|
Name |
Accession |
Description |
Interval |
E-value |
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
38-400 |
6.83e-162 |
|
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: 459.80 E-value: 6.83e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 38 VVIKDGKIVYAGQHTD----DYDATETIDASGKVVSPALVDAHTHLTFGGSREHEMSLKRQGKSYLEILEMGGGILSTVN 113
Cdd:cd01296 1 IAIRDGRIAAVGPAASlpapGPAAAEEIDAGGRAVTPGLVDCHTHLVFAGDRVDEFAARLAGASYEEILAAGGGILSTVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 114 ATRETSEDDLFKKAEHDLLTMIKHGVLAVESKSGYGLDRENELKQLKVSNRLAEKYDLDMKHTFLGPHAVPKEASSNEAF 193
Cdd:cd01296 81 ATRAASEDELFASALRRLARMLRHGTTTVEVKSGYGLDLETELKMLRVIRRLKEEGPVDLVSTFLGAHAVPPEYKGREEY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 194 LEEMIA-LLPEVK--QYADFADIFCETGVFTIEQSQHYMQKAKEAGFKVKIHADEIDPLGGLELAIDEQAISADHLVASS 270
Cdd:cd01296 161 IDLVIEeVLPAVAeeNLADFCDVFCEKGAFSLEQSRRILEAAKEAGLPVKIHADELSNIGGAELAAELGALSADHLEHTS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 271 DKGKEKLRNSDTVAVLLPATTFYLGkEDYADARGMLDNNGAIALATDYNPGSSVTNNLQLVMAIAALKLKLSPNEVWNAV 350
Cdd:cd01296 241 DEGIAALAEAGTVAVLLPGTAFSLR-ETYPPARKLIDAGVPVALGTDFNPGSSPTSSMPLVMHLACRLMRMTPEEALTAA 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 612671876 351 TVNAAKAIDI--NAGTINTGDKANLVIWDAPNHEYIPYHFGINHAEKVIKDG 400
Cdd:cd01296 320 TINAAAALGLgeTVGSLEVGKQADLVILDAPSYEHLAYRFGVNLVEYVIKNG 371
|
|
| hutI |
TIGR01224 |
imidazolonepropionase; This enzyme catalyzes the third step in histidine degradation. [Energy ... |
35-402 |
6.39e-148 |
|
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: 424.52 E-value: 6.39e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 35 NGTVVIKDGKIVYAGQHTD--DYDATETIDASGKVVSPALVDAHTHLTFGGSREHEMSLKRQGKSYLEILEMGGGILSTV 112
Cdd:TIGR01224 3 DAVILIHGGKIVWIGQLAAlpGEEATEIIDCGGGLVTPGLVDPHTHLVFAGDRVNEFEMKLQGASYLEILAQGGGILSTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 113 NATRETSEDDLFKKAEHDLLTMIKHGVLAVESKSGYGLDRENELKQLKVSNRLAEKYDLDMKHTFLGPHAVPKEASSNE- 191
Cdd:TIGR01224 83 RATRAASEEELLKLALFRLKSMLRSGTTTAEVKSGYGLDLETELKMLRAAKALHEEQPVDVVTTFLGAHAVPPEFQGRPd 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 192 AFLEEMIA-LLPEVK--QYADFADIFCETGVFTIEQSQHYMQKAKEAGFKVKIHADEIDPLGGLELAIDEQAISADHLVA 268
Cdd:TIGR01224 163 DYVDGICEeLIPQVAeeGLASFADVFCEAGVFSVEQSRRILQAAQEAGLPVKLHAEELSNLGGAELAAKLGAVSADHLEH 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 269 SSDKGKEKLRNSDTVAVLLPATTFYLGkEDYADARGMLDNNGAIALATDYNPGSSVTNNLQLVMAIAALKLKLSPNEVWN 348
Cdd:TIGR01224 243 ASDAGIKALAEAGTVAVLLPGTTFYLR-ETYPPARQLIDYGVPVALATDLNPGSSPTLSMQLIMSLACRLMKMTPEEALH 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 612671876 349 AVTVNAAKAIDI--NAGTINTGDKANLVIWDAPNHEYIPYHFGINHAEKVIKDGKV 402
Cdd:TIGR01224 322 AATVNAAYALGLgeERGTLEAGRDADLVILSAPSYAEIPYHYGVNHVHAVIKNGNI 377
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
32-406 |
3.74e-68 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 220.60 E-value: 3.74e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 32 VVKNGTVVIKDGKIVYAGQHTDDY--DATETIDASGKVVSPALVDAHTHLTFGGSREHEMslkrqgksyleilEMGGGIL 109
Cdd:COG1228 25 VIENGTVLVEDGKIAAVGPAADLAvpAGAEVIDATGKTVLPGLIDAHTHLGLGGGRAVEF-------------EAGGGIT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 110 STVnatretsedDLFKKAEHDLLTMIKHGVLAVESKSGYGL-----DRENELKQLKVSNRLAEKYDLDMkhtFLGPHAVp 184
Cdd:COG1228 92 PTV---------DLVNPADKRLRRALAAGVTTVRDLPGGPLglrdaIIAGESKLLPGPRVLAAGPALSL---TGGAHAR- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 185 keassneaFLEEMIALLPEVKQY-ADFADIFCETG--VFTIEQSQHYMQKAKEAGFKVKIHADEIDplgGLELAIDEQAI 261
Cdd:COG1228 159 --------GPEEARAALRELLAEgADYIKVFAEGGapDFSLEELRAILEAAHALGLPVAAHAHQAD---DIRLAVEAGVD 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 262 SADHLVASSDKGKEKLRNSDTVaVLLPATTFYLGKED-----------------YADARGMLDNNGAIALATDYNPGSSV 324
Cdd:COG1228 228 SIEHGTYLDDEVADLLAEAGTV-VLVPTLSLFLALLEgaaapvaakarkvreaaLANARRLHDAGVPVALGTDAGVGVPP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 325 TNNLQLVMAIAAlKLKLSPNEVWNAVTVNAAKAIDI--NAGTINTGDKANLVIWDAPNHEYIPYhfgINHAEKVIKDGKV 402
Cdd:COG1228 307 GRSLHRELALAV-EAGLTPEEALRAATINAAKALGLddDVGSLEPGKLADLVLLDGDPLEDIAY---LEDVRAVMKDGRV 382
|
....
gi 612671876 403 IVDN 406
Cdd:COG1228 383 VDRS 386
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
28-406 |
1.28e-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: 1.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 28 DELNVVKNGTVVIKDGKIVYAGQHTD---DYDATETIDASGKVVSPALVDAHTHLtfggsrehEMSLKR---QGKSYLEI 101
Cdd:COG0402 14 PAGGVLEDGAVLVEDGRIAAVGPGAElpaRYPAAEVIDAGGKLVLPGLVNTHTHL--------PQTLLRglaDDLPLLDW 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 102 LEmgggiLSTVNATRETSEDDLFKKAEHDLLTMIKHGVLAV--------ES---------KSG------YGL-------- 150
Cdd:COG0402 86 LE-----EYIWPLEARLDPEDVYAGALLALAEMLRSGTTTVadfyyvhpESadalaeaaaEAGiravlgRGLmdrgfpdg 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 151 DRENELKQLKVSNRLAEKY---DLDMKHTFLGPHAVPkeaSSNEAFLEEMIALlpevkqyadfadifcetgvftieqsqh 227
Cdd:COG0402 161 LREDADEGLADSERLIERWhgaADGRIRVALAPHAPY---TVSPELLRAAAAL--------------------------- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 228 ymqkAKEAGFKVKIHA----DEID------PLGGLEL-----AIDEQAISAdHLVASSDKGKEKLRNSDTVAVLLPATTF 292
Cdd:COG0402 211 ----ARELGLPLHTHLaetrDEVEwvlelyGKRPVEYldelgLLGPRTLLA-HCVHLTDEEIALLAETGASVAHCPTSNL 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 293 YLGKeDYADARGMLDNNGAIALATDynpGSSVTNNLQL--VMAIAAL--KLK------LSPNEVWNAVTVNAAKAIDIN- 361
Cdd:COG0402 286 KLGS-GIAPVPRLLAAGVRVGLGTD---GAASNNSLDMfeEMRLAALlqRLRggdptaLSAREALEMATLGGARALGLDd 361
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 612671876 362 -AGTINTGDKANLVIWDAPNHEYIP---------YHFGINHAEKVIKDGKVIVDN 406
Cdd:COG0402 362 eIGSLEPGKRADLVVLDLDAPHLAPlhdplsalvYAADGRDVRTVWVAGRVVVRD 416
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
28-406 |
2.02e-23 |
|
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: 101.12 E-value: 2.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 28 DELNVVKNGTVVIKDGKIVYAGQHTD--DYDATETIDASGKVVSPALVDAHTHLTfggsreheMSLKRqgkSYLEILEMg 105
Cdd:cd01298 12 DPRRVLEDGDVLVEDGRIVAVGPALPlpAYPADEVIDAKGKVVMPGLVNTHTHLA--------MTLLR---GLADDLPL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 106 ggiLSTVNAT-----RETSEDDLFKKAEHDLLTMIKHGVL---------------AVEsKSG------YGL------DRE 153
Cdd:cd01298 80 ---MEWLKDLiwpleRLLTEEDVYLGALLALAEMIRSGTTtfadmyffypdavaeAAE-ELGiravlgRGImdlgteDVE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 154 NELKQLKVSNRLAEKY---DLDMKHTFLGPHAVPkeaSSNEAFLEEMIAL-----------LPEVKqyADFADIFCETGV 219
Cdd:cd01298 156 ETEEALAEAERLIREWhgaADGRIRVALAPHAPY---TCSDELLREVAELareygvplhihLAETE--DEVEESLEKYGK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 220 FTIEqsqhymqkakeagfkvkiHADEIDPLGglelaidEQAISAdHLVASSDKGKEKLRNSDTVAVLLPATTFYLGKEdY 299
Cdd:cd01298 231 RPVE------------------YLEELGLLG-------PDVVLA-HCVWLTDEEIELLAETGTGVAHNPASNMKLASG-I 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 300 ADARGMLDNNGAIALATDynpGSSVTNNLQLV--MAIAALKLK--------LSPNEVWNAVTVNAAKAIDIN-AGTINTG 368
Cdd:cd01298 284 APVPEMLEAGVNVGLGTD---GAASNNNLDMFeeMRLAALLQKlahgdptaLPAEEALEMATIGGAKALGLDeIGSLEVG 360
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 612671876 369 DKANLVIWDAPNHEYIPYHFGINHA---------EKVIKDGKVIVDN 406
Cdd:cd01298 361 KKADLILIDLDGPHLLPVHDPISHLvysanggdvDTVIVNGRVVMED 407
|
|
| PRK06038 |
PRK06038 |
N-ethylammeline chlorohydrolase; Provisional |
33-406 |
3.49e-18 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180363 [Multi-domain] Cd Length: 430 Bit Score: 85.96 E-value: 3.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 33 VKNGTVVIKDGKIVYAGQHTDDyDATETIDASGKVVSPALVDAHTHLTfggsreheMSLKRQGKSYLEILEMGGGILSTV 112
Cdd:PRK06038 19 LKKGSVVIEDGTITEVSESTPG-DADTVIDAKGSVVMPGLVNTHTHAA--------MTLFRGYADDLPLAEWLNDHIWPA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 113 NAtrETSEDDLFKKAEHDLLTMIKHGVL--------------AVESKS-----GYGL-------DRENELKQ----LKVS 162
Cdd:PRK06038 90 EA--KLTAEDVYAGSLLACLEMIKSGTTsfadmyfymdevakAVEESGlraalSYGMidlgddeKGEAELKEgkrfVKEW 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 163 NRLAEkydlDMKHTFLGPHAvPKEASsneaflEEmiaLLPEVKQYADFADIFCETGVFTIEQSQHYMqkaKEAGFKVKIH 242
Cdd:PRK06038 168 HGAAD----GRIKVMYGPHA-PYTCS------EE---FLSKVKKLANKDGVGIHIHVLETEAELNQM---KEQYGMCSVN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 243 A-DEIDPLGGLELAIdeqaisadHLVASSDKGKEKLRNSDTVAVLLPATTFYLGkEDYADARGMLDNNGAIALATDynpG 321
Cdd:PRK06038 231 YlDDIGFLGPDVLAA--------HCVWLSDGDIEILRERGVNVSHNPVSNMKLA-SGIAPVPKLLERGVNVSLGTD---G 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 322 SSVTNNLQL--VMAIAALKLKLS--------PNEVWNAVTVNAAKAIDINAGTINTGDKANLVI-----------WDAPN 380
Cdd:PRK06038 299 CASNNNLDMfeEMKTAALLHKVNtmdptalpARQVLEMATVNGAKALGINTGMLKEGYLADIIIvdmnkphltpvRDVPS 378
|
410 420
....*....|....*....|....*.
gi 612671876 381 HeyIPYHFGINHAEKVIKDGKVIVDN 406
Cdd:PRK06038 379 H--LVYSASGSDVDTTIVDGRILMED 402
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
38-403 |
7.62e-18 |
|
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: 84.61 E-value: 7.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 38 VVIKDGKIVYAGQHTDDYDATETIDASGKVVSPALVDAHTHL----TFGGSREHEMSLKrqgksyleilemGGGILSTVN 113
Cdd:cd01293 17 IAIEDGRIAAIGPALAVPPDAEEVDAKGRLVLPAFVDPHIHLdktfTGGRWPNNSGGTL------------LEAIIAWEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 114 ATRETSEDDLFKKAEHDLLTMIKHGVLA----VESksgyglDRENELKQLKVSNRLAEKYD--LDMKHTFLGPHAVPKEa 187
Cdd:cd01293 85 RKLLLTAEDVKERAERALELAIAHGTTAirthVDV------DPAAGLKALEALLELREEWAdlIDLQIVAFPQHGLLST- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 188 SSNEAFLEEMIALLPEVKQYADFAdifcetgvFTIEQSQHYMQK----AKEAGFKVKIHADEIDPLG--GLELAIDEQA- 260
Cdd:cd01293 158 PGGEELMREALKMGADVVGGIPPA--------EIDEDGEESLDTlfelAQEHGLDIDLHLDETDDPGsrTLEELAEEAEr 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 261 ------ISADHLVASSDKGKEKLRN-------SDTVAVLLPATTFYL-GKEDYADARG------MLDNNG-AIALATD-- 317
Cdd:cd01293 230 rgmqgrVTCSHATALGSLPEAEVSRladllaeAGISVVSLPPINLYLqGREDTTPKRRgvtpvkELRAAGvNVALGSDnv 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 318 YNPGSSV-TNNLQLVMAIAALKLKLSPNE----VWNAVTVNAAKAIDINAGTINTGDKANLVIWDAPNheyiPYHF--GI 390
Cdd:cd01293 310 RDPWYPFgSGDMLEVANLAAHIAQLGTPEdlalALDLITGNAARALGLEDYGIKVGCPADLVLLDAED----VAEAvaRQ 385
|
410
....*....|...
gi 612671876 391 NHAEKVIKDGKVI 403
Cdd:cd01293 386 PPRRVVIRKGRVV 398
|
|
| PRK08393 |
PRK08393 |
N-ethylammeline chlorohydrolase; Provisional |
28-404 |
2.53e-16 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 181411 [Multi-domain] Cd Length: 424 Bit Score: 80.23 E-value: 2.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 28 DELNVVKnGTVVIKDGKIVYAGQHTDDyDATETIDASGKVVSPALVDAHTHLTFGGSR--EHEMSLKRQGKSYLEILEmg 105
Cdd:PRK08393 14 ENLKVIR-ADVLIEGNKIVEVKRNINK-PADTVIDASGSVVSPGFINAHTHSPMVLLRglADDVPLMEWLQNYIWPRE-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 106 ggilstvnatRETSEDDLFKKAEHDLLTMIKHGVL--------------AVESKS-----GYGL----DRENELKQLKVS 162
Cdd:PRK08393 90 ----------RKLKRKDIYWGAYLGLLEMIKSGTTtfvdmyfhmeevakATLEVGlrgylSYGMvdlgDEEKREKEIKET 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 163 NRLAE---KYDLDMKHTFLGPHAvPKEASsneafleemIALLPEVKQYADfadifcETGVFTIEQSQHYMQKAKEAGFKV 239
Cdd:PRK08393 160 EKLMEfieKLNSPRVHFVFGPHA-PYTCS---------LALLKWVREKAR------EWNKLITIHLSETMDEIKQIREKY 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 240 -KIHADEIDPLGGLelaiDEQAISAdHLVASSDKGKEKLRNSDTVAVLLPATTFYLGKEDYAdARGMLDNNGAIALATDy 318
Cdd:PRK08393 224 gKSPVVLLDEIGFL----NEDVIAA-HGVWLSSRDIRILASAGVTVAHNPASNMKLGSGVMP-LRKLLNAGVNVALGTD- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 319 npGSSVTNNLQLV--MAIAALKLK---LSPN-----EVWNAVTVNAAKAIDINAGTINTGDKANLVIWDAPNHEYIPYHF 388
Cdd:PRK08393 297 --GAASNNNLDMLreMKLAALLHKvhnLDPTiadaeTVFRMATQNGAKALGLKAGVIKEGYLADIAVIDFNRPHLRPINN 374
|
410 420
....*....|....*....|....*
gi 612671876 389 GINH---------AEKVIKDGKVIV 404
Cdd:PRK08393 375 PISHlvysangndVETTIVDGKIVM 399
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
72-357 |
8.70e-14 |
|
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: 71.21 E-value: 8.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 72 LVDAHTHLTFGGSREHemslkrqgksyleilemggGILSTVNATRETSEDDLFKKAEHDLLTMIKHGVLAVESKSGYGLD 151
Cdd:cd01292 1 FIDTHVHLDGSALRGT-------------------RLNLELKEAEELSPEDLYEDTLRALEALLAGGVTTVVDMGSTPPP 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 152 RENELKQLKVSNRLAEKYDLDMKHTFLGPHAVPKEASSNEAFLEEMIALLPEVKQYADFADIFCETGVFTIEQSQHYMQK 231
Cdd:cd01292 62 TTTKAAIEAVAEAARASAGIRVVLGLGIPGVPAAVDEDAEALLLELLRRGLELGAVGLKLAGPYTATGLSDESLRRVLEE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 232 AKEAGFKVKIHADE-IDPLGGLELAID----EQAISADHLVASSDKGKEKLRNSDTVAVLLPATTFYLG--KEDYADARG 304
Cdd:cd01292 142 ARKLGLPVVIHAGElPDPTRALEDLVAllrlGGRVVIGHVSHLDPELLELLKEAGVSLEVCPLSNYLLGrdGEGAEALRR 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 612671876 305 MLDNNGAIALATDYNPGSSVTNNLQLV-MAIAALKLKLSPNEVWNAVTVNAAKA 357
Cdd:cd01292 222 LLELGIRVTLGTDGPPHPLGTDLLALLrLLLKVLRLGLSLEEALRLATINPARA 275
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
67-403 |
8.28e-13 |
|
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: 69.07 E-value: 8.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 67 VVSPALVDAHTHLTFGGSRehemslkrqgksyleilemgggilstvnaTRETSEDDLFKKAEHDLLTMIKHGvlaVESKS 146
Cdd:pfam01979 1 IVLPGLIDAHVHLEMGLLR-----------------------------GIPVPPEFAYEALRLGITTMLKSG---TTTVL 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 147 GYGLDRENELKQLKvsnRLAEKYDLDMkhTFLGPHAVPKEASSNEAFLEEMIALLPEVKQYADFADIFCETGV------- 219
Cdd:pfam01979 49 DMGATTSTGIEALL---EAAEELPLGL--RFLGPGCSLDTDGELEGRKALREKLKAGAEFIKGMADGVVFVGLaphgapt 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 220 FTIEQSQHYMQKAKEAGFKVKIHADEIDplGGLELAIDeqAISADHLVASSDKGKEKLRNSDTVA------VLLPATTFY 293
Cdd:pfam01979 124 FSDDELKAALEEAKKYGLPVAIHALETK--GEVEDAIA--AFGGGIEHGTHLEVAESGGLLDIIKlilahgVHLSPTEAN 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 294 LGKE-------------------DYADARGMLDNNGAIALATDyNPGSSVTNNLQLVMAIAAL-----KLKLSPNEVWNA 349
Cdd:pfam01979 200 LLAEhlkgagvahcpfsnsklrsGRIALRKALEDGVKVGLGTD-GAGSGNSLNMLEELRLALElqfdpEGGLSPLEALRM 278
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 612671876 350 VTVNAAKA--IDINAGTINTGDKANLVIWDAPNHEYIPYHFGINHAEKVIKDGKVI 403
Cdd:pfam01979 279 ATINPAKAlgLDDKVGSIEVGKDADLVVVDLDPLAAFFGLKPDGNVKKVIVKGKIV 334
|
|
| PRK06380 |
PRK06380 |
metal-dependent hydrolase; Provisional |
36-406 |
1.17e-12 |
|
metal-dependent hydrolase; Provisional
Pssm-ID: 180548 [Multi-domain] Cd Length: 418 Bit Score: 69.14 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 36 GTVVIKDGKIVYAGqhTDDYDATETIDASGKVVSPALVDAHTHLTFGGSR----------------EHEMSLKRQG---K 96
Cdd:PRK06380 22 GNVYIEGNKIVYVG--DVNEEADYIIDATGKVVMPGLINTHAHVGMTASKglfddvdleeflmktfKYDSKRTREGiynS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 97 SYLEILEM-GGGILSTVNATreTSEDDLFKKAEhdlltmiKHGVLAVESKSGygLDRE-NELKQLKVSNrlAEKYDLDMK 174
Cdd:PRK06380 100 AKLGMYEMiNSGITAFVDLY--YSEDIIAKAAE-------ELGIRAFLSWAV--LDEEiTTQKGDPLNN--AENFIREHR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 175 HT-----FLGPHAVpkEASSNEAFLEemiallpeVKQYADFADIFCETGVFtiEQSQHYMQKAKEAGFKVKIHADEIDPL 249
Cdd:PRK06380 167 NEelvtpSIGVQGI--YVANDETYLK--------AKEIAEKYDTIMHMHLS--ETRKEVYDHVKRTGERPVEHLEKIGFL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 250 gglelaiDEQAISAdHLVASSDKGKEKLRNSDTVAVLLPATTFYLGKEDYADARGMLDNNGAIALATDYNpGSSVTNNLQ 329
Cdd:PRK06380 235 -------NSKLIAA-HCVWATYHEIKLLSKNGVKVSWNSVSNFKLGTGGSPPIPEMLDNGINVTIGTDSN-GSNNSLDMF 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 330 LVMAIAALKLKlspNEVWNA-----------VTVNAAKAIDINAGTINTGDKANLVIWDAPNHEYIP-----------YH 387
Cdd:PRK06380 306 EAMKFSALSVK---NERWDAsiikaqeildfATINAAKALELNAGSIEVGKLADLVILDARAPNMIPtrknnivsnivYS 382
|
410
....*....|....*....
gi 612671876 388 FGINHAEKVIKDGKVIVDN 406
Cdd:PRK06380 383 LNPLNVDHVIVNGKILKEN 401
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
32-79 |
7.30e-12 |
|
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: 66.65 E-value: 7.30e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 612671876 32 VVKNGTVV-----------IKDGKIVYAGQHTDDYDATETIDASGKVVSPALVDAHTHL 79
Cdd:COG0044 1 LIKNGRVVdpggleradvlIEDGRIAAIGPDLAAPEAAEVIDATGLLVLPGLIDLHVHL 59
|
|
| COG3653 |
COG3653 |
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and ... |
32-78 |
6.34e-11 |
|
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442870 [Multi-domain] Cd Length: 528 Bit Score: 64.04 E-value: 6.34e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 32 VVKNGTVV-------------IKDGKIVYAGQhTDDYDATETIDASGKVVSPALVDAHTH 78
Cdd:COG3653 5 LIRGGTVVdgtgappfradvaIKGGRIVAVGD-LAAAEAARVIDATGLVVAPGFIDIHTH 63
|
|
| COG3964 |
COG3964 |
Predicted amidohydrolase [General function prediction only]; |
32-85 |
1.91e-10 |
|
Predicted amidohydrolase [General function prediction only];
Pssm-ID: 443164 [Multi-domain] Cd Length: 376 Bit Score: 62.11 E-value: 1.91e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 612671876 32 VVKNGTVV-------------IKDGKIVYAGQHTDDYDATETIDASGKVVSPALVDAHTHLTFGGSR 85
Cdd:COG3964 3 LIKGGRVIdpangidgvmdiaIKDGKIAAVAKDIDAAEAKKVIDASGLYVTPGLIDLHTHVFPGGTD 69
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
42-403 |
3.30e-10 |
|
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: 61.17 E-value: 3.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 42 DGKIVYAGQHTDDYDATETIDASGKVVSPALVDAHTHL-------TFGGSREHEMS-------------------LKRQ- 94
Cdd:cd01309 1 DGKIVAVGAEITTPADAEVIDAKGKHVTPGLIDAHSHLgldeeggVRETSDANEETdpvtphvraidginpddeaFKRAr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 95 --GKSYLEILEMGGGIL---STVNATRETSEDDLFKKAEHDlltmIKhgvLAVES--KSGYGlDRENE-----------L 156
Cdd:cd01309 81 agGVTTVQVLPGSANLIggqGVVIKTDGGTIEDMFIKAPAG----LK---MALGEnpKRVYG-GKGKEpatrmgvaallR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 157 KQLKVSNRLAEKYDLDMKHTFLGPHAVPKeassneafLEEMIALLP---EVKQYADFADifcetgvfTIEQSqhyMQKAK 233
Cdd:cd01309 153 DAFIKAQEYGRKYDLGKNAKKDPPERDLK--------LEALLPVLKgeiPVRIHAHRAD--------DILTA---IRIAK 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 234 EAGFKVKI--HADEidplgglelaideqaisadHLVAssdkgkEKLRNSDTVAVLLPATTFYLGKEDYAD----ARGMLD 307
Cdd:cd01309 214 EFGIKITIehGAEG-------------------YKLA------DELAKHGIPVIYGPTLTLPKKVEEVNDaidtNAYLLK 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 308 NNG-AIALATDYNpgSSVTNNLQLVmAIAALKLKLSPNEVWNAVTVNAAKA--IDINAGTINTGDKANLVIWDAPNHEYI 384
Cdd:cd01309 269 KGGvAFAISSDHP--VLNIRNLNLE-AAKAVKYGLSYEEALKAITINPAKIlgIEDRVGSLEPGKDADLVVWNGDPLEPT 345
|
410
....*....|....*....
gi 612671876 385 PYhfginhAEKVIKDGKVI 403
Cdd:cd01309 346 SK------PEQVYIDGRLV 358
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
36-88 |
3.53e-10 |
|
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: 61.54 E-value: 3.53e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 612671876 36 GTVVIKDGKIVYAGQHTDDYDATETIDASGKVVSPALVDAHTHLTFGGSREHE 88
Cdd:cd01315 18 ADIAVKGGKIAAIGPDIANTEAEEVIDAGGLVVMPGLIDTHVHINEPGRTEWE 70
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
38-104 |
7.13e-10 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 60.58 E-value: 7.13e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 612671876 38 VVIKDGKIVYAGqhTDDY------DATETIDASGKVVSPALVDAHTHLTFGGSREHEMSLkRQGKSYLEILEM 104
Cdd:COG1574 30 VAVRDGRIVAVG--SDAEvralagPATEVIDLGGKTVLPGFIDAHVHLLGGGLALLGVDL-SGARSLDELLAR 99
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
32-85 |
9.23e-10 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 60.19 E-value: 9.23e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 612671876 32 VVKNGTVV-----------IKDGKIVYAGQHTDDydatETIDASGKVVSPALVDAHTHLT--FGGSR 85
Cdd:PRK08323 4 LIKNGTVVtaddtykadvlIEDGKIAAIGANLGD----EVIDATGKYVMPGGIDPHTHMEmpFGGTV 66
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
38-104 |
2.75e-09 |
|
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: 58.86 E-value: 2.75e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 612671876 38 VVIKDGKIVYAGqhtDDYDA-------TETIDASGKVVSPALVDAHTHLTFGGSREHEMSLkRQGKSYLEILEM 104
Cdd:cd01300 2 VAVRDGRIVAVG---SDAEAkalkgpaTEVIDLKGKTVLPGFIDSHSHLLLGGLSLLWLDL-SGVTSKEEALAR 71
|
|
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
32-79 |
3.61e-09 |
|
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: 58.38 E-value: 3.61e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 612671876 32 VVKNGTVV-----------IKDGKIVYAGQHTDDYDATETIDASGKVVSPALVDAHTHL 79
Cdd:cd01314 2 IIKNGTIVtadgsfkadilIEDGKIVAIGPNLEAPGGVEVIDATGKYVLPGGIDPHTHL 60
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
59-384 |
5.89e-09 |
|
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of carbamoyl aspartate to dihydroorotate, a key reaction in pyrimidine biosynthesis. This subgroup also contains proteins that lack the active site, like unc-33, a C.elegans protein involved in axon growth.
Pssm-ID: 238642 [Multi-domain] Cd Length: 374 Bit Score: 57.25 E-value: 5.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 59 ETIDASGKVVSPALVDAHTHLtfggsREhemslkrQGKSYLEILEMG------GGILS---------------TVNATRE 117
Cdd:cd01317 3 EVIDAEGKILAPGLVDLHVHL-----RE-------PGFEYKETLESGakaaaaGGFTTvvcmpntnpvidnpaVVELLKN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 118 TSEDDLFKKAEH--------------DLLTMIKHGVLAVESKSGYGLDreNELkqLKVSNRLAEKYDLDMKH-------- 175
Cdd:cd01317 71 RAKDVGIVRVLPigaltkglkgeeltEIGELLEAGAVGFSDDGKPIQD--AEL--LRRALEYAAMLDLPIIVhpedpsla 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 176 -----------TFLGPHAVPKEASsnEAFLEEMIALLPEVKQYADFADIFCETGVFTIEqsqhymqKAKEAGfkVKIHAD 244
Cdd:cd01317 147 gggvmnegkvaSRLGLPGIPPEAE--TIMVARDLELAEATGARVHFQHLSTARSLELIR-------KAKAKG--LPVTAE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 245 eidplgglelaideqaISADHLVASSdkgkEKLRNSDTVAVLLPAttfyLGKEDYADA-RGMLdNNGAI-ALATDYNP-- 320
Cdd:cd01317 216 ----------------VTPHHLLLDD----EALESYDTNAKVNPP----LRSEEDREAlIEAL-KDGTIdAIASDHAPht 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 321 -------------GSSvtnNLQLVMAIAAL----KLKLSPNEVWNAVTVNAAKAIDINAGTINTGDKANLVIWDaPNHEY 383
Cdd:cd01317 271 deekdlpfaeappGII---GLETALPLLWTllvkGGLLTLPDLIRALSTNPAKILGLPPGRLEVGAPADLVLFD-PDAEW 346
|
.
gi 612671876 384 I 384
Cdd:cd01317 347 I 347
|
|
| archeal_chlorohydrolases |
cd01305 |
Predicted chlorohydrolases. These metallo-dependent hydrolases from archea are part of the ... |
67-357 |
7.77e-09 |
|
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: 56.25 E-value: 7.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 67 VVSPALVDAHTHLtfGGSREHEMslkRQGKSYLEILEMGGGILSTVnaTRETSEDDLFKKAEHDLLTMIKHGVlavesks 146
Cdd:cd01305 1 ILIPALVNAHTHL--GDSAIKEV---GDGLPLDDLVAPPDGLKHRL--LAQADDRELAEAMRKVLRDMRETGI------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 147 GYGLD-RENELKQLKVSNRLAEKYDLdmkhTFLGPHAVPKEASSNEAFLEEMIALLPEVKQYADFADIfcetgvftieqs 225
Cdd:cd01305 67 GAFADfREGGVEGIELLRRALGKLPV----PFEVILGRPTEPDDPEILLEVADGLGLSSANDVDLEDI------------ 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 226 qhyMQKAKEAGFKVKIHADEIDPLGG---LELAIDEQAISADHLVASSDKGKEKLRNSDTVAVLLPATTFYLGKEDyADA 302
Cdd:cd01305 131 ---LELLRRRGKLFAIHASETRESVGmtdIERALDLEPDLLVHGTHLTDEDLELVRENGVPVVLCPRSNLYFGVGI-PPV 206
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 612671876 303 RGMLDNNGAIALATDyNPGSSVTN---NLQLVMAIAALKLKLSPNEVWNAVTVNAAKA 357
Cdd:cd01305 207 AELLKLGIKVLLGTD-NVMVNEPDmwaEMEFLAKYSRLQGYLSPLEILRMATVNAAEF 263
|
|
| PRK08044 |
PRK08044 |
allantoinase AllB; |
32-162 |
4.59e-08 |
|
allantoinase AllB;
Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 54.86 E-value: 4.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 32 VVKNGTVV-----------IKDGKIVYAGQHTDDydATETIDASGKVVSPALVDAHTHLTfggsrehemslkRQGKSYLE 100
Cdd:PRK08044 6 IIKNGTVIlenearvvdiaVKGGKIAAIGQDLGD--AKEVMDASGLVVSPGMVDAHTHIS------------EPGRSHWE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 101 ILEMG------GGI-------LSTVNAT-RETSEDDLFKKAEhdlltmikhGVLAVESKS-----GYGLDRENELKQLKV 161
Cdd:PRK08044 72 GYETGtraaakGGIttmiempLNQLPATvDRASIELKFDAAK---------GKLTIDAAQlgglvSYNLDRLHELDEVGV 142
|
.
gi 612671876 162 S 162
Cdd:PRK08044 143 V 143
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
32-95 |
4.60e-08 |
|
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: 54.61 E-value: 4.60e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 612671876 32 VVKNGTVV-------------IKDGKIVYAGQhTDDYDATETIDASGKVVSPALVDAHTH--LTFGGSREHEMSLkRQG 95
Cdd:cd01297 3 VIRNGTVVdgtgappftadvgIRDGRIAAIGP-ILSTSAREVIDAAGLVVAPGFIDVHTHydGQVFWDPDLRPSS-RQG 79
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
32-78 |
6.09e-08 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 54.72 E-value: 6.09e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 32 VVKNGTVV-------------IKDGKIVYAGQHTDDydATETIDASGKVVSPALVDAHTH 78
Cdd:COG1001 8 VIKNGRLVnvftgeilegdiaIAGGRIAGVGDYIGE--ATEVIDAAGRYLVPGFIDGHVH 65
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
24-79 |
8.70e-08 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 54.05 E-value: 8.70e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 612671876 24 GKELDELNVVKNGTVVIKDGKIVYAGQhTDDYDATETIDASGKVVSPALVDAHTHL 79
Cdd:PRK09357 8 GRVIDPKGLDEVADVLIDDGKIAAIGE-NIEAEGAEVIDATGLVVAPGLVDLHVHL 62
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
22-377 |
2.17e-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: 52.58 E-value: 2.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 22 LKGKELDELNVVKNGTVVIKDGKIVYAGQHTDDYDATETIDASGKVVSPALVDAHTHltfggsrehemslkrqgksylei 101
Cdd:cd00854 3 IKNARILTPGGLEDGAVLVEDGKIVAIGPEDELEEADEIIDLKGQYLVPGFIDIHIH----------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 102 lemGGGILSTVNATretsEDDLFKKAEHdlltMIKHGV---LAVESKSgyglDRENELKQLKVsnrLAEKYDLDMKHTFL 178
Cdd:cd00854 60 ---GGGGADFMDGT----AEALKTIAEA----LAKHGTtsfLPTTVTA----PPEEIAKALAA---IAEAIAEGQGAEIL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 179 GPH------AVPKEASSNEAFLEE------------------MIALLPEVKQYADFADIFCETGVF--------TIEQsq 226
Cdd:cd00854 122 GIHlegpfiSPEKKGAHPPEYLRApdpeelkkwleaagglikLVTLAPELDGALELIRYLVERGIIvsighsdaTYEQ-- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 227 hyMQKAKEAGFKV---------KIHADEIDPLGGLELAIDEQA-ISAD--HL------VASSDKGKEKL-------Rnsd 281
Cdd:cd00854 200 --AVAAFEAGATHvthlfnamsPLHHREPGVVGAALSDDDVYAeLIADgiHVhpaavrLAYRAKGADKIvlvtdamA--- 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 282 tvAVLLPATTFYLGKEDY--ADARGMLDnNGAIAlatdynpGSSVTNNLQLVMAIAalKLKLSPNEVWNAVTVNAAKAID 359
Cdd:cd00854 275 --AAGLPDGEYELGGQTVtvKDGVARLA-DGTLA-------GSTLTMDQAVRNMVK--WGGCPLEEAVRMASLNPAKLLG 342
|
410 420
....*....|....*....|
gi 612671876 360 INA--GTINTGDKANLVIWD 377
Cdd:cd00854 343 LDDrkGSLKPGKDADLVVLD 362
|
|
| PRK05985 |
PRK05985 |
cytosine deaminase; Provisional |
38-85 |
2.84e-07 |
|
cytosine deaminase; Provisional
Pssm-ID: 180337 [Multi-domain] Cd Length: 391 Bit Score: 52.24 E-value: 2.84e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 612671876 38 VVIKDGKIVYAGQHTDDYDATETIDASGKVVSPALVDAHTHL--TFGGSR 85
Cdd:PRK05985 19 ILIRDGRIAAIGPALAAPPGAEVEDGGGALALPGLVDGHIHLdkTFWGDP 68
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
38-83 |
3.95e-07 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 51.77 E-value: 3.95e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 612671876 38 VVIKDGKIVYAGQHTDDYDATETIDASGKVVSPALVDAHTHLTFGG 83
Cdd:PRK09237 21 IAIEDGKIAAVAGDIDGSQAKKVIDLSGLYVSPGWIDLHVHVYPGS 66
|
|
| PRK07213 |
PRK07213 |
chlorohydrolase; Provisional |
22-375 |
4.43e-07 |
|
chlorohydrolase; Provisional
Pssm-ID: 235969 [Multi-domain] Cd Length: 375 Bit Score: 51.58 E-value: 4.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 22 LKGKELDelnvVKNGTVVIKDGKIVyagQHTDDYDATETIDASGKVVsPALVDAHTHLtfGGSrehemSLKRQG--KSYL 99
Cdd:PRK07213 10 LYGEDFE----PKKGNLVIEDGIIK---GFTNEVHEGNVIDAKGLVI-PPLINAHTHI--GDS-----SIKDIGigKSLD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 100 EILEMGGGIlstVNATRETSEDDLFKKAEHD-LLTMIKHGVlavesksGYGLD-RENELKQLKVSNRLAekYDLDMKHTF 177
Cdd:PRK07213 75 ELVKPPNGL---KHKFLNSCSDKELVEGMKEgLYDMYNNGI-------KAFCDfREGGIKGINLLKKAS--SDLPIKPII 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 178 LGPhavPKEASSNEAFLeemiallpEVKQYADFADIFCETGV--FTIEQSQHYMQKAKEAGFKVKIHADEidPLGGLELA 255
Cdd:PRK07213 143 LGR---PTEADENELKK--------EIREILKNSDGIGLSGAneYSDEELKFICKECKREKKIFSIHAAE--HKGSVEYS 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 256 ID-------EQAISAD-------HLVASSDKGKEKLRNSDTVAVLLPAT--TFYLGkedYADARGMLDNNGAIALATDYn 319
Cdd:PRK07213 210 LEkygmteiERLINLGfkpdfivHATHPSNDDLELLKENNIPVVVCPRAnaSFNVG---LPPLNEMLEKGILLGIGTDN- 285
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 612671876 320 pgssvtnnlqlVMAIA---------ALKL-KLSPNEVWNAVTVNAAKAID-INAGTINTGDKANLVI 375
Cdd:PRK07213 286 -----------FMANSpsifremefIYKLyHIEPKEILKMATINGAKILGlINVGLIEEGFKADFTF 341
|
|
| Met_dep_hydrolase_D |
cd01312 |
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ... |
43-396 |
7.00e-07 |
|
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: 50.91 E-value: 7.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 43 GKIVYAGQH---TDDYDATETIDASGKVVSPALVDAHTHLTFGGSrehemslkrqgKSYLEILEMGGGILSTVNATRETS 119
Cdd:cd01312 1 DKILEVGDYeklEKRYPGAKHEFFPNGVLLPGLINAHTHLEFSAN-----------VAQFTYGRFRAWLLSVINSRDELL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 120 EDDLFKKAEHDLLTMIKHGVLAVESKSGYGLD-----------------------RENELKQLkVSNRLAEKydLDMKHT 176
Cdd:cd01312 70 KQPWEEAIRQGIRQMLESGTTSIGAISSDGSLlpalassglrgvffnevigsnpsAIDFKGET-FLERFKRS--KSFESQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 177 FLGPHAVPKEASSNEAFLeeMIALLPEVKQY-----ADFADIFCETGVFTIEQS------QHYMQKAKEAGFKVKIhaDE 245
Cdd:cd01312 147 LFIPAISPHAPYSVHPEL--AQDLIDLAKKLnlplsTHFLESKEEREWLEESKGwfkhfwESFLKLPKPKKLATAI--DF 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 246 IDPLGGLElaideQAISADHLVASSDKGKEKLRNSDTVAVLLPATTFYLGKEdYADARGMLDNNGAIALATDynpGSSVT 325
Cdd:cd01312 223 LDMLGGLG-----TRVSFVHCVYANLEEAEILASRGASIALCPRSNRLLNGG-KLDVSELKKAGIPVSLGTD---GLSSN 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 326 NNLQLVMAIAALkLKLSPNEVWNA--------VTVNAAKAIDINAGTINTGDKANLVIWDAP---NHEYIPYHFgINHAE 394
Cdd:cd01312 294 ISLSLLDELRAL-LDLHPEEDLLElaselllmATLGGARALGLNNGEIEAGKRADFAVFELPgpgIKEQAPLQF-ILHAK 371
|
..
gi 612671876 395 KV 396
Cdd:cd01312 372 EV 373
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
28-80 |
1.17e-06 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 50.38 E-value: 1.17e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 612671876 28 DELNVVKNGTVVIKDGKIVYAGQHTDDYDATETIDASGKVVSPALVDAHTHLT 80
Cdd:PRK07228 14 NAKREIVDGDVLIEDDRIAAVGDRLDLEDYDDHIDATGKVVIPGLIQGHIHLC 66
|
|
| FwdA |
COG1229 |
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion]; |
32-78 |
1.44e-06 |
|
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion];
Pssm-ID: 440842 Cd Length: 554 Bit Score: 50.19 E-value: 1.44e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 612671876 32 VVKNGTVV--------------IKDGKIVYAgqhTDDYDATETIDASGKVVSPALVDAHTH 78
Cdd:COG1229 4 IIKNGRVYdpangidgevmdiaIKDGKIVEE---PSDPKDAKVIDASGKVVMAGGVDIHTH 61
|
|
| PRK12394 |
PRK12394 |
metallo-dependent hydrolase; |
29-84 |
1.93e-06 |
|
metallo-dependent hydrolase;
Pssm-ID: 183497 [Multi-domain] Cd Length: 379 Bit Score: 49.37 E-value: 1.93e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 612671876 29 ELNVVKNGTVVIKDGKIVYAGQHtDDYDATETIDASGKVVSPALVDAHTHLTFGGS 84
Cdd:PRK12394 16 ARNINEINNLRIINDIIVDADKY-PVASETRIIHADGCIVTPGLIDYHAHVFYDGT 70
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
27-78 |
4.21e-06 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 48.56 E-value: 4.21e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 612671876 27 LDELNVVKNGTVVIKDGKIVYAGQHTDDydATETIDASGKVVSPALVDAHTH 78
Cdd:COG1820 8 FTGDGVLEDGALLIEDGRIAAIGPGAEP--DAEVIDLGGGYLAPGFIDLHVH 57
|
|
| PRK15493 |
PRK15493 |
bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase; |
27-384 |
4.29e-06 |
|
bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase;
Pssm-ID: 185390 [Multi-domain] Cd Length: 435 Bit Score: 48.52 E-value: 4.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 27 LDELN-VVKNGTVVIKDGKI--VYAGQHTDDYDATETIDASGKVVSPALVDAHTHLTFGGSR-------------EHEMS 90
Cdd:PRK15493 13 MNEQNeVIENGYIIVENDQIidVNSGEFASDFEVDEVIDMKGKWVLPGLVNTHTHVVMSLLRgigddmllqpwleTRIWP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 91 LKRQGKSYLEILEMGGGILSTVNATrETSEDDLFKKAEHD----LLTMIKHGVLAVESKSGYGL-DRENELKQLKVSNRL 165
Cdd:PRK15493 93 LESQFTPELAVASTELGLLEMVKSG-TTSFSDMFNPIGVDqdaiMETVSRSGMRAAVSRTLFSFgTKEDEKKAIEEAEKY 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 166 AEKY--DLDMKHTFLGPHAvPKEASSNeaFLEEMIALLPEVKQYADFADIFCETGVFTIEqsQHYMQKAKEAGFKVKIHA 243
Cdd:PRK15493 172 VKRYynESGMLTTMVAPHS-PYTCSTE--LLEECARIAVENQTMVHIHLSETEREVRDIE--AQYGKRPVEYAASCGLFK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 244 DEIDPLGGLELAIDEQAISADHLVASSDKgkeklrnsdtvavllPATTFYLGkEDYADARGMLDNNGAIALATDynpGSS 323
Cdd:PRK15493 247 RPTVIAHGVVLNDNERAFLAEHDVRVAHN---------------PNSNLKLG-SGIANVKAMLEAGIKVGIATD---SVA 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 612671876 324 VTNNLQLV--MAIAALKLK--------LSPNEVWNAVTVNAAKAIDI-NAGTINTGDKANLVIWDAPNHEYI 384
Cdd:PRK15493 308 SNNNLDMFeeMRIATLLQKgihqdataLPVETALTLATKGAAEVIGMkQTGSLEVGKCADFITIDPSNKPHL 379
|
|
| D-hydantoinase |
TIGR02033 |
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily ... |
33-79 |
5.62e-06 |
|
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily converts 5,6-dihydrouracil to 3-ureidopropanoate but also acts on dihydrothymine and hydantoin. The enzyme is a metalloenzyme.
Pssm-ID: 273937 [Multi-domain] Cd Length: 454 Bit Score: 48.15 E-value: 5.62e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 612671876 33 VKNGTVV-----------IKDGKIVYAGQHTDDYDATETIDASGKVVSPALVDAHTHL 79
Cdd:TIGR02033 3 IKGGTVVnaddvfqadvlIEGGKIVAVGDNLIPPDAVEVIDATGKYVLPGGIDVHTHL 60
|
|
| PRK07203 |
PRK07203 |
putative aminohydrolase SsnA; |
31-103 |
1.30e-05 |
|
putative aminohydrolase SsnA;
Pssm-ID: 235963 [Multi-domain] Cd Length: 442 Bit Score: 47.24 E-value: 1.30e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 612671876 31 NVVKNGTVVIKDGKIVYAGQHTD---DYDATETIDASGKVVSPALVDAHTHLTFGGSRehEMSLK-RQGKSYLEILE 103
Cdd:PRK07203 17 PVIEDGAIAIEGNVIVEIGTTDElkaKYPDAEFIDAKGKLIMPGLINSHNHIYSGLAR--GMMANiPPPPDFISILK 91
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
36-79 |
2.71e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 46.15 E-value: 2.71e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 612671876 36 GTVVIKDGKIVYAGQHTDDYDAtETIDASGKVVSPALVDAHTHL 79
Cdd:PRK08204 24 GDILIEGDRIAAVAPSIEAPDA-EVVDARGMIVMPGLVDTHRHT 66
|
|
| PRK07627 |
PRK07627 |
dihydroorotase; Provisional |
33-74 |
3.55e-05 |
|
dihydroorotase; Provisional
Pssm-ID: 181059 [Multi-domain] Cd Length: 425 Bit Score: 45.82 E-value: 3.55e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 612671876 33 VKNGTVV-------------IKDGKIVYAGQHTDDYDATETIDASGKVVSPALVD 74
Cdd:PRK07627 5 IKGGRLIdpaagtdrqadlyVAAGKIAAIGQAPAGFNADKTIDASGLIVCPGLVD 59
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
59-404 |
4.66e-05 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 45.21 E-value: 4.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 59 ETIDASGKVVSPALVDAHTHLTFGGSREHEMSL-----KRQGKSYLEILEMGGGIL-STVNATRETSEDDLFKKAEHD-- 130
Cdd:pfam07969 1 EVIDAKGRLVLPGFVDPHTHLDGGGLNLRELRLpdvlpNAVVKGQAGRTPKGRWLVgEGWDEAQFAETRFPYALADLDev 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 131 -------LLTMIKH-----------------------GVLAVESKS----GYGLDRENELKQLKVSNRLAEKYDLDMKH- 175
Cdd:pfam07969 81 apdgpvlLRALHTHaavansaaldlagitkatedppgGEIARDANGegltGLLREGAYALPPLLAREAEAAAVAAALAAl 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 176 ---------------TFLGPHAVPKEASSNE------AFLEEMIALLPEVKQYADFADIF--CETGVFTIEQSQHY---- 228
Cdd:pfam07969 161 pgfgitsvdggggnvHSLDDYEPLRELTAAEklkellDAPERLGLPHSIYELRIGAMKLFadGVLGSRTAALTEPYfdap 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 229 ---------------MQKAKEAGFKVKIHADEIDPLGGLELAIDEQAI--------SADH---LVASSDKGKEKLRNSDT 282
Cdd:pfam07969 241 gtgwpdfedealaelVAAARERGLDVAIHAIGDATIDTALDAFEAVAEklgnqgrvRIEHaqgVVPYTYSQIERVAALGG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 283 VAVLLPATTFYLGKED-----YADARG------MLDNNGAIALATDYNPGS---------SVTNNLQLVMAIAALKLKLS 342
Cdd:pfam07969 321 AAGVQPVFDPLWGDWLqdrlgAERARGltpvkeLLNAGVKVALGSDAPVGPfdpwprigaAVMRQTAGGGEVLGPDEELS 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 612671876 343 PNEVWNAVTVNAAKAI--DINAGTINTGDKANLVIWDAP----NHEYIPYhfgiNHAEKVIKDGKVIV 404
Cdd:pfam07969 401 LEEALALYTSGPAKALglEDRKGTLGVGKDADLVVLDDDpltvDPPAIAD----IRVRLTVVDGRVVY 464
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
38-85 |
7.99e-05 |
|
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: 44.24 E-value: 7.99e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 612671876 38 VVIKDGKIVYAGQHTDDYDATETIDASGKVVSPALVDAHTHLTFGGSR 85
Cdd:cd01307 2 VAIENGKIAAVGAALAAPAATQIVDAGGCYVSPGWIDLHVHVYQGGTR 49
|
|
| PRK09045 |
PRK09045 |
TRZ/ATZ family hydrolase; |
32-93 |
8.36e-05 |
|
TRZ/ATZ family hydrolase;
Pssm-ID: 236366 [Multi-domain] Cd Length: 443 Bit Score: 44.52 E-value: 8.36e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 612671876 32 VVKNGTVVIKDGKIVY---AGQHTDDYDATETIDASGKVVSPALVDAHTHLTfggsreheMSLKR 93
Cdd:PRK09045 25 VLEDHAVAIRDGRIVAilpRAEARARYAAAETVELPDHVLIPGLINAHTHAA--------MSLLR 81
|
|
| PRK06687 |
PRK06687 |
TRZ/ATZ family protein; |
29-85 |
9.01e-05 |
|
TRZ/ATZ family protein;
Pssm-ID: 180657 [Multi-domain] Cd Length: 419 Bit Score: 44.61 E-value: 9.01e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 612671876 29 ELNVVKNGTVVIKDGKIVYAGQHTDDY--DATETIDASGKVVSPALVDAHTHLTFGGSR 85
Cdd:PRK06687 15 DFHVYLDGILAVKDSQIVYVGQDKPAFleQAEQIIDYQGAWIMPGLVNCHTHSAMTGLR 73
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
32-129 |
9.66e-05 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 44.53 E-value: 9.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 32 VVKNGTVV-----------IKDGKIVYAGqHTDDYDATETIDASGKVVSPALVDAHTHLtfggsREhemslkrQGKSYLE 100
Cdd:PRK09060 8 ILKGGTVVnpdgegradigIRDGRIAAIG-DLSGASAGEVIDCRGLHVLPGVIDSQVHF-----RE-------PGLEHKE 74
|
90 100 110
....*....|....*....|....*....|....*....
gi 612671876 101 ILEMG--GGILSTVNATRE--------TSEDDLFKKAEH 129
Cdd:PRK09060 75 DLETGsrAAVLGGVTAVFEmpntnpltTTAEALADKLAR 113
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
32-79 |
9.95e-05 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 44.30 E-value: 9.95e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 612671876 32 VVKNGTVV-----------IKDGKIVYAGQHTDDydATETIDASGKVVSPALVDAHTHL 79
Cdd:PRK13404 7 VIRGGTVVtatdtfqadigIRGGRIAALGEGLGP--GAREIDATGRLVLPGGVDSHCHI 63
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
32-87 |
1.11e-04 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 44.31 E-value: 1.11e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 612671876 32 VVKNGTVV-----------IKDGKIVYAGQHTDDyDATETIDASGKVVSPALVDAHTHLTFGGsREH 87
Cdd:PRK06189 6 IIRGGKVVtpegvyradigIKNGKIAEIAPEISS-PAREIIDADGLYVFPGMIDVHVHFNEPG-RTH 70
|
|
| PRK07583 |
PRK07583 |
cytosine deaminase; |
38-142 |
1.21e-04 |
|
cytosine deaminase;
Pssm-ID: 236062 Cd Length: 438 Bit Score: 44.20 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 38 VVIKDGKI---VYAGQHTDDYDAtetIDASGKVVSPALVDAHTHLTFGgsreHEMslKRQGKSyleilemGG---GILST 111
Cdd:PRK07583 43 IEIADGKIaaiLPAGGAPDELPA---VDLKGRMVWPCFVDMHTHLDKG----HIW--PRSPNP-------DGtfpGALDA 106
|
90 100 110
....*....|....*....|....*....|...
gi 612671876 112 VNATRET--SEDDLFKKAEHDLLTMIKHGVLAV 142
Cdd:PRK07583 107 VTADREAhwSAEDLYRRMEFGLRCAYAHGTSAI 139
|
|
| PRK09061 |
PRK09061 |
D-glutamate deacylase; Validated |
38-78 |
1.56e-04 |
|
D-glutamate deacylase; Validated
Pssm-ID: 236369 [Multi-domain] Cd Length: 509 Bit Score: 43.92 E-value: 1.56e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 612671876 38 VVIKDGKIVYAGqhTDDYDATETIDASGKVVSPALVDAHTH 78
Cdd:PRK09061 41 VGIKGGKIAAVG--TAAIEGDRTIDATGLVVAPGFIDLHAH 79
|
|
| PRK07572 |
PRK07572 |
cytosine deaminase; Validated |
40-85 |
1.89e-04 |
|
cytosine deaminase; Validated
Pssm-ID: 181039 Cd Length: 426 Bit Score: 43.47 E-value: 1.89e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 612671876 40 IKDGKIVYAGQHTDDyDATETIDASGKVVSPALVDAHTH----LTFGGSR 85
Cdd:PRK07572 22 IAGGRIAAVEPGLQA-EAAEEIDAAGRLVSPPFVDPHFHmdatLSYGLPR 70
|
|
| FMDH_A |
cd01304 |
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive ... |
33-78 |
2.66e-04 |
|
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: 43.17 E-value: 2.66e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 33 VKNGTVV--------------IKDGKIVyagQHTDDYDATETIDASGKVVSPALVDAHTH 78
Cdd:cd01304 1 IKNGTVYdplngingekmdifIRDGKIV---ESSSGAKPAKVIDASGKVVMAGGVDMHSH 57
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
35-79 |
2.85e-04 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 42.92 E-value: 2.85e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 612671876 35 NGTVVIKDGKIVY---AGQHTDDYDatETIDASGKVVSPALVDAHTHL 79
Cdd:PRK08203 23 DGGLVVEGGRIVEvgpGGALPQPAD--EVFDARGHVVTPGLVNTHHHF 68
|
|
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
1-77 |
3.54e-04 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 42.47 E-value: 3.54e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 612671876 1 MNDLIINHiAELILPrstdkplkgkelDElnvVKNGTVVIKDGKIVYAGQhtDDYDATETIDASGKVVSPALVDAHT 77
Cdd:PRK15446 1 MMEMILSN-ARLVLP------------DE---VVDGSLLIEDGRIAAIDP--GASALPGAIDAEGDYLLPGLVDLHT 59
|
|
| PRK09059 |
PRK09059 |
dihydroorotase; Validated |
36-87 |
3.72e-04 |
|
dihydroorotase; Validated
Pssm-ID: 181631 [Multi-domain] Cd Length: 429 Bit Score: 42.33 E-value: 3.72e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 612671876 36 GTVVIKDGKIVYAGQHTDDY---DATETIDASGKVVSPALVDAHTHLTFGGSrEH 87
Cdd:PRK09059 23 GTVLIEDGVIVAAGKGAGNQgapEGAEIVDCAGKAVAPGLVDARVFVGEPGA-EH 76
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
31-92 |
4.95e-04 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 41.95 E-value: 4.95e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 612671876 31 NVVKNGTVVIKDGKIVYAGQHTDDYDATETIDASGKVVSPALVDAHTHLtfggsREHEMSLK 92
Cdd:PRK02382 15 NSLQPRDVRIDGGKITAVGKDLDGSSSEEVIDARGMLLLPGGIDVHVHF-----REPGYTHK 71
|
|
| Met_dep_hydrolase_A |
cd01299 |
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ... |
59-86 |
5.17e-04 |
|
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: 41.90 E-value: 5.17e-04
10 20
....*....|....*....|....*...
gi 612671876 59 ETIDASGKVVSPALVDAHTHLTFGGSRE 86
Cdd:cd01299 2 QVIDLGGKTLMPGLIDAHTHLGSDPGDL 29
|
|
| Isoaspartyl-dipeptidase |
cd01308 |
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
22-93 |
7.03e-04 |
|
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of the degradative pathway to eliminate proteins with beta-L-isoaspartyl peptide bonds, bonds whereby the beta-group of an aspartate forms the peptide link with the amino group of the following amino acid. Formation of this bond is a spontaneous nonenzymatic reaction in nature and can profoundly effect the function of the protein. Isoaspartyl dipeptidase is an octameric enzyme that contains a binuclear zinc center in the active site of each subunit and shows a strong preference of hydrolyzing Asp-Leu dipeptides.
Pssm-ID: 238633 [Multi-domain] Cd Length: 387 Bit Score: 41.61 E-value: 7.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 22 LKGKELDELNVVKNGTVVIKDGKI--VYAGQHTDDYDATETIDASGKVVSPALVDAHTHLTFGG------SREHEMSLKR 93
Cdd:cd01308 4 IKNAEVYAPEYLGKKDILIAGGKIlaIEDQLNLPGYENVTVVDLHGKILVPGFIDQHVHIIGGGgeggpsTRTPEVTLSD 83
|
|
| PLN02942 |
PLN02942 |
dihydropyrimidinase |
32-79 |
7.26e-04 |
|
dihydropyrimidinase
Pssm-ID: 178530 Cd Length: 486 Bit Score: 41.75 E-value: 7.26e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 612671876 32 VVKNGTVV-----------IKDGKIVYAGQHTDDYDATETIDASGKVVSPALVDAHTHL 79
Cdd:PLN02942 8 LIKGGTVVnahhqeladvyVEDGIIVAVAPNLKVPDDVRVIDATGKFVMPGGIDPHTHL 66
|
|
| PRK10027 |
PRK10027 |
cryptic adenine deaminase; Provisional |
36-79 |
1.06e-03 |
|
cryptic adenine deaminase; Provisional
Pssm-ID: 182201 [Multi-domain] Cd Length: 588 Bit Score: 41.35 E-value: 1.06e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 612671876 36 GTVVIKDGKIVYAGQHTDDYDATETIDASGKVVSPALVDAHTHL 79
Cdd:PRK10027 50 GPIVIKGRYIAGVGAEYADAPALQRIDARGATAVPGFIDAHLHI 93
|
|
| AdeC |
cd01295 |
Adenine deaminase (AdeC) directly deaminates adenine to form hypoxanthine. This reaction is ... |
62-405 |
2.13e-03 |
|
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: 39.90 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 62 DASGKVVSPALVDAHTHltfggsrehemslkrqgksyleilemgggILSTVNATREtseddlFKKAehdlltMIKHGVLA 141
Cdd:cd01295 1 DAEGKYIVPGFIDAHLH-----------------------------IESSMLTPSE------FAKA------VLPHGTTT 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 142 VESK-------SGygldreneLKQLKVSNRLAEKYDLDMkhtFLG-PHAVPKE-ASSNEAFL--EEMIALL--PEVKQYA 208
Cdd:cd01295 40 VIADpheianvAG--------VDGIEFMLEDAKKTPLDI---FWMlPSCVPATpFETSGAELtaEDIKELLehPEVVGLG 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 209 DFADIFcetGVFTIEQSQHY-MQKAKEAGFKVKIHAdeidP-LGGLELAIDEQA-ISADHLVASSDKGKEKLRN------ 279
Cdd:cd01295 109 EVMDFP---GVIEGDDEMLAkIQAAKKAGKPVDGHA----PgLSGEELNAYMAAgISTDHEAMTGEEALEKLRLgmyvml 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671876 280 -----SDTVAVLLPATTfylgkEDYADaRGMLDNNGaiALATDYNPGSSVTNNLQLvmaiaALKLKLSPNEVWNAVTVNA 354
Cdd:cd01295 182 regsiAKNLEALLPAIT-----EKNFR-RFMFCTDD--VHPDDLLSEGHLDYIVRR-----AIEAGIPPEDAIQMATINP 248
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 612671876 355 AKAIDI-NAGTINTGDKANLVIWDAPNHeyipyhfgiNHAEKVIKDGKVIVD 405
Cdd:cd01295 249 AECYGLhDLGAIAPGRIADIVILDDLEN---------FNITTVLAKGIAVVE 291
|
|
| PRK06151 |
PRK06151 |
N-ethylammeline chlorohydrolase; Provisional |
34-78 |
4.34e-03 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180428 [Multi-domain] Cd Length: 488 Bit Score: 39.25 E-value: 4.34e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 612671876 34 KNGTVVIKDGKIVYAGQHTDDyDATETIDASGKVVSPALVDAHTH 78
Cdd:PRK06151 22 RDGEVVFEGDRILFVGHRFDG-EVDRVIDAGNALVGPGFIDLDAL 65
|
|
| GDEase |
cd01303 |
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ... |
17-78 |
4.51e-03 |
|
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the conversion of guanine to xanthine and ammonia, the first step to utilize guanine as a nitrogen source. This reaction also removes the guanine base from the pool and therefore can play a role in the regulation of cellular GTP and the guanylate nucleotide pool.
Pssm-ID: 238628 [Multi-domain] Cd Length: 429 Bit Score: 39.18 E-value: 4.51e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 612671876 17 STDKPLKGKELDELNVVKNGTVVIKDGKIVYAGQHTDDY----DATETIDASGKVVSPALVDAHTH 78
Cdd:cd01303 8 TKSLPELELVEDALRVVEDGLIVVVDGNIIAAGAAETLKraakPGARVIDSPNQFILPGFIDTHIH 73
|
|
| |
