|
Name |
Accession |
Description |
Interval |
E-value |
| PRK06846 |
PRK06846 |
putative deaminase; Validated |
49-460 |
0e+00 |
|
putative deaminase; Validated
Pssm-ID: 235873 [Multi-domain] Cd Length: 410 Bit Score: 731.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587782 49 ITDPHYYLDNVLLETGFDYENGVAVQTRTARQTVEIQDGKIVALRENKQHPDATLPHYDAGGKLMLPTTRDMHIHLDKTF 128
Cdd:PRK06846 1 ITDPHYWLTNVRLETGFDYENGVIVQTETALCTLEIQDGKIVAIRPNKQVPDATLPTYDANGLLMLPAFREMHIHLDKTY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587782 129 YGGPWRSLnRPAgTTIQDMIKLEQKMLPELQPYTQERAEKLIDLLQSKGTTIARSHCNIEPVSGLKNLQNLQAVLARRQA 208
Cdd:PRK06846 81 YGGPWKAC-RPA-KTIQDRIELEQKELPELLPTTQERAEKLIELLQSKGATHIRSHCNIDPVIGLKNLENLQAALERYKD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587782 209 GFECEIVAFPQHGLLLSKSEPLMREAMQAGAHYVGGLDPTSVDGAMEKSLDTMFQIALDYDKGVDIHLHETTPAGVAAIN 288
Cdd:PRK06846 159 GFTYEIVAFPQHGLLRSNSEPLMREAMKMGAHLVGGVDPASVDGAIEKSLDTMFQIAVDFNKGVDIHLHDTGPLGVATIK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587782 289 YMVETVEKTpQLKGKLTISHAFALATLNEQQVDELAHRMAAQQISIASTVPIGTLHMPLKQLHDKGVKVMTGTDSVIDHW 368
Cdd:PRK06846 239 YLVETTEEA-QWKGKVTISHAFALGDLNEEEVEELAERLAAQGISITSTVPIGRLHMPIPLLHDKGVKVSLGTDSVIDHW 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587782 369 SPYGLGDMLEKANLYAQLYIRPNEQNLSRSLFLATGDVLPLNEKGERVWPKAQDDASFVLVDASCSAEAVARISPRTATF 448
Cdd:PRK06846 318 SPFGTGDMLEKANLLAELYRWSDERSLSRSLALATGGVLPLNDEGERVWPKVGDEASFVLVDASCSAEAVARQSPRTAVF 397
|
410
....*....|..
gi 446587782 449 HKGQLVWGSVAG 460
Cdd:PRK06846 398 HKGQLVAGSLAG 409
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
55-454 |
1.39e-148 |
|
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: 428.97 E-value: 1.39e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587782 55 YLDNVLLETGfdyengvavqtRTARQTVEIQDGKIVALRENKQHPDAtLPHYDAGGKLMLPTTRDMHIHLDKTFYGGPWR 134
Cdd:cd01293 1 LLRNARLADG-----------GTALVDIAIEDGRIAAIGPALAVPPD-AEEVDAKGRLVLPAFVDPHIHLDKTFTGGRWP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587782 135 SLNRpaGTTIQDMIKLEQKMLPELQPYTQERAEKLIDLLQSKGTTIARSHCNIEPVSGLKNLQNLQAVLARRQAGFECEI 214
Cdd:cd01293 69 NNSG--GTLLEAIIAWEERKLLLTAEDVKERAERALELAIAHGTTAIRTHVDVDPAAGLKALEALLELREEWADLIDLQI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587782 215 VAFPQHGLLLSK-SEPLMREAMQAGAHYVGGLDPTSVDGAMEKSLDTMFQIALDYDKGVDIHLHETTPAGVAAINYMVET 293
Cdd:cd01293 147 VAFPQHGLLSTPgGEELMREALKMGADVVGGIPPAEIDEDGEESLDTLFELAQEHGLDIDLHLDETDDPGSRTLEELAEE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587782 294 VEKTPqLKGKLTISHAFALATLNEQQVDELAHRMAAQQISIASTVPIG-------------TLHMPLKQLHDKGVKVMTG 360
Cdd:cd01293 227 AERRG-MQGRVTCSHATALGSLPEAEVSRLADLLAEAGISVVSLPPINlylqgredttpkrRGVTPVKELRAAGVNVALG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587782 361 TDSVIDHWSPYGLGDMLEKANLYAQLYIRPNEQNLSRSLFLATGDVLPLNEKgERVWPKAQDDASFVLVDASCSAEAVAR 440
Cdd:cd01293 306 SDNVRDPWYPFGSGDMLEVANLAAHIAQLGTPEDLALALDLITGNAARALGL-EDYGIKVGCPADLVLLDAEDVAEAVAR 384
|
410
....*....|....
gi 446587782 441 ISPRTATFHKGQLV 454
Cdd:cd01293 385 QPPRRVVIRKGRVV 398
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
158-454 |
1.22e-07 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 53.69 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587782 158 LQPYTQERAEKLID--LLQSKGTTIARSHCNIEPVSGLKNLQNLQAVLArrqAGFECEIVAFPQHGLLLSKSEPLMREAM 235
Cdd:pfam07969 141 PPLLAREAEAAAVAaaLAALPGFGITSVDGGGGNVHSLDDYEPLRELTA---AEKLKELLDAPERLGLPHSIYELRIGAM 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587782 236 QAGAHYVGGLDPTSVDGAMEKSLDTMFQ----------IALDYDKGVDIHLHettPAGVAAINYMVETVEKTPQ---LKG 302
Cdd:pfam07969 218 KLFADGVLGSRTAALTEPYFDAPGTGWPdfedealaelVAAARERGLDVAIH---AIGDATIDTALDAFEAVAEklgNQG 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587782 303 KLTISHAFALATLNEQQVDELAHRMAAQQISIASTVPIGTLHM------------PLKQLHDKGVKVMTGTDS---VIDH 367
Cdd:pfam07969 295 RVRIEHAQGVVPYTYSQIERVAALGGAAGVQPVFDPLWGDWLQdrlgaerargltPVKELLNAGVKVALGSDApvgPFDP 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587782 368 WSPYGLGDMLEKANLYAqLYIRPNEQNLSRSLFLATGDV-LPLNEKGERVWPKAQDDASFVLVDA---SCSAEAVARISP 443
Cdd:pfam07969 375 WPRIGAAVMRQTAGGGE-VLGPDEELSLEEALALYTSGPaKALGLEDRKGTLGVGKDADLVVLDDdplTVDPPAIADIRV 453
|
330
....*....|.
gi 446587782 444 RtATFHKGQLV 454
Cdd:pfam07969 454 R-LTVVDGRVV 463
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK06846 |
PRK06846 |
putative deaminase; Validated |
49-460 |
0e+00 |
|
putative deaminase; Validated
Pssm-ID: 235873 [Multi-domain] Cd Length: 410 Bit Score: 731.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587782 49 ITDPHYYLDNVLLETGFDYENGVAVQTRTARQTVEIQDGKIVALRENKQHPDATLPHYDAGGKLMLPTTRDMHIHLDKTF 128
Cdd:PRK06846 1 ITDPHYWLTNVRLETGFDYENGVIVQTETALCTLEIQDGKIVAIRPNKQVPDATLPTYDANGLLMLPAFREMHIHLDKTY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587782 129 YGGPWRSLnRPAgTTIQDMIKLEQKMLPELQPYTQERAEKLIDLLQSKGTTIARSHCNIEPVSGLKNLQNLQAVLARRQA 208
Cdd:PRK06846 81 YGGPWKAC-RPA-KTIQDRIELEQKELPELLPTTQERAEKLIELLQSKGATHIRSHCNIDPVIGLKNLENLQAALERYKD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587782 209 GFECEIVAFPQHGLLLSKSEPLMREAMQAGAHYVGGLDPTSVDGAMEKSLDTMFQIALDYDKGVDIHLHETTPAGVAAIN 288
Cdd:PRK06846 159 GFTYEIVAFPQHGLLRSNSEPLMREAMKMGAHLVGGVDPASVDGAIEKSLDTMFQIAVDFNKGVDIHLHDTGPLGVATIK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587782 289 YMVETVEKTpQLKGKLTISHAFALATLNEQQVDELAHRMAAQQISIASTVPIGTLHMPLKQLHDKGVKVMTGTDSVIDHW 368
Cdd:PRK06846 239 YLVETTEEA-QWKGKVTISHAFALGDLNEEEVEELAERLAAQGISITSTVPIGRLHMPIPLLHDKGVKVSLGTDSVIDHW 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587782 369 SPYGLGDMLEKANLYAQLYIRPNEQNLSRSLFLATGDVLPLNEKGERVWPKAQDDASFVLVDASCSAEAVARISPRTATF 448
Cdd:PRK06846 318 SPFGTGDMLEKANLLAELYRWSDERSLSRSLALATGGVLPLNDEGERVWPKVGDEASFVLVDASCSAEAVARQSPRTAVF 397
|
410
....*....|..
gi 446587782 449 HKGQLVWGSVAG 460
Cdd:PRK06846 398 HKGQLVAGSLAG 409
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
55-454 |
1.39e-148 |
|
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: 428.97 E-value: 1.39e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587782 55 YLDNVLLETGfdyengvavqtRTARQTVEIQDGKIVALRENKQHPDAtLPHYDAGGKLMLPTTRDMHIHLDKTFYGGPWR 134
Cdd:cd01293 1 LLRNARLADG-----------GTALVDIAIEDGRIAAIGPALAVPPD-AEEVDAKGRLVLPAFVDPHIHLDKTFTGGRWP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587782 135 SLNRpaGTTIQDMIKLEQKMLPELQPYTQERAEKLIDLLQSKGTTIARSHCNIEPVSGLKNLQNLQAVLARRQAGFECEI 214
Cdd:cd01293 69 NNSG--GTLLEAIIAWEERKLLLTAEDVKERAERALELAIAHGTTAIRTHVDVDPAAGLKALEALLELREEWADLIDLQI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587782 215 VAFPQHGLLLSK-SEPLMREAMQAGAHYVGGLDPTSVDGAMEKSLDTMFQIALDYDKGVDIHLHETTPAGVAAINYMVET 293
Cdd:cd01293 147 VAFPQHGLLSTPgGEELMREALKMGADVVGGIPPAEIDEDGEESLDTLFELAQEHGLDIDLHLDETDDPGSRTLEELAEE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587782 294 VEKTPqLKGKLTISHAFALATLNEQQVDELAHRMAAQQISIASTVPIG-------------TLHMPLKQLHDKGVKVMTG 360
Cdd:cd01293 227 AERRG-MQGRVTCSHATALGSLPEAEVSRLADLLAEAGISVVSLPPINlylqgredttpkrRGVTPVKELRAAGVNVALG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587782 361 TDSVIDHWSPYGLGDMLEKANLYAQLYIRPNEQNLSRSLFLATGDVLPLNEKgERVWPKAQDDASFVLVDASCSAEAVAR 440
Cdd:cd01293 306 SDNVRDPWYPFGSGDMLEVANLAAHIAQLGTPEDLALALDLITGNAARALGL-EDYGIKVGCPADLVLLDAEDVAEAVAR 384
|
410
....*....|....
gi 446587782 441 ISPRTATFHKGQLV 454
Cdd:cd01293 385 QPPRRVVIRKGRVV 398
|
|
| PRK05985 |
PRK05985 |
cytosine deaminase; Provisional |
78-454 |
1.38e-90 |
|
cytosine deaminase; Provisional
Pssm-ID: 180337 [Multi-domain] Cd Length: 391 Bit Score: 280.67 E-value: 1.38e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587782 78 ARQTVEIQDGKIVALRENKQHPdATLPHYDAGGKLMLPTTRDMHIHLDKTFYGGPWRSlNRPaGTTIQDMIKLEQKMLPE 157
Cdd:PRK05985 15 AAVDILIRDGRIAAIGPALAAP-PGAEVEDGGGALALPGLVDGHIHLDKTFWGDPWYP-NEP-GPSLRERIANERRRRAA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587782 158 LQPYTQERAEKLIDLLQSKGTTIARSHCNIEPVSGLKNLQnlqAVLARRQA---GFECEIVAFPQHGLLLSK-SEPLMRE 233
Cdd:PRK05985 92 SGHPAAERALALARAAAAAGTTAMRSHVDVDPDAGLRHLE---AVLAARETlrgLIDIQIVAFPQSGVLSRPgTAELLDA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587782 234 AMQAGAHYVGGLDPTSVDGAMEKSLDTMFQIALDYDKGVDIHLHETTPAGVAAINYMVETVeKTPQLKGKLTISHAFALA 313
Cdd:PRK05985 169 ALRAGADVVGGLDPAGIDGDPEGQLDIVFGLAERHGVGIDIHLHEPGELGAFQLERIAART-RALGMQGRVAVSHAFCLG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587782 314 TLNEQQVDELAHRMAAQQISIASTVPIGTLHMPLKQLHDKGVKVMTGTDSVIDHWSPYGLGDMLEKANLYAQLYIRPNEQ 393
Cdd:PRK05985 248 DLPEREVDRLAERLAEAGVAIMTNAPGSVPVPPVAALRAAGVTVFGGNDGIRDTWWPYGNGDMLERAMLIGYRSGFRTDD 327
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446587782 394 NLSRSLFLATG---DVLPLNEKGERVwpkaQDDASFVLVDASCSAEAVARISPRTATFHKGQLV 454
Cdd:PRK05985 328 ELAAALDCVTHggaRALGLEDYGLAV----GARADFVLVDAETVAEAVVAVPVRRLVVRGGRIV 387
|
|
| PRK07572 |
PRK07572 |
cytosine deaminase; Validated |
84-454 |
4.03e-22 |
|
cytosine deaminase; Validated
Pssm-ID: 181039 Cd Length: 426 Bit Score: 98.17 E-value: 4.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587782 84 IQDGKIVALRENKQHPDATLphYDAGGKLMLPTTRDMHIHLDKTF-YGGPwrSLNRpAGTTIQDmIKLEQKMLPELqpyT 162
Cdd:PRK07572 22 IAGGRIAAVEPGLQAEAAEE--IDAAGRLVSPPFVDPHFHMDATLsYGLP--RVNA-SGTLLEG-IALWGELKPLL---T 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587782 163 QE----RAEKLIDLLQSKGTTIARSHCNI-EPvsGLKNLQNLQAVLARRQAGFECEIVAFPQHGLLLSK-SEPLMREAMQ 236
Cdd:PRK07572 93 QEalveRALRYCDWAVARGLLAIRSHVDVcDP--RLLAVEALLEVRERVAPYLDLQLVAFPQDGVLRSPgAVDNLERALD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587782 237 AGAHYVGGL---DPTSVDGAmeKSLDTMFQIALDYDKGVDIHLHETT-PagvaaINYMVETVEKTPQ---LKGKLTISHA 309
Cdd:PRK07572 171 MGVDVVGGIphfERTMADGA--ESVRLLCEIAAERGLRVDMHCDESDdP-----LSRHIETLAAETQrlgLQGRVAGSHL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587782 310 FALATLNEQQVDELAHRMAAQQISIastVPIGTLHMPLKQLHDK----------------GVKVMTGTDSVIDHWSPYGL 373
Cdd:PRK07572 244 TSMHSMDNYYVSKLIPLMAEAGVNA---IANPLINITLQGRHDTypkrrgmtrvpelmaaGINVAFGHDCVMDPWYSLGS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587782 374 GDMLEKANL---YAQLyirpNEQNLSRSLFLA----TGDVLPLNEKGERVwpkaQDDASFVLVDASCSAEAVaRISP-RT 445
Cdd:PRK07572 321 GDMLEVAHMglhVAQM----TGQDAMRACFDAvtvnPARIMGLEGYGLEP----GCNADLVLLQARDPIEAI-RLRAaRL 391
|
....*....
gi 446587782 446 ATFHKGQLV 454
Cdd:PRK07572 392 AVIRRGKVI 400
|
|
| PRK09230 |
PRK09230 |
cytosine deaminase; Provisional |
69-378 |
3.41e-18 |
|
cytosine deaminase; Provisional
Pssm-ID: 181713 Cd Length: 426 Bit Score: 86.29 E-value: 3.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587782 69 NGVAVQTRTARQTVEIQDGKIVALRENKQHPDATLPHYDAGGKLMLPTTRDMHIHLDKTFYGGP--W-----------RS 135
Cdd:PRK09230 9 KNARLPGKEGLWQITIEDGKISAIEPQSEASLEAGEVLDAEGGLAIPPFIEPHIHLDTTQTAGEpnWnqsgtlfegieRW 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587782 136 LNRPAGTTIQDMikleqkmlpelqpytQERAEKLIDLLQSKGTTIARSHCNI-EPvsglkNLQNLQAVLARRQAG---FE 211
Cdd:PRK09230 89 AERKALLTHEDV---------------KQRAWQTLKWQIANGIQHVRTHVDVsDP-----TLTALKAMLEVKEEVapwVD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587782 212 CEIVAFPQHGLL-LSKSEPLMREAMQAGAHYVGGL---DPTSVDGAmeKSLDTMFQIALDYDKGVDIHLHETTPAGvaai 287
Cdd:PRK09230 149 LQIVAFPQEGILsYPNGEALLEEALRLGADVVGAIphfEFTREYGV--ESLHKAFALAQKYDRLIDVHCDEIDDEQ---- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587782 288 NYMVETVEKTP---QLKGKLTISHAFALATLNEQQVDELAHRMAAQQISIASTvPIGTLHMP--------------LKQL 350
Cdd:PRK09230 223 SRFVETVAALAhreGMGARVTASHTTAMHSYNGAYTSRLFRLLKMSGINFVAN-PLVNIHLQgrfdtypkrrgitrVKEM 301
|
330 340
....*....|....*....|....*...
gi 446587782 351 HDKGVKVMTGTDSVIDHWSPYGLGDMLE 378
Cdd:PRK09230 302 LEAGINVCFGHDDVFDPWYPLGTANMLQ 329
|
|
| PRK07583 |
PRK07583 |
cytosine deaminase; |
82-378 |
1.15e-09 |
|
cytosine deaminase;
Pssm-ID: 236062 Cd Length: 438 Bit Score: 60.00 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587782 82 VEIQDGKIVALRENKQHPDaTLPHYDAGGKLMLPTTRDMHIHLDKtfyGGPW-RSLNrPAGTTIQdmikleqkmlpELQP 160
Cdd:PRK07583 43 IEIADGKIAAILPAGGAPD-ELPAVDLKGRMVWPCFVDMHTHLDK---GHIWpRSPN-PDGTFPG-----------ALDA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587782 161 YTQERAE--KLIDL-------LQSK---GTTIARSHCN-IEPVSG--LKNLQNLQAVLARR---QAgfeceIVAFPQHGL 222
Cdd:PRK07583 107 VTADREAhwSAEDLyrrmefgLRCAyahGTSAIRTHLDsFAPQAAisWEVFAELREAWAGRialQA-----VSLVPLDAY 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587782 223 LLSKSEPLMREAMQAGAhYVGGLDPTSVDgaMEKSLDTMFQIALDYDKGVDIHLHETTPAGVAAINYMVETVEKTpQLKG 302
Cdd:PRK07583 182 LTDAGERLADLVAEAGG-LLGGVTYMNPD--LDAQLDRLFRLARERGLDLDLHVDETGDPASRTLKAVAEAALRN-GFEG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587782 303 KLTISHAFALATLNEQQVDELAHRMAAQQISIAStVPIGTLHM---------------PLKQLHDKGVKVMTGTDSVIDH 367
Cdd:PRK07583 258 KVTCGHCCSLAVQPEEQAQATIALVAEAGIAIVS-LPMCNLYLqdrqpgrtprwrgvtLVHELKAAGIPVAVASDNCRDP 336
|
330
....*....|.
gi 446587782 368 WSPYGLGDMLE 378
Cdd:PRK07583 337 FYAYGDHDMLE 347
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
158-454 |
1.22e-07 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 53.69 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587782 158 LQPYTQERAEKLID--LLQSKGTTIARSHCNIEPVSGLKNLQNLQAVLArrqAGFECEIVAFPQHGLLLSKSEPLMREAM 235
Cdd:pfam07969 141 PPLLAREAEAAAVAaaLAALPGFGITSVDGGGGNVHSLDDYEPLRELTA---AEKLKELLDAPERLGLPHSIYELRIGAM 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587782 236 QAGAHYVGGLDPTSVDGAMEKSLDTMFQ----------IALDYDKGVDIHLHettPAGVAAINYMVETVEKTPQ---LKG 302
Cdd:pfam07969 218 KLFADGVLGSRTAALTEPYFDAPGTGWPdfedealaelVAAARERGLDVAIH---AIGDATIDTALDAFEAVAEklgNQG 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587782 303 KLTISHAFALATLNEQQVDELAHRMAAQQISIASTVPIGTLHM------------PLKQLHDKGVKVMTGTDS---VIDH 367
Cdd:pfam07969 295 RVRIEHAQGVVPYTYSQIERVAALGGAAGVQPVFDPLWGDWLQdrlgaerargltPVKELLNAGVKVALGSDApvgPFDP 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587782 368 WSPYGLGDMLEKANLYAqLYIRPNEQNLSRSLFLATGDV-LPLNEKGERVWPKAQDDASFVLVDA---SCSAEAVARISP 443
Cdd:pfam07969 375 WPRIGAAVMRQTAGGGE-VLGPDEELSLEEALALYTSGPaKALGLEDRKGTLGVGKDADLVVLDDdplTVDPPAIADIRV 453
|
330
....*....|.
gi 446587782 444 RtATFHKGQLV 454
Cdd:pfam07969 454 R-LTVVDGRVV 463
|
|
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
69-148 |
9.69e-04 |
|
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: 41.43 E-value: 9.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587782 69 NGVAVQ-TRTARQTVEIQDGKIVALRENKQhPDATLPHYDAGGKLMLPTTRDMHIHLDKTFYGGP----WRSLNRPA--- 140
Cdd:cd01314 5 NGTIVTaDGSFKADILIEDGKIVAIGPNLE-APGGVEVIDATGKYVLPGGIDPHTHLELPFMGTVtaddFESGTRAAaag 83
|
....*....
gi 446587782 141 GTT-IQDMI 148
Cdd:cd01314 84 GTTtIIDFA 92
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
81-147 |
1.27e-03 |
|
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: 1.27e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446587782 81 TVEIQDGKIVALRENKQHPDATlPHYDAGGKLMLPTTRDMHIHLD---KTFYGGPW---RSLNRPAGTTIQDM 147
Cdd:cd01315 19 DIAVKGGKIAAIGPDIANTEAE-EVIDAGGLVVMPGLIDTHVHINepgRTEWEGFEtgtKAAAAGGITTIIDM 90
|
|
| PRK06886 |
PRK06886 |
hypothetical protein; Validated |
121-376 |
1.85e-03 |
|
hypothetical protein; Validated
Pssm-ID: 180740 Cd Length: 329 Bit Score: 40.20 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587782 121 HIHLDKTFyggpwrsLNRPAGTTIQDMIKLEQK--MLPELQP-YTQE----RAEKLIDLLQSKGTTIARSHCNIEPVSGL 193
Cdd:PRK06886 26 HAHADRAF-------TMTPEKIAIYHYANLQQKwdLVDEVKRnSTVEdyyaRFSQAIELMISQGVTAFGTFVDIDPICED 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587782 194 KNLQNLQAVLARRQAGFECEIVAFPQHGLLLSKSEPLMREAMQAgAHYVGGLdPTSVDGAMEKSLDTMfQIALDYDK--G 271
Cdd:PRK06886 99 RAIIAAHKAREVYKHDIILKFANQTLKGVIEPTAKKWFDIGSEM-VDMIGGL-PYRDELDYGRGLEAM-DILLDTAKslG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587782 272 VDIHLH---ETTPAGVAAINYMVETVEKTPQlkGKLTISHAFALATLNEQQVDELAHRMAAQQISIAStVPIGTLHM--- 345
Cdd:PRK06886 176 KMVHVHvdqFNTPKEKETEQLCDKTIEHGMQ--GRVVAIHGISIGAHSKEYRYRLYQKMREADMMVIA-CPMAWIDSnrk 252
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 446587782 346 -----------PLKQLHDKGVKVMTGTDSVIDHWSPYGLGDM 376
Cdd:PRK06886 253 edlmpfhnaltPADEMIPEGITVALGTDNICDYMVPLCEGDM 294
|
|
| PRK08393 |
PRK08393 |
N-ethylammeline chlorohydrolase; Provisional |
79-387 |
7.40e-03 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 181411 [Multi-domain] Cd Length: 424 Bit Score: 38.63 E-value: 7.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587782 79 RQTVEIQDGKIVALRENKQHPDATLphYDAGGKLMLPTTRDMHIHLDKTFYGGPWRSLnrPAGTTIQDMI-KLEQKMLPE 157
Cdd:PRK08393 20 RADVLIEGNKIVEVKRNINKPADTV--IDASGSVVSPGFINAHTHSPMVLLRGLADDV--PLMEWLQNYIwPRERKLKRK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587782 158 LQPYTQERAekLIDLLQSKGTTIARSHCNIEPVSglknlqnlqavlarrQAGFECEIVAFPQHGLL----LSKSEPLMRE 233
Cdd:PRK08393 96 DIYWGAYLG--LLEMIKSGTTTFVDMYFHMEEVA---------------KATLEVGLRGYLSYGMVdlgdEEKREKEIKE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587782 234 AMQAgAHYVGGLDPTSVDGAMEK------SLDTMFQI---ALDYDKGVDIHLHETTpagvAAINYMVETVEKTPQ----- 299
Cdd:PRK08393 159 TEKL-MEFIEKLNSPRVHFVFGPhapytcSLALLKWVrekAREWNKLITIHLSETM----DEIKQIREKYGKSPVvllde 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587782 300 ---LKGKLTISHAfalATLNEQQVDELAHRMAAQQISIASTVPIGTLHMPLKQLHDKGVKVMTGTDSVIdhwSPYGLgDM 376
Cdd:PRK08393 234 igfLNEDVIAAHG---VWLSSRDIRILASAGVTVAHNPASNMKLGSGVMPLRKLLNAGVNVALGTDGAA---SNNNL-DM 306
|
330
....*....|.
gi 446587782 377 LEKANLYAQLY 387
Cdd:PRK08393 307 LREMKLAALLH 317
|
|
| |
