|
Name |
Accession |
Description |
Interval |
E-value |
| Auracyanin |
cd04233 |
Auracyanins A and B and similar proteins; This subfamily includes both auracyanins A and B ... |
1386-1507 |
1.14e-49 |
|
Auracyanins A and B and similar proteins; This subfamily includes both auracyanins A and B from the photosynthetic bacterium Chloroflexus aurantiacus and similar proteins. Auracyanins A and B are very similar blue copper proteins with 38% sequence identity and are homologous to the bacterial redox protein Azurin. However, auracyanin A is expressed only when C. aurantiacus cells are grown in light, whereas auracyanin B is expressed in both dark and light conditions. Thus, auracyanin A may function as a redox partner in photosynthesis, while auracyanin B may function in aerobic respiration.
:
Pssm-ID: 259895 [Multi-domain] Cd Length: 121 Bit Score: 171.66 E-value: 1.14e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726212427 1386 ARDITIET-GTNLSYTMRTMRVSAGQPIALTLSNPDVVPHNWALAKPGTIDRVGELADRLISDPEAalRHYIPATTDVLA 1464
Cdd:cd04233 1 ATTITIKAvPGELKFDKTRLTVKAGSKVTLTFENPDDMPHNLVIVKPGSLEKVGEAALAMGADGPA--KNYVPDSPDVLA 78
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1726212427 1465 HTDVVLPGERFTIYFNAPSQKGHYPYLCTFPGHWKVMNGVMIV 1507
Cdd:cd04233 79 ATPLVNPGETETLTFTAPTEPGTYPYVCTYPGHWAIMKGVLIV 121
|
|
| DUF6797 |
pfam20601 |
Domain of unknown function (DUF6797); This presumed domain is functionally uncharacterized. ... |
788-862 |
1.89e-18 |
|
Domain of unknown function (DUF6797); This presumed domain is functionally uncharacterized. This domain is found in bacteria, and is around 100 amino acids in length. This domain is found in association with pfam13442. There is a conserved sequence motif GPLP.
:
Pssm-ID: 466750 Cd Length: 96 Bit Score: 81.88 E-value: 1.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726212427 788 CFNPDTLTYEAVWRGGFVHFSSHRHGFLDGLKIDGELL--------------------PIPEQSKPDQPFRYQGFYRTGD 847
Cdd:pfam20601 2 CFDTDTMRVAAAWTGGFLDWSGIRFGGEGTPTPVGDVLfatpngpgwahpggsfddprPLPYGPLPKEWARYRGLYLHGD 81
|
90
....*....|....*
gi 1726212427 848 RVVFAYRIGDQDFLD 862
Cdd:pfam20601 82 RVVLSYTVGGTEVLE 96
|
|
| CxxCH_TIGR02603 super family |
cl28188 |
putative heme-binding domain, Pirellula/Verrucomicrobium type; This model represents a domain ... |
513-648 |
3.92e-18 |
|
putative heme-binding domain, Pirellula/Verrucomicrobium type; This model represents a domain limited to very few species but expanded into large paralogous families in some species that conain it. We find it in over 20 copies each in Pirellula sp. strain 1 (phylum Planctomycetes) and Verrucomicrobium spinosum DSM 4136 (phylum Verrucomicrobia), and no matches above trusted cutoff an any other species so far. This domain, about 140 amino acids long, contains an absolutely conserved motif CxxCH, the cytochrome c family heme-binding site signature (PS00190).
The actual alignment was detected with superfamily member TIGR02603:
Pssm-ID: 274224 Cd Length: 133 Bit Score: 82.02 E-value: 3.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726212427 513 GDPQRGLQTFAdanSACLSCHRIGQHGGSVGPELTSIGKQrKPEELVESVLWPKRHIPPEYLAHLVLDESGRTHQGYLVR 592
Cdd:TIGR02603 1 GDAARGKAVFA---KVCYLCHRIGGQGVDFGPNLTTVGTK-GKEYLLEAILDPSRTVAPGFETYRVTTKDGRILAGLVAS 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1726212427 593 QDDEEIVLRDPASdppAETAIAIDEIVLQREVG-TLMPDNLAGAMSDEDLSGLLKFL 648
Cdd:TIGR02603 77 ETADPLTIKMPGG---VEQVVPREEIKKRKHLPvSLMPEGLEMGLSDQDLADLVAYL 130
|
|
| YcjR |
COG1082 |
Sugar phosphate isomerase/epimerase [Carbohydrate transport and metabolism]; |
38-276 |
2.78e-09 |
|
Sugar phosphate isomerase/epimerase [Carbohydrate transport and metabolism];
:
Pssm-ID: 440699 [Multi-domain] Cd Length: 254 Bit Score: 59.64 E-value: 2.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726212427 38 IVPFDAKKRGPAERAEMVRRLGLRRVayDWRAEHVPTFE-EEILQY-KKHGLEYFAFWGSHDDAFRLFEKHDMHPQIWQ- 114
Cdd:COG1082 5 LSTYSLPDLDLEEALRAAAELGYDGV--ELAGGDLDEADlAELRAAlADHGLEISSLHAPGLNLAPDPEVREAALERLKr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726212427 115 -----------------MLRPVEGQSQTDRVKAAASQLLPLVRRTGKLGSKLGLYNH-GGWGGEPENMIAVCDYLrehhN 176
Cdd:COG1082 83 aidlaaelgakvvvvhpGSPPPPDLPPEEAWDRLAERLRELAELAEEAGVTLALENHeGTFVNTPEEALRLLEAV----D 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726212427 177 ADHVGIVYNLHHGHGHIDDFAEVLESLKPYLLCLNINGMtrNGDQRgqkiLPLGEGEYDVQ-LLAAIRHSGYEGPIGILG 255
Cdd:COG1082 159 SPNVGLLLDTGHALLAGEDPVELLRKLGDRIKHVHLKDA--DGDQH----LPPGEGDIDFAaILRALKEAGYDGWLSLEV 232
|
250 260
....*....|....*....|..
gi 1726212427 256 HTQDDVELR-LRDNLDGLHWLL 276
Cdd:COG1082 233 ESDPDDPEEaARESLEYLRKLL 254
|
|
| YvrE super family |
cl34598 |
Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase ... |
933-1104 |
1.55e-08 |
|
Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase YvrE is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
The actual alignment was detected with superfamily member COG3386:
Pssm-ID: 442613 [Multi-domain] Cd Length: 266 Bit Score: 57.59 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726212427 933 AFLPDGSALVCTM-QGDVWRVTgfqfpSKTSSWRRFASGLHHALGIVADEDGIFVLGRD--QITRLHDLNGDF-----EA 1004
Cdd:COG3386 14 VWDPDGRLYWVDIpGGRIHRYD-----PDGGAVEVFAEPSGRPNGLAFDPDGRLLVADHgrGLVRFDPADGEVtvladEY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726212427 1005 DYHECFSNayqtsaaghDFICglerDPDGNFYIAS-----GNQGLMRLSPDGqRAETIATGFRNPDGLGLLPDGT---VT 1076
Cdd:COG3386 89 GKPLNRPN---------DGVV----DPDGRLYFTDmgeylPTGALYRVDPDG-SLRVLADGLTFPNGIAFSPDGRtlyVA 154
|
170 180
....*....|....*....|....*...
gi 1726212427 1077 VpasegswTPASMICAVDPDRTGPLNER 1104
Cdd:COG3386 155 D-------TGAGRIYRFDLDADGTLGNR 175
|
|
| Laminin_G_3 super family |
cl48183 |
Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin ... |
331-450 |
1.04e-06 |
|
Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin A-like lectin/glucanases superfamily.
The actual alignment was detected with superfamily member pfam13385:
Pssm-ID: 463865 [Multi-domain] Cd Length: 151 Bit Score: 50.08 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726212427 331 PDSNG--YNILVASDpkrSGDHWEI-FSNNGTGNFTAYLPGMQPDHVHSDAMICDGKPHTVTMVYQPTRVRLLVDGKPVA 407
Cdd:pfam13385 27 PDSLPgwARAIISSS---GGGGYSLgLDGDGRLRFAVNGGNGGWDTVTSGASVPLGQWTHVAVTYDGGTLRLYVNGVLVG 103
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1726212427 408 DQAIQSRGRDGVAGKLAIGRLVEGRIGCRGNIHWVRISKGVRT 450
Cdd:pfam13385 104 SSTLTGGPPPGTGGPLYIGRSPGGDDYFNGLIDEVRIYDRALS 146
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Auracyanin |
cd04233 |
Auracyanins A and B and similar proteins; This subfamily includes both auracyanins A and B ... |
1386-1507 |
1.14e-49 |
|
Auracyanins A and B and similar proteins; This subfamily includes both auracyanins A and B from the photosynthetic bacterium Chloroflexus aurantiacus and similar proteins. Auracyanins A and B are very similar blue copper proteins with 38% sequence identity and are homologous to the bacterial redox protein Azurin. However, auracyanin A is expressed only when C. aurantiacus cells are grown in light, whereas auracyanin B is expressed in both dark and light conditions. Thus, auracyanin A may function as a redox partner in photosynthesis, while auracyanin B may function in aerobic respiration.
Pssm-ID: 259895 [Multi-domain] Cd Length: 121 Bit Score: 171.66 E-value: 1.14e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726212427 1386 ARDITIET-GTNLSYTMRTMRVSAGQPIALTLSNPDVVPHNWALAKPGTIDRVGELADRLISDPEAalRHYIPATTDVLA 1464
Cdd:cd04233 1 ATTITIKAvPGELKFDKTRLTVKAGSKVTLTFENPDDMPHNLVIVKPGSLEKVGEAALAMGADGPA--KNYVPDSPDVLA 78
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1726212427 1465 HTDVVLPGERFTIYFNAPSQKGHYPYLCTFPGHWKVMNGVMIV 1507
Cdd:cd04233 79 ATPLVNPGETETLTFTAPTEPGTYPYVCTYPGHWAIMKGVLIV 121
|
|
| BlueCu |
COG3241 |
Azurin [Energy production and conversion]; |
1369-1508 |
1.16e-46 |
|
Azurin [Energy production and conversion];
Pssm-ID: 442473 [Multi-domain] Cd Length: 158 Bit Score: 164.70 E-value: 1.16e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726212427 1369 AMATRSVPNPYQKKLAGARDITIETGTNLSYTMRTMRVSAGQPIALTLSNP-----DVVPHNWALAKPGTIDRVGELADr 1443
Cdd:COG3241 17 ELATAAKATPAAAAAAADCEITIEANDAMKFDKKEITVKAGKEVTLTLKNTgklpkDAMGHNWVLTKPGDDQAVGAAGA- 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1726212427 1444 lisdPEAALRHYIPA-TTDVLAHTDVVLPGERFTIYFNAPSQKGHYPYLCTFPGHWKVMNGVMIVE 1508
Cdd:COG3241 96 ----AAGADNNYVPPdDDRVIAHTKLIGGGESDTITFTAPKEPGDYPFFCSFPGHWALMKGTLIVE 157
|
|
| DUF6797 |
pfam20601 |
Domain of unknown function (DUF6797); This presumed domain is functionally uncharacterized. ... |
788-862 |
1.89e-18 |
|
Domain of unknown function (DUF6797); This presumed domain is functionally uncharacterized. This domain is found in bacteria, and is around 100 amino acids in length. This domain is found in association with pfam13442. There is a conserved sequence motif GPLP.
Pssm-ID: 466750 Cd Length: 96 Bit Score: 81.88 E-value: 1.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726212427 788 CFNPDTLTYEAVWRGGFVHFSSHRHGFLDGLKIDGELL--------------------PIPEQSKPDQPFRYQGFYRTGD 847
Cdd:pfam20601 2 CFDTDTMRVAAAWTGGFLDWSGIRFGGEGTPTPVGDVLfatpngpgwahpggsfddprPLPYGPLPKEWARYRGLYLHGD 81
|
90
....*....|....*
gi 1726212427 848 RVVFAYRIGDQDFLD 862
Cdd:pfam20601 82 RVVLSYTVGGTEVLE 96
|
|
| CxxCH_TIGR02603 |
TIGR02603 |
putative heme-binding domain, Pirellula/Verrucomicrobium type; This model represents a domain ... |
513-648 |
3.92e-18 |
|
putative heme-binding domain, Pirellula/Verrucomicrobium type; This model represents a domain limited to very few species but expanded into large paralogous families in some species that conain it. We find it in over 20 copies each in Pirellula sp. strain 1 (phylum Planctomycetes) and Verrucomicrobium spinosum DSM 4136 (phylum Verrucomicrobia), and no matches above trusted cutoff an any other species so far. This domain, about 140 amino acids long, contains an absolutely conserved motif CxxCH, the cytochrome c family heme-binding site signature (PS00190).
Pssm-ID: 274224 Cd Length: 133 Bit Score: 82.02 E-value: 3.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726212427 513 GDPQRGLQTFAdanSACLSCHRIGQHGGSVGPELTSIGKQrKPEELVESVLWPKRHIPPEYLAHLVLDESGRTHQGYLVR 592
Cdd:TIGR02603 1 GDAARGKAVFA---KVCYLCHRIGGQGVDFGPNLTTVGTK-GKEYLLEAILDPSRTVAPGFETYRVTTKDGRILAGLVAS 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1726212427 593 QDDEEIVLRDPASdppAETAIAIDEIVLQREVG-TLMPDNLAGAMSDEDLSGLLKFL 648
Cdd:TIGR02603 77 ETADPLTIKMPGG---VEQVVPREEIKKRKHLPvSLMPEGLEMGLSDQDLADLVAYL 130
|
|
| azurin |
TIGR02695 |
azurin; Azurin is a blue copper-binding protein in the plastocyanin/azurin family (see ... |
1388-1503 |
1.70e-11 |
|
azurin; Azurin is a blue copper-binding protein in the plastocyanin/azurin family (see pfam00127). It serves as a redox partner to enzymes such as nitrite reductase or arsenite oxidase. The most closely related copper-binding proteins to this family are auracyanins, as in Chloroflexus aurantiacus, which have similar redox activities. [Energy metabolism, Electron transport]
Pssm-ID: 131742 [Multi-domain] Cd Length: 125 Bit Score: 62.87 E-value: 1.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726212427 1388 DITIETGTNLSYTMRTMRVSAG-QPIALTLSNPDVVP-----HNWALAKPGTIDRVGELADRLISDpeaalRHYIPATTD 1461
Cdd:TIGR02695 2 EVTVESNDNMQFNTKSISVPKScKEFTVNLKHTGKLPkavmgHNWVLAKSADMQAVAKDGMGAGAD-----NNYVKPGDA 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1726212427 1462 -VLAHTDVVLPGERFTIYFNAP--SQKGHYPYLCTFPGHWKVMNG 1503
Cdd:TIGR02695 77 rVIAHTKVIGGGEKTSVTFDVSklSAGEDYTFFCSFPGHWAMMRG 121
|
|
| YcjR |
COG1082 |
Sugar phosphate isomerase/epimerase [Carbohydrate transport and metabolism]; |
38-276 |
2.78e-09 |
|
Sugar phosphate isomerase/epimerase [Carbohydrate transport and metabolism];
Pssm-ID: 440699 [Multi-domain] Cd Length: 254 Bit Score: 59.64 E-value: 2.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726212427 38 IVPFDAKKRGPAERAEMVRRLGLRRVayDWRAEHVPTFE-EEILQY-KKHGLEYFAFWGSHDDAFRLFEKHDMHPQIWQ- 114
Cdd:COG1082 5 LSTYSLPDLDLEEALRAAAELGYDGV--ELAGGDLDEADlAELRAAlADHGLEISSLHAPGLNLAPDPEVREAALERLKr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726212427 115 -----------------MLRPVEGQSQTDRVKAAASQLLPLVRRTGKLGSKLGLYNH-GGWGGEPENMIAVCDYLrehhN 176
Cdd:COG1082 83 aidlaaelgakvvvvhpGSPPPPDLPPEEAWDRLAERLRELAELAEEAGVTLALENHeGTFVNTPEEALRLLEAV----D 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726212427 177 ADHVGIVYNLHHGHGHIDDFAEVLESLKPYLLCLNINGMtrNGDQRgqkiLPLGEGEYDVQ-LLAAIRHSGYEGPIGILG 255
Cdd:COG1082 159 SPNVGLLLDTGHALLAGEDPVELLRKLGDRIKHVHLKDA--DGDQH----LPPGEGDIDFAaILRALKEAGYDGWLSLEV 232
|
250 260
....*....|....*....|..
gi 1726212427 256 HTQDDVELR-LRDNLDGLHWLL 276
Cdd:COG1082 233 ESDPDDPEEaARESLEYLRKLL 254
|
|
| YvrE |
COG3386 |
Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase ... |
933-1104 |
1.55e-08 |
|
Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase YvrE is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 442613 [Multi-domain] Cd Length: 266 Bit Score: 57.59 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726212427 933 AFLPDGSALVCTM-QGDVWRVTgfqfpSKTSSWRRFASGLHHALGIVADEDGIFVLGRD--QITRLHDLNGDF-----EA 1004
Cdd:COG3386 14 VWDPDGRLYWVDIpGGRIHRYD-----PDGGAVEVFAEPSGRPNGLAFDPDGRLLVADHgrGLVRFDPADGEVtvladEY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726212427 1005 DYHECFSNayqtsaaghDFICglerDPDGNFYIAS-----GNQGLMRLSPDGqRAETIATGFRNPDGLGLLPDGT---VT 1076
Cdd:COG3386 89 GKPLNRPN---------DGVV----DPDGRLYFTDmgeylPTGALYRVDPDG-SLRVLADGLTFPNGIAFSPDGRtlyVA 154
|
170 180
....*....|....*....|....*...
gi 1726212427 1077 VpasegswTPASMICAVDPDRTGPLNER 1104
Cdd:COG3386 155 D-------TGAGRIYRFDLDADGTLGNR 175
|
|
| Laminin_G_3 |
pfam13385 |
Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin ... |
331-450 |
1.04e-06 |
|
Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin A-like lectin/glucanases superfamily.
Pssm-ID: 463865 [Multi-domain] Cd Length: 151 Bit Score: 50.08 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726212427 331 PDSNG--YNILVASDpkrSGDHWEI-FSNNGTGNFTAYLPGMQPDHVHSDAMICDGKPHTVTMVYQPTRVRLLVDGKPVA 407
Cdd:pfam13385 27 PDSLPgwARAIISSS---GGGGYSLgLDGDGRLRFAVNGGNGGWDTVTSGASVPLGQWTHVAVTYDGGTLRLYVNGVLVG 103
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1726212427 408 DQAIQSRGRDGVAGKLAIGRLVEGRIGCRGNIHWVRISKGVRT 450
Cdd:pfam13385 104 SSTLTGGPPPGTGGPLYIGRSPGGDDYFNGLIDEVRIYDRALS 146
|
|
| AP_endonuc_2 |
pfam01261 |
Xylose isomerase-like TIM barrel; This TIM alpha/beta barrel structure is found in xylose ... |
53-272 |
4.31e-05 |
|
Xylose isomerase-like TIM barrel; This TIM alpha/beta barrel structure is found in xylose isomerase and in endonuclease IV (EC:3.1.21.2). This domain is also found in the N termini of bacterial myo-inositol catabolism proteins. These are involved in the myo-inositol catabolism pathway, and is required for growth on myo-inositol in Rhizobium leguminosarum bv. viciae.
Pssm-ID: 426164 [Multi-domain] Cd Length: 248 Bit Score: 46.98 E-value: 4.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726212427 53 EMVRRLGLRRVAYDWRAEHVPTFEEEILQY-----KKHGLE-------YFAFWGSHDDAFRLFEKHDMHPQI-------- 112
Cdd:pfam01261 2 AAAAELGFDGVELFTRRWFRPPLSDEEAEElkaalKEHGLEivvhapyLGDNLASPDEEEREKAIDRLKRAIelaaalga 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726212427 113 WQMLRP---VEGQSQTDRVKAAASQLLPLVRRTGKLGSKLGLYNHGGWGGEPENMIAVCDYLREHHNADHVGIVYNLHHG 189
Cdd:pfam01261 82 KLVVFHpgsDLGDDPEEALARLAESLRELADLAEREGVRLALEPLAGKGTNVGNTFEEALEIIDEVDSPNVGVCLDTGHL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726212427 190 H--GHIDDFAEVLesLKPYLLCLNINGMTRNGDQRGQKILPLGEGEYDVQ-LLAAIRHSGYEGPIGILGHTQDDVELRLR 266
Cdd:pfam01261 162 FaaGDGDLFELRL--GDRYIGHVHLKDSKNPLGSGPDRHVPIGEGVIDFEaLFRALKEIGYDGPLSLETFNDGPPEEGAR 239
|
....*.
gi 1726212427 267 DNLDGL 272
Cdd:pfam01261 240 EGLEWL 245
|
|
| Piru_Ver_Nterm |
TIGR02604 |
putative membrane-bound dehydrogenase domain; All proteins that score above the trusted cutoff ... |
967-1066 |
4.33e-05 |
|
putative membrane-bound dehydrogenase domain; All proteins that score above the trusted cutoff score of 45 to this model are large proteins of either Pirellula sp. 1 or Verrucomicrobium spinosum. These proteins all contain, in addition to this domain, several hundred residues of highly variable sequence, and then a well-conserved C-terminal domain (TIGR02603) that features a putative cytochrome c-type heme binding motif CXXCH. The membrane-bound L-sorbosone dehydrogenase from Acetobacter liquefaciens (Gluconacetobacter liquefaciens) (SP|Q44091) is homologous to this domain but lacks additional sequence regions shared by members of this family and belongs to a different clade of the larger family of homologs. It and its closely related homologs are excluded from the this model by scoring between the trusted (45) and noise (18) cutoffs.
Pssm-ID: 274225 [Multi-domain] Cd Length: 367 Bit Score: 47.44 E-value: 4.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726212427 967 FASGLHHALGIVADEDGIFVLGRDQITRLHDLNGDFEADY-HECFSNAYQTSAAGHD-FICGLERDPDGNFYIASGNQG- 1043
Cdd:TIGR02604 67 FAEEVQMLTGLAVAVGGVYVATPPHILRLRDKDGDGKAEDkREVLLSGFNGQAASHHhSLNGLKWGPDGRLYFNCGNTLa 146
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1726212427 1044 -------------------LMRLSPDGQRAETIATGFRNPDG 1066
Cdd:TIGR02604 147 skvttpgrsdesrqgiggfLFRMNPDGGRLRIVAGGFQNPYG 188
|
|
| Copper-bind |
pfam00127 |
Copper binding proteins, plastocyanin/azurin family; |
1394-1508 |
2.52e-03 |
|
Copper binding proteins, plastocyanin/azurin family;
Pssm-ID: 395076 [Multi-domain] Cd Length: 99 Bit Score: 38.89 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726212427 1394 GTNLSYTMRTMRVSAGQPIalTLSNPDVVPHNWALAKPGTIDrvGELADRLisdpeaalrhyipattDVLAHTDVVLPGE 1473
Cdd:pfam00127 9 SGDMVFEPKEITVKKGEKV--TFVNNAGMPHNVVFDKDGVPA--GVDADKV----------------KMGDHTKLIGGGE 68
|
90 100 110
....*....|....*....|....*....|....*.
gi 1726212427 1474 RFTIYFNAPsqkGHYPYLCTfPgHW-KVMNGVMIVE 1508
Cdd:pfam00127 69 TYSVTFDLA---GTYGFFCT-P-HQgAGMVGKVTVE 99
|
|
| SGL |
pfam08450 |
SMP-30/Gluconolactonase/LRE-like region; This family describes a region that is found in ... |
977-1101 |
7.78e-03 |
|
SMP-30/Gluconolactonase/LRE-like region; This family describes a region that is found in proteins expressed by a variety of eukaryotic and prokaryotic species. These proteins include various enzymes, such as senescence marker protein 30 (SMP-30), gluconolactonase and luciferin-regenerating enzyme (LRE). SMP-30 is known to hydrolyse diisopropyl phosphorofluoridate in the liver, and has been noted as having sequence similarity, in the region described in this family, with PON1 and LRE.
Pssm-ID: 462480 [Multi-domain] Cd Length: 246 Bit Score: 39.94 E-value: 7.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726212427 977 IVADEDGIFVLGRD--QITRLHDLNGDFEADYHecfSNayqtsaaghDFICglerDPDGNFYIAS---------GNQGLM 1045
Cdd:pfam08450 55 IVALKDGVALLDLAtgELTPLADPEDDDWPLNR---FN---------DGKV----DPDGRFWFGTmgddeapggDPGALY 118
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1726212427 1046 RLSPDGQrAETIATGFRNPDGLGLLPDGTvTVPASEgswTPASMICAVDPDRTGPL 1101
Cdd:pfam08450 119 RLDPDGK-LTRVLDGLTISNGLAWSPDGR-TLYFAD---SPARKIWAYDYDLDGGL 169
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Auracyanin |
cd04233 |
Auracyanins A and B and similar proteins; This subfamily includes both auracyanins A and B ... |
1386-1507 |
1.14e-49 |
|
Auracyanins A and B and similar proteins; This subfamily includes both auracyanins A and B from the photosynthetic bacterium Chloroflexus aurantiacus and similar proteins. Auracyanins A and B are very similar blue copper proteins with 38% sequence identity and are homologous to the bacterial redox protein Azurin. However, auracyanin A is expressed only when C. aurantiacus cells are grown in light, whereas auracyanin B is expressed in both dark and light conditions. Thus, auracyanin A may function as a redox partner in photosynthesis, while auracyanin B may function in aerobic respiration.
Pssm-ID: 259895 [Multi-domain] Cd Length: 121 Bit Score: 171.66 E-value: 1.14e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726212427 1386 ARDITIET-GTNLSYTMRTMRVSAGQPIALTLSNPDVVPHNWALAKPGTIDRVGELADRLISDPEAalRHYIPATTDVLA 1464
Cdd:cd04233 1 ATTITIKAvPGELKFDKTRLTVKAGSKVTLTFENPDDMPHNLVIVKPGSLEKVGEAALAMGADGPA--KNYVPDSPDVLA 78
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1726212427 1465 HTDVVLPGERFTIYFNAPSQKGHYPYLCTFPGHWKVMNGVMIV 1507
Cdd:cd04233 79 ATPLVNPGETETLTFTAPTEPGTYPYVCTYPGHWAIMKGVLIV 121
|
|
| BlueCu |
COG3241 |
Azurin [Energy production and conversion]; |
1369-1508 |
1.16e-46 |
|
Azurin [Energy production and conversion];
Pssm-ID: 442473 [Multi-domain] Cd Length: 158 Bit Score: 164.70 E-value: 1.16e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726212427 1369 AMATRSVPNPYQKKLAGARDITIETGTNLSYTMRTMRVSAGQPIALTLSNP-----DVVPHNWALAKPGTIDRVGELADr 1443
Cdd:COG3241 17 ELATAAKATPAAAAAAADCEITIEANDAMKFDKKEITVKAGKEVTLTLKNTgklpkDAMGHNWVLTKPGDDQAVGAAGA- 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1726212427 1444 lisdPEAALRHYIPA-TTDVLAHTDVVLPGERFTIYFNAPSQKGHYPYLCTFPGHWKVMNGVMIVE 1508
Cdd:COG3241 96 ----AAGADNNYVPPdDDRVIAHTKLIGGGESDTITFTAPKEPGDYPFFCSFPGHWALMKGTLIVE 157
|
|
| Azurin |
cd13922 |
Azurin is a redox partner for enzymes such as nitrite reductase or arsenite oxidase; Azurin is ... |
1387-1507 |
2.30e-23 |
|
Azurin is a redox partner for enzymes such as nitrite reductase or arsenite oxidase; Azurin is a bacterial blue copper-binding protein. It serves as a redox partner to enzymes such as nitrite reductase or arsenite oxidase. The copper of Azurin is tetrahedrally coordinated by a cysteine, 2 histidines, and a methionine residue. The electron transfer reactions are carried out with the Cu center transitioning between the oxidized Cu(II) form and the reduced Cu(I) form. Azurin can function as a tumor suppressor; it forms a complex with p53 that triggers apoptosis in various human cancer cells.
Pssm-ID: 259989 [Multi-domain] Cd Length: 125 Bit Score: 96.86 E-value: 2.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726212427 1387 RDITIETGTNLSYTMRTMRVSAGQ-PIALTLSNPDVVP-----HNWALAKPGTIDRVGELADRlisdpeAALRHYIPA-- 1458
Cdd:cd13922 1 CEVTIEGNDQMKFDTKEITVKAGCkEFTVTLKHTGKLPknvmgHNWVLLKTGDVQAVANDGAA------AGADNDYVPpg 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1726212427 1459 TTDVLAHTDVVLPGERFTIYFNAP--SQKGHYPYLCTFPGHWKVMNGVMIV 1507
Cdd:cd13922 75 DARVIAHTKLIGGGESDSVTFTVSklAAGGDYTFFCSFPGHYAMMKGKLVV 125
|
|
| DUF6797 |
pfam20601 |
Domain of unknown function (DUF6797); This presumed domain is functionally uncharacterized. ... |
788-862 |
1.89e-18 |
|
Domain of unknown function (DUF6797); This presumed domain is functionally uncharacterized. This domain is found in bacteria, and is around 100 amino acids in length. This domain is found in association with pfam13442. There is a conserved sequence motif GPLP.
Pssm-ID: 466750 Cd Length: 96 Bit Score: 81.88 E-value: 1.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726212427 788 CFNPDTLTYEAVWRGGFVHFSSHRHGFLDGLKIDGELL--------------------PIPEQSKPDQPFRYQGFYRTGD 847
Cdd:pfam20601 2 CFDTDTMRVAAAWTGGFLDWSGIRFGGEGTPTPVGDVLfatpngpgwahpggsfddprPLPYGPLPKEWARYRGLYLHGD 81
|
90
....*....|....*
gi 1726212427 848 RVVFAYRIGDQDFLD 862
Cdd:pfam20601 82 RVVLSYTVGGTEVLE 96
|
|
| CxxCH_TIGR02603 |
TIGR02603 |
putative heme-binding domain, Pirellula/Verrucomicrobium type; This model represents a domain ... |
513-648 |
3.92e-18 |
|
putative heme-binding domain, Pirellula/Verrucomicrobium type; This model represents a domain limited to very few species but expanded into large paralogous families in some species that conain it. We find it in over 20 copies each in Pirellula sp. strain 1 (phylum Planctomycetes) and Verrucomicrobium spinosum DSM 4136 (phylum Verrucomicrobia), and no matches above trusted cutoff an any other species so far. This domain, about 140 amino acids long, contains an absolutely conserved motif CxxCH, the cytochrome c family heme-binding site signature (PS00190).
Pssm-ID: 274224 Cd Length: 133 Bit Score: 82.02 E-value: 3.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726212427 513 GDPQRGLQTFAdanSACLSCHRIGQHGGSVGPELTSIGKQrKPEELVESVLWPKRHIPPEYLAHLVLDESGRTHQGYLVR 592
Cdd:TIGR02603 1 GDAARGKAVFA---KVCYLCHRIGGQGVDFGPNLTTVGTK-GKEYLLEAILDPSRTVAPGFETYRVTTKDGRILAGLVAS 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1726212427 593 QDDEEIVLRDPASdppAETAIAIDEIVLQREVG-TLMPDNLAGAMSDEDLSGLLKFL 648
Cdd:TIGR02603 77 ETADPLTIKMPGG---VEQVVPREEIKKRKHLPvSLMPEGLEMGLSDQDLADLVAYL 130
|
|
| Azurin_like |
cd13843 |
Azurin and similar redox proteins; Azurin is a bacterial blue copper-binding protein. It ... |
1389-1507 |
4.15e-14 |
|
Azurin and similar redox proteins; Azurin is a bacterial blue copper-binding protein. It serves as a redox partner to enzymes such as nitrite reductase or arsenite oxidase. The copper of Azurin is tetrahedrally coordinated by a cysteine, 2 histidines, and a methionine residue. The electron transfer reactions are carried out with the Cu center transitioning between the oxidized Cu(II) form and the reduced Cu(I) form. Azurin can function as tumor suppressor; it forms a complex with p53 that triggers apoptosis in various human cancer cells. Auracyanins A and B are from photosynthetic bacteria. They are very similar blue copper proteins with 38% sequence identity and they are homologous to the bacterial redox protein Azurin. However, auracyanin A is expressed only when C. aurantiacus cells are grown in light, whereas auracyanin B is expressed under dark and in light. Thus, auracyanin A may function as a redox partner in photosynthesis, while auracyanin B may function in aerobic respiration.
Pssm-ID: 259912 [Multi-domain] Cd Length: 124 Bit Score: 70.27 E-value: 4.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726212427 1389 ITIETGTNLSYTMRTMRVSAG-QPIALTLSNPDVVP-----HNWALAKPGTIDRVGElaDRLISDPEAalrHYIPATTD- 1461
Cdd:cd13843 2 VEIGGNDEMQFSKTSITVSAScKEFTVNLKHNGKLPknvmgHNWVLVKSADAGGVAN--AGMAAGADN---NYLKPDDSr 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1726212427 1462 VLAHTDVVLPGERFTIYFNAPSQK--GHYPYLCTFPGHWKVMNGVMIV 1507
Cdd:cd13843 77 VIAHTPLIGGGETDSVTFTVSKLEagEDYTYFCTFPGHFALMKGTLTL 124
|
|
| azurin |
TIGR02695 |
azurin; Azurin is a blue copper-binding protein in the plastocyanin/azurin family (see ... |
1388-1503 |
1.70e-11 |
|
azurin; Azurin is a blue copper-binding protein in the plastocyanin/azurin family (see pfam00127). It serves as a redox partner to enzymes such as nitrite reductase or arsenite oxidase. The most closely related copper-binding proteins to this family are auracyanins, as in Chloroflexus aurantiacus, which have similar redox activities. [Energy metabolism, Electron transport]
Pssm-ID: 131742 [Multi-domain] Cd Length: 125 Bit Score: 62.87 E-value: 1.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726212427 1388 DITIETGTNLSYTMRTMRVSAG-QPIALTLSNPDVVP-----HNWALAKPGTIDRVGELADRLISDpeaalRHYIPATTD 1461
Cdd:TIGR02695 2 EVTVESNDNMQFNTKSISVPKScKEFTVNLKHTGKLPkavmgHNWVLAKSADMQAVAKDGMGAGAD-----NNYVKPGDA 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1726212427 1462 -VLAHTDVVLPGERFTIYFNAP--SQKGHYPYLCTFPGHWKVMNG 1503
Cdd:TIGR02695 77 rVIAHTKVIGGGEKTSVTFDVSklSAGEDYTFFCSFPGHWAMMRG 121
|
|
| YcjR |
COG1082 |
Sugar phosphate isomerase/epimerase [Carbohydrate transport and metabolism]; |
38-276 |
2.78e-09 |
|
Sugar phosphate isomerase/epimerase [Carbohydrate transport and metabolism];
Pssm-ID: 440699 [Multi-domain] Cd Length: 254 Bit Score: 59.64 E-value: 2.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726212427 38 IVPFDAKKRGPAERAEMVRRLGLRRVayDWRAEHVPTFE-EEILQY-KKHGLEYFAFWGSHDDAFRLFEKHDMHPQIWQ- 114
Cdd:COG1082 5 LSTYSLPDLDLEEALRAAAELGYDGV--ELAGGDLDEADlAELRAAlADHGLEISSLHAPGLNLAPDPEVREAALERLKr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726212427 115 -----------------MLRPVEGQSQTDRVKAAASQLLPLVRRTGKLGSKLGLYNH-GGWGGEPENMIAVCDYLrehhN 176
Cdd:COG1082 83 aidlaaelgakvvvvhpGSPPPPDLPPEEAWDRLAERLRELAELAEEAGVTLALENHeGTFVNTPEEALRLLEAV----D 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726212427 177 ADHVGIVYNLHHGHGHIDDFAEVLESLKPYLLCLNINGMtrNGDQRgqkiLPLGEGEYDVQ-LLAAIRHSGYEGPIGILG 255
Cdd:COG1082 159 SPNVGLLLDTGHALLAGEDPVELLRKLGDRIKHVHLKDA--DGDQH----LPPGEGDIDFAaILRALKEAGYDGWLSLEV 232
|
250 260
....*....|....*....|..
gi 1726212427 256 HTQDDVELR-LRDNLDGLHWLL 276
Cdd:COG1082 233 ESDPDDPEEaARESLEYLRKLL 254
|
|
| YvrE |
COG3386 |
Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase ... |
933-1104 |
1.55e-08 |
|
Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase YvrE is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 442613 [Multi-domain] Cd Length: 266 Bit Score: 57.59 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726212427 933 AFLPDGSALVCTM-QGDVWRVTgfqfpSKTSSWRRFASGLHHALGIVADEDGIFVLGRD--QITRLHDLNGDF-----EA 1004
Cdd:COG3386 14 VWDPDGRLYWVDIpGGRIHRYD-----PDGGAVEVFAEPSGRPNGLAFDPDGRLLVADHgrGLVRFDPADGEVtvladEY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726212427 1005 DYHECFSNayqtsaaghDFICglerDPDGNFYIAS-----GNQGLMRLSPDGqRAETIATGFRNPDGLGLLPDGT---VT 1076
Cdd:COG3386 89 GKPLNRPN---------DGVV----DPDGRLYFTDmgeylPTGALYRVDPDG-SLRVLADGLTFPNGIAFSPDGRtlyVA 154
|
170 180
....*....|....*....|....*...
gi 1726212427 1077 VpasegswTPASMICAVDPDRTGPLNER 1104
Cdd:COG3386 155 D-------TGAGRIYRFDLDADGTLGNR 175
|
|
| COG4454 |
COG4454 |
Uncharacterized copper-binding protein, cupredoxin-like subfamily [General function prediction ... |
1386-1508 |
5.25e-07 |
|
Uncharacterized copper-binding protein, cupredoxin-like subfamily [General function prediction only];
Pssm-ID: 443552 [Multi-domain] Cd Length: 151 Bit Score: 50.73 E-value: 5.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726212427 1386 ARDITIETGTNLSYTMRTMRVSAGQPIALTLSNPDVVPHNWALAKPGTIDRVGELADRlisDPEaaLRHyipattdVLAH 1465
Cdd:COG4454 41 TRTITVTMGDTMRFTPDSIEVKAGETVRFVVTNPGKLKHEFVLGTFAELAEHAKVMAK---MPD--MEH-------GDPN 108
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1726212427 1466 TDVVLPGERFTIYFNaPSQKGHYPYLCTFPGHWKV-MNGVMIVE 1508
Cdd:COG4454 109 EVELAPGETGELVWT-FTKAGTFEFACLIPGHYEAgMTGKIVVK 151
|
|
| Laminin_G_3 |
pfam13385 |
Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin ... |
331-450 |
1.04e-06 |
|
Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin A-like lectin/glucanases superfamily.
Pssm-ID: 463865 [Multi-domain] Cd Length: 151 Bit Score: 50.08 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726212427 331 PDSNG--YNILVASDpkrSGDHWEI-FSNNGTGNFTAYLPGMQPDHVHSDAMICDGKPHTVTMVYQPTRVRLLVDGKPVA 407
Cdd:pfam13385 27 PDSLPgwARAIISSS---GGGGYSLgLDGDGRLRFAVNGGNGGWDTVTSGASVPLGQWTHVAVTYDGGTLRLYVNGVLVG 103
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1726212427 408 DQAIQSRGRDGVAGKLAIGRLVEGRIGCRGNIHWVRISKGVRT 450
Cdd:pfam13385 104 SSTLTGGPPPGTGGPLYIGRSPGGDDYFNGLIDEVRIYDRALS 146
|
|
| AP_endonuc_2 |
pfam01261 |
Xylose isomerase-like TIM barrel; This TIM alpha/beta barrel structure is found in xylose ... |
53-272 |
4.31e-05 |
|
Xylose isomerase-like TIM barrel; This TIM alpha/beta barrel structure is found in xylose isomerase and in endonuclease IV (EC:3.1.21.2). This domain is also found in the N termini of bacterial myo-inositol catabolism proteins. These are involved in the myo-inositol catabolism pathway, and is required for growth on myo-inositol in Rhizobium leguminosarum bv. viciae.
Pssm-ID: 426164 [Multi-domain] Cd Length: 248 Bit Score: 46.98 E-value: 4.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726212427 53 EMVRRLGLRRVAYDWRAEHVPTFEEEILQY-----KKHGLE-------YFAFWGSHDDAFRLFEKHDMHPQI-------- 112
Cdd:pfam01261 2 AAAAELGFDGVELFTRRWFRPPLSDEEAEElkaalKEHGLEivvhapyLGDNLASPDEEEREKAIDRLKRAIelaaalga 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726212427 113 WQMLRP---VEGQSQTDRVKAAASQLLPLVRRTGKLGSKLGLYNHGGWGGEPENMIAVCDYLREHHNADHVGIVYNLHHG 189
Cdd:pfam01261 82 KLVVFHpgsDLGDDPEEALARLAESLRELADLAEREGVRLALEPLAGKGTNVGNTFEEALEIIDEVDSPNVGVCLDTGHL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726212427 190 H--GHIDDFAEVLesLKPYLLCLNINGMTRNGDQRGQKILPLGEGEYDVQ-LLAAIRHSGYEGPIGILGHTQDDVELRLR 266
Cdd:pfam01261 162 FaaGDGDLFELRL--GDRYIGHVHLKDSKNPLGSGPDRHVPIGEGVIDFEaLFRALKEIGYDGPLSLETFNDGPPEEGAR 239
|
....*.
gi 1726212427 267 DNLDGL 272
Cdd:pfam01261 240 EGLEWL 245
|
|
| Piru_Ver_Nterm |
TIGR02604 |
putative membrane-bound dehydrogenase domain; All proteins that score above the trusted cutoff ... |
967-1066 |
4.33e-05 |
|
putative membrane-bound dehydrogenase domain; All proteins that score above the trusted cutoff score of 45 to this model are large proteins of either Pirellula sp. 1 or Verrucomicrobium spinosum. These proteins all contain, in addition to this domain, several hundred residues of highly variable sequence, and then a well-conserved C-terminal domain (TIGR02603) that features a putative cytochrome c-type heme binding motif CXXCH. The membrane-bound L-sorbosone dehydrogenase from Acetobacter liquefaciens (Gluconacetobacter liquefaciens) (SP|Q44091) is homologous to this domain but lacks additional sequence regions shared by members of this family and belongs to a different clade of the larger family of homologs. It and its closely related homologs are excluded from the this model by scoring between the trusted (45) and noise (18) cutoffs.
Pssm-ID: 274225 [Multi-domain] Cd Length: 367 Bit Score: 47.44 E-value: 4.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726212427 967 FASGLHHALGIVADEDGIFVLGRDQITRLHDLNGDFEADY-HECFSNAYQTSAAGHD-FICGLERDPDGNFYIASGNQG- 1043
Cdd:TIGR02604 67 FAEEVQMLTGLAVAVGGVYVATPPHILRLRDKDGDGKAEDkREVLLSGFNGQAASHHhSLNGLKWGPDGRLYFNCGNTLa 146
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1726212427 1044 -------------------LMRLSPDGQRAETIATGFRNPDG 1066
Cdd:TIGR02604 147 skvttpgrsdesrqgiggfLFRMNPDGGRLRIVAGGFQNPYG 188
|
|
| YvrE |
COG3386 |
Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase ... |
933-1099 |
4.77e-05 |
|
Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase YvrE is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 442613 [Multi-domain] Cd Length: 266 Bit Score: 46.81 E-value: 4.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726212427 933 AFLPDGSALVCTM-----QGDVWRVtgfqfpSKTSSWRRFASGLHHALGIVADEDG--IFV--LGRDQITRLhDLNGDFE 1003
Cdd:COG3386 99 VVDPDGRLYFTDMgeylpTGALYRV------DPDGSLRVLADGLTFPNGIAFSPDGrtLYVadTGAGRIYRF-DLDADGT 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726212427 1004 ADYHECFSnayqTSAAGHDFICGLERDPDGNFYIAS-GNQGLMRLSPDGQRAETIATGFRNPDGL---GllPDGT---VT 1076
Cdd:COG3386 172 LGNRRVFA----DLPDGPGGPDGLAVDADGNLWVALwGGGGVVRFDPDGELLGRIELPERRPTNVafgG--PDLRtlyVT 245
|
170 180
....*....|....*....|...
gi 1726212427 1077 vpaSEGSWTPASMICAVDPDRTG 1099
Cdd:COG3386 246 ---TARSLPLAGALFRVRVDVPG 265
|
|
| COG3292 |
COG3292 |
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms]; |
902-1073 |
6.42e-05 |
|
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
Pssm-ID: 442521 [Multi-domain] Cd Length: 924 Bit Score: 47.68 E-value: 6.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726212427 902 IQLGSGTPYAVDTIGLPFDNPWNALmfcgghaFLPDGSALVCTMQGDVWRvtgfqFPSKTSSWRRF--ASGL--HHALGI 977
Cdd:COG3292 296 LDPKTGKFKRYNPNGLPSNSVYSIL-------EDSDGNLWIGTSGGGLYR-----YDPKTGKFTKFseDNGLsnNFIRSI 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726212427 978 VADEDG-IFVLGRDQITRLHDLNGDFEAdyhecFSNAYQTSAAGHDFICGLERDPDGNFYIASGNQGLMRLSPDGQRAET 1056
Cdd:COG3292 364 LEDSDGnLWVGTNGGLYRLDPKTGKFTN-----FTHDPDKNGLSSNYINSIFEDSDGRLWIGTDGGGLYRYDPKTGKFKH 438
|
170 180
....*....|....*....|...
gi 1726212427 1057 iatgFRNPDGL------GLLPDG 1073
Cdd:COG3292 439 ----FTTKDGLpsntiySILEDD 457
|
|
| Cupredoxin |
cd00920 |
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ... |
1384-1506 |
1.34e-04 |
|
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in inter-molecular electron transfer reactions. Cupredoxins are blue copper proteins, having an intense blue color due to the presence of a mononuclear type 1 (T1) copper site. Structurally, the cupredoxin-like fold consists of a beta-sandwich with 7 strands in 2 beta-sheets, which is arranged in a Greek-key beta-barrel. Some of these proteins have lost the ability to bind copper. The majority of family members contain multiple cupredoxin domain repeats: ceruloplasmin and the coagulation factors V/VIII have six repeats; laccase, ascorbate oxidase, spore coat protein A, and multicopper oxidase CueO contain three repeats; and nitrite reductase has two repeats. Others are mono-domain cupredoxins, such as plastocyanin, pseudoazurin, plantacyanin, azurin, rusticyanin, stellacyanin, quinol oxidase, and the periplasmic domain of cytochrome c oxidase subunit II.
Pssm-ID: 259860 [Multi-domain] Cd Length: 110 Bit Score: 42.99 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726212427 1384 AGARDITIETGTNLSYTMRTMRVSAGQPIALTLSNPDVVPHNWALAKPGTIDRVGELADRLISDPEAALRhyipattdvl 1463
Cdd:cd00920 5 ASDWGWSFTYNGVLLFGPPVLVVPVGDTVRVQFVNKLGENHSVTIAGFGVPVVAMAGGANPGLVNTLVIG---------- 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1726212427 1464 ahtdvvlPGERFTIYFNaPSQKGHYPYLCTFPGHWKV-MNGVMI 1506
Cdd:cd00920 75 -------PGESAEVTFT-TDQAGVYWFYCTIPGHNHAgMVGTIN 110
|
|
| Copper-bind |
pfam00127 |
Copper binding proteins, plastocyanin/azurin family; |
1394-1508 |
2.52e-03 |
|
Copper binding proteins, plastocyanin/azurin family;
Pssm-ID: 395076 [Multi-domain] Cd Length: 99 Bit Score: 38.89 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726212427 1394 GTNLSYTMRTMRVSAGQPIalTLSNPDVVPHNWALAKPGTIDrvGELADRLisdpeaalrhyipattDVLAHTDVVLPGE 1473
Cdd:pfam00127 9 SGDMVFEPKEITVKKGEKV--TFVNNAGMPHNVVFDKDGVPA--GVDADKV----------------KMGDHTKLIGGGE 68
|
90 100 110
....*....|....*....|....*....|....*.
gi 1726212427 1474 RFTIYFNAPsqkGHYPYLCTfPgHW-KVMNGVMIVE 1508
Cdd:pfam00127 69 TYSVTFDLA---GTYGFFCT-P-HQgAGMVGKVTVE 99
|
|
| COG3292 |
COG3292 |
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms]; |
939-1076 |
3.15e-03 |
|
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
Pssm-ID: 442521 [Multi-domain] Cd Length: 924 Bit Score: 42.28 E-value: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726212427 939 SALVCTMQGDVWRVTG---FQFPSKTSSWRRFASGL---HHALGIVADEDGIFVLGRDQ----------ITRLHDLNGDF 1002
Cdd:COG3292 127 RSIAEDSDGNIWVGTSnglYRYDPKTGKFKRFTLDGlpsNTITSLAEDADGNLWVDSDGnlwigtdgngLYRLDPNTGKF 206
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1726212427 1003 EAdyhecFSNAYQTSAAGHDFICGLERDPDGNFYIASGNQGLMRLSPDGQRAETIATGFRNPdglglLPDGTVT 1076
Cdd:COG3292 207 EH-----ITHDPDPNSLSSNSIYSLFEDREGNLWVGTYGGGLNYLDPNNSKFKSYRHNDPNG-----LSGNSVR 270
|
|
| SGL |
pfam08450 |
SMP-30/Gluconolactonase/LRE-like region; This family describes a region that is found in ... |
977-1101 |
7.78e-03 |
|
SMP-30/Gluconolactonase/LRE-like region; This family describes a region that is found in proteins expressed by a variety of eukaryotic and prokaryotic species. These proteins include various enzymes, such as senescence marker protein 30 (SMP-30), gluconolactonase and luciferin-regenerating enzyme (LRE). SMP-30 is known to hydrolyse diisopropyl phosphorofluoridate in the liver, and has been noted as having sequence similarity, in the region described in this family, with PON1 and LRE.
Pssm-ID: 462480 [Multi-domain] Cd Length: 246 Bit Score: 39.94 E-value: 7.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726212427 977 IVADEDGIFVLGRD--QITRLHDLNGDFEADYHecfSNayqtsaaghDFICglerDPDGNFYIAS---------GNQGLM 1045
Cdd:pfam08450 55 IVALKDGVALLDLAtgELTPLADPEDDDWPLNR---FN---------DGKV----DPDGRFWFGTmgddeapggDPGALY 118
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1726212427 1046 RLSPDGQrAETIATGFRNPDGLGLLPDGTvTVPASEgswTPASMICAVDPDRTGPL 1101
Cdd:pfam08450 119 RLDPDGK-LTRVLDGLTISNGLAWSPDGR-TLYFAD---SPARKIWAYDYDLDGGL 169
|
|
| Phytase-like |
pfam13449 |
Esterase-like activity of phytase; This is a repeated domain that carries several highly ... |
1026-1179 |
9.52e-03 |
|
Esterase-like activity of phytase; This is a repeated domain that carries several highly conserved Glu and Asp residues indicating the likelihood that the domain incorporates the enzymic activity of the PLC-like phospho-diesterase part of the proteins.
Pssm-ID: 433217 [Multi-domain] Cd Length: 284 Bit Score: 39.96 E-value: 9.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726212427 1026 GLERDPDGNFYIAS-GNQGLMRLSPDGQRAETIAT------------GFRN---PDGLGLLPDGTVTVPASEGSWtpasm 1089
Cdd:pfam13449 72 GIAVAPDGTFWVSSeGGPFILRFDLDGRLLRELPLpadflpdpspdaGLRRnkgFEGLALSPDGRGLYAALERPL----- 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726212427 1090 icavDPDRTGPLNERAAIPHFgyrGPREGVTPELPLAYLprsLDNSSGGQVFVDSDswgplsgqllhFSFGRGSHFLVL- 1168
Cdd:pfam13449 147 ----AQDGPGAPGSPLRILEY---DLATKGQTGGQFAYP---LDPVPAPGGNGLSD-----------LLALDDGRLLVLe 205
|
170
....*....|.
gi 1726212427 1169 RDRVGGQAQGA 1179
Cdd:pfam13449 206 RDFSLGLGNTK 216
|
|
| |
