFVVLdpAATPllalRTARAESLEEllfalmtlgddrAVAETYVA 425


                  ....*
gi 1002231449 565 GKQAY 569
Cdd:PRK09228  426 GRPVY 430
ATZ_TRZ_like cd01298
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ...
 38-130 5.17e-03

TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. Atrazine, a chlorinated herbizide, can be catabolized by a variety of different bacteria. The first three steps of the atrazine dehalogenation pathway are catalyzed by atrazine chlorohydrolase (AtzA), hydroxyatrazine ethylaminohydrolase (AtzB), and N-isopropylammelide N-isopropylaminohydrolase (AtzC). All three enzymes belong to the superfamily of metal dependent hydrolases. AtzA and AtzB, beside other related enzymes are represented in this CD.


Pssm-ID: 238623 [Multi-domain]  Cd Length: 411  Bit Score: 39.49  E-value: 5.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002231449  38 MILANATIYTADPAMPFAE-AMAVRAGRVLRVG-----GYYSVKElkgrhtmELNLSGNVVLPGFIDSHVHFidgglqlA 111
Cdd:cd01298     1 ILIRNGTIVTTDPRRVLEDgDVLVEDGRIVAVGpalplPAYPADE-------VIDAKGKVVMPGLVNTHTHL-------A 66

                          90
                  ....*....|....*....
gi 1002231449 112 RVPLRGVTSKDDFINRVKE 130
Cdd:cd01298    67 MTLLRGLADDLPLMEWLKD 85
PRK04250 PRK04250
dihydroorotase; Provisional
 60-105 5.24e-03

dihydroorotase; Provisional


Pssm-ID: 235265 [Multi-domain]  Cd Length: 398  Bit Score: 39.37  E-value: 5.24e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1002231449  60 VRAGRVLRVggyySVKELKGRHTmeLNLSGNVVLPGFIDSHVHFID 105
Cdd:PRK04250   19 IENGRISKI----SLRDLKGKEV--IKVKGGIILPGLIDVHVHLRD 58
GDEase cd01303
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ...
 457-565 6.40e-03

Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the conversion of guanine to xanthine and ammonia, the first step to utilize guanine as a nitrogen source. This reaction also removes the guanine base from the pool and therefore can play a role in the regulation of cellular GTP and the guanylate nucleotide pool.


Pssm-ID: 238628 [Multi-domain]  Cd Length: 429  Bit Score: 39.18  E-value: 6.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002231449 457 FRSLLDGGAHLAFGSDwpVS---DINPLQAIRTA--VSR---KPVGWEVPWIPAERLSLddslkaHTISAAYACFLDHVL 528
Cdd:cd01303   303 VRKLLDAGIKVGLGTD--VGggtSFSMLDTLRQAykVSRllgYELGGHAKLSPAEAFYL------ATLGGAEALGLDDKI 374

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1002231449 529 GSLSEGKYADFVIL------PSTSWNEFGSDITD------------HVLATYVNG 565
Cdd:cd01303   375 GNFEVGKEFDAVVIdpsatpLLADRMFRVESLEEalfkflylgddrNIREVYVAG 429
PRK09045 PRK09045
TRZ/ATZ family hydrolase;
460-540 6.89e-03

TRZ/ATZ family hydrolase;


Pssm-ID: 236366 [Multi-domain]  Cd Length: 443  Bit Score: 39.12  E-value: 6.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002231449 460 LLDGGAHLAFGSDWPVS--DINPLQAIRTA-VSRKPVGWEVPWIPAERlslddSLKAHTISAAYACFLDHVLGSLSEGKY 536
Cdd:PRK09045  297 LLQAGVNVALGTDGAASnnDLDLFGEMRTAaLLAKAVAGDATALPAHT-----ALRMATLNGARALGLDDEIGSLEPGKQ 371


                  ....
gi 1002231449 537 ADFV 540
Cdd:PRK09045  372 ADLV 375
PRK08204 PRK08204
hypothetical protein; Provisional
 495-548 9.20e-03

hypothetical protein; Provisional


Pssm-ID: 181288 [Multi-domain]  Cd Length: 449  Bit Score: 38.83  E-value: 9.20e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1002231449 495 WEVPWIPAERLSL--DDSLKAHTISAAYACFLDHVLGSLSEGKYADFVILPSTSWN 548
Cdd:PRK08204  330 LREGGMPPPRLTLtaRQVLEWATIEGARALGLEDRIGSLTPGKQADLVLIDATDLN 385
 
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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