|
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: 719.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585073 49 ITDPHYYLDNVLLETGFDYENGVAVQTRTARQTVEIQNGKIVALRENKQHPDATLPHYDAGDKLMLPTTRDMHIHLDKTF 128
Cdd:PRK06846 1 ITDPHYWLTNVRLETGFDYENGVIVQTETALCTLEIQDGKIVAIRPNKQVPDATLPTYDANGLLMLPAFREMHIHLDKTY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585073 129 YGGPWRSLnRPAgTTIQDMIKLEQKMLLELQPYTQERAEKLIDLLQSKGTTIARSHCNIEPVSGLKNLQNLQAVLARRQA 208
Cdd:PRK06846 81 YGGPWKAC-RPA-KTIQDRIELEQKELPELLPTTQERAEKLIELLQSKGATHIRSHCNIDPVIGLKNLENLQAALERYKD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585073 209 GFECEIVAFPQHGLLLSKSEPLMREAMQAGAHYVGGLDPTSVDGAMEKSLDTMFQIALDYDKGVDIHLHETTPAGVAAIN 288
Cdd:PRK06846 159 GFTYEIVAFPQHGLLRSNSEPLMREAMKMGAHLVGGVDPASVDGAIEKSLDTMFQIAVDFNKGVDIHLHDTGPLGVATIK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585073 289 YMVETVEKTpQLKGKLTISHAFALATLNEQQVDELANRMVVQQISIASTVPIGTLHMPLKQLHDKGVKVMTGTDSVIDHW 368
Cdd:PRK06846 239 YLVETTEEA-QWKGKVTISHAFALGDLNEEEVEELAERLAAQGISITSTVPIGRLHMPIPLLHDKGVKVSLGTDSVIDHW 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585073 369 SPYGLGDMLEKANLYAQLYIRPNEQNLSRSLFLATGDVLPLNEKGERVWPKAQDDASFVLVDASCSAEAVARISPRTATF 448
Cdd:PRK06846 318 SPFGTGDMLEKANLLAELYRWSDERSLSRSLALATGGVLPLNDEGERVWPKVGDEASFVLVDASCSAEAVARQSPRTAVF 397
|
410
....*....|..
gi 446585073 449 HKGQLVWGSVAG 460
Cdd:PRK06846 398 HKGQLVAGSLAG 409
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
55-454 |
7.91e-146 |
|
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: 422.04 E-value: 7.91e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585073 55 YLDNVLLETGfdyengvavqtRTARQTVEIQNGKIVALRENKQHPDAtLPHYDAGDKLMLPTTRDMHIHLDKTFYGGPWR 134
Cdd:cd01293 1 LLRNARLADG-----------GTALVDIAIEDGRIAAIGPALAVPPD-AEEVDAKGRLVLPAFVDPHIHLDKTFTGGRWP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585073 135 SLNRpaGTTIQDMIKLEQKMLLELQPYTQERAEKLIDLLQSKGTTIARSHCNIEPVSGLKNLQNLQAVLARRQAGFECEI 214
Cdd:cd01293 69 NNSG--GTLLEAIIAWEERKLLLTAEDVKERAERALELAIAHGTTAIRTHVDVDPAAGLKALEALLELREEWADLIDLQI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585073 215 VAFPQHGLLLSK-SEPLMREAMQAGAHYVGGLDPTSVDGAMEKSLDTMFQIALDYDKGVDIHLHETTPAGVAAINYMVET 293
Cdd:cd01293 147 VAFPQHGLLSTPgGEELMREALKMGADVVGGIPPAEIDEDGEESLDTLFELAQEHGLDIDLHLDETDDPGSRTLEELAEE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585073 294 VEKTPqLKGKLTISHAFALATLNEQQVDELANRMVVQQISIASTVPIG-------------TLHMPLKQLHDKGVKVMTG 360
Cdd:cd01293 227 AERRG-MQGRVTCSHATALGSLPEAEVSRLADLLAEAGISVVSLPPINlylqgredttpkrRGVTPVKELRAAGVNVALG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585073 361 TDSVIDHWSPYGLGDMLEKANLYAQLYIRPNEQNLSRSLFLATGDVLPLNEKgERVWPKAQDDASFVLVDASCSAEAVAR 440
Cdd:cd01293 306 SDNVRDPWYPFGSGDMLEVANLAAHIAQLGTPEDLALALDLITGNAARALGL-EDYGIKVGCPADLVLLDAEDVAEAVAR 384
|
410
....*....|....
gi 446585073 441 ISPRTATFHKGQLV 454
Cdd:cd01293 385 QPPRRVVIRKGRVV 398
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
150-454 |
3.09e-08 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 55.62 E-value: 3.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585073 150 LEQKMLLELQPYTQERAEKLID--LLQSKGTTIARSHCNIEPVSGLKNLQNLQAVLArrqAGFECEIVAFPQHGLLLSKS 227
Cdd:pfam07969 133 LREGAYALPPLLAREAEAAAVAaaLAALPGFGITSVDGGGGNVHSLDDYEPLRELTA---AEKLKELLDAPERLGLPHSI 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585073 228 EPLMREAMQAGAHYVGGLDPTSVDGAMEKSLDTMFQ----------IALDYDKGVDIHLHettPAGVAAINYMVETVEKT 297
Cdd:pfam07969 210 YELRIGAMKLFADGVLGSRTAALTEPYFDAPGTGWPdfedealaelVAAARERGLDVAIH---AIGDATIDTALDAFEAV 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585073 298 PQ---LKGKLTISHAFALATLNEQQVDELANRMVVQQISIASTVPIGTLHM------------PLKQLHDKGVKVMTGTD 362
Cdd:pfam07969 287 AEklgNQGRVRIEHAQGVVPYTYSQIERVAALGGAAGVQPVFDPLWGDWLQdrlgaerargltPVKELLNAGVKVALGSD 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585073 363 S---VIDHWSPYGLGDMLEKANLYAqLYIRPNEQNLSRSLFLATGDvlP---LNEKGERVWPKAQDDASFVLVDA---SC 433
Cdd:pfam07969 367 ApvgPFDPWPRIGAAVMRQTAGGGE-VLGPDEELSLEEALALYTSG--PakaLGLEDRKGTLGVGKDADLVVLDDdplTV 443
|
330 340
....*....|....*....|.
gi 446585073 434 SAEAVARISPRtATFHKGQLV 454
Cdd:pfam07969 444 DPPAIADIRVR-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: 719.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585073 49 ITDPHYYLDNVLLETGFDYENGVAVQTRTARQTVEIQNGKIVALRENKQHPDATLPHYDAGDKLMLPTTRDMHIHLDKTF 128
Cdd:PRK06846 1 ITDPHYWLTNVRLETGFDYENGVIVQTETALCTLEIQDGKIVAIRPNKQVPDATLPTYDANGLLMLPAFREMHIHLDKTY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585073 129 YGGPWRSLnRPAgTTIQDMIKLEQKMLLELQPYTQERAEKLIDLLQSKGTTIARSHCNIEPVSGLKNLQNLQAVLARRQA 208
Cdd:PRK06846 81 YGGPWKAC-RPA-KTIQDRIELEQKELPELLPTTQERAEKLIELLQSKGATHIRSHCNIDPVIGLKNLENLQAALERYKD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585073 209 GFECEIVAFPQHGLLLSKSEPLMREAMQAGAHYVGGLDPTSVDGAMEKSLDTMFQIALDYDKGVDIHLHETTPAGVAAIN 288
Cdd:PRK06846 159 GFTYEIVAFPQHGLLRSNSEPLMREAMKMGAHLVGGVDPASVDGAIEKSLDTMFQIAVDFNKGVDIHLHDTGPLGVATIK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585073 289 YMVETVEKTpQLKGKLTISHAFALATLNEQQVDELANRMVVQQISIASTVPIGTLHMPLKQLHDKGVKVMTGTDSVIDHW 368
Cdd:PRK06846 239 YLVETTEEA-QWKGKVTISHAFALGDLNEEEVEELAERLAAQGISITSTVPIGRLHMPIPLLHDKGVKVSLGTDSVIDHW 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585073 369 SPYGLGDMLEKANLYAQLYIRPNEQNLSRSLFLATGDVLPLNEKGERVWPKAQDDASFVLVDASCSAEAVARISPRTATF 448
Cdd:PRK06846 318 SPFGTGDMLEKANLLAELYRWSDERSLSRSLALATGGVLPLNDEGERVWPKVGDEASFVLVDASCSAEAVARQSPRTAVF 397
|
410
....*....|..
gi 446585073 449 HKGQLVWGSVAG 460
Cdd:PRK06846 398 HKGQLVAGSLAG 409
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
55-454 |
7.91e-146 |
|
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: 422.04 E-value: 7.91e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585073 55 YLDNVLLETGfdyengvavqtRTARQTVEIQNGKIVALRENKQHPDAtLPHYDAGDKLMLPTTRDMHIHLDKTFYGGPWR 134
Cdd:cd01293 1 LLRNARLADG-----------GTALVDIAIEDGRIAAIGPALAVPPD-AEEVDAKGRLVLPAFVDPHIHLDKTFTGGRWP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585073 135 SLNRpaGTTIQDMIKLEQKMLLELQPYTQERAEKLIDLLQSKGTTIARSHCNIEPVSGLKNLQNLQAVLARRQAGFECEI 214
Cdd:cd01293 69 NNSG--GTLLEAIIAWEERKLLLTAEDVKERAERALELAIAHGTTAIRTHVDVDPAAGLKALEALLELREEWADLIDLQI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585073 215 VAFPQHGLLLSK-SEPLMREAMQAGAHYVGGLDPTSVDGAMEKSLDTMFQIALDYDKGVDIHLHETTPAGVAAINYMVET 293
Cdd:cd01293 147 VAFPQHGLLSTPgGEELMREALKMGADVVGGIPPAEIDEDGEESLDTLFELAQEHGLDIDLHLDETDDPGSRTLEELAEE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585073 294 VEKTPqLKGKLTISHAFALATLNEQQVDELANRMVVQQISIASTVPIG-------------TLHMPLKQLHDKGVKVMTG 360
Cdd:cd01293 227 AERRG-MQGRVTCSHATALGSLPEAEVSRLADLLAEAGISVVSLPPINlylqgredttpkrRGVTPVKELRAAGVNVALG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585073 361 TDSVIDHWSPYGLGDMLEKANLYAQLYIRPNEQNLSRSLFLATGDVLPLNEKgERVWPKAQDDASFVLVDASCSAEAVAR 440
Cdd:cd01293 306 SDNVRDPWYPFGSGDMLEVANLAAHIAQLGTPEDLALALDLITGNAARALGL-EDYGIKVGCPADLVLLDAEDVAEAVAR 384
|
410
....*....|....
gi 446585073 441 ISPRTATFHKGQLV 454
Cdd:cd01293 385 QPPRRVVIRKGRVV 398
|
|
| PRK05985 |
PRK05985 |
cytosine deaminase; Provisional |
78-454 |
6.86e-89 |
|
cytosine deaminase; Provisional
Pssm-ID: 180337 [Multi-domain] Cd Length: 391 Bit Score: 276.04 E-value: 6.86e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585073 78 ARQTVEIQNGKIVALRENKQHPdATLPHYDAGDKLMLPTTRDMHIHLDKTFYGGPWRSlNRPaGTTIQDMIKLEQKMLLE 157
Cdd:PRK05985 15 AAVDILIRDGRIAAIGPALAAP-PGAEVEDGGGALALPGLVDGHIHLDKTFWGDPWYP-NEP-GPSLRERIANERRRRAA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585073 158 LQPYTQERAEKLIDLLQSKGTTIARSHCNIEPVSGLKNLQnlqAVLARRQA---GFECEIVAFPQHGLLLSK-SEPLMRE 233
Cdd:PRK05985 92 SGHPAAERALALARAAAAAGTTAMRSHVDVDPDAGLRHLE---AVLAARETlrgLIDIQIVAFPQSGVLSRPgTAELLDA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585073 234 AMQAGAHYVGGLDPTSVDGAMEKSLDTMFQIALDYDKGVDIHLHETTPAGVAAINYMVETVeKTPQLKGKLTISHAFALA 313
Cdd:PRK05985 169 ALRAGADVVGGLDPAGIDGDPEGQLDIVFGLAERHGVGIDIHLHEPGELGAFQLERIAART-RALGMQGRVAVSHAFCLG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585073 314 TLNEQQVDELANRMVVQQISIASTVPIGTLHMPLKQLHDKGVKVMTGTDSVIDHWSPYGLGDMLEKANLYAQLYIRPNEQ 393
Cdd:PRK05985 248 DLPEREVDRLAERLAEAGVAIMTNAPGSVPVPPVAALRAAGVTVFGGNDGIRDTWWPYGNGDMLERAMLIGYRSGFRTDD 327
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446585073 394 NLSRSLFLATG---DVLPLNEKGERVwpkaQDDASFVLVDASCSAEAVARISPRTATFHKGQLV 454
Cdd:PRK05985 328 ELAAALDCVTHggaRALGLEDYGLAV----GARADFVLVDAETVAEAVVAVPVRRLVVRGGRIV 387
|
|
| PRK07572 |
PRK07572 |
cytosine deaminase; Validated |
84-454 |
1.79e-19 |
|
cytosine deaminase; Validated
Pssm-ID: 181039 Cd Length: 426 Bit Score: 90.08 E-value: 1.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585073 84 IQNGKIVALRENKQHPDATLphYDAGDKLMLPTTRDMHIHLDKTF-YGGPwrSLNRpAGTTIQDmIKL--EQKMLLelqp 160
Cdd:PRK07572 22 IAGGRIAAVEPGLQAEAAEE--IDAAGRLVSPPFVDPHFHMDATLsYGLP--RVNA-SGTLLEG-IALwgELKPLL---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585073 161 yTQE----RAEKLIDLLQSKGTTIARSHCNI-EPvsGLKNLQNLQAVLARRQAGFECEIVAFPQHGLLLSK-SEPLMREA 234
Cdd:PRK07572 92 -TQEalveRALRYCDWAVARGLLAIRSHVDVcDP--RLLAVEALLEVRERVAPYLDLQLVAFPQDGVLRSPgAVDNLERA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585073 235 MQAGAHYVGGL---DPTSVDGAmeKSLDTMFQIALDYDKGVDIHLHETT-PagvaaINYMVETVEKTPQ---LKGKLTIS 307
Cdd:PRK07572 169 LDMGVDVVGGIphfERTMADGA--ESVRLLCEIAAERGLRVDMHCDESDdP-----LSRHIETLAAETQrlgLQGRVAGS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585073 308 HAFALATLNEQQVDELANRMVVQQISIastVPIGTLHMPLKQLHDK----------------GVKVMTGTDSVIDHWSPY 371
Cdd:PRK07572 242 HLTSMHSMDNYYVSKLIPLMAEAGVNA---IANPLINITLQGRHDTypkrrgmtrvpelmaaGINVAFGHDCVMDPWYSL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585073 372 GLGDMLEKANL---YAQLyirpNEQNLSRSLFLA----TGDVLPLNEKGERVwpkaQDDASFVLVDASCSAEAVaRISP- 443
Cdd:PRK07572 319 GSGDMLEVAHMglhVAQM----TGQDAMRACFDAvtvnPARIMGLEGYGLEP----GCNADLVLLQARDPIEAI-RLRAa 389
|
410
....*....|.
gi 446585073 444 RTATFHKGQLV 454
Cdd:PRK07572 390 RLAVIRRGKVI 400
|
|
| PRK09230 |
PRK09230 |
cytosine deaminase; Provisional |
69-378 |
7.43e-18 |
|
cytosine deaminase; Provisional
Pssm-ID: 181713 Cd Length: 426 Bit Score: 85.52 E-value: 7.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585073 69 NGVAVQTRTARQTVEIQNGKIVALRENKQHPDATLPHYDAGDKLMLPTTRDMHIHLDKTFYGG-PwrSLNRpAGTTIQDM 147
Cdd:PRK09230 9 KNARLPGKEGLWQITIEDGKISAIEPQSEASLEAGEVLDAEGGLAIPPFIEPHIHLDTTQTAGeP--NWNQ-SGTLFEGI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585073 148 IKL-EQKMLLELQPyTQERAEKLIDLLQSKGTTIARSHCNI-EPvsglkNLQNLQAVLARRQAG---FECEIVAFPQHGL 222
Cdd:PRK09230 86 ERWaERKALLTHED-VKQRAWQTLKWQIANGIQHVRTHVDVsDP-----TLTALKAMLEVKEEVapwVDLQIVAFPQEGI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585073 223 L-LSKSEPLMREAMQAGAHYVGGL---DPTSVDGAmeKSLDTMFQIALDYDKGVDIHLHETTPAGvaaiNYMVETVEKTP 298
Cdd:PRK09230 160 LsYPNGEALLEEALRLGADVVGAIphfEFTREYGV--ESLHKAFALAQKYDRLIDVHCDEIDDEQ----SRFVETVAALA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585073 299 ---QLKGKLTISHAFALATLNEQQVDELANRMVVQQISIASTvPIGTLHMP--------------LKQLHDKGVKVMTGT 361
Cdd:PRK09230 234 hreGMGARVTASHTTAMHSYNGAYTSRLFRLLKMSGINFVAN-PLVNIHLQgrfdtypkrrgitrVKEMLEAGINVCFGH 312
|
330
....*....|....*..
gi 446585073 362 DSVIDHWSPYGLGDMLE 378
Cdd:PRK09230 313 DDVFDPWYPLGTANMLQ 329
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
150-454 |
3.09e-08 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 55.62 E-value: 3.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585073 150 LEQKMLLELQPYTQERAEKLID--LLQSKGTTIARSHCNIEPVSGLKNLQNLQAVLArrqAGFECEIVAFPQHGLLLSKS 227
Cdd:pfam07969 133 LREGAYALPPLLAREAEAAAVAaaLAALPGFGITSVDGGGGNVHSLDDYEPLRELTA---AEKLKELLDAPERLGLPHSI 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585073 228 EPLMREAMQAGAHYVGGLDPTSVDGAMEKSLDTMFQ----------IALDYDKGVDIHLHettPAGVAAINYMVETVEKT 297
Cdd:pfam07969 210 YELRIGAMKLFADGVLGSRTAALTEPYFDAPGTGWPdfedealaelVAAARERGLDVAIH---AIGDATIDTALDAFEAV 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585073 298 PQ---LKGKLTISHAFALATLNEQQVDELANRMVVQQISIASTVPIGTLHM------------PLKQLHDKGVKVMTGTD 362
Cdd:pfam07969 287 AEklgNQGRVRIEHAQGVVPYTYSQIERVAALGGAAGVQPVFDPLWGDWLQdrlgaerargltPVKELLNAGVKVALGSD 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585073 363 S---VIDHWSPYGLGDMLEKANLYAqLYIRPNEQNLSRSLFLATGDvlP---LNEKGERVWPKAQDDASFVLVDA---SC 433
Cdd:pfam07969 367 ApvgPFDPWPRIGAAVMRQTAGGGE-VLGPDEELSLEEALALYTSG--PakaLGLEDRKGTLGVGKDADLVVLDDdplTV 443
|
330 340
....*....|....*....|.
gi 446585073 434 SAEAVARISPRtATFHKGQLV 454
Cdd:pfam07969 444 DPPAIADIRVR-LTVVDGRVV 463
|
|
| PRK07583 |
PRK07583 |
cytosine deaminase; |
82-378 |
4.99e-08 |
|
cytosine deaminase;
Pssm-ID: 236062 Cd Length: 438 Bit Score: 54.99 E-value: 4.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585073 82 VEIQNGKIVALRENKQHPDaTLPHYDAGDKLMLPTTRDMHIHLDKtfyGGPW-RSLNrPAGT-------TIQDMIK---- 149
Cdd:PRK07583 43 IEIADGKIAAILPAGGAPD-ELPAVDLKGRMVWPCFVDMHTHLDK---GHIWpRSPN-PDGTfpgaldaVTADREAhwsa 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585073 150 --LEQKMLLELQ-PYTQeraeklidllqskGTTIARSHCN-IEPVSG--LKNLQNLQAVLARR---QAgfeceIVAFPQH 220
Cdd:PRK07583 118 edLYRRMEFGLRcAYAH-------------GTSAIRTHLDsFAPQAAisWEVFAELREAWAGRialQA-----VSLVPLD 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585073 221 GLLLSKSEPLMREAMQAGAhYVGGLDPTSVDgaMEKSLDTMFQIALDYDKGVDIHLHETTPAGVAAINYMVETVEKTpQL 300
Cdd:PRK07583 180 AYLTDAGERLADLVAEAGG-LLGGVTYMNPD--LDAQLDRLFRLARERGLDLDLHVDETGDPASRTLKAVAEAALRN-GF 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585073 301 KGKLTISHAFALATLNEQQVDELANRMVVQQISIAStVPIGTLHM---------------PLKQLHDKGVKVMTGTDSVI 365
Cdd:PRK07583 256 EGKVTCGHCCSLAVQPEEQAQATIALVAEAGIAIVS-LPMCNLYLqdrqpgrtprwrgvtLVHELKAAGIPVAVASDNCR 334
|
330
....*....|...
gi 446585073 366 DHWSPYGLGDMLE 378
Cdd:PRK07583 335 DPFYAYGDHDMLE 347
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
81-147 |
2.43e-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: 39.97 E-value: 2.43e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446585073 81 TVEIQNGKIVALRENKQHPDATlPHYDAGDKLMLPTTRDMHIHLD---KTFYGGPW---RSLNRPAGTTIQDM 147
Cdd:cd01315 19 DIAVKGGKIAAIGPDIANTEAE-EVIDAGGLVVMPGLIDTHVHINepgRTEWEGFEtgtKAAAAGGITTIIDM 90
|
|
| PRK06886 |
PRK06886 |
hypothetical protein; Validated |
121-376 |
5.72e-03 |
|
hypothetical protein; Validated
Pssm-ID: 180740 Cd Length: 329 Bit Score: 38.66 E-value: 5.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585073 121 HIHLDKTFyggpwrsLNRPAGTTIQDMIKLEQKMLL--ELQP-YTQE----RAEKLIDLLQSKGTTIARSHCNIEPVSGL 193
Cdd:PRK06886 26 HAHADRAF-------TMTPEKIAIYHYANLQQKWDLvdEVKRnSTVEdyyaRFSQAIELMISQGVTAFGTFVDIDPICED 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585073 194 KNLQNLQAVLARRQAGFECEIVAFPQHGLLLSKSEPLMREAMQAgAHYVGGLdPTSVDGAMEKSLDTMfQIALDYDK--G 271
Cdd:PRK06886 99 RAIIAAHKAREVYKHDIILKFANQTLKGVIEPTAKKWFDIGSEM-VDMIGGL-PYRDELDYGRGLEAM-DILLDTAKslG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585073 272 VDIHLH---ETTPAGVAAINYMVETVEKTPQlkGKLTISHAFALATLNEQQVDELANRMVVQQISIAStVPIGTLHM--- 345
Cdd:PRK06886 176 KMVHVHvdqFNTPKEKETEQLCDKTIEHGMQ--GRVVAIHGISIGAHSKEYRYRLYQKMREADMMVIA-CPMAWIDSnrk 252
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 446585073 346 -----------PLKQLHDKGVKVMTGTDSVIDHWSPYGLGDM 376
Cdd:PRK06886 253 edlmpfhnaltPADEMIPEGITVALGTDNICDYMVPLCEGDM 294
|
|
| PRK09228 |
PRK09228 |
guanine deaminase; Provisional |
84-191 |
7.82e-03 |
|
guanine deaminase; Provisional
Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 38.63 E-value: 7.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585073 84 IQNGKIVA------LRenKQHP-DATLPHYdaGDKLMLPTTRDMHIHLDKTfyggpwrslnrpagttiqDMIKLEQKMLL 156
Cdd:PRK09228 36 VEDGRIVAagpyaeLR--AQLPaDAEVTDY--RGKLILPGFIDTHIHYPQT------------------DMIASYGEQLL 93
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 446585073 157 E-LQPYT--QER-----------AEKLIDLLQSKGTTIARSHCNIEPVS 191
Cdd:PRK09228 94 DwLNTYTfpEERrfadpayarevAEFFLDELLRNGTTTALVFGTVHPQS 142
|
|
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
69-148 |
8.63e-03 |
|
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: 38.35 E-value: 8.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585073 69 NGVAVQ-TRTARQTVEIQNGKIVALRENKQhPDATLPHYDAGDKLMLPTTRDMHIHLDKTFYGGP----WRSLNRPA--- 140
Cdd:cd01314 5 NGTIVTaDGSFKADILIEDGKIVAIGPNLE-APGGVEVIDATGKYVLPGGIDPHTHLELPFMGTVtaddFESGTRAAaag 83
|
....*....
gi 446585073 141 GTT-IQDMI 148
Cdd:cd01314 84 GTTtIIDFA 92
|
|
| |
