|
Name |
Accession |
Description |
Interval |
E-value |
| PhnP |
COG1235 |
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ... |
22-304 |
1.42e-39 |
|
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism];
Pssm-ID: 440848 [Multi-domain] Cd Length: 259 Bit Score: 139.26 E-value: 1.42e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648339138 22 IVVLGTTQDAGSPQIGCTKACCknLFSKPDQTRQVVSLGLFDPNKKIsyLFEATPDISKQLRLLktfSKTATDLpNGIFL 101
Cdd:COG1235 3 VTFLGSGSSGGVPQIGCDCPVC--ASTDPRYGRTRSSILVEADGTRL--LIDAGPDLREQLLRL---GLDPSKI-DAILL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648339138 102 THAHIGHYTGLIYLGkEAINAKQLPIYAMPKMKTFLEQNGPWSQLVTQQNILIKDLSCNQPLRLSDsLSVTPILVPHRDe 181
Cdd:COG1235 75 THEHADHIAGLDDLR-PRYGPNPIPVYATPGTLEALERRFPYLFAPYPGKLEFHEIEPGEPFEIGG-LTVTPFPVPHDA- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648339138 182 ySETVGYLISGPRKKLLFIPDIdkwEKWNQDINTLIKQVDFALIDAtffdaaeinNRPISEIPHPFVIESMNRFALMPLK 261
Cdd:COG1235 152 -GDPVGYRIEDGGKKLAYATDT---GYIPEEVLELLRGADLLILDA---------TYDDPEPGHLSNEEALELLARLGPK 218
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2648339138 262 ekqKIHFIHFNHTNpllNINS----EASEQILKAGFKTAKQGLKFEL 304
Cdd:COG1235 219 ---RLVLTHLSPDN---NDHEldydELEAALLPAGVEVAYDGMEIEL 259
|
|
| Lactamase_B_2 |
pfam12706 |
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ... |
70-271 |
2.02e-17 |
|
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and is related to pfam00753.
Pssm-ID: 432732 [Multi-domain] Cd Length: 196 Bit Score: 78.51 E-value: 2.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648339138 70 YLFEATPDISKQLRLLKTFSKTATDLPNGIFLTHAHIGHYTGLIYLGKEAinakQLPIYAMPKMKTFLEQNGPWSQLVTQ 149
Cdd:pfam12706 3 ILIDPGPDLRQQALPALQPGRLRDDPIDAVLLTHDHYDHLAGLLDLREGR----PRPLYAPLGVLAHLRRNFPYLFLLEH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648339138 150 QNILIKDLSCNQPLRLSDS-LSVTPILVPH------RDEYSETVGYLISGPRKKLLFIPDIDKWEKwnqDINTLIKQVDF 222
Cdd:pfam12706 79 YGVRVHEIDWGESFTVGDGgLTVTATPARHgsprglDPNPGDTLGFRIEGPGKRVYYAGDTGYFPD---EIGERLGGADL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2648339138 223 ALIDATFFDAAEinnrpISEIPHPFVIESMnRFALMpLKEKQKIhFIHF 271
Cdd:pfam12706 156 LLLDGGAWRDDE-----MIHMGHMTPEEAV-EAAAD-LGARRKV-LIHI 196
|
|
| PRK05184 |
PRK05184 |
pyrroloquinoline quinone biosynthesis protein PqqB; Provisional |
22-304 |
1.29e-13 |
|
pyrroloquinoline quinone biosynthesis protein PqqB; Provisional
Pssm-ID: 235361 [Multi-domain] Cd Length: 302 Bit Score: 69.85 E-value: 1.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648339138 22 IVVLGTTQDAGSPQIGCTKACCKNLFSKPDQTR---Q---VVSlglfdPNKKISYLFEATPDISKQLRllktfsktAT-- 93
Cdd:PRK05184 3 IIVLGSAAGGGFPQWNCNCPNCRGARAGTIRAKprtQssiAVS-----ADGEDWVLLNASPDIRQQIQ--------ATpa 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648339138 94 --------DLP-NGIFLTHAHIGHYTGLIYLgKEainaKQ-LPIYAMPKMKTFLEQNGP------------WSQLVTQQN 151
Cdd:PRK05184 70 lqparglrDTPiAAVVLTDGQIDHTTGLLTL-RE----GQpFPVYATPAVLEDLSTGFPifnvldhyggvqRRPIALDGP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648339138 152 ILIKDLScnqplrlsdSLSVTPILV--------PHRDEYSE--TVGYLISGPR--KKLLFIPDIDKWEkwnQDINTLIKQ 219
Cdd:PRK05184 145 FAVPGLP---------GLRFTAFPVpskappysPHRSDPEPgdNIGLRIEDRAtgKRLFYAPGLAEVT---DALRARLAG 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648339138 220 VDFALIDATFF-------------DAAEINNRPISEiphPF-VIEsmnrfALMPLKEKQKIhFIHFNHTNPLLNINSEAS 285
Cdd:PRK05184 213 ADCVLFDGTLWtddemiragvgtkTGRRMGHLPQSG---PGgMIA-----ALARLPIARKI-LIHINNTNPILDEDSPER 283
|
330
....*....|....*....
gi 2648339138 286 EQILKAGFKTAKQGLKFEL 304
Cdd:PRK05184 284 AELEAAGIEVAHDGMEIEL 302
|
|
| PQQB-like_MBL-fold |
cd16274 |
Coenzyme pyrroloquinoline quinone (PQQ) synthesis protein B and related proteins; MBL-fold ... |
22-209 |
2.79e-11 |
|
Coenzyme pyrroloquinoline quinone (PQQ) synthesis protein B and related proteins; MBL-fold metallo hydrolase domainhydrolase domain; PQQB is essential for the synthesis of the cofactor pyrroloquinoline quinone (PQQ) in Klebsiella pneumonia. PqqB is not directly involved in the PQQ biosynthesis but may serve as a carrier for PQQ when PQQ is released from PqqC. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.
Pssm-ID: 293832 [Multi-domain] Cd Length: 220 Bit Score: 61.87 E-value: 2.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648339138 22 IVVLGTTQDAGSPQIGCTKACCKNLFSKPDQTR---Q---VVSlglfdPNKKISYLFEATPDISKQLRLLKTF--SKTAT 93
Cdd:cd16274 3 IKVLGSAAGGGFPQWNCNCPNCALARAGDGRATartQssiAVS-----ADGENWVLINASPDIRQQIEATPELqpRPGLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648339138 94 DLP-NGIFLTHAHIGHYTGLIYLgKEainAKQLPIYAMPKMKTFLEQNGP------WSQLVTQQNILikdlsCNQPLRLS 166
Cdd:cd16274 78 DTPiAAVLLTDAEIDHTTGLLSL-RE---GQPLTVYATAPVLEDLTTNFPffvllhAYGGVRRHRIL-----PGEPFTLA 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2648339138 167 D--SLSVTPILVP----------HRDEYSETVGYLISGPR--KKLLFIPDIDKWEKW 209
Cdd:cd16274 149 GcpGLTVTPFPVPgkaplysehrDAPEPGDTIGLRIEDGRtgGRLFYAPGCAAVTDE 205
|
|
| Lactamase_B |
smart00849 |
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ... |
96-139 |
6.82e-03 |
|
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins contain this domain. These proteins include thiolesterases, members of the glyoxalase II family, that catalyse the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid and a competence protein that is essential for natural transformation in Neisseria gonorrhoeae and could be a transporter involved in DNA uptake. Except for the competence protein these proteins bind two zinc ions per molecule as cofactor.
Pssm-ID: 214854 [Multi-domain] Cd Length: 177 Bit Score: 36.76 E-value: 6.82e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2648339138 96 PNGIFLTHAHIGHYTGLIYLGKeainAKQLPIYAMPKMKTFLEQ 139
Cdd:smart00849 36 IDAIILTHGHPDHIGGLPELLE----APGAPVYAPEGTAELLKD 75
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PhnP |
COG1235 |
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ... |
22-304 |
1.42e-39 |
|
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism];
Pssm-ID: 440848 [Multi-domain] Cd Length: 259 Bit Score: 139.26 E-value: 1.42e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648339138 22 IVVLGTTQDAGSPQIGCTKACCknLFSKPDQTRQVVSLGLFDPNKKIsyLFEATPDISKQLRLLktfSKTATDLpNGIFL 101
Cdd:COG1235 3 VTFLGSGSSGGVPQIGCDCPVC--ASTDPRYGRTRSSILVEADGTRL--LIDAGPDLREQLLRL---GLDPSKI-DAILL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648339138 102 THAHIGHYTGLIYLGkEAINAKQLPIYAMPKMKTFLEQNGPWSQLVTQQNILIKDLSCNQPLRLSDsLSVTPILVPHRDe 181
Cdd:COG1235 75 THEHADHIAGLDDLR-PRYGPNPIPVYATPGTLEALERRFPYLFAPYPGKLEFHEIEPGEPFEIGG-LTVTPFPVPHDA- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648339138 182 ySETVGYLISGPRKKLLFIPDIdkwEKWNQDINTLIKQVDFALIDAtffdaaeinNRPISEIPHPFVIESMNRFALMPLK 261
Cdd:COG1235 152 -GDPVGYRIEDGGKKLAYATDT---GYIPEEVLELLRGADLLILDA---------TYDDPEPGHLSNEEALELLARLGPK 218
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2648339138 262 ekqKIHFIHFNHTNpllNINS----EASEQILKAGFKTAKQGLKFEL 304
Cdd:COG1235 219 ---RLVLTHLSPDN---NDHEldydELEAALLPAGVEVAYDGMEIEL 259
|
|
| Lactamase_B_2 |
pfam12706 |
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ... |
70-271 |
2.02e-17 |
|
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and is related to pfam00753.
Pssm-ID: 432732 [Multi-domain] Cd Length: 196 Bit Score: 78.51 E-value: 2.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648339138 70 YLFEATPDISKQLRLLKTFSKTATDLPNGIFLTHAHIGHYTGLIYLGKEAinakQLPIYAMPKMKTFLEQNGPWSQLVTQ 149
Cdd:pfam12706 3 ILIDPGPDLRQQALPALQPGRLRDDPIDAVLLTHDHYDHLAGLLDLREGR----PRPLYAPLGVLAHLRRNFPYLFLLEH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648339138 150 QNILIKDLSCNQPLRLSDS-LSVTPILVPH------RDEYSETVGYLISGPRKKLLFIPDIDKWEKwnqDINTLIKQVDF 222
Cdd:pfam12706 79 YGVRVHEIDWGESFTVGDGgLTVTATPARHgsprglDPNPGDTLGFRIEGPGKRVYYAGDTGYFPD---EIGERLGGADL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2648339138 223 ALIDATFFDAAEinnrpISEIPHPFVIESMnRFALMpLKEKQKIhFIHF 271
Cdd:pfam12706 156 LLLDGGAWRDDE-----MIHMGHMTPEEAV-EAAAD-LGARRKV-LIHI 196
|
|
| PRK05184 |
PRK05184 |
pyrroloquinoline quinone biosynthesis protein PqqB; Provisional |
22-304 |
1.29e-13 |
|
pyrroloquinoline quinone biosynthesis protein PqqB; Provisional
Pssm-ID: 235361 [Multi-domain] Cd Length: 302 Bit Score: 69.85 E-value: 1.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648339138 22 IVVLGTTQDAGSPQIGCTKACCKNLFSKPDQTR---Q---VVSlglfdPNKKISYLFEATPDISKQLRllktfsktAT-- 93
Cdd:PRK05184 3 IIVLGSAAGGGFPQWNCNCPNCRGARAGTIRAKprtQssiAVS-----ADGEDWVLLNASPDIRQQIQ--------ATpa 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648339138 94 --------DLP-NGIFLTHAHIGHYTGLIYLgKEainaKQ-LPIYAMPKMKTFLEQNGP------------WSQLVTQQN 151
Cdd:PRK05184 70 lqparglrDTPiAAVVLTDGQIDHTTGLLTL-RE----GQpFPVYATPAVLEDLSTGFPifnvldhyggvqRRPIALDGP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648339138 152 ILIKDLScnqplrlsdSLSVTPILV--------PHRDEYSE--TVGYLISGPR--KKLLFIPDIDKWEkwnQDINTLIKQ 219
Cdd:PRK05184 145 FAVPGLP---------GLRFTAFPVpskappysPHRSDPEPgdNIGLRIEDRAtgKRLFYAPGLAEVT---DALRARLAG 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648339138 220 VDFALIDATFF-------------DAAEINNRPISEiphPF-VIEsmnrfALMPLKEKQKIhFIHFNHTNPLLNINSEAS 285
Cdd:PRK05184 213 ADCVLFDGTLWtddemiragvgtkTGRRMGHLPQSG---PGgMIA-----ALARLPIARKI-LIHINNTNPILDEDSPER 283
|
330
....*....|....*....
gi 2648339138 286 EQILKAGFKTAKQGLKFEL 304
Cdd:PRK05184 284 AELEAAGIEVAHDGMEIEL 302
|
|
| ElaC |
COG1234 |
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis]; |
82-232 |
1.95e-11 |
|
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440847 [Multi-domain] Cd Length: 250 Bit Score: 62.91 E-value: 1.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648339138 82 LRLLKTFSKTATDLpNGIFLTHAHIGHYTGLIYL-------GKEainaKQLPIYAMPKMKTFLEQNGPWSQLVTQQNILI 154
Cdd:COG1234 40 QRQLLRAGLDPRDI-DAIFITHLHGDHIAGLPGLlstrslaGRE----KPLTIYGPPGTKEFLEALLKASGTDLDFPLEF 114
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2648339138 155 KDLSCNQPLRLsDSLSVTPILVPHRdeySETVGYLISGPRKKLLFIPDidkwEKWNQDINTLIKQVDFALIDATFFDA 232
Cdd:COG1234 115 HEIEPGEVFEI-GGFTVTAFPLDHP---VPAYGYRFEEPGRSLVYSGD----TRPCEALVELAKGADLLIHEATFLDE 184
|
|
| PQQB-like_MBL-fold |
cd16274 |
Coenzyme pyrroloquinoline quinone (PQQ) synthesis protein B and related proteins; MBL-fold ... |
22-209 |
2.79e-11 |
|
Coenzyme pyrroloquinoline quinone (PQQ) synthesis protein B and related proteins; MBL-fold metallo hydrolase domainhydrolase domain; PQQB is essential for the synthesis of the cofactor pyrroloquinoline quinone (PQQ) in Klebsiella pneumonia. PqqB is not directly involved in the PQQ biosynthesis but may serve as a carrier for PQQ when PQQ is released from PqqC. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.
Pssm-ID: 293832 [Multi-domain] Cd Length: 220 Bit Score: 61.87 E-value: 2.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648339138 22 IVVLGTTQDAGSPQIGCTKACCKNLFSKPDQTR---Q---VVSlglfdPNKKISYLFEATPDISKQLRLLKTF--SKTAT 93
Cdd:cd16274 3 IKVLGSAAGGGFPQWNCNCPNCALARAGDGRATartQssiAVS-----ADGENWVLINASPDIRQQIEATPELqpRPGLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648339138 94 DLP-NGIFLTHAHIGHYTGLIYLgKEainAKQLPIYAMPKMKTFLEQNGP------WSQLVTQQNILikdlsCNQPLRLS 166
Cdd:cd16274 78 DTPiAAVLLTDAEIDHTTGLLSL-RE---GQPLTVYATAPVLEDLTTNFPffvllhAYGGVRRHRIL-----PGEPFTLA 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2648339138 167 D--SLSVTPILVP----------HRDEYSETVGYLISGPR--KKLLFIPDIDKWEKW 209
Cdd:cd16274 149 GcpGLTVTPFPVPgkaplysehrDAPEPGDTIGLRIEDGRtgGRLFYAPGCAAVTDE 205
|
|
| RNaseZ_MBL-fold |
cd16272 |
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ... |
50-227 |
2.45e-08 |
|
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as tRNase Z or 3' tRNase) catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors. Two forms of RNase Z exist in eukaryotes, one long (ELAC2) and one short form (ELAC1), the former may have resulted from a duplication of the shorter enzyme. Only the short form exists in bacteria. It includes the C-terminus of human ELAC2 and Escherichia coli zinc phosphodiesterase (ZiPD, also known as ecoZ, tRNase Z, or RNase BN) is a 3' tRNA-processing endonuclease, encoded by the elaC gene. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.
Pssm-ID: 293830 [Multi-domain] Cd Length: 180 Bit Score: 52.65 E-value: 2.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648339138 50 PDQTRQVVSLGLFDPNKKIsyLFEATPDISKqlRLLKTfsKTATDLPNGIFLTHAHIGHYTGLIYL---GKEAINAKQLP 126
Cdd:cd16272 11 PSLTRNTSSYLLETGGTRI--LLDCGEGTVY--RLLKA--GVDPDKLDAIFLSHFHLDHIGGLPTLlfaRRYGGRKKPLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648339138 127 IYAMPKMKTFLEQNGPWSQLVTQQ--NILIKDLSCNQPLRLSDSLSVTPILVPHRDeysETVGYLISGPRKKLLFIPDID 204
Cdd:cd16272 85 IYGPKGIKEFLEKLLNFPVEILPLgfPLEIEELEEGGEVLELGDLKVEAFPVKHSV---ESLGYRIEAEGKSIVYSGDTG 161
|
170 180
....*....|....*....|...
gi 2648339138 205 KwekwNQDINTLIKQVDFALIDA 227
Cdd:cd16272 162 P----CENLVELAKGADLLIHEC 180
|
|
| metallo-hydrolase-like_MBL-fold |
cd07732 |
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ... |
50-203 |
1.11e-06 |
|
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Includes functionally uncharacterized Enterococcus faecalis EF2904. Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily.Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.
Pssm-ID: 293818 [Multi-domain] Cd Length: 202 Bit Score: 48.38 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648339138 50 PDQTRQVVSLGLFDPNKKISYLfeatPDISKQLRLLKTFSKTAtdlpngIFLTHAHIGHYtGLI-YLGKEainakqLPIY 128
Cdd:cd07732 40 FDEVLDFLELGLLPDIVGLYRD----PLLLGGLRSEEDPSVDA------VLLSHAHLDHY-GLLnYLRPD------IPVY 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648339138 129 AMPK----MKTFLEQNGPwSQLVTQQnilIKDLSCNQPLRLSDsLSVTPILVPHR--DEYsetvGYLISGPRKKLLFIPD 202
Cdd:cd07732 103 MGEAtkriLKALLPFFGE-GDPVPRN---IRVFESGKSFTIGD-FTVTPYLVDHSapGAY----AFLIEAPGKRIFYTGD 173
|
.
gi 2648339138 203 I 203
Cdd:cd07732 174 F 174
|
|
| PRK02113 |
PRK02113 |
MBL fold metallo-hydrolase; |
22-178 |
1.70e-05 |
|
MBL fold metallo-hydrolase;
Pssm-ID: 179371 [Multi-domain] Cd Length: 252 Bit Score: 45.16 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648339138 22 IVVLGTTQDAGSPQIGCTKACCKNlfSKPDQTRQVVSLGLFDPNKKIsyLFEATPDISKQLRLLKtFSKTatdlpNGIFL 101
Cdd:PRK02113 3 IRILGSGTSTGVPEIGCTCPVCTS--KDPRDNRLRTSALVETEGARI--LIDCGPDFREQMLRLP-FGKI-----DAVLI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648339138 102 THAHIGHYTGLIYLgKEAINAKQLPIYAMPKMKTFLEQNGPW----SQLVTQQNILIKDLSCNQPLRLSDsLSVTPILVP 177
Cdd:PRK02113 73 THEHYDHVGGLDDL-RPFCRFGEVPIYAEQYVAERLRSRMPYcfveHSYPGVPNIPLREIEPDRPFLVNH-TEVTPLRVM 150
|
.
gi 2648339138 178 H 178
Cdd:PRK02113 151 H 151
|
|
| TaR3-like_MBL-fold |
cd07715 |
MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold ... |
99-232 |
3.52e-05 |
|
MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold metallo-hydrolase domain; Myxococcus xanthus Tar3 may function as an ammonium regulator/effector protein involved in biosynthesis of the antibiotic TA. Some are members of this subgroup are annotated as ribonucleases. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.
Pssm-ID: 293801 [Multi-domain] Cd Length: 212 Bit Score: 44.02 E-value: 3.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648339138 99 IFLTHAHIGHYTGL--------------IYLG-------KEAINAKQLPIYampkmktFleqngPWSQLVTQQNILIKDL 157
Cdd:cd07715 61 LLLSHTHWDHIQGFpffapaydpgnrihIYGPhkdggslEEVLRRQMSPPY-------F-----PVPLEELLAAIEFHDL 128
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2648339138 158 SCNQPLRLsDSLSVTPILVPHRDeysETVGYLISGPRKKLLFIPDI---DKWEKWNQDINTLIKQVDFALIDATFFDA 232
Cdd:cd07715 129 EPGEPFSI-GGVTVTTIPLNHPG---GALGYRIEEDGKSVVYATDTehyPDDGESDEALLEFARGADLLIHDAQYTDE 202
|
|
| metallo-hydrolase-like_MBL-fold |
cd16279 |
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ... |
22-217 |
4.93e-05 |
|
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily.Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry. Some members of this subgroup are named as octanoyltransferase (also known as lipoate-protein ligase B).
Pssm-ID: 293837 [Multi-domain] Cd Length: 193 Bit Score: 43.23 E-value: 4.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648339138 22 IVVLGTTQDAGSPQIGCTKACCKNLFSKPDQTRqvVSLGLFDPNKKIsyLFEATPDISKQLrllktfsktatdLPNGI-- 99
Cdd:cd16279 3 LTFLGTGTSSGVPVIGCDCGVCDSSDPKNRRLR--SSILIETGGKNI--LIDTGPDFRQQA------------LRAGIrk 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648339138 100 ----FLTHAHIGHYTGL------IYLGKEAInakqlPIYAMPKMKTFLEQNGPWSQLVTQQN----ILIKDLSCNQPLRL 165
Cdd:cd16279 67 ldavLLTHAHADHIHGLddlrpfNRLQQRPI-----PVYASEETLDDLKRRFPYFFAATGGGgvpkLDLHIIEPDEPFTI 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2648339138 166 SDsLSVTPILVPHRDEYSetVGYLISgprkKLLFIPDI-----DKWEKWnQDINTLI 217
Cdd:cd16279 142 GG-LEITPLPVLHGKLPS--LGFRFG----DFAYLTDVseipeESLEKL-RGLDVLI 190
|
|
| YycJ-like_MBL-fold |
cd07733 |
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ... |
64-203 |
2.92e-04 |
|
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold metallo hydrolase domain; Includes the uncharacterized Bacillus subtilis YycJ protein. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.
Pssm-ID: 293819 [Multi-domain] Cd Length: 151 Bit Score: 40.32 E-value: 2.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648339138 64 PNKKIsyLFEATPDISKQLRLLKTFSKTATDLpNGIFLTHAHIGHYTGLIYLGKeainAKQLPIYAMPKMKTFLEQNGPW 143
Cdd:cd07733 17 EDGKL--LIDAGLSGRKITGRLAEIGRDPEDI-DAILVTHEHADHIKGLGVLAR----KYNVPIYATAGTLRAMERKVGL 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648339138 144 SQLVTQQNilikdLSCNQPLRLSDsLSVTPILVPHrDEYsETVGYLISGPRKKLLFIPDI 203
Cdd:cd07733 90 IDVDQKQI-----FEPGETFSIGD-FDVESFGVSH-DAA-DPVGYRFEEGGRRFGMLTDL 141
|
|
| class_II_PDE_MBL-fold |
cd07735 |
class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium ... |
89-213 |
2.35e-03 |
|
class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium discoideum PDE1 and PDE7, and related proteins; MBL-fold metallo-hydrolase domain; Cyclic nucleotide phosphodiesterases (PDEs) decompose the second messengers cyclic adenosine and guanosine 3',5'-monophosphate (cAMP and cGMP, respectively). Saccharomyces cerevisiae PDE1 and Dictyostelium discoideum PDE1 and PDE7, have dual cAMP/cGMP specificity. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.
Pssm-ID: 293821 Cd Length: 259 Bit Score: 38.73 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648339138 89 SKTATDLPNGI---FLTHAHIGHYTGLIylgkeaINA--------KQLPIYAMP----KMKTFLEQNGPWSQLVTQQN-- 151
Cdd:cd07735 56 QKAAYELYQRIrhyLITHAHLDHIAGLP------LLSpndggqrgSPKTIYGLPetidALKKHIFNWVIWPDFTSIPSgk 129
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2648339138 152 ILIKDLSCNQP--LRLSDSLSVTPILVPHRDEYSetVGYLISGPRKKLLFI----PDIDKWEKWNQDI 213
Cdd:cd07735 130 YPYLRLEPIEPeyPIALTGLSVTAFPVSHGVPVS--TAFLIRDGGDSFLFFgdtgPDSVSKSPRLDAL 195
|
|
| Lactamase_B |
smart00849 |
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ... |
96-139 |
6.82e-03 |
|
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins contain this domain. These proteins include thiolesterases, members of the glyoxalase II family, that catalyse the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid and a competence protein that is essential for natural transformation in Neisseria gonorrhoeae and could be a transporter involved in DNA uptake. Except for the competence protein these proteins bind two zinc ions per molecule as cofactor.
Pssm-ID: 214854 [Multi-domain] Cd Length: 177 Bit Score: 36.76 E-value: 6.82e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2648339138 96 PNGIFLTHAHIGHYTGLIYLGKeainAKQLPIYAMPKMKTFLEQ 139
Cdd:smart00849 36 IDAIILTHGHPDHIGGLPELLE----APGAPVYAPEGTAELLKD 75
|
|
| |
