|
Name |
Accession |
Description |
Interval |
E-value |
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
33-386 |
2.73e-152 |
|
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: 434.38 E-value: 2.73e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 33 VVIDGDRIVWAGESNRAP----AADKTVDAGGRAMIPGFVDSHSHLVFAGDRTQEFNARMSGRPYS-----AGGIRTTVA 103
Cdd:cd01296 1 IAIRDGRIAAVGPAASLPapgpAAAEEIDAGGRAVTPGLVDCHTHLVFAGDRVDEFAARLAGASYEeilaaGGGILSTVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 104 ATRAASDDELSANVARYLAEALRQGTTTCETKSGYGLTVEDEARALRIAARH------TDEVTFLGAHIVSPDYADDPAg 177
Cdd:cd01296 81 ATRAASEDELFASALRRLARMLRHGTTTVEVKSGYGLDLETELKMLRVIRRLkeegpvDLVSTFLGAHAVPPEYKGREE- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 178 YVDLVTGPMLDACA--PHARWIDVFCEQGAFDGDQARAVLTAGIAKGLHPRVHANQLGHGPGVQLAVELDAASADHCTHL 255
Cdd:cd01296 160 YIDLVIEEVLPAVAeeNLADFCDVFCEKGAFSLEQSRRILEAAKEAGLPVKIHADELSNIGGAELAAELGALSADHLEHT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 256 TDADIDALGQGDTVATLLPGAEFSTRAVWPDARRLLDAGATVALSTDCNPGSSFTSSMPFCIALAVRDMGMTPDEAVRAA 335
Cdd:cd01296 240 SDEGIAALAEAGTVAVLLPGTAFSLRETYPPARKLIDAGVPVALGTDFNPGSSPTSSMPLVMHLACRLMRMTPEEALTAA 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 948140606 336 TAGGAAALRR-TDIGRIAPGARADLLLLDAPSHVHLAYRPGVPLADAVWQRG 386
Cdd:cd01296 320 TINAAAALGLgETVGSLEVGKQADLVILDAPSYEHLAYRFGVNLVEYVIKNG 371
|
|
| hutI |
TIGR01224 |
imidazolonepropionase; This enzyme catalyzes the third step in histidine degradation. [Energy ... |
28-387 |
3.70e-113 |
|
imidazolonepropionase; This enzyme catalyzes the third step in histidine degradation. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273512 [Multi-domain] Cd Length: 377 Bit Score: 335.15 E-value: 3.70e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 28 IRDAAVVIDGDRIVWAGESNRAPA--ADKTVDAGGRAMIPGFVDSHSHLVFAGDRTQEFNARMSGRPY-----SAGGIRT 100
Cdd:TIGR01224 1 IEDAVILIHGGKIVWIGQLAALPGeeATEIIDCGGGLVTPGLVDPHTHLVFAGDRVNEFEMKLQGASYleilaQGGGILS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 101 TVAATRAASDDELSANVARYLAEALRQGTTTCETKSGYGLTVEDEARALRIAARHTDEV------TFLGAHIVSPDYADD 174
Cdd:TIGR01224 81 TVRATRAASEEELLKLALFRLKSMLRSGTTTAEVKSGYGLDLETELKMLRAAKALHEEQpvdvvtTFLGAHAVPPEFQGR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 175 PAGYVDLVTGPMLDACAPH--ARWIDVFCEQGAFDGDQARAVLTAGIAKGLHPRVHANQLGHGPGVQLAVELDAASADHC 252
Cdd:TIGR01224 161 PDDYVDGICEELIPQVAEEglASFADVFCEAGVFSVEQSRRILQAAQEAGLPVKLHAEELSNLGGAELAAKLGAVSADHL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 253 THLTDADIDALGQGDTVATLLPGAEFSTRAVWPDARRLLDAGATVALSTDCNPGSSFTSSMPFCIALAVRDMGMTPDEAV 332
Cdd:TIGR01224 241 EHASDAGIKALAEAGTVAVLLPGTTFYLRETYPPARQLIDYGVPVALATDLNPGSSPTLSMQLIMSLACRLMKMTPEEAL 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 948140606 333 RAATAGGAAALRRTDI-GRIAPGARADLLLLDAPSHVHLAYRPGVPLADAVWQRGA 387
Cdd:TIGR01224 321 HAATVNAAYALGLGEErGTLEAGRDADLVILSAPSYAEIPYHYGVNHVHAVIKNGN 376
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
21-389 |
2.18e-65 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 212.90 E-value: 2.18e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 21 DGSPLGLIRDAAVVIDGDRIVWAGESN--RAPAADKTVDAGGRAMIPGFVDSHSHLVFAGDRTQEFNArmsgrpysAGGI 98
Cdd:COG1228 19 DGTGGGVIENGTVLVEDGKIAAVGPAAdlAVPAGAEVIDATGKTVLPGLIDAHTHLGLGGGRAVEFEA--------GGGI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 99 RTTVaatraasddELSANVARYLAEALRQGTTTCETKSGYGLtvedearALRIAARHTDEVTFLGAHIVSPDYA-DDPAG 177
Cdd:COG1228 91 TPTV---------DLVNPADKRLRRALAAGVTTVRDLPGGPL-------GLRDAIIAGESKLLPGPRVLAAGPAlSLTGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 178 YVDLV---TGPMLDACAPH-ARWIDVFCEQG--AFDGDQARAVLTAGIAKGLHPRVHANQLGhgpGVQLAVELDAASADH 251
Cdd:COG1228 155 AHARGpeeARAALRELLAEgADYIKVFAEGGapDFSLEELRAILEAAHALGLPVAAHAHQAD---DIRLAVEAGVDSIEH 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 252 CTHLTDADIDALGQGDTVaTLLPGAEFSTR------------------AVWPDARRLLDAGATVALSTDCNPGSSFTSSM 313
Cdd:COG1228 232 GTYLDDEVADLLAEAGTV-VLVPTLSLFLAllegaaapvaakarkvreAALANARRLHDAGVPVALGTDAGVGVPPGRSL 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 948140606 314 PFCIALAVRdMGMTPDEAVRAATAGGAAALRRTD-IGRIAPGARADLLLLDAPSHVHLAYRPGVplaDAVWQRGARV 389
Cdd:COG1228 311 HRELALAVE-AGLTPEEALRAATINAAKALGLDDdVGSLEPGKLADLVLLDGDPLEDIAYLEDV---RAVMKDGRVV 383
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
3-384 |
1.13e-24 |
|
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: 104.52 E-value: 1.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 3 TTAITDiACLVTNDPclgdgsPLGLIRDAAVVIDGDRIVWAGESNRAPA---ADKTVDAGGRAMIPGFVDSHSHLVFAGD 79
Cdd:COG0402 1 DLLIRG-AWVLTMDP------AGGVLEDGAVLVEDGRIAAVGPGAELPArypAAEVIDAGGKLVLPGLVNTHTHLPQTLL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 80 RTqefnarmsgrpYSAGG-----IRTTVAATRAASDDELSANVARY-LAEALRQGTTT-CETKSGYGLTVEDEARALR-- 150
Cdd:COG0402 74 RG-----------LADDLplldwLEEYIWPLEARLDPEDVYAGALLaLAEMLRSGTTTvADFYYVHPESADALAEAAAea 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 151 -IAARHTDEVTflgAHIVSPDYADDPAGYVDL---------------------------VTGPMLDACAPHARWIDVF-- 200
Cdd:COG0402 143 gIRAVLGRGLM---DRGFPDGLREDADEGLADserlierwhgaadgrirvalaphapytVSPELLRAAAALARELGLPlh 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 201 --CEQGAFDGDQARAvltagiAKGLHPRVHANQLGH-GPGVQLAveldaasadHCTHLTDADIDALGQGDTVATLLPGAE 277
Cdd:COG0402 220 thLAETRDEVEWVLE------LYGKRPVEYLDELGLlGPRTLLA---------HCVHLTDEEIALLAETGASVAHCPTSN 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 278 FSTRAVWPDARRLLDAGATVALSTDcNPGSSFTSSMPFCIALA-----VRDMG---MTPDEAVRAATAGGAAALRRTD-I 348
Cdd:COG0402 285 LKLGSGIAPVPRLLAAGVRVGLGTD-GAASNNSLDMFEEMRLAallqrLRGGDptaLSAREALEMATLGGARALGLDDeI 363
|
410 420 430
....*....|....*....|....*....|....*.
gi 948140606 349 GRIAPGARADLLLLDaPSHVHLAyrpgvPLADAVWQ 384
Cdd:COG0402 364 GSLEPGKRADLVVLD-LDAPHLA-----PLHDPLSA 393
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
12-383 |
6.92e-17 |
|
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: 81.48 E-value: 6.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 12 LVTNDPCLGDGsPLGLIRDAAVVIDGDRI--VWAGESNRAPAADKTVDAGGRAMIPGFVDSHSHLVfagdrtqefnarMS 89
Cdd:cd01298 2 LIRNGTIVTTD-PRRVLEDGDVLVEDGRIvaVGPALPLPAYPADEVIDAKGKVVMPGLVNTHTHLA------------MT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 90 -GRPYSAGG-----IRTTVAATRAASDDELSANVARY-LAEALRQGTTT-CE-------------TKSG------YGLT- 141
Cdd:cd01298 69 lLRGLADDLplmewLKDLIWPLERLLTEEDVYLGALLaLAEMIRSGTTTfADmyffypdavaeaaEELGiravlgRGIMd 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 142 -----VEDEARALRIAARHTDEvtflgahivspdYADDPAGYVDLVTGP---------MLDACAPHARWIDVF----CEQ 203
Cdd:cd01298 149 lgtedVEETEEALAEAERLIRE------------WHGAADGRIRVALAPhapytcsdeLLREVAELAREYGVPlhihLAE 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 204 GAFDGDQARAvltagiAKGLHPRVHANQLGH-GPGVQLAveldaasadHCTHLTDADIDALGQGDTVATLLPGAEFSTRA 282
Cdd:cd01298 217 TEDEVEESLE------KYGKRPVEYLEELGLlGPDVVLA---------HCVWLTDEEIELLAETGTGVAHNPASNMKLAS 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 283 VWPDARRLLDAGATVALSTD---CNPGSSFTSSMPFCiALAVRDMG-----MTPDEAVRAATAGGAAALRRTDIGRIAPG 354
Cdd:cd01298 282 GIAPVPEMLEAGVNVGLGTDgaaSNNNLDMFEEMRLA-ALLQKLAHgdptaLPAEEALEMATIGGAKALGLDEIGSLEVG 360
|
410 420 430
....*....|....*....|....*....|....*...
gi 948140606 355 ARADLLLLD------APSH---VHLAYRPGVPLADAVW 383
Cdd:cd01298 361 KKADLILIDldgphlLPVHdpiSHLVYSANGGDVDTVI 398
|
|
| Met_dep_hydrolase_A |
cd01299 |
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ... |
53-364 |
4.90e-11 |
|
Metallo-dependent hydrolases, subgroup A 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: 238624 [Multi-domain] Cd Length: 342 Bit Score: 63.47 E-value: 4.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 53 DKTVDAGGRAMIPGFVDSHSHLvfagdrtqefnarMSGRPYSAGGIRTTVAatraasddELSANVARYLAEALRQGTTTC 132
Cdd:cd01299 1 AQVIDLGGKTLMPGLIDAHTHL-------------GSDPGDLPLDLALPVE--------YRTIRATRQARAALRAGFTTV 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 133 ETKSGYGLTVEDEA---------------RALRIAARHTDevtflGAHIVSPDYADDPAGYVDLVTGpMLDACAPHAR-- 195
Cdd:cd01299 60 RDAGGADYGLLRDAidaglipgprvfasgRALSQTGGHGD-----PRGLSGLFPAGGLAAVVDGVEE-VRAAVREQLRrg 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 196 --WIDVFC-----------EQGAFDGDQARAVLTAGIAKGLHPRVHAnqlgHGP-GVQLAVELDAASADHCTHLTDADID 261
Cdd:cd01299 134 adQIKIMAtggvlspgdppPDTQFSEEELRAIVDEAHKAGLYVAAHA----YGAeAIRRAIRAGVDTIEHGFLIDDETIE 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 262 ALGQGD-----TVATLLPGAEFSTRAVWPDA----------------RRLLDAGATVALSTDCNPGSSFTSSMPFCIALA 320
Cdd:cd01299 210 LMKEKGiflvpTLATYEALAAEGAAPGLPADsaekvalvleagrdalRRAHKAGVKIAFGTDAGFPVPPHGWNARELELL 289
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 948140606 321 VRDmGMTPDEAVRAATAGGAAALRRTD-IGRIAPGARADLLLLDA 364
Cdd:cd01299 290 VKA-GGTPAEALRAATANAAELLGLSDeLGVIEAGKLADLLVVDG 333
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
33-366 |
8.40e-11 |
|
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) catalyze the deamination of cytosine, producing uracil and ammonia. They play an important role in pyrimidine salvage. CDs are present in prokaryotes and fungi, but not mammalian cells. The bacterial enzymes, but not the fungal enzymes, are related to the adenosine deaminases (ADA). The bacterial enzymes are iron dependent and hexameric.
Pssm-ID: 238618 [Multi-domain] Cd Length: 398 Bit Score: 63.03 E-value: 8.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 33 VVIDGDRIVWAGESNRAPAADKTVDAGGRAMIPGFVDSHSHL--VFAGDRTQEFNarmsgRPYSAGGIRTTVAATRAASD 110
Cdd:cd01293 17 IAIEDGRIAAIGPALAVPPDAEEVDAKGRLVLPAFVDPHIHLdkTFTGGRWPNNS-----GGTLLEAIIAWEERKLLLTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 111 DELSANVARYLAEALRQGTT-------------------TCETKSGY--------------GLTVEDEARAL-RIAARHT 156
Cdd:cd01293 92 EDVKERAERALELAIAHGTTairthvdvdpaaglkaleaLLELREEWadlidlqivafpqhGLLSTPGGEELmREALKMG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 157 DEVtfLGAhIVSPDYADDPAGYVDLvtgpMLDACAPHARWIDVFC-EQGAFDGDQARAVLTAGIAKGLHPRV---HANQL 232
Cdd:cd01293 172 ADV--VGG-IPPAEIDEDGEESLDT----LFELAQEHGLDIDLHLdETDDPGSRTLEELAEEAERRGMQGRVtcsHATAL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 233 GHGPGVQLAVELDAasadhcthLTDADID--ALGQGDTVATLLPGAEFSTRAVWPdARRLLDAGATVALSTDC--NPGSS 308
Cdd:cd01293 245 GSLPEAEVSRLADL--------LAEAGISvvSLPPINLYLQGREDTTPKRRGVTP-VKELRAAGVNVALGSDNvrDPWYP 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 948140606 309 FTSSMPFCIA-LAVRDMGMTPDEAVRAATAGGAAALRRTD---IGRIAPGARADLLLLDAPS 366
Cdd:cd01293 316 FGSGDMLEVAnLAAHIAQLGTPEDLALALDLITGNAARALgleDYGIKVGCPADLVLLDAED 377
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
63-372 |
8.79e-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: 62.52 E-value: 8.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 63 MIPGFVDSHSHLVFagdrtqefnarmsgrpysaggirtTVAATRAASDDELSANVARYLAEALRQGTTTCEtksGYGLTV 142
Cdd:pfam01979 2 VLPGLIDAHVHLEM------------------------GLLRGIPVPPEFAYEALRLGITTMLKSGTTTVL---DMGATT 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 143 EDEARALRIAARHTDEVTFLGAHIVSPDYADDPAGYVDLV--------------TGPMLDACAPHARWIDVFceqgafdg 208
Cdd:pfam01979 55 STGIEALLEAAEELPLGLRFLGPGCSLDTDGELEGRKALReklkagaefikgmaDGVVFVGLAPHGAPTFSD-------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 209 DQARAVLTAGIAKGLHPRVHAN---------QLGHGPGVQLAVELDAAS-----------ADHCTHLTDADIDALGQ--- 265
Cdd:pfam01979 127 DELKAALEEAKKYGLPVAIHALetkgevedaIAAFGGGIEHGTHLEVAEsgglldiikliLAHGVHLSPTEANLLAEhlk 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 266 GDTVAtLLPGAEFSTRAVWPDARRLLDAGATVALSTDcNPGSSFTSSMPFCIALAV-----RDMGMTPDEAVRAATAGGA 340
Cdd:pfam01979 207 GAGVA-HCPFSNSKLRSGRIALRKALEDGVKVGLGTD-GAGSGNSLNMLEELRLALelqfdPEGGLSPLEALRMATINPA 284
|
330 340 350
....*....|....*....|....*....|...
gi 948140606 341 AALRRTD-IGRIAPGARADLLLLDAPSHVHLAY 372
Cdd:pfam01979 285 KALGLDDkVGSIEVGKDADLVVVDLDPLAAFFG 317
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
32-78 |
4.05e-10 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 61.35 E-value: 4.05e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 948140606 32 AVVIDGDRIVWAGES----NRAPAADKTVDAGGRAMIPGFVDSHSHLVFAG 78
Cdd:COG1574 29 AVAVRDGRIVAVGSDaevrALAGPATEVIDLGGKTVLPGFIDAHVHLLGGG 79
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
67-333 |
2.92e-09 |
|
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: 57.34 E-value: 2.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 67 FVDSHSHLVFAGDRTQEFNARMSGRPYSAGGirTTVAATRAASDdelsanvarylaEALRQGTTTCETKSGYGL--TVED 144
Cdd:cd01292 1 FIDTHVHLDGSALRGTRLNLELKEAEELSPE--DLYEDTLRALE------------ALLAGGVTTVVDMGSTPPptTTKA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 145 EARALRIAARHTDEVTFLGAHIVSPDYADDPAGYVDLVTGPMLDACAPHARWIDVFCEQGAF--DGDQARAVLTAGIAKG 222
Cdd:cd01292 67 AIEAVAEAARASAGIRVVLGLGIPGVPAAVDEDAEALLLELLRRGLELGAVGLKLAGPYTATglSDESLRRVLEEARKLG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 223 LHPRVHANQLGHGPG-----VQLAVELDAASADHCTHLTDADIDALGQGD---TVATLLPGAEFSTRAVWPDARRLLDAG 294
Cdd:cd01292 147 LPVVIHAGELPDPTRaledlVALLRLGGRVVIGHVSHLDPELLELLKEAGvslEVCPLSNYLLGRDGEGAEALRRLLELG 226
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 948140606 295 ATVALSTDCNPGSSFTS-SMPFCIALAVRDMGMTPDEAVR 333
Cdd:cd01292 227 IRVTLGTDGPPHPLGTDlLALLRLLLKVLRLGLSLEEALR 266
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
32-78 |
1.94e-08 |
|
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: 55.78 E-value: 1.94e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 948140606 32 AVVIDGDRIVWAGESNRAPA----ADKTVDAGGRAMIPGFVDSHSHLVFAG 78
Cdd:cd01300 1 AVAVRDGRIVAVGSDAEAKAlkgpATEVIDLKGKTVLPGFIDSHSHLLLGG 51
|
|
| Met_dep_hydrolase_E |
cd01313 |
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ... |
251-382 |
2.51e-08 |
|
Metallo-dependent hydrolases, subgroup D 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: 238638 [Multi-domain] Cd Length: 418 Bit Score: 55.54 E-value: 2.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 251 HCTHLTDADIDALGQGDTVATLLPGAEFSTRAVWPDARRLLDAGATVALSTDCNPGSSFTSSM-PFCIALAVRD------ 323
Cdd:cd01313 262 HATHLTDNETLLLGRSGAVVGLCPTTEANLGDGIFPAAALLAAGGRIGIGSDSNARIDLLEELrQLEYSQRLRDrarnvl 341
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 948140606 324 ---MGMTPDEAVRAATAGGAAALRRtDIGRIAPGARADLLLLDApSHVHLAYRPGVPLADAV 382
Cdd:cd01313 342 ataGGSSARALLDAALAGGAQALGL-ATGALEAGARADLLSLDL-DHPSLAGALPDTLLDAW 401
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
1-382 |
9.59e-08 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 53.85 E-value: 9.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 1 MTTTAITDiACLVTNDPCLGDgsplglIRDAAVVIDGDRIVWAGESNRAPAADkTVDAGGRAMIPGFVDSHSHL------ 74
Cdd:PRK08204 1 MKRTLIRG-GTVLTMDPAIGD------LPRGDILIEGDRIAAVAPSIEAPDAE-VVDARGMIVMPGLVDTHRHTwqsvlr 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 75 -VFAGDRTQEFNARMSGRpysaggirttvAATRAASDDELSANVARYLaEALRQGTTTCETKSGYGLTVE--DEA-RALR 150
Cdd:PRK08204 73 gIGADWTLQTYFREIHGN-----------LGPMFRPEDVYIANLLGAL-EALDAGVTTLLDWSHINNSPEhaDAAiRGLA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 151 ---IAAR------------HTDEVTFLGAHI--VSPDYADDPAGYVDLVtgpmLDACAPHARWIDVfceqgafdgdqARA 213
Cdd:PRK08204 141 eagIRAVfahgspgpspywPFDSVPHPREDIrrVKKRYFSSDDGLLTLG----LAIRGPEFSSWEV-----------ARA 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 214 VLTAGIAKGLHPRVHANQLGHGPGVQLAVELDAA---SAD----HCTHLTDADIDALGQGDTVATLLPGAEFSTRAVWPD 286
Cdd:PRK08204 206 DFRLARELGLPISMHQGFGPWGATPRGVEQLHDAgllGPDlnlvHGNDLSDDELKLLADSGGSFSVTPEIEMMMGHGYPV 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 287 ARRLLDAGATVALSTDCNPGSS--FTSSMPFCIA---------------LAVRDMGMTPDEAVRAATAGGAAALRRTD-I 348
Cdd:PRK08204 286 TGRLLAHGVRPSLGVDVVTSTGgdMFTQMRFALQaerardnavhlreggMPPPRLTLTARQVLEWATIEGARALGLEDrI 365
|
410 420 430
....*....|....*....|....*....|....
gi 948140606 349 GRIAPGARADLLLLDAPShVHLAyrpgvPLADAV 382
Cdd:PRK08204 366 GSLTPGKQADLVLIDATD-LNLA-----PVHDPV 393
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
28-108 |
1.38e-07 |
|
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: 53.17 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 28 IRDAAVVIDGDRIVWAGESNRAPAADKTVDAGGRAMIPGFVDSHSHLvfagdrtqefnaRMSGRPYsAGGIRTtvaATRA 107
Cdd:COG0044 13 LERADVLIEDGRIAAIGPDLAAPEAAEVIDATGLLVLPGLIDLHVHL------------REPGLEH-KEDIET---GTRA 76
|
.
gi 948140606 108 A 108
Cdd:COG0044 77 A 77
|
|
| PRK06151 |
PRK06151 |
N-ethylammeline chlorohydrolase; Provisional |
27-371 |
1.61e-07 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180428 [Multi-domain] Cd Length: 488 Bit Score: 53.12 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 27 LIRDAAVVIDGDRIVWAGESNRAPaADKTVDAGGRAMIPGFVDSHS-----HLVFAGDRTQEFNA-RMSGRPYSAGGIRt 100
Cdd:PRK06151 20 LLRDGEVVFEGDRILFVGHRFDGE-VDRVIDAGNALVGPGFIDLDAlsdldTTILGLDNGPGWAKgRVWSRDYVEAGRR- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 101 tvaatRAASDDELsANVARY-LAEALRQGTTTC-----ETKSGYGLTVEDEARALRIAARHTDEVtFLGAHIVSPDYADD 174
Cdd:PRK06151 98 -----EMYTPEEL-AFQKRYaFAQLLRNGITTAmpiasLFYRQWAETYAEFAAAAEAAGRLGLRV-YLGPAYRSGGSVLE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 175 PAGYVDLVTGPMLdACAPHARWIDVFCEQGAFDGDQARAVL---------------TAGIAK--GLHPRVHANQ------ 231
Cdd:PRK06151 171 ADGSLEVVFDEAR-GLAGLEEAIAFIKRVDGAHNGLVRGMLapdrietctvdllrrTAAAARelGCPVRLHCAQgvleve 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 232 -----LGHGPGVQLA-VEL--DAASADHCTHLTDADIDALGQGDTVATL---------LPGAEFSTRAVWPDARRLLDAG 294
Cdd:PRK06151 250 tvrrlHGTTPLEWLAdVGLlgPRLLIPHATYISGSPRLNYSGGDDLALLaehgvsivhCPLVSARHGSALNSFDRYREAG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 295 ATVALSTDCNPgSSFTSSMPFCIALAvRDMGMTPDEA-----VRAATAGGAAALRRTDIGRIAPGARADLLLLDApSHVH 369
Cdd:PRK06151 330 INLALGTDTFP-PDMVMNMRVGLILG-RVVEGDLDAAsaadlFDAATLGGARALGRDDLGRLAPGAKADIVVFDL-DGLH 406
|
..
gi 948140606 370 LA 371
Cdd:PRK06151 407 MG 408
|
|
| COG3653 |
COG3653 |
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and ... |
20-131 |
7.93e-07 |
|
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442870 [Multi-domain] Cd Length: 528 Bit Score: 50.94 E-value: 7.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 20 GDGSPLgliRDAAVVIDGDRIVWAGESNRAPAAdKTVDAGGRAMIPGFVDSHSHlvfagdrtqefnarmsgrpysaggir 99
Cdd:COG3653 14 GTGAPP---FRADVAIKGGRIVAVGDLAAAEAA-RVIDATGLVVAPGFIDIHTH-------------------------- 63
|
90 100 110
....*....|....*....|....*....|..
gi 948140606 100 ttvaatraaSDDELSANvaRYLAEALRQGTTT 131
Cdd:COG3653 64 ---------YDLQLLWD--PRLEPSLRQGVTT 84
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
26-390 |
1.32e-06 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 50.10 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 26 GLIRDAAVVIDGDRIVWAGEsnRAPAADKTVDAGGRAMIPGFVDSH-----SHLVFAgdrtqEFnARMSgrpySAGGIRT 100
Cdd:COG1001 20 GEILEGDIAIAGGRIAGVGD--YIGEATEVIDAAGRYLVPGFIDGHvhiesSMVTPA-----EF-ARAV----LPHGTTT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 101 TVAatraasdD--ELsANVA-----RYLAEALRQG--------------TTTCETkSGYGLTVEDEARALRIaarhtDEV 159
Cdd:COG1001 88 VIA-------DphEI-ANVLglegvRYMLEAAEGLpldifvmlpscvpaTPGLET-AGAVLGAEDLAELLDH-----PRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 160 TFLGahivspdyaddpagyvdlvtgpmldacapharwiDVFCEQGAFDGDQ-ARAVLTAGIAKGLHprVHanqlGHGPGV 238
Cdd:COG1001 154 IGLG----------------------------------EVMNFPGVLNGDPrMLAKIAAALAAGKV--ID----GHAPGL 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 239 qLAVELDA-ASA----DH-CTHLTDAdIDALGQGDTV-----------ATLLPG-AEFstravwpDARRlldagatVALS 300
Cdd:COG1001 194 -SGKDLNAyAAAgirsDHeCTTAEEA-LEKLRRGMYVmiregsaakdlPALLPAvTEL-------NSRR-------CALC 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 301 TD-CNPGSSFTS-SMPFCIALAVRdMGMTPDEAVRAATAGGAAALRRTDIGRIAPGARADLLLLDAPSHVHlayrpgvpl 378
Cdd:COG1001 258 TDdRHPDDLLEEgHIDHVVRRAIE-LGLDPVTAIQMATLNAAEHFGLKDLGAIAPGRRADIVLLDDLEDFK--------- 327
|
410
....*....|..
gi 948140606 379 ADAVWQRGARVA 390
Cdd:COG1001 328 VEKVYADGKLVA 339
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
26-363 |
1.57e-06 |
|
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: 49.50 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 26 GLIRDAAVVIDGDRIVWAGESNRAPAADKTVDAGGRAMIPGFVDSHSHlvfagdrtqefnarmsgrpySAGGirttvAAT 105
Cdd:cd00854 12 GGLEDGAVLVEDGKIVAIGPEDELEEADEIIDLKGQYLVPGFIDIHIH--------------------GGGG-----ADF 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 106 RAASDDELsANVARYLAealRQGTT----TCETKSgygltVEDEARALRIAARHTDE-----------------VTFLGA 164
Cdd:cd00854 67 MDGTAEAL-KTIAEALA---KHGTTsflpTTVTAP-----PEEIAKALAAIAEAIAEgqgaeilgihlegpfisPEKKGA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 165 H----IVSPD------YADDPAGYVDLVTgpmldaCAP----HARWIDVFCEQG--------AFDGDQARAVLTAGIA-- 220
Cdd:cd00854 138 HppeyLRAPDpeelkkWLEAAGGLIKLVT------LAPeldgALELIRYLVERGiivsighsDATYEQAVAAFEAGAThv 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 221 -------KGLHPR----------------------VHAnqlgHGPGVQLAveLDAASADHCTHLTDAdIDALGQGDTVAT 271
Cdd:cd00854 212 thlfnamSPLHHRepgvvgaalsdddvyaeliadgIHV----HPAAVRLA--YRAKGADKIVLVTDA-MAAAGLPDGEYE 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 272 LlpGAEFSTraVWPDARRLldAGATVAlstdcnpGSsfTSSMPFCIALAVRDMGMTPDEAVRAATAGGAAALRRTD-IGR 350
Cdd:cd00854 285 L--GGQTVT--VKDGVARL--ADGTLA-------GS--TLTMDQAVRNMVKWGGCPLEEAVRMASLNPAKLLGLDDrKGS 349
|
410
....*....|...
gi 948140606 351 IAPGARADLLLLD 363
Cdd:cd00854 350 LKPGKDADLVVLD 362
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
28-75 |
1.70e-06 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 49.61 E-value: 1.70e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 948140606 28 IRDAAVVIDGDRIVWAGESNRAPAADKTVDAGGRAMIPGFVDSHSHLV 75
Cdd:PRK07228 19 IVDGDVLIEDDRIAAVGDRLDLEDYDDHIDATGKVVIPGLIQGHIHLC 66
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
24-376 |
1.91e-06 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 49.33 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 24 PLGLIRDAAVVIDGDRIVWAGEsnRAPAADKTVDAGGRAMIPGFVDSHSHlvfagdrtqefnarmsGrpysAGGirttvA 103
Cdd:COG1820 10 GDGVLEDGALLIEDGRIAAIGP--GAEPDAEVIDLGGGYLAPGFIDLHVH----------------G----GGG-----V 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 104 ATRAASDDELsANVARYLAealRQGTT----TCETksgygLTVEDEARALRIAARHTDEVT---FLGAH----------- 165
Cdd:COG1820 63 DFMDGTPEAL-RTIARAHA---RHGTTsflpTTIT-----APPEDLLRALAAIAEAIEQGGgagILGIHlegpflspekk 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 166 -------IVSPD------YADDPAGYVDLVTgpmldaCAP----HARWIDVFCEQGAF--------DGDQARAVLTAGI- 219
Cdd:COG1820 134 gahppeyIRPPDpeeldrLLEAAGGLIKLVT------LAPelpgALEFIRYLVEAGVVvslghtdaTYEQARAAFEAGAt 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 220 --------AKGLHPRvHANQLG-------------------HGPGVQLAveLDAASADHCTHLTDAdIDALGQGDTVATL 272
Cdd:COG1820 208 hvthlfnaMSPLHHR-EPGVVGaalddddvyaeliadgihvHPAAVRLA--LRAKGPDRLILVTDA-MAAAGLPDGEYEL 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 273 LPgaefstRAVWPDARRLLDAGATVAlstdcnpGSsfTSSMPFCIALAVRDMGMTPDEAVRAATAGGAAALRRTD-IGRI 351
Cdd:COG1820 284 GG------LEVTVKDGVARLADGTLA-------GS--TLTMDDAVRNLVEWTGLPLEEAVRMASLNPARALGLDDrKGSI 348
|
410 420
....*....|....*....|....*
gi 948140606 352 APGARADLLLLDAPSHVHLAYRPGV 376
Cdd:COG1820 349 APGKDADLVVLDDDLNVRATWVGGE 373
|
|
| PRK09229 |
PRK09229 |
N-formimino-L-glutamate deiminase; Validated |
251-389 |
1.07e-05 |
|
N-formimino-L-glutamate deiminase; Validated
Pssm-ID: 236420 [Multi-domain] Cd Length: 456 Bit Score: 47.15 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 251 HCTHLTDADIDALGQGDTVATLLPgaefSTRA-----VWPdARRLLDAGATVALSTDCNpgssftssmpFCI-------- 317
Cdd:PRK09229 271 HATHLTDAETARLARSGAVAGLCP----TTEAnlgdgIFP-AVDYLAAGGRFGIGSDSH----------VSIdlveelrl 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 318 -------------ALAVRDMGMTPDEAVRAATAGGAAALRRtDIGRIAPGARADLLLLDaPSHVHLAYRPGVPLADA--- 381
Cdd:PRK09229 336 leygqrlrdrrrnVLAAAAQPSVGRRLFDAALAGGAQALGR-AIGGLAVGARADLVVLD-LDHPALAGREGDALLDRwvf 413
|
170
....*....|....*..
gi 948140606 382 ---------VWQRGARV 389
Cdd:PRK09229 414 aggdaavrdVWVAGRWV 430
|
|
| GDEase |
cd01303 |
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ... |
14-382 |
1.13e-05 |
|
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: 47.27 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 14 TNDPCLGDG-SPLGLIRDAAVVIDGDRIVWAG----ESNRAPAADKTVDAGGRAMIPGFVDSHSHLvfagdrTQefnARM 88
Cdd:cd01303 9 KSLPELELVeDALRVVEDGLIVVVDGNIIAAGaaetLKRAAKPGARVIDSPNQFILPGFIDTHIHA------PQ---YAN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 89 SGrpySAGGI-------RTTVAATRAASDDELSANVA-RYLAEALRQGTTTCetkSGYGlTVEDEA-RALRIAARHTDEV 159
Cdd:cd01303 80 IG---SGLGEplldwleTYTFPEEAKFADPAYAREVYgRFLDELLRNGTTTA---CYFA-TIHPEStEALFEEAAKRGQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 160 TFLGAhiVSPDYADdPAGYVDLVTGPMLDACAPHARWIDVF--------------CEQGAFDGDQARA-------VLT-- 216
Cdd:cd01303 153 AIAGK--VCMDRNA-PEYYRDTAESSYRDTKRLIERWHGKSgrvkpaitprfapsCSEELLAALGKLAkehpdlhIQThi 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 217 ----AGIA--KGLHPRV--------HANQLGhgPGVQLAveldaasadHCTHLTDADIDALGQ-GDTVA------TLLPG 275
Cdd:cd01303 230 senlDEIAwvKELFPGArdyldvydKYGLLT--EKTVLA---------HCVHLSEEEFNLLKErGASVAhcptsnLFLGS 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 276 AEFstravwpDARRLLDAGATVALSTDCNPGSSFtsSMPFCIALAV-----------RDMGMTPDEAVRAATAGGAAALR 344
Cdd:cd01303 299 GLF-------DVRKLLDAGIKVGLGTDVGGGTSF--SMLDTLRQAYkvsrllgyelgGHAKLSPAEAFYLATLGGAEALG 369
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 948140606 345 RTD-IGRIAPGARADLLLLD--APSHVHLAYRPGVPLADAV 382
Cdd:cd01303 370 LDDkIGNFEVGKEFDAVVIDpsATPLLADRMFRVESLEEAL 410
|
|
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
28-390 |
1.30e-05 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 46.71 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 28 IRDAAVVIDGDRIVWAGESNRAPAADktVDAGGRAMIPGFVDSHS-HL--VFAGDRTQEFNARMSGRPY----SAGGIRT 100
Cdd:PRK15446 17 VVDGSLLIEDGRIAAIDPGASALPGA--IDAEGDYLLPGLVDLHTdNLekHLAPRPGVDWPADAALAAHdaqlAAAGITT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 101 TVAATRAASDDEL---SANVARYLAEALRQGTTtcetksgygltvEDEARA-LRIAARHtdEVTFLGAHIVSPDYADDPA 176
Cdd:PRK15446 95 VFDALSVGDEEDGglrSRDLARKLIDAIEEARA------------RGLLRAdHRLHLRC--ELTNPDALELFEALLAHPR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 177 gyVDLVTgpMLDAcAPHAR-------WIDVFCEQGAFDGDQARAVLTagiakglhpRVHANQLGHGPG-----VQLAVEL 244
Cdd:PRK15446 161 --VDLVS--LMDH-TPGQRqfrdlekYREYYAGKYGLSDEEFDAFVE---------ERIALSARYAPPnrraiAALARAR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 245 DAASADHCTHlTDADID-ALGQGDTVA---TLLPGAEFSTRA-----------V-------WPDARRLLDAGATVALSTD 302
Cdd:PRK15446 227 GIPLASHDDD-TPEHVAeAHALGVAIAefpTTLEAARAARALgmsvlmgapnvVrggshsgNVSALDLAAAGLLDILSSD 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 303 CNPGSSFTSsmPFCIAlavRDMGMTPDEAVRAATAGGAAALRRTDIGRIAPGARADLLLLDApshvhlayRPGVPLADAV 382
Cdd:PRK15446 306 YYPASLLDA--AFRLA---DDGGLDLPQAVALVTANPARAAGLDDRGEIAPGKRADLVRVRR--------AGGLPVVRAV 372
|
....*...
gi 948140606 383 WQRGARVA 390
Cdd:PRK15446 373 WRGGRRVF 380
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
20-73 |
1.53e-05 |
|
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: 46.52 E-value: 1.53e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 948140606 20 GDGSPlGLIRDaaVVIDGDRIVWAGeSNRAPAADKTVDAGGRAMIPGFVDSHSH 73
Cdd:cd01297 12 GTGAP-PFTAD--VGIRDGRIAAIG-PILSTSAREVIDAAGLVVAPGFIDVHTH 61
|
|
| PRK09228 |
PRK09228 |
guanine deaminase; Provisional |
28-132 |
2.26e-05 |
|
guanine deaminase; Provisional
Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 46.34 E-value: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 28 IRDAAVVIDGDRIVWAGE----SNRAPAADKTVDAGGRAMIPGFVDSHSHLvfagdrTQefnARMSGrPYSAGGI----R 99
Cdd:PRK09228 29 IEDGLLLVEDGRIVAAGPyaelRAQLPADAEVTDYRGKLILPGFIDTHIHY------PQ---TDMIA-SYGEQLLdwlnT 98
|
90 100 110
....*....|....*....|....*....|....
gi 948140606 100 TTVAATRAASDDELSANVA-RYLAEALRQGTTTC 132
Cdd:PRK09228 99 YTFPEERRFADPAYAREVAeFFLDELLRNGTTTA 132
|
|
| PRK05985 |
PRK05985 |
cytosine deaminase; Provisional |
31-80 |
2.81e-05 |
|
cytosine deaminase; Provisional
Pssm-ID: 180337 [Multi-domain] Cd Length: 391 Bit Score: 45.69 E-value: 2.81e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 948140606 31 AAVVIDGDRIVWAGESNRAPAADKTVDAGGRAMIPGFVDSHSHL--VFAGDR 80
Cdd:PRK05985 17 VDILIRDGRIAAIGPALAAPPGAEVEDGGGALALPGLVDGHIHLdkTFWGDP 68
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
28-74 |
2.97e-05 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 46.00 E-value: 2.97e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 948140606 28 IRDAAVVIDGDRIVWAGESNRAPA-ADKTVDAGGRAMIPGFVDSHSHL 74
Cdd:PRK08203 21 IADGGLVVEGGRIVEVGPGGALPQpADEVFDARGHVVTPGLVNTHHHF 68
|
|
| PRK08393 |
PRK08393 |
N-ethylammeline chlorohydrolase; Provisional |
22-73 |
3.56e-05 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 181411 [Multi-domain] Cd Length: 424 Bit Score: 45.56 E-value: 3.56e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 948140606 22 GSPLGLIRdAAVVIDGDRIVWAGESNRAPAaDKTVDAGGRAMIPGFVDSHSH 73
Cdd:PRK08393 13 GENLKVIR-ADVLIEGNKIVEVKRNINKPA-DTVIDASGSVVSPGFINAHTH 62
|
|
| PRK06380 |
PRK06380 |
metal-dependent hydrolase; Provisional |
33-80 |
3.58e-05 |
|
metal-dependent hydrolase; Provisional
Pssm-ID: 180548 [Multi-domain] Cd Length: 418 Bit Score: 45.64 E-value: 3.58e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 948140606 33 VVIDGDRIVWAGESNraPAADKTVDAGGRAMIPGFVDSHSHLVFAGDR 80
Cdd:PRK06380 24 VYIEGNKIVYVGDVN--EEADYIIDATGKVVMPGLINTHAHVGMTASK 69
|
|
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
27-74 |
4.90e-05 |
|
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: 45.29 E-value: 4.90e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 948140606 27 LIRDAAVV-----------IDGDRIVWAGESNRAPAADKTVDAGGRAMIPGFVDSHSHL 74
Cdd:cd01314 2 IIKNGTIVtadgsfkadilIEDGKIVAIGPNLEAPGGVEVIDATGKYVLPGGIDPHTHL 60
|
|
| PRK06038 |
PRK06038 |
N-ethylammeline chlorohydrolase; Provisional |
26-74 |
5.20e-05 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180363 [Multi-domain] Cd Length: 430 Bit Score: 45.13 E-value: 5.20e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 948140606 26 GLIRDAAVVIDGDRIVWAGESNRApAADKTVDAGGRAMIPGFVDSHSHL 74
Cdd:PRK06038 17 GDLKKGSVVIEDGTITEVSESTPG-DADTVIDAKGSVVMPGLVNTHTHA 64
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
26-73 |
8.81e-05 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 44.48 E-value: 8.81e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 948140606 26 GLIRDAAVVIDGDRIVWAGESNRAPAADKTVDAGGRAMIPGFVDSHSH 73
Cdd:PRK09236 15 GKIFEGDVLIENGRIAKIASSISAKSADTVIDAAGRYLLPGMIDDQVH 62
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
24-74 |
9.85e-05 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 44.03 E-value: 9.85e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 948140606 24 PLGLIRDAAVVIDGDRIVWAGEsNRAPAADKTVDAGGRAMIPGFVDSHSHL 74
Cdd:PRK09357 13 PKGLDEVADVLIDDGKIAAIGE-NIEAEGAEVIDATGLVVAPGLVDLHVHL 62
|
|
| PRK07203 |
PRK07203 |
putative aminohydrolase SsnA; |
12-74 |
1.08e-04 |
|
putative aminohydrolase SsnA;
Pssm-ID: 235963 [Multi-domain] Cd Length: 442 Bit Score: 44.16 E-value: 1.08e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 948140606 12 LVTNDPClgdgSPLglIRDAAVVIDGDRIV----WAGESNRAPAADKtVDAGGRAMIPGFVDSHSHL 74
Cdd:PRK07203 9 AITRDPA----KPV--IEDGAIAIEGNVIVeigtTDELKAKYPDAEF-IDAKGKLIMPGLINSHNHI 68
|
|
| pyrC_multi |
TIGR00857 |
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
26-74 |
1.31e-04 |
|
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: 43.59 E-value: 1.31e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 948140606 26 GLIRDAAVVIDGDRIVwAGESNRAPAADKTVDAGGRAMIPGFVDSHSHL 74
Cdd:TIGR00857 1 GKETEVDILVEGGRIK-KIGKLRIPPDAEVIDAKGLLVLPGFIDLHVHL 48
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
31-74 |
2.82e-04 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 42.85 E-value: 2.82e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 948140606 31 AAVVIDGDRIVWAGesnrAPAADKTVDAGGRAMIPGFVDSHSHL 74
Cdd:PRK08323 19 ADVLIEDGKIAAIG----ANLGDEVIDATGKYVMPGGIDPHTHM 58
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
28-74 |
3.14e-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: 42.66 E-value: 3.14e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 948140606 28 IRDAAVVIDGDRIVWAGESNRAPAADKTVDAGGRAMIPGFVDSHSHL 74
Cdd:cd01315 15 VREADIAVKGGKIAAIGPDIANTEAEEVIDAGGLVVMPGLIDTHVHI 61
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
22-78 |
4.42e-04 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 42.14 E-value: 4.42e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 948140606 22 GSPLGLIRDaaVVIDGDRIVWAGESNRAPAADKTVDAGGRAMIPGFVDSHSHlVFAG 78
Cdd:PRK09237 12 ANGIDGVID--IAIEDGKIAAVAGDIDGSQAKKVIDLSGLYVSPGWIDLHVH-VYPG 65
|
|
| ADA |
cd01320 |
Adenosine deaminase (ADA) is a monomeric zinc dependent enzyme which catalyzes the ... |
220-333 |
8.95e-04 |
|
Adenosine deaminase (ADA) is a monomeric zinc dependent enzyme which catalyzes the irreversible hydrolytic deamination of both adenosine, as well as desoxyadenosine, to ammonia and inosine or desoxyinosine, respectively. ADA plays an important role in the purine pathway. Low, as well as high levels of ADA activity have been linked to several diseases.
Pssm-ID: 238645 Cd Length: 325 Bit Score: 41.04 E-value: 8.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 220 AKGLHPRVHANQLGHGPGVQLAVELDAAS-ADHCTHLTD--ADIDALGQGDTVATLLPGAEFSTRAVWPDA----RRLLD 292
Cdd:cd01320 184 EAGLRLTAHAGEAGGPESVRDALDLLGAErIGHGIRAIEdpELVKRLAERNIPLEVCPTSNVQTGAVKSLAehplRELLD 263
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 948140606 293 AGATVALSTDcNPGSSFTsSMPFCIALAVRDMGMTPDEAVR 333
Cdd:cd01320 264 AGVKVTINTD-DPTVFGT-YLTDEYELLAEAFGLTEEELKK 302
|
|
| PRK10027 |
PRK10027 |
cryptic adenine deaminase; Provisional |
33-74 |
9.62e-04 |
|
cryptic adenine deaminase; Provisional
Pssm-ID: 182201 [Multi-domain] Cd Length: 588 Bit Score: 41.35 E-value: 9.62e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 948140606 33 VVIDGDRIVWAGESNRAPAADKTVDAGGRAMIPGFVDSHSHL 74
Cdd:PRK10027 52 IVIKGRYIAGVGAEYADAPALQRIDARGATAVPGFIDAHLHI 93
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
19-390 |
1.05e-03 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 40.98 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 19 LGDGSPLGLIRDAAVVIDGDRIVWAGESNRAPAADKTVD---------AGGRAMIPGFVDSHSHLV------FAGDRTQE 83
Cdd:pfam07969 33 LPDVLPNAVVKGQAGRTPKGRWLVGEGWDEAQFAETRFPyaladldevAPDGPVLLRALHTHAAVAnsaaldLAGITKAT 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 84 FNARMSGRPYSAGG-------IRTTVAATRAASDDELSANVARYLAEALRQGTTTCETKSGYGLTVEDEARALRIAAR-- 154
Cdd:pfam07969 113 EDPPGGEIARDANGegltgllREGAYALPPLLAREAEAAAVAAALAALPGFGITSVDGGGGNVHSLDDYEPLRELTAAek 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 155 HTDEVTFLGAHIVSPDYADDPAGYVDLVTGPMLD---ACAPHARWIDVFCEQGAFDGDQARAVLTAGIAKGLHPRVHANQ 231
Cdd:pfam07969 193 LKELLDAPERLGLPHSIYELRIGAMKLFADGVLGsrtAALTEPYFDAPGTGWPDFEDEALAELVAAARERGLDVAIHAIG 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 232 LGHGPGVQLAVEL--------DAASADHCT---HLTDADIDALG--------QGDTVATLLPGAEFSTRAV----WPDAR 288
Cdd:pfam07969 273 DATIDTALDAFEAvaeklgnqGRVRIEHAQgvvPYTYSQIERVAalggaagvQPVFDPLWGDWLQDRLGAErargLTPVK 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 289 RLLDAGATVALSTDCNPGS---------SFTSSMPFCIALAVRDMGMTPDEAVRAATAGGAAALRRTD-IGRIAPGARAD 358
Cdd:pfam07969 353 ELLNAGVKVALGSDAPVGPfdpwprigaAVMRQTAGGGEVLGPDEELSLEEALALYTSGPAKALGLEDrKGTLGVGKDAD 432
|
410 420 430
....*....|....*....|....*....|...
gi 948140606 359 LLLLDA-PSHVHLAYRPGVpLADAVWQRGARVA 390
Cdd:pfam07969 433 LVVLDDdPLTVDPPAIADI-RVRLTVVDGRVVY 464
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
26-73 |
1.35e-03 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 40.79 E-value: 1.35e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 948140606 26 GLIRDAAVVIDGDRIVWAGESNRAPAADKTVDAGGRAMIPGFVDSHSH 73
Cdd:PRK02382 15 NSLQPRDVRIDGGKITAVGKDLDGSSSEEVIDARGMLLLPGGIDVHVH 62
|
|
| PRK09061 |
PRK09061 |
D-glutamate deacylase; Validated |
28-84 |
1.35e-03 |
|
D-glutamate deacylase; Validated
Pssm-ID: 236369 [Multi-domain] Cd Length: 509 Bit Score: 40.83 E-value: 1.35e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 948140606 28 IRDaaVVIDGDRIVWAGESnrAPAADKTVDAGGRAMIPGFVDSHSH-LVFAGDRTQEF 84
Cdd:PRK09061 38 VRD--VGIKGGKIAAVGTA--AIEGDRTIDATGLVVAPGFIDLHAHgQSVAAYRMQAF 91
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
54-74 |
1.56e-03 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 40.59 E-value: 1.56e-03
|
| archeal_chlorohydrolases |
cd01305 |
Predicted chlorohydrolases. These metallo-dependent hydrolases from archea are part of the ... |
238-302 |
2.66e-03 |
|
Predicted chlorohydrolases. These metallo-dependent hydrolases from archea are 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. They 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. Some members of this subgroup are predicted to be chlorohyrolases.
Pssm-ID: 238630 [Multi-domain] Cd Length: 263 Bit Score: 39.31 E-value: 2.66e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 948140606 238 VQLAVELDAASADHCTHLTDADIDALGQGDTVATLLPGAEFSTRAVWPDARRLLDAGATVALSTD 302
Cdd:cd01305 157 IERALDLEPDLLVHGTHLTDEDLELVRENGVPVVLCPRSNLYFGVGIPPVAELLKLGIKVLLGTD 221
|
|
| PRK07575 |
PRK07575 |
dihydroorotase; Provisional |
24-73 |
2.82e-03 |
|
dihydroorotase; Provisional
Pssm-ID: 236055 [Multi-domain] Cd Length: 438 Bit Score: 39.66 E-value: 2.82e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 948140606 24 PLGLIRDAAVVIDGDRIVWAGESNRAPAADKTVDAGGRAMIPGFVDSHSH 73
Cdd:PRK07575 15 PSGELLLGDVLVEDGKIVAIAPEISATAVDTVIDAEGLTLLPGVIDPQVH 64
|
|
| PhnM |
cd01306 |
PhnM is believed to be a subunit of the membrane associated C-P lyase complex. C-P lyase is ... |
284-386 |
4.04e-03 |
|
PhnM is believed to be a subunit of the membrane associated C-P lyase complex. C-P lyase is thought to catalyze the direct cleavage of inactivated C-P bonds to yield inorganic phosphate and the corresponding hydrocarbons. It is responsible for cleavage of alkylphosphonates, which are utilized as sole phosphorus sources by many bacteria.
Pssm-ID: 238631 Cd Length: 325 Bit Score: 38.80 E-value: 4.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 284 WPDARRLLDAGATVALSTDCNPGSSFTSsmPFCIAlavRDMGMTPDEAVRAATAGGAAALRRTDIGRIAPGARADLLLLD 363
Cdd:cd01306 236 NVSARELAAHGLLDILSSDYVPASLLHA--AFRLA---DLGGWSLPEAVALVSANPARAVGLTDRGSIAPGKRADLILVD 310
|
90 100
....*....|....*....|...
gi 948140606 364 APshvhlayrPGVPLADAVWQRG 386
Cdd:cd01306 311 DM--------DGVPVVRTVWRGG 325
|
|
| A_deaminase |
pfam00962 |
Adenosine deaminase; |
219-333 |
4.80e-03 |
|
Adenosine deaminase;
Pssm-ID: 425964 Cd Length: 330 Bit Score: 38.56 E-value: 4.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 219 IAKGLHPRVHANQLGHGPGVQLAV-ELDAASADHCTHLTD--ADIDALGQGDTVATLLPGAEFSTRAVWPDA----RRLL 291
Cdd:pfam00962 185 RDAGLHLTVHAGEAGGPQSVWEALdDLGAERIGHGVRSAEdpRLLDRLADRQIPLEICPTSNVQTGAVASLAehplKTFL 264
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 948140606 292 DAGATVALSTDcNPGsSFTSSMPFCIALAVRDMGMTPDEAVR 333
Cdd:pfam00962 265 RAGVPVSLNTD-DPL-MFGSDLLDEYQVAKRAPGFDEEELAR 304
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
32-73 |
4.83e-03 |
|
Metallo-dependent hydrolases, subgroup B 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: 238632 [Multi-domain] Cd Length: 338 Bit Score: 38.85 E-value: 4.83e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 948140606 32 AVVIDGDRIVWAGESNRAPAADKTVDAGGRAMIPGFVDSHSH 73
Cdd:cd01307 1 DVAIENGKIAAVGAALAAPAATQIVDAGGCYVSPGWIDLHVH 42
|
|
| FMDH_A |
cd01304 |
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive ... |
36-158 |
5.61e-03 |
|
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive the energy for autotrophic growth from methanogenesis, the reduction of CO2 with molecular hydrogen as the electron donor. FMDH catalyzes the first step in methanogenesis, the formyl-methanofuran synthesis. In this step, CO2 is bound to methanofuran and subsequently reduced to the formyl state with electrons derived from hydrogen.
Pssm-ID: 238629 [Multi-domain] Cd Length: 541 Bit Score: 38.93 E-value: 5.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948140606 36 DGdRIVwagESNRAPAADKTVDAGGRAMIPGFVDSHSHLvfAGDRTqefNARMSGRPysaggirttvaatraasDDELSA 115
Cdd:cd01304 24 DG-KIV---ESSSGAKPAKVIDASGKVVMAGGVDMHSHI--AGGKV---NVGRILRP-----------------EDHRRD 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 948140606 116 NVARYLAEALRQGTTTCET-KSGY-----GLTVEDEARALRIAARHTDE 158
Cdd:cd01304 78 PVPKGALRRAGVGFSVPSTlATGYryaemGYTTAFEAAMPPLNARHTHE 126
|
|
| PRK07572 |
PRK07572 |
cytosine deaminase; Validated |
29-74 |
6.15e-03 |
|
cytosine deaminase; Validated
Pssm-ID: 181039 Cd Length: 426 Bit Score: 38.46 E-value: 6.15e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 948140606 29 RDAAVVIDGDRIVWAGESNRAPAADkTVDAGGRAMIPGFVDSHSHL 74
Cdd:PRK07572 16 TGIDIGIAGGRIAAVEPGLQAEAAE-EIDAAGRLVSPPFVDPHFHM 60
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
36-74 |
9.65e-03 |
|
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: 37.68 E-value: 9.65e-03
10 20 30
....*....|....*....|....*....|....*....
gi 948140606 36 DGdRIVWAGESNRAPAADKTVDAGGRAMIPGFVDSHSHL 74
Cdd:cd01309 1 DG-KIVAVGAEITTPADAEVIDAKGKHVTPGLIDAHSHL 38
|
|
| PRK09045 |
PRK09045 |
TRZ/ATZ family hydrolase; |
27-73 |
9.81e-03 |
|
TRZ/ATZ family hydrolase;
Pssm-ID: 236366 [Multi-domain] Cd Length: 443 Bit Score: 37.97 E-value: 9.81e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 948140606 27 LIRDAAVVIDGDRIVW---AGESNRAPAADKTVDAGGRAMIPGFVDSHSH 73
Cdd:PRK09045 25 VLEDHAVAIRDGRIVAilpRAEARARYAAAETVELPDHVLIPGLINAHTH 74
|
|
| |
