|
Name |
Accession |
Description |
Interval |
E-value |
| hutI |
TIGR01224 |
imidazolonepropionase; This enzyme catalyzes the third step in histidine degradation. [Energy ... |
33-406 |
1.36e-159 |
|
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: 454.18 E-value: 1.36e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 33 HALIVRQGKIRDIVPESSLYLTHDNT-FDMQGRLITPGLIDCHTHLVFGGNRAGEWEQRLNGVSYQQISAQGGGINATVS 111
Cdd:TIGR01224 4 AVILIHGGKIVWIGQLAALPGEEATEiIDCGGGLVTPGLVDPHTHLVFAGDRVNEFEMKLQGASYLEILAQGGGILSTVR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 112 ATRSATDEQLLHVAHQRMEQLIKEGVTLLEIKSGYGLDLPTEEKILRVVAALAAENIVEISPTLLAAHATPAEYRDDPDG 191
Cdd:TIGR01224 84 ATRAASEEELLKLALFRLKSMLRSGTTTAEVKSGYGLDLETELKMLRAAKALHEEQPVDVVTTFLGAHAVPPEFQGRPDD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 192 YITLVCETILPQLWEQGLFETVDLFCESVGFSLAQSERVFQAAQALGIPIKGHVEQLSLLGGAQLVSRYHGLSADHIEYL 271
Cdd:TIGR01224 164 YVDGICEELIPQVAEEGLASFADVFCEAGVFSVEQSRRILQAAQEAGLPVKLHAEELSNLGGAELAAKLGAVSADHLEHA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 272 DEAGVAAMSQSGTVGVLLPGAFYFLKeEQRPPIALLRQYQVPMAVATDFNPGTSPFISLHWAMNMACVQFGLTPEEAWAG 351
Cdd:TIGR01224 244 SDAGIKALAEAGTVAVLLPGTTFYLR-ETYPPARQLIDYGVPVALATDLNPGSSPTLSMQLIMSLACRLMKMTPEEALHA 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1915297345 352 VTRHAARALGRHATHGQLKAGFVADFVVWDATLPVEILYEPGRNPLYQRVFKGQI 406
Cdd:TIGR01224 323 ATVNAAYALGLGEERGTLEAGRDADLVILSAPSYAEIPYHYGVNHVHAVIKNGNI 377
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
35-404 |
3.76e-155 |
|
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: 442.47 E-value: 3.76e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 35 LIVRQGKIRDIVPESSL---YLTHDNTFDMQGRLITPGLIDCHTHLVFGGNRAGEWEQRLNGVSYQQISAQGGGINATVS 111
Cdd:cd01296 1 IAIRDGRIAAVGPAASLpapGPAAAEEIDAGGRAVTPGLVDCHTHLVFAGDRVDEFAARLAGASYEEILAAGGGILSTVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 112 ATRSATDEQLLHVAHQRMEQLIKEGVTLLEIKSGYGLDLPTEEKILRVVAALAAENIVEISPTLLAAHATPAEYRDDPDg 191
Cdd:cd01296 81 ATRAASEDELFASALRRLARMLRHGTTTVEVKSGYGLDLETELKMLRVIRRLKEEGPVDLVSTFLGAHAVPPEYKGREE- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 192 YITLVCETILPQLWEQGLFETVDLFCESVGFSLAQSERVFQAAQALGIPIKGHVEQLSLLGGAQLVSRYHGLSADHIEYL 271
Cdd:cd01296 160 YIDLVIEEVLPAVAEENLADFCDVFCEKGAFSLEQSRRILEAAKEAGLPVKIHADELSNIGGAELAAELGALSADHLEHT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 272 DEAGVAAMSQSGTVGVLLPGAFYFLKeEQRPPIALLRQYQVPMAVATDFNPGTSPFISLHWAMNMACVQFGLTPEEAWAG 351
Cdd:cd01296 240 SDEGIAALAEAGTVAVLLPGTAFSLR-ETYPPARKLIDAGVPVALGTDFNPGSSPTSSMPLVMHLACRLMRMTPEEALTA 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1915297345 352 VTRHAARALGRHATHGQLKAGFVADFVVWDATLPVEILYEPGRNPLYQRVFKG 404
Cdd:cd01296 319 ATINAAAALGLGETVGSLEVGKQADLVILDAPSYEHLAYRFGVNLVEYVIKNG 371
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
6-406 |
2.38e-81 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 254.89 E-value: 2.38e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 6 PDDVIWRNVRLATMDPErgtpyGLLDGHALIVRQGKIRDIVPESSLYL-THDNTFDMQGRLITPGLIDCHTHLVFGGNRA 84
Cdd:COG1228 7 AGTLLITNATLVDGTGG-----GVIENGTVLVEDGKIAAVGPAADLAVpAGAEVIDATGKTVLPGLIDAHTHLGLGGGRA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 85 GEWEQrlngvsyqqisaqGGGINATVsatrsatdeQLLHVAHQRMEQLIKEGVTLLEIKSGYGLDLP-----TEEKIL-- 157
Cdd:COG1228 82 VEFEA-------------GGGITPTV---------DLVNPADKRLRRALAAGVTTVRDLPGGPLGLRdaiiaGESKLLpg 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 158 -RVVAALAAeniveISPTLLAAHATPAEyrddpdgyitlvCETILPQLWEQGlFETVDLFCE--SVGFSLAQSERVFQAA 234
Cdd:COG1228 140 pRVLAAGPA-----LSLTGGAHARGPEE------------ARAALRELLAEG-ADYIKVFAEggAPDFSLEELRAILEAA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 235 QALGIPIKGHVEQLSllgGAQLVSRYHGLSADHIEYLDEAGVAAMSQSGTVgVLLPGAFYFL-----------------K 297
Cdd:COG1228 202 HALGLPVAAHAHQAD---DIRLAVEAGVDSIEHGTYLDDEVADLLAEAGTV-VLVPTLSLFLallegaaapvaakarkvR 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 298 EEQRPPIALLRQYQVPMAVATDFNPGTSPFISLHWAMNMAcVQFGLTPEEAWAGVTRHAARALGRHATHGQLKAGFVADF 377
Cdd:COG1228 278 EAALANARRLHDAGVPVALGTDAGVGVPPGRSLHRELALA-VEAGLTPEEALRAATINAAKALGLDDDVGSLEPGKLADL 356
|
410 420
....*....|....*....|....*....
gi 1915297345 378 VVWDATLPVEILYepgRNPLYQRVFKGQI 406
Cdd:COG1228 357 VLLDGDPLEDIAY---LEDVRAVMKDGRV 382
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
8-383 |
1.30e-22 |
|
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: 98.75 E-value: 1.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 8 DVIWRNVRLATMDPERGtpygLLDGHALIVRQGKIRDIVPESSLYLTH--DNTFDMQGRLITPGLIDCHTHLVFGGNRA- 84
Cdd:COG0402 1 DLLIRGAWVLTMDPAGG----VLEDGAVLVEDGRIAAVGPGAELPARYpaAEVIDAGGKLVLPGLVNTHTHLPQTLLRGl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 85 ---GEWEQRLNGVSYQqisaqggginatvsATRSATDEQLLHVAHQRMEQLIKEGVT-LLEIksGYGLDLPTEEkilrVV 160
Cdd:COG0402 77 addLPLLDWLEEYIWP--------------LEARLDPEDVYAGALLALAEMLRSGTTtVADF--YYVHPESADA----LA 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 161 AALAAENI-VEISPTLLAAHAtPAEYRDDPDGYITLVCETIlpQLWEQGLFETVDL-----FCESVgfSLAQSERVFQAA 234
Cdd:COG0402 137 EAAAEAGIrAVLGRGLMDRGF-PDGLREDADEGLADSERLI--ERWHGAADGRIRValaphAPYTV--SPELLRAAAALA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 235 QALGIPIKGHV-EQLSLLggAQLVSRYhGLSAdhIEYLDEAGV------------------AAMSQSGTVGVLLPGAFYF 295
Cdd:COG0402 212 RELGLPLHTHLaETRDEV--EWVLELY-GKRP--VEYLDELGLlgprtllahcvhltdeeiALLAETGASVAHCPTSNLK 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 296 LkEEQRPPIALLRQYQVPMAVATD---FNPGTSPFISLHWAMNMACVQFG----LTPEEAWAGVTRHAARALGRHATHGQ 368
Cdd:COG0402 287 L-GSGIAPVPRLLAAGVRVGLGTDgaaSNNSLDMFEEMRLAALLQRLRGGdptaLSAREALEMATLGGARALGLDDEIGS 365
|
410
....*....|....*
gi 1915297345 369 LKAGFVADFVVWDAT 383
Cdd:COG0402 366 LEPGKRADLVVLDLD 380
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
70-359 |
1.73e-17 |
|
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: 82.00 E-value: 1.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 70 LIDCHTHLVFGGNRAGEWEQRLNGVSYqqisaqggginatvsatrsATDEQLLHVAHQRMEQLIKEGVTLLEIKSGYGLD 149
Cdd:cd01292 1 FIDTHVHLDGSALRGTRLNLELKEAEE-------------------LSPEDLYEDTLRALEALLAGGVTTVVDMGSTPPP 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 150 LPTEEKILRVVAALAAENIVEISPTLLAAHATPAEYRDDPDGYITLVceTILPQLWEQGLFETVDlfCESVGFSLAQSER 229
Cdd:cd01292 62 TTTKAAIEAVAEAARASAGIRVVLGLGIPGVPAAVDEDAEALLLELL--RRGLELGAVGLKLAGP--YTATGLSDESLRR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 230 VFQAAQALGIPIKGHVEQLSLLGGA--QLVSRY---HGLSADHIEYLDEAGVAAMSQSGTVGVLLPGAFYFL--KEEQRP 302
Cdd:cd01292 138 VLEEARKLGLPVVIHAGELPDPTRAleDLVALLrlgGRVVIGHVSHLDPELLELLKEAGVSLEVCPLSNYLLgrDGEGAE 217
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 303 PIALLRQYQVPMAVATDFNPGTS---PFISLHWAMNMAcvQFGLTPEEAWAGVTRHAARA 359
Cdd:cd01292 218 ALRRLLELGIRVTLGTDGPPHPLgtdLLALLRLLLKVL--RLGLSLEEALRLATINPARA 275
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
12-392 |
2.16e-16 |
|
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: 80.37 E-value: 2.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 12 RNVRLATmdpERGTPYGLLdghaliVRQGKIRDIVPESSLYlTHDNTFDMQGRLITPGLIDCHTHL----VFGGNRAGew 87
Cdd:cd01293 3 RNARLAD---GGTALVDIA------IEDGRIAAIGPALAVP-PDAEEVDAKGRLVLPAFVDPHIHLdktfTGGRWPNN-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 88 eqrlngvsyqQISAQGGGINATVSATRSATDEQLLhvahQRMEQLIKE----GVT-------------------LLEIKS 144
Cdd:cd01293 71 ----------SGGTLLEAIIAWEERKLLLTAEDVK----ERAERALELaiahGTTairthvdvdpaaglkaleaLLELRE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 145 GYG--LDL-----PTE--------EKILRVVAALAAENIVEIsptllaahaTPAEYRDDPDGYITLVCEtiLPQlwEQGL 209
Cdd:cd01293 137 EWAdlIDLqivafPQHgllstpggEELMREALKMGADVVGGI---------PPAEIDEDGEESLDTLFE--LAQ--EHGL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 210 feTVDLFC-ESVGFSLAQSERVFQAAQALGIPIK---GHVEQLSLLGGAQLvsryhglsADHIEYLDEAGVAAMSqSGTV 285
Cdd:cd01293 204 --DIDLHLdETDDPGSRTLEELAEEAERRGMQGRvtcSHATALGSLPEAEV--------SRLADLLAEAGISVVS-LPPI 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 286 GVLLPGAFY-FLKEEQRPPIALLRQYQVPMAVATD-----FNP-GT-SPFISLHWAMNMAcvqfGLTPEE----AWAGVT 353
Cdd:cd01293 273 NLYLQGREDtTPKRRGVTPVKELRAAGVNVALGSDnvrdpWYPfGSgDMLEVANLAAHIA----QLGTPEdlalALDLIT 348
|
410 420 430
....*....|....*....|....*....|....*....
gi 1915297345 354 RHAARALGrhATHGQLKAGFVADFVVWDATLPVEILYEP 392
Cdd:cd01293 349 GNAARALG--LEDYGIKVGCPADLVLLDAEDVAEAVARQ 385
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
25-387 |
2.34e-12 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 67.82 E-value: 2.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 25 TPYGLLDGHALIVRQGKIRDIVPESSLyltHDNTFDMQGRLITPGLIDCHTHlvfGgnrageweqrlngvsyqqisaqGG 104
Cdd:COG1820 9 TGDGVLEDGALLIEDGRIAAIGPGAEP---DAEVIDLGGGYLAPGFIDLHVH---G----------------------GG 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 105 GINATvsatrSATDEQLLHVAhqrmEQLIKEGVTLLeiksgygldLPT-----EEKILRVVAALA---AENIV------- 169
Cdd:COG1820 61 GVDFM-----DGTPEALRTIA----RAHARHGTTSF---------LPTtitapPEDLLRALAAIAeaiEQGGGagilgih 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 170 -E---ISPTLLAAH-------ATPAEYR---DDPDGYITLVceTILPQLweQGLFETVDLFCE-----SVGFSLAQSERV 230
Cdd:COG1820 123 lEgpfLSPEKKGAHppeyirpPDPEELDrllEAAGGLIKLV--TLAPEL--PGALEFIRYLVEagvvvSLGHTDATYEQA 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 231 fQAAQALGIPIKGHveqlslLGGA--QLVSRYHGLsadhieyldeAGVAAMSQSGTVGV------LLPGAF---YFLKEE 299
Cdd:COG1820 199 -RAAFEAGATHVTH------LFNAmsPLHHREPGV----------VGAALDDDDVYAELiadgihVHPAAVrlaLRAKGP 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 300 QRppIALlrqyqV--PMAvATDFNPGTSPFISLHW-----------------AMNMA-CVQF-----GLTPEEAWAGVTR 354
Cdd:COG1820 262 DR--LIL-----VtdAMA-AAGLPDGEYELGGLEVtvkdgvarladgtlagsTLTMDdAVRNlvewtGLPLEEAVRMASL 333
|
410 420 430
....*....|....*....|....*....|...
gi 1915297345 355 HAARALGRHATHGQLKAGFVADFVVWDATLPVE 387
Cdd:COG1820 334 NPARALGLDDRKGSIAPGKDADLVVLDDDLNVR 366
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
65-406 |
2.20e-10 |
|
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: 61.36 E-value: 2.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 65 LITPGLIDCHTHLVFGGNRAgeweqrlngvsyqqisaqggginatvsatRSATDEQLLHVAHQRMEQLIKEGVTLLeiks 144
Cdd:pfam01979 1 IVLPGLIDAHVHLEMGLLRG-----------------------------IPVPPEFAYEALRLGITTMLKSGTTTV---- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 145 gygLDLPTEEKILRVVAALAAENIVeISPTLLAAHATPAEyRDDPDGYITlVCETILPQLWEQGLFETVDLFC-----ES 219
Cdd:pfam01979 48 ---LDMGATTSTGIEALLEAAEELP-LGLRFLGPGCSLDT-DGELEGRKA-LREKLKAGAEFIKGMADGVVFVglaphGA 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 220 VGFSLAQSERVFQAAQALGIPIKGHVeqLSLLGGAQLVSRYHGLSADHIEYLDEAG-------VAAMSQSGT-------- 284
Cdd:pfam01979 122 PTFSDDELKAALEEAKKYGLPVAIHA--LETKGEVEDAIAAFGGGIEHGTHLEVAEsgglldiIKLILAHGVhlsptean 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 285 --------VGVLLPGAFYFLKEEQRPPIALLRQYQVPMAVATDFNPGTSPFISLHWAMNMACVQF----GLTPEEAWAGV 352
Cdd:pfam01979 200 llaehlkgAGVAHCPFSNSKLRSGRIALRKALEDGVKVGLGTDGAGSGNSLNMLEELRLALELQFdpegGLSPLEALRMA 279
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1915297345 353 TRHAARALGRHATHGQLKAGFVADFVVWDATLPVEILYEPGRNPLYQRVFKGQI 406
Cdd:pfam01979 280 TINPAKALGLDDKVGSIEVGKDADLVVVDLDPLAAFFGLKPDGNVKKVIVKGKI 333
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
8-382 |
4.07e-10 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 61.35 E-value: 4.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 8 DVIWRNVRLATMDPERGTPyglldgHALIVRQGKIRDIVPES---SLYLTHDNTFDMQGRLITPGLIDCHTHLVFGGNRA 84
Cdd:COG1574 9 DLLLTNGRIYTMDPAQPVA------EAVAVRDGRIVAVGSDAevrALAGPATEVIDLGGKTVLPGFIDAHVHLLGGGLAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 85 GEWeqRLNGV-SYQQISA---------------QGGGINAT---------------VSATR------------------- 114
Cdd:COG1574 83 LGV--DLSGArSLDELLArlraaaaelppgewiLGRGWDESlwpegrfptradldaVSPDRpvvltrvdghaawvnsaal 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 115 ------------------------------------------SATDEQLLHVAHQRMEQLIKEGVTLLeiksgygLDLPT 152
Cdd:COG1574 161 elagitadtpdpeggeierdadgeptgvlreaamdlvraaipPPTPEELRAALRAALRELASLGITSV-------HDAGL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 153 EEKILRVVAALAAEN--IVEISptlLAAHATPAEYRDdpdgyitlVCETILPQLWEQGLFE--TVDLFC----------- 217
Cdd:COG1574 234 GPDDLAAYRELAAAGelPLRVV---LYLGADDEDLEE--------LLALGLRTGYGDDRLRvgGVKLFAdgslgsrtaal 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 218 --------ESVG---FSLAQSERVFQAAQALGIPIKGH------VEQlsLLGGAQLVSRYHGLSA-----DHIEYLDEAG 275
Cdd:COG1574 303 lepyaddpGNRGlllLDPEELRELVRAADAAGLQVAVHaigdaaVDE--VLDAYEAARAANGRRDrrhriEHAQLVDPDD 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 276 VAAMSQSGTVGVLLP------GAFY--FLKEEQRP---PIALLRQYQVPMAVATDFnPGTS--PFISLHWAMN---MACV 339
Cdd:COG1574 381 LARFAELGVIASMQPthatsdGDWAedRLGPERAArayPFRSLLDAGAPLAFGSDA-PVEPldPLLGIYAAVTrrtPSGR 459
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1915297345 340 QFG----LTPEEAWAGVTRHAARALGRHATHGQLKAGFVADFVVWDA 382
Cdd:COG1574 460 GLGpeerLTVEEALRAYTIGAAYAAFEEDEKGSLEPGKLADFVVLDR 506
|
|
| Met_dep_hydrolase_A |
cd01299 |
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ... |
56-382 |
4.28e-10 |
|
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: 60.77 E-value: 4.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 56 DNTFDMQGRLITPGLIDCHTHLVFGGNRAGEWEQrlngvsyqqisaqggginatvsatrsATDEQLLHVAHQRMEQLIKE 135
Cdd:cd01299 1 AQVIDLGGKTLMPGLIDAHTHLGSDPGDLPLDLA--------------------------LPVEYRTIRATRQARAALRA 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 136 GVTL-LEIKSGYGLDL--PTEEKIL---RVVAALAAeniveISPTllAAHATPAEYRDD-PDGYITLVCETI------LP 202
Cdd:cd01299 55 GFTTvRDAGGADYGLLrdAIDAGLIpgpRVFASGRA-----LSQT--GGHGDPRGLSGLfPAGGLAAVVDGVeevraaVR 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 203 QLWEQGlfetVDLF--------------CESVGFSLAQSERVFQAAQALGIPIKGHVE-----QLSLLGGAQLVsrYHGL 263
Cdd:cd01299 128 EQLRRG----ADQIkimatggvlspgdpPPDTQFSEEELRAIVDEAHKAGLYVAAHAYgaeaiRRAIRAGVDTI--EHGF 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 264 sadhieYLDEAGVAAMSQSGTVGVLLPGAFYFLKEEQRPP--------------------IALLRQYQVPMAVATDFNPG 323
Cdd:cd01299 202 ------LIDDETIELMKEKGIFLVPTLATYEALAAEGAAPglpadsaekvalvleagrdaLRRAHKAGVKIAFGTDAGFP 275
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1915297345 324 TSPFISLHWAMNMAcVQFGLTPEEAWAGVTRHAARALGRHATHGQLKAGFVADFVVWDA 382
Cdd:cd01299 276 VPPHGWNARELELL-VKAGGTPAEALRAATANAAELLGLSDELGVIEAGKLADLLVVDG 333
|
|
| Met_dep_hydrolase_D |
cd01312 |
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ... |
40-381 |
1.39e-09 |
|
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: 238637 [Multi-domain] Cd Length: 381 Bit Score: 59.39 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 40 GKIRDIVPESSLYLTHDNT---FDMQGrLITPGLIDCHTHLVFGGNRA-------GEWEQRLngvsyqqisaqgggINAT 109
Cdd:cd01312 1 DKILEVGDYEKLEKRYPGAkheFFPNG-VLLPGLINAHTHLEFSANVAqftygrfRAWLLSV--------------INSR 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 110 VSATRSATDEQLLhvahQRMEQLIKEGVTLLEIKSGYGLDLPT-EEKILRVVAALAA--ENIVEI--------------- 171
Cdd:cd01312 66 DELLKQPWEEAIR----QGIRQMLESGTTSIGAISSDGSLLPAlASSGLRGVFFNEVigSNPSAIdfkgetflerfkrsk 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 172 ---SPTLLAAHATPAEYRDDPDGYITLvcetilPQLWEQ-------GLFET---VDLFCESVGFSLAQSERVFQAA--QA 236
Cdd:cd01312 142 sfeSQLFIPAISPHAPYSVHPELAQDL------IDLAKKlnlplstHFLESkeeREWLEESKGWFKHFWESFLKLPkpKK 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 237 LGIPIKgHVEQLSLLGGAqlvsryhgLSADHIEYLDEAGVAAMSQSGTVGVLLPGAFYFLKEeQRPPIALLRQYQVPMAV 316
Cdd:cd01312 216 LATAID-FLDMLGGLGTR--------VSFVHCVYANLEEAEILASRGASIALCPRSNRLLNG-GKLDVSELKKAGIPVSL 285
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1915297345 317 ATDfnpGTSPFISLHWAMNM-----ACVQFGL--TPEEAWAGVTRHAARALGRHAthGQLKAGFVADFVVWD 381
Cdd:cd01312 286 GTD---GLSSNISLSLLDELralldLHPEEDLleLASELLLMATLGGARALGLNN--GEIEAGKRADFAVFE 352
|
|
| PRK12394 |
PRK12394 |
metallo-dependent hydrolase; |
8-376 |
3.99e-09 |
|
metallo-dependent hydrolase;
Pssm-ID: 183497 [Multi-domain] Cd Length: 379 Bit Score: 57.85 E-value: 3.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 8 DVIWRNVRLAtmDPERGTpyglLDGHALIVRQGKIRDIVPESSLYLThdNTFDMQGRLITPGLIDCHTHLVFGGNRagew 87
Cdd:PRK12394 4 DILITNGHII--DPARNI----NEINNLRIINDIIVDADKYPVASET--RIIHADGCIVTPGLIDYHAHVFYDGTE---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 88 eqrlNGVSyQQISAQGGGINATVSATRSATDEQLLH---VAHQRMEQlIKEGVTLLEI-KSGYGLDLPT------EEKIl 157
Cdd:PRK12394 72 ----GGVR-PDMYMPPNGVTTVVDAGSAGTANFDAFyrtVICASKVR-IKAFLTVSPPgQTWSGYQENYdpdnidENKI- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 158 rvvaalaaeniveisptllaaHATPAEYRDDPDGYITLVCETILPQLWEQGLFETVDLfcesvgfslaqservfqaAQAL 237
Cdd:PRK12394 145 ---------------------HALFRQYRNVLQGLKLRVQTEDIAEYGLKPLTETLRI------------------ANDL 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 238 GIPIKGHVEQlSLLGGAQLVSR----------YHGLSAdhiEYLDEAG--VAAMSQSGTVGVLLP---GAFYFLKEEQRP 302
Cdd:PRK12394 186 RCPVAVHSTH-PVLPMKELVSLlrrgdiiahaFHGKGS---TILTEEGavLAEVRQARERGVIFDaanGRSHFDMNVARR 261
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1915297345 303 PIAllrQYQVPMAVATDFNPGT---SPFISLHWAMNMAcVQFGLTPEEAWAGVTRHAARALGRHATHGQLKAGFVAD 376
Cdd:PRK12394 262 AIA---NGFLPDIISSDLSTITklaWPVYSLPWVLSKY-LALGMALEDVINACTHTPAVLMGMAAEIGTLAPGAFAD 334
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
12-385 |
6.10e-09 |
|
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: 57.60 E-value: 6.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 12 RNVRLATMDPERGTPYGlldghALIVRQGKIRDIVPESSLYLTHDNTF-DMQGRLITPGLIDCHTHLVFGGNRAG----- 85
Cdd:cd01298 4 RNGTIVTTDPRRVLEDG-----DVLVEDGRIVAVGPALPLPAYPADEViDAKGKVVMPGLVNTHTHLAMTLLRGLaddlp 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 86 --EW--------EQRLNGVSyQQISAQGGGINATVSATRSATDEQLLHvahqrMEQLIKEgVTLLEIKS--GYGL-DLPT 152
Cdd:cd01298 79 lmEWlkdliwplERLLTEED-VYLGALLALAEMIRSGTTTFADMYFFY-----PDAVAEA-AEELGIRAvlGRGImDLGT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 153 EEKILRVVAALAAENIVEisptllaahatpaEYRDDPDGYITLVcetILPqlweqglfetvdlfCESVGFSLAQSERVFQ 232
Cdd:cd01298 152 EDVEETEEALAEAERLIR-------------EWHGAADGRIRVA---LAP--------------HAPYTCSDELLREVAE 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 233 AAQALGIPIKGHV----------------------EQLSLLGG-AQLVsryHG--LSADHIEYLDEAGVAAMSQSGTVGV 287
Cdd:cd01298 202 LAREYGVPLHIHLaetedeveeslekygkrpveylEELGLLGPdVVLA---HCvwLTDEEIELLAETGTGVAHNPASNMK 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 288 LLPGAfyflkeeqrPPIALLRQYQVPMAVATD---FNPGTSPFISLHWAMNMACVQFG----LTPEEAWAGVTRHAARAL 360
Cdd:cd01298 279 LASGI---------APVPEMLEAGVNVGLGTDgaaSNNNLDMFEEMRLAALLQKLAHGdptaLPAEEALEMATIGGAKAL 349
|
410 420
....*....|....*....|....*
gi 1915297345 361 GRHAThGQLKAGFVADFVVWDATLP 385
Cdd:cd01298 350 GLDEI-GSLEVGKKADLILIDLDGP 373
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
34-379 |
3.42e-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: 55.39 E-value: 3.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 34 ALIVRQGKIRDIVPE---SSLYLTHDNTFDMQGRLITPGLIDCHTHLVFGG---------------------------NR 83
Cdd:cd01300 1 AVAVRDGRIVAVGSDaeaKALKGPATEVIDLKGKTVLPGFIDSHSHLLLGGlsllwldlsgvtskeealariredaaaAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 84 AGEWEQ----------------------------------------------RLNGVSYQQISAQGGGI------NAT-- 109
Cdd:cd01300 81 PGEWILgfgwdesllgegryptraeldavspdrpvlllrrdghsawvnsaalRLAGITRDTPDPPGGEIvrdadgEPTgv 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 110 ---------VSATRSATDEQLLHVAHQRMEQLIKEGVT-LLEIKSGYGLDLPT-------EEKILRVVAALaaeniVEIS 172
Cdd:cd01300 161 lveaaaalvLEAVPPPTPEERRAALRAAARELASLGVTtVHDAGGGAADDIEAyrrlaaaGELTLRVRVAL-----YVSP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 173 PTLLAAHATPAEYRDDPDGYITLVCetilpqlweqglfetVDLF----------------------CESVGFSLAQSERV 230
Cdd:cd01300 236 LAEDLLEELGARKNGAGDDRLRLGG---------------VKLFadgslgsrtaalsepyldspgtGGLLLISPEELEEL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 231 FQAAQALGIPIKGH-------------VEQLsllgGAQLVSRYHGLSADHIEYLDEAGVAAMSQSGTVGVLLPG------ 291
Cdd:cd01300 301 VRAADEAGLQVAIHaigdravdtvldaLEAA----LKDNPRADHRHRIEHAQLVSPDDIPRFAKLGVIASVQPNhlysdg 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 292 ---AFYFLKEEQR---PPIALLRQYQVPMAVATDFNPGT-SPFISLHWAMN--------MACVQFGLTPEEAWAGVTRHA 356
Cdd:cd01300 377 daaEDRRLGEERAkrsYPFRSLLDAGVPVALGSDAPVAPpDPLLGIWAAVTrktpgggvLGNPEERLSLEEALRAYTIGA 456
|
490 500
....*....|....*....|...
gi 1915297345 357 ARALGRHATHGQLKAGFVADFVV 379
Cdd:cd01300 457 AYAIGEEDEKGSLEPGKLADFVV 479
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
58-382 |
1.60e-07 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 53.30 E-value: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 58 TFDMQGRLITPGLIDCHTHLVFGGNRAGEweQRLNGVSYQQISA------------QGGGINATVSA------TRSATDE 119
Cdd:pfam07969 2 VIDAKGRLVLPGFVDPHTHLDGGGLNLRE--LRLPDVLPNAVVKgqagrtpkgrwlVGEGWDEAQFAetrfpyALADLDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 120 QL----LHVAHQ------------------------RMEQLIKEGVT-----LLEIKSGYGLDLPTEEK----ILRVVAA 162
Cdd:pfam07969 80 VApdgpVLLRALhthaavansaaldlagitkatedpPGGEIARDANGegltgLLREGAYALPPLLAREAeaaaVAAALAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 163 LAAENIVEISptllaAHATPAEYRDDPDGYITLVCETILPQL------WEQGL------FETVDLF-------------- 216
Cdd:pfam07969 160 LPGFGITSVD-----GGGGNVHSLDDYEPLRELTAAEKLKELldaperLGLPHsiyelrIGAMKLFadgvlgsrtaalte 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 217 -------CESVGFSLAQSERVFQAAQALGIPIKGHVEQ----LSLLGGAQLVSRYHGL----SADHIEYLD--------- 272
Cdd:pfam07969 235 pyfdapgTGWPDFEDEALAELVAAARERGLDVAIHAIGdatiDTALDAFEAVAEKLGNqgrvRIEHAQGVVpytysqier 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 273 --EAGVAAMSQSGTVGVLLPGAFYFLKEEQR---PPIALLRQYQVPMAVATDFNPGT-SPFISLHWA------MNMACVQ 340
Cdd:pfam07969 315 vaALGGAAGVQPVFDPLWGDWLQDRLGAERArglTPVKELLNAGVKVALGSDAPVGPfDPWPRIGAAvmrqtaGGGEVLG 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1915297345 341 FG--LTPEEAWAGVTRHAARALGRHATHGQLKAGFVADFVVWDA 382
Cdd:pfam07969 395 PDeeLSLEEALALYTSGPAKALGLEDRKGTLGVGKDADLVVLDD 438
|
|
| PRK09228 |
PRK09228 |
guanine deaminase; Provisional |
267-382 |
2.01e-07 |
|
guanine deaminase; Provisional
Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 52.89 E-value: 2.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 267 HIEYLDEAGVAAMSQSGTVGVLLP--------GAFyflkeeqrpPIALLRQYQVPMAVATDFNPGTSpFISLHwAMNMAC 338
Cdd:PRK09228 270 HCIHLEDRERRRLAETGAAIAFCPtsnlflgsGLF---------DLKRADAAGVRVGLGTDVGGGTS-FSMLQ-TMNEAY 338
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1915297345 339 -VQ----FGLTPEEAWAGVTRHAARALGRHATHGQLKAGFVADFVVWDA 382
Cdd:PRK09228 339 kVQqlqgYRLSPFQAFYLATLGGARALGLDDRIGNLAPGKEADFVVLDP 387
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
40-381 |
2.76e-07 |
|
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: 51.93 E-value: 2.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 40 GKIRDIVPESSlylTHDNT--FDMQGRLITPGLIDCHTHL-------VFGGNRAGEW----------------------E 88
Cdd:cd01309 2 GKIVAVGAEIT---TPADAevIDAKGKHVTPGLIDAHSHLgldeeggVRETSDANEEtdpvtphvraidginpddeafkR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 89 QRLNGVSYQQI---SAQ-GGGINATVsATRSATDEQLLHVAHQRMEQLIKEGVtlleiKSGYGLdlPTEEKILRV-VAAL 163
Cdd:cd01309 79 ARAGGVTTVQVlpgSANlIGGQGVVI-KTDGGTIEDMFIKAPAGLKMALGENP-----KRVYGG--KGKEPATRMgVAAL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 164 AAENIVEISPTLLAAHATPAEYRDDPDgyITLVCETILPQLweQGlfeTVDLFCESvgfslaqsERVFQAAQALGIP--- 240
Cdd:cd01309 151 LRDAFIKAQEYGRKYDLGKNAKKDPPE--RDLKLEALLPVL--KG---EIPVRIHA--------HRADDILTAIRIAkef 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 241 -IKGHVEqlsllggaqlvsryHGLSADHI-EYLDEAGVaamsqSGTVGVLL--PGAFYFLKEEQRPPIALLRQYQVPMAV 316
Cdd:cd01309 216 gIKITIE--------------HGAEGYKLaDELAKHGI-----PVIYGPTLtlPKKVEEVNDAIDTNAYLLKKGGVAFAI 276
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1915297345 317 ATDFNPGTSPFISLHWAMnmaCVQFGLTPEEAWAGVTRHAARALGRHATHGQLKAGFVADFVVWD 381
Cdd:cd01309 277 SSDHPVLNIRNLNLEAAK---AVKYGLSYEEALKAITINPAKILGIEDRVGSLEPGKDADLVVWN 338
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
25-236 |
3.74e-07 |
|
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: 51.81 E-value: 3.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 25 TPYGLLDGHALIVRQGKIRDIVPESSLYlTHDNTFDMQGRLITPGLIDCHTHlvfGgnrageweqrlngvsyqqisaqGG 104
Cdd:cd00854 9 LTPGGLEDGAVLVEDGKIVAIGPEDELE-EADEIIDLKGQYLVPGFIDIHIH---G----------------------GG 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 105 GINATvsatrSATDEQLLHVAhqrmEQLIKEGVTLLeiksgygldLPT-----EEKILRVVAALAAENIVEISPTLLAAH 179
Cdd:cd00854 63 GADFM-----DGTAEALKTIA----EALAKHGTTSF---------LPTtvtapPEEIAKALAAIAEAIAEGQGAEILGIH 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 180 ------------ATPAEYRDDPD------------GYITLVceTILPQLweQGLFETVDLFCE-----SVGFSLAQSERV 230
Cdd:cd00854 125 legpfispekkgAHPPEYLRAPDpeelkkwleaagGLIKLV--TLAPEL--DGALELIRYLVErgiivSIGHSDATYEQA 200
|
....*.
gi 1915297345 231 FQAAQA 236
Cdd:cd00854 201 VAAFEA 206
|
|
| PRK09045 |
PRK09045 |
TRZ/ATZ family hydrolase; |
29-76 |
1.39e-06 |
|
TRZ/ATZ family hydrolase;
Pssm-ID: 236366 [Multi-domain] Cd Length: 443 Bit Score: 50.30 E-value: 1.39e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1915297345 29 LLDGHALIVRQGKIRDIVP--ESSLYLTHDNTFDMQGRLITPGLIDCHTH 76
Cdd:PRK09045 25 VLEDHAVAIRDGRIVAILPraEARARYAAAETVELPDHVLIPGLINAHTH 74
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
12-77 |
6.16e-06 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 47.88 E-value: 6.16e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1915297345 12 RNVRLatMDPergtpYGLLDGHALIVRQGKIRDIVPESSLylTHDNTFDMQGRLITPGLIDCHTHL 77
Cdd:PRK09357 6 KNGRV--IDP-----KGLDEVADVLIDDGKIAAIGENIEA--EGAEVIDATGLVVAPGLVDLHVHL 62
|
|
| Isoaspartyl-dipeptidase |
cd01308 |
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
35-152 |
1.67e-05 |
|
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: 46.61 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 35 LIVRQGKIRDIVPESSLYLTHDNT-FDMQGRLITPGLIDCHTHLVFGGNRAGeWEQRLNGVSYQQISaQGG-----GINA 108
Cdd:cd01308 20 ILIAGGKILAIEDQLNLPGYENVTvVDLHGKILVPGFIDQHVHIIGGGGEGG-PSTRTPEVTLSDLT-TAGvttvvGCLG 97
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1915297345 109 TVSATRSATDeqLLHVAHqrmeQLIKEGVTLLEIKSGYglDLPT 152
Cdd:cd01308 98 TDGISRSMED--LLAKAR----ALEEEGITCFVYTGSY--EVPT 133
|
|
| nagA |
PRK11170 |
N-acetylglucosamine-6-phosphate deacetylase; Provisional |
25-72 |
1.72e-05 |
|
N-acetylglucosamine-6-phosphate deacetylase; Provisional
Pssm-ID: 183010 Cd Length: 382 Bit Score: 46.51 E-value: 1.72e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1915297345 25 TPYGLLDGHALIVRQGKIRDIVPESSLyLTHDNTFDMQGRLITPGLID 72
Cdd:PRK11170 11 TGHEVLDDHAVVIADGLIEAVCPVAEL-PPGIEQRDLNGAILSPGFID 57
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
16-77 |
2.16e-05 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 46.38 E-value: 2.16e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1915297345 16 LATMDPERGTpygLLDGHaLIVRQGKIRDIVPESSLYLTHDNTFDMQGRLITPGLIDCHTHL 77
Cdd:PRK08203 11 IVTMDAARRE---IADGG-LVVEGGRIVEVGPGGALPQPADEVFDARGHVVTPGLVNTHHHF 68
|
|
| AdeC |
cd01295 |
Adenine deaminase (AdeC) directly deaminates adenine to form hypoxanthine. This reaction is ... |
232-381 |
2.91e-05 |
|
Adenine deaminase (AdeC) directly deaminates adenine to form hypoxanthine. This reaction is part of one of the adenine salvage pathways, as well as the degradation pathway. It is important for adenine utilization as a purine, as well as a nitrogen source in bacteria and archea.
Pssm-ID: 238620 [Multi-domain] Cd Length: 422 Bit Score: 46.06 E-value: 2.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 232 QAAQALGIPIKGHVEQLSllgGAQL-VSRYHGLSADH----IEYLDE---AGVAAMSQSGTVG----VLLPGafyfLKEE 299
Cdd:cd01295 128 QAAKKAGKPVDGHAPGLS---GEELnAYMAAGISTDHeamtGEEALEklrLGMYVMLREGSIAknleALLPA----ITEK 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 300 QRPPIALlrqyqvpmaVATDFNPGtspFI----SLHWAMNMAcVQFGLTPEEAWAGVTRHAARALGRHaTHGQLKAGFVA 375
Cdd:cd01295 201 NFRRFMF---------CTDDVHPD---DLlsegHLDYIVRRA-IEAGIPPEDAIQMATINPAECYGLH-DLGAIAPGRIA 266
|
....*.
gi 1915297345 376 DFVVWD 381
Cdd:cd01295 267 DIVILD 272
|
|
| COG3964 |
COG3964 |
Predicted amidohydrolase [General function prediction only]; |
8-81 |
6.25e-05 |
|
Predicted amidohydrolase [General function prediction only];
Pssm-ID: 443164 [Multi-domain] Cd Length: 376 Bit Score: 44.77 E-value: 6.25e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1915297345 8 DVIWRNVRLAtmDPERGTpygllDGHALI-VRQGKIRDiVPESSLYLTHDNTFDMQGRLITPGLIDCHTHLVFGG 81
Cdd:COG3964 1 DLLIKGGRVI--DPANGI-----DGVMDIaIKDGKIAA-VAKDIDAAEAKKVIDASGLYVTPGLIDLHTHVFPGG 67
|
|
| PRK07583 |
PRK07583 |
cytosine deaminase; |
1-77 |
9.73e-05 |
|
cytosine deaminase;
Pssm-ID: 236062 Cd Length: 438 Bit Score: 44.20 E-value: 9.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 1 MQQFF---PDDVIW-RNVR-----LATMDPERGTPYGLLDGHaLIVRQGKIRDIVPESSlylTHDNT--FDMQGRLITPG 69
Cdd:PRK07583 1 MSSFFslpESGRYWlKNARvpaalLEGGVPPGDTLEGLVLVD-IEIADGKIAAILPAGG---APDELpaVDLKGRMVWPC 76
|
....*...
gi 1915297345 70 LIDCHTHL 77
Cdd:PRK07583 77 FVDMHTHL 84
|
|
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
8-75 |
3.18e-04 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 42.47 E-value: 3.18e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1915297345 8 DVIWRNVRLATMDpergtpyGLLDGhALIVRQGKIRDIVPESSlylTHDNTFDMQGRLITPGLIDCHT 75
Cdd:PRK15446 3 EMILSNARLVLPD-------EVVDG-SLLIEDGRIAAIDPGAS---ALPGAIDAEGDYLLPGLVDLHT 59
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
12-77 |
4.03e-04 |
|
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: 42.39 E-value: 4.03e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1915297345 12 RNVRLatMDPERGTPYGLLdghaliVRQGKIRDIVPESSLyLTHDNTFDMQGRLITPGLIDCHTHL 77
Cdd:COG0044 3 KNGRV--VDPGGLERADVL------IEDGRIAAIGPDLAA-PEAAEVIDATGLLVLPGLIDLHVHL 59
|
|
| PRK07203 |
PRK07203 |
putative aminohydrolase SsnA; |
13-77 |
5.12e-04 |
|
putative aminohydrolase SsnA;
Pssm-ID: 235963 [Multi-domain] Cd Length: 442 Bit Score: 41.84 E-value: 5.12e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1915297345 13 NVRLATMDPERgtPYglLDGHALIVRQGKIRDIVPESSLYLTHDNT--FDMQGRLITPGLIDCHTHL 77
Cdd:PRK07203 6 NGTAITRDPAK--PV--IEDGAIAIEGNVIVEIGTTDELKAKYPDAefIDAKGKLIMPGLINSHNHI 68
|
|
| GDEase |
cd01303 |
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ... |
267-403 |
7.76e-04 |
|
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: 41.49 E-value: 7.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 267 HIEYLDEAGVAAMSQSGTVGVLLP--------GAFyflkeeqrpPIALLRQYQVPMAVATDFNPGTSP----------FI 328
Cdd:cd01303 267 HCVHLSEEEFNLLKERGASVAHCPtsnlflgsGLF---------DVRKLLDAGIKVGLGTDVGGGTSFsmldtlrqayKV 337
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1915297345 329 SLHWAMNMACVQFgLTPEEAWAGVTRHAARALGRHATHGQLKAGFVADFVVWDATL-PVEILYEPGRNPLYQRVFK 403
Cdd:cd01303 338 SRLLGYELGGHAK-LSPAEAFYLATLGGAEALGLDDKIGNFEVGKEFDAVVIDPSAtPLLADRMFRVESLEEALFK 412
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
8-88 |
9.36e-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: 41.12 E-value: 9.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 8 DVIWRNVRLATmdpergtPYGLLDGhALIVRQGKIRDIVPESSLYLTHDnTFDMQGRLITPGLIDCHTHLvfggNRAG-- 85
Cdd:cd01315 1 DLVIKNGRVVT-------PDGVREA-DIAVKGGKIAAIGPDIANTEAEE-VIDAGGLVVMPGLIDTHVHI----NEPGrt 67
|
...
gi 1915297345 86 EWE 88
Cdd:cd01315 68 EWE 70
|
|
| PRK05985 |
PRK05985 |
cytosine deaminase; Provisional |
7-77 |
2.90e-03 |
|
cytosine deaminase; Provisional
Pssm-ID: 180337 [Multi-domain] Cd Length: 391 Bit Score: 39.53 E-value: 2.90e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1915297345 7 DDVIWRNVRLATMDPergtpyglldgHALIVRQGKIRDIVPESSLYLTHDnTFDMQGRLITPGLIDCHTHL 77
Cdd:PRK05985 2 TDLLFRNVRPAGGAA-----------VDILIRDGRIAAIGPALAAPPGAE-VEDGGGALALPGLVDGHIHL 60
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
8-78 |
3.11e-03 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 39.60 E-value: 3.11e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1915297345 8 DVIWRNVRLATMDPERGTPYGlldghALIVRQGKIRDIVPESSLyLTHDNTFDMQGRLITPGLIDCHTHLV 78
Cdd:PRK07228 2 TILIKNAGIVTMNAKREIVDG-----DVLIEDDRIAAVGDRLDL-EDYDDHIDATGKVVIPGLIQGHIHLC 66
|
|
| PRK06846 |
PRK06846 |
putative deaminase; Validated |
12-406 |
3.60e-03 |
|
putative deaminase; Validated
Pssm-ID: 235873 [Multi-domain] Cd Length: 410 Bit Score: 39.22 E-value: 3.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 12 RNVRLAT---MDPER--GTPYGLldgHALIVRQGKIRDIVPESSLYLTHDNTFDMQGRLITPGLIDCHTHL--VFGGnra 84
Cdd:PRK06846 9 TNVRLETgfdYENGVivQTETAL---CTLEIQDGKIVAIRPNKQVPDATLPTYDANGLLMLPAFREMHIHLdkTYYG--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 85 GEWE--QRLNGVsyqqisaqggginatvsATRSATDEQ----LLHVAHQRMEQLIKegvtlLEIKSGygldlpteekilr 158
Cdd:PRK06846 83 GPWKacRPAKTI-----------------QDRIELEQKelpeLLPTTQERAEKLIE-----LLQSKG------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 159 vvaALAAENIVEISPT-----LLAAHATPAEYRDDpdgyitLVCETI-LPQlweQGLFETvdlfcesvgfslaQSERVFQ 232
Cdd:PRK06846 128 ---ATHIRSHCNIDPViglknLENLQAALERYKDG------FTYEIVaFPQ---HGLLRS-------------NSEPLMR 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 233 AAQALGI-------P--IKGHVEQlSLLGGAQLVSRYHGLSADHIEYLDEAGVAAMS-------QSGTVG-VLLPGAFYF 295
Cdd:PRK06846 183 EAMKMGAhlvggvdPasVDGAIEK-SLDTMFQIAVDFNKGVDIHLHDTGPLGVATIKylvetteEAQWKGkVTISHAFAL 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 296 --LKEEQR------------------------PPIALLRQYQVPMAVATD-FNPGTSPFIS---LHWAmNMACVQFGLTP 345
Cdd:PRK06846 262 gdLNEEEVeelaerlaaqgisitstvpigrlhMPIPLLHDKGVKVSLGTDsVIDHWSPFGTgdmLEKA-NLLAELYRWSD 340
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1915297345 346 EeawagvtRHAARALgRHATHGQL-----------KAGFVADFVVWDATLPVEILYEpgRNPLYQRVFKGQI 406
Cdd:PRK06846 341 E-------RSLSRSL-ALATGGVLplndegervwpKVGDEASFVLVDASCSAEAVAR--QSPRTAVFHKGQL 402
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
12-386 |
4.12e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 39.22 E-value: 4.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 12 RNVRLATMDPERGTpyglLDGHALIVRQGKIRDIVPesSLYLTHDNTFDMQGRLITPGLIDCHTHLvfggnrageWEQRL 91
Cdd:PRK08204 7 RGGTVLTMDPAIGD----LPRGDILIEGDRIAAVAP--SIEAPDAEVVDARGMIVMPGLVDTHRHT---------WQSVL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 92 NGVsYQQISAQGG--GINATVSATRSATDE---QLLHVAHQrmeqlIKEGVTLLeiksgygLD----LPTEEKILRVVAA 162
Cdd:PRK08204 72 RGI-GADWTLQTYfrEIHGNLGPMFRPEDVyiaNLLGALEA-----LDAGVTTL-------LDwshiNNSPEHADAAIRG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 163 LAAENIVEIsptllAAHATP----------------------AEYRDDPDGYITLVCETILPQL--WEQGLFEtvdlfce 218
Cdd:PRK08204 139 LAEAGIRAV-----FAHGSPgpspywpfdsvphpredirrvkKRYFSSDDGLLTLGLAIRGPEFssWEVARAD------- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 219 svgfslaqservFQAAQALGIPIKGHVEQLSLLGGAQLVSRYHG---LSAD----HIEYLDEAGVAAMSQSGT------V 285
Cdd:PRK08204 207 ------------FRLARELGLPISMHQGFGPWGATPRGVEQLHDaglLGPDlnlvHGNDLSDDELKLLADSGGsfsvtpE 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 286 GVLLPGAFYflkeeqrPPIALLRQYQVPMAVATDFNPGTS--PFISLHWAM---------------NMACVQFGLTPEEA 348
Cdd:PRK08204 275 IEMMMGHGY-------PVTGRLLAHGVRPSLGVDVVTSTGgdMFTQMRFALqaerardnavhlregGMPPPRLTLTARQV 347
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1915297345 349 WAGVTRHAARALGRHATHGQLKAGFVADFVVWDAT----LPV 386
Cdd:PRK08204 348 LEWATIEGARALGLEDRIGSLTPGKQADLVLIDATdlnlAPV 389
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
9-81 |
4.99e-03 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 38.68 E-value: 4.99e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1915297345 9 VIWRNVRLatMDPERGTPyGLLDghaLIVRQGKI----RDIVPESSlylthDNTFDMQGRLITPGLIDCHTHLVFGG 81
Cdd:PRK09237 1 LLLRGGRV--IDPANGID-GVID---IAIEDGKIaavaGDIDGSQA-----KKVIDLSGLYVSPGWIDLHVHVYPGS 66
|
|
| PLN02795 |
PLN02795 |
allantoinase |
25-110 |
5.16e-03 |
|
allantoinase
Pssm-ID: 178392 [Multi-domain] Cd Length: 505 Bit Score: 38.99 E-value: 5.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297345 25 TPYGLLDGhALIVRQGKIRDIVPES--SLYLTHDNTFDMQGRLITPGLIDCHTHLvfggNRAG--EWEQRLNGVSyqqiS 100
Cdd:PLN02795 55 TPAGVIPG-AVEVEGGRIVSVTKEEeaPKSQKKPHVLDYGNAVVMPGLIDVHVHL----NEPGrtEWEGFPTGTK----A 125
|
90
....*....|
gi 1915297345 101 AQGGGINATV 110
Cdd:PLN02795 126 AAAGGITTLV 135
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
333-381 |
8.38e-03 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 38.29 E-value: 8.38e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1915297345 333 AMNMACVQFG---LTPEEA--WAgvTRHAARALGRHAThGQLKAGFVADFVVWD 381
Cdd:PRK08203 338 ALLLQRLRYGpdaMTAREAleWA--TLGGARVLGRDDI-GSLAPGKLADLALFD 388
|
|
| |
