|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11578 |
PRK11578 |
macrolide transporter subunit MacA; Provisional |
1-370 |
0e+00 |
|
macrolide transporter subunit MacA; Provisional
Pssm-ID: 183211 [Multi-domain] Cd Length: 370 Bit Score: 651.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296743 1 MNLKGKRRKLFLLLAVVVLAGGFWLWKVLNAPVPQYQTLIVRPGELQQNVLATGKLDALRKVDVGAQVSGQLKTLSVEIG 80
Cdd:PRK11578 1 MKKRKKVKKRYLIALVIVLAGGITLWRILNAPVPTYQTLIVRPGDLQQSVLATGKLDALRKVDVGAQVSGQLKTLSVAIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296743 81 DKVKKGQLLGVIDPEQAQNQIREVEAKLMELRAQRAQAQAERNLAQITLTRQQALAKTQAISKQDLDTAATELAVKQAQI 160
Cdd:PRK11578 81 DKVKKDQLLGVIDPEQAENQIKEVEATLMELRAQRQQAEAELKLARVTLSRQQRLAKTQAVSQQDLDTAATELAVKQAQI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296743 161 GTIDAQIKRNQASLDTAKTNLDYTQIVAPMAGEVTQITTLQGQTVIAAQQAPNILTLADMSTMLVKAQVSEADVIHLKPG 240
Cdd:PRK11578 161 GTIDAQIKRNQASLDTAKTNLDYTRIVAPMAGEVTQITTLQGQTVIAAQQAPNILTLADMSTMLVKAQVSEADVIHLKPG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296743 241 QKAWFTVLGDPQTRYEGVLKDILPTPEKVNDAIFYYARFEVPNPQGVLRLDMTAQVHIQLTGVKNVLTVPLSALGESAGD 320
Cdd:PRK11578 241 QKAWFTVLGDPLTRYEGVLKDILPTPEKVNDAIFYYARFEVPNPNGLLRLDMTAQVHIQLTDVKNVLTIPLSALGDPVGD 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 823296743 321 NRYKVKVLRNGETREREVVIGARNDTDVVVVKGLEEGEEVVTSESLPGAA 370
Cdd:PRK11578 321 NRYKVKLLRNGETREREVTIGARNDTDVEIVKGLEAGDEVIIGEAKPGAA 370
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
41-363 |
2.93e-79 |
|
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope biogenesis, Defense mechanisms];
Pssm-ID: 440606 [Multi-domain] Cd Length: 324 Bit Score: 246.01 E-value: 2.93e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296743 41 VRPGELQQNVLATGKLDALRKVDVGAQVSGQLKTLSVEIGDKVKKGQLLGVIDPEQAQNQireveakLMELRAQRAQAQA 120
Cdd:COG0845 3 VERGDVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAA-------LAQAQAQLAAAQA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296743 121 ERNLAQITLTRQQALAKTQAISKQDLDTAATELAVKQaqigtidAQIKRNQASLDTAKTNLDYTQIVAPMAGEVTQITTL 200
Cdd:COG0845 76 QLELAKAELERYKALLKKGAVSQQELDQAKAALDQAQ-------AALAAAQAALEQARANLAYTTIRAPFDGVVGERNVE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296743 201 QGQTVIAAQQapnILTLADMSTMLVKAQVSEADVIHLKPGQKAWFTVLGDPQTRYEGVLKDILPTPEKVNDAifYYARFE 280
Cdd:COG0845 149 PGQLVSAGTP---LFTIADLDPLEVEFDVPESDLARLKVGQPVTVTLDAGPGKTFEGKVTFIDPAVDPATRT--VRVRAE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296743 281 VPNPQGVLRLDMTAQVHIQLTGVKNVLTVPLSALGESAGDNRykVKVLRNGET-REREVVIGARNDTDVVVVKGLEEGEE 359
Cdd:COG0845 224 LPNPDGLLRPGMFVRVRIVLGERENALLVPASAVVRDGGGAY--VFVVDADGKvERRPVTLGRRDGDQVEVLSGLKAGDR 301
|
....
gi 823296743 360 VVTS 363
Cdd:COG0845 302 VVVS 305
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
38-363 |
1.31e-53 |
|
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion protein) component of the RND family of transporters. RND refers to Resistance, Nodulation, and cell Division. It is, in part, a subfamily of pfam00529 (Pfam release 7.5) but hits substantial numbers of proteins missed by that model. The related HlyD secretion protein, for which pfam00529 is named, is outside the scope of this model. Attributed functions imply outward transport. These functions include nodulation, acriflavin resistance, heavy metal efflux, and multidrug resistance proteins. Most members of this family are found in Gram-negative bacteria. The proposed function of MFP proteins is to bring the inner and outer membranes together and enable transport to the outside of the outer membrane. Note, however, that a few members of this family are found in Gram-positive bacteria, where there is no outer membrane. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 273776 [Multi-domain] Cd Length: 322 Bit Score: 179.82 E-value: 1.31e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296743 38 TLIVRPGELQQNVLATGKLDALRKVDVGAQVSGQLKTLSVEIGDKVKKGQLLGVIDPEQAQnqireveAKLMELRAQRAQ 117
Cdd:TIGR01730 3 VATVESETLANTLTFPGSLEAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQ-------LALQAALAQLAA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296743 118 AQAERNLAQITLTRQQALAKTQAISKQDLDTAATELAVKQaqigtidAQIKRNQASLDTAKTNLDYTQIVAPMAGEVTQI 197
Cdd:TIGR01730 76 AEAQLELAQRSFERAERLVKRNAVSQADLDDAKAAVEAAQ-------ADLEAAKASLASAQLNLRYTEIRAPFDGTIGRR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296743 198 TTLQGQTVIAAQqapNILTLADMSTMLVKAQVSEADVIHLKPGQKAWFTVLGDPQTRYEGVLKDILPTPEKVNDAIFYYA 277
Cdd:TIGR01730 149 LVEVGAYVTAGQ---TLATIVDLDPLEADFSVPERDLPQLRRGQTLTVELDALPGEEFKGKLRFIDPRVDSGTGTVRVRA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296743 278 RFevPNPQGVLRLDMTAQVHIQLTGVKNVLTVPLSALGEsaGDNRYKVKVLRN-GETREREVVIGARNDTDVVVVKGLEE 356
Cdd:TIGR01730 226 TF--PNPDGRLLPGMFGRVTISLKVRSSAIVVPTQAVIE--DLNGKYVYVVKNdGKVSKRPVEVGLRNGGYVEIESGLKA 301
|
....*..
gi 823296743 357 GEEVVTS 363
Cdd:TIGR01730 302 GDQIVTA 308
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
36-300 |
6.79e-46 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 159.83 E-value: 6.79e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296743 36 YQTLIVRPGELQQNVLATGKLDAlRKVDVGAQVSGQLKTLSVEIGDKVKKGQLLGVIDPEQAQNQIREVEAKL------- 108
Cdd:COG1566 21 LALWAAGRNGPDEPVTADGRVEA-RVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAALAQAEAQLaaaeaql 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296743 109 -------------MELRAQRAQAQAERNLAQITLTRQQALAKTQAISKQDLDTAATELAVKQAQ---------------- 159
Cdd:COG1566 100 arleaelgaeaeiAAAEAQLAAAQAQLDLAQRELERYQALYKKGAVSQQELDEARAALDAAQAQleaaqaqlaqaqaglr 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296743 160 ----IGTIDAQIKRNQASLDTAKTNLDYTQIVAPMAGEVTQITTLQGQTVIAAQQapnILTLADMSTMLVKAQVSEADVI 235
Cdd:COG1566 180 eeeeLAAAQAQVAQAEAALAQAELNLARTTIRAPVDGVVTNLNVEPGEVVSAGQP---LLTIVPLDDLWVEAYVPETDLG 256
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 823296743 236 HLKPGQKAWFTVLGDPQTRYEGVLKDILPTPEKV--------NDAIFYYARFEVPNPQGV-LRLDMTAQVHIQL 300
Cdd:COG1566 257 RVKPGQPVEVRVDAYPDRVFEGKVTSISPGAGFTsppknatgNVVQRYPVRIRLDNPDPEpLRPGMSATVEIDT 330
|
|
| PRK10476 |
PRK10476 |
multidrug transporter subunit MdtN; |
61-262 |
2.94e-22 |
|
multidrug transporter subunit MdtN;
Pssm-ID: 182488 [Multi-domain] Cd Length: 346 Bit Score: 96.25 E-value: 2.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296743 61 KVDVGAQVSGQLKTLSVEIGDKVKKGQLLGVIDP-------EQAQNQIREVEAKLMELR--------------AQRAQAQ 119
Cdd:PRK10476 48 VVHVASEVGGRIVELAVTENQAVKKGDLLFRIDPrpyeltvAQAQADLALADAQIMTTQrsvdaersnaasanEQVERAR 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296743 120 AERNLAQITLTRQQALAKTQAISKQDLDTAAT-----ELAVKQAQ---------IGTID---AQIKRNQASLDTAKTNLD 182
Cdd:PRK10476 128 ANAKLATRTLERLEPLLAKGYVSAQQVDQARTaqrdaEVSLNQALlqaqaaaaaVGGVDalvAQRAAREAALAIAELHLE 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296743 183 YTQIVAPMAGEVTQITTLQGQTVIAAQqapNILTLADMSTMLVKAQVSEADVIHLKPGQKAWFTVLGDPQTRYEGVLKDI 262
Cdd:PRK10476 208 DTTVRAPFDGRVVGLKVSVGEFAAPMQ---PIFTLIDTDHWYAIANFRETDLKNIRVGDCATVYSMIDRGRPFEGKVDSI 284
|
|
| PRK11556 |
PRK11556 |
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit; |
30-362 |
1.86e-21 |
|
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 183194 [Multi-domain] Cd Length: 415 Bit Score: 94.86 E-value: 1.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296743 30 NAPVPQYQTLIVRPGELQQNVLATGKLDALRKVDVGAQVSGQLKTLSVEIGDKVKKGQLLGVIDPEQAQNQIREVEAKLM 109
Cdd:PRK11556 56 SGPLAPVQAATATEQAVPRYLTGLGTVTAANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPRPFKVALAQAQGQLA 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296743 110 ELRAqrAQAQAERNLAqitltRQQALAKTQAISKQDLDTaatelavKQAQIGTIDAQIKRNQASLDTAKTNLDYTQIVAP 189
Cdd:PRK11556 136 KDQA--TLANARRDLA-----RYQQLAKTNLVSRQELDA-------QQALVSETEGTIKADEASVASAQLQLDYSRITAP 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296743 190 MAGEV--------TQITTlqGQT---VIAAQQAP--NILTL--ADMSTMLvKAQVSEADVIhlkpgQKAWFTvlGDPQTR 254
Cdd:PRK11556 202 ISGRVglkqvdvgNQISS--GDTtgiVVITQTHPidLVFTLpeSDIATVV-QAQKAGKPLV-----VEAWDR--TNSKKL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296743 255 YEGVLKDILPTPEKVNDAIFYYARFevPNPQGVLRLDMTAQVHIQLTGVKNVLTVPLSALgeSAGDNRYKVKVLrNGETR 334
Cdd:PRK11556 272 SEGTLLSLDNQIDATTGTIKLKARF--NNQDDALFPNQFVNARMLVDTLQNAVVIPTAAL--QMGNEGHFVWVL-NDENK 346
|
330 340 350
....*....|....*....|....*....|
gi 823296743 335 --EREVVIGARNDTDVVVVKGLEEGEEVVT 362
Cdd:PRK11556 347 vsKHLVTPGIQDSQKVVISAGLSAGDRVVT 376
|
|
| PRK03598 |
PRK03598 |
putative efflux pump membrane fusion protein; Provisional |
60-267 |
8.05e-19 |
|
putative efflux pump membrane fusion protein; Provisional
Pssm-ID: 235136 [Multi-domain] Cd Length: 331 Bit Score: 86.17 E-value: 8.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296743 60 RKVDVGAQVSGQLKTLSVEIGDKVKKGQLLGVIDPEQAQNQIREVEA----------KLME---------LRAQRAQAQA 120
Cdd:PRK03598 42 RTVNLGFRVGGRLASLAVDEGDAVKAGQVLGELDAAPYENALMQAKAnvsvaqaqldLMLAgyrdeeiaqARAAVKQAQA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296743 121 ERNLAQITLTRQQALAKTQAISKQDLDTAATELAVKQAQ-------------------IGTIDAQIKRNQASLDTAKTNL 181
Cdd:PRK03598 122 AYDYAQNFYNRQQGLWKSRTISANDLENARSSRDQAQATlksaqdklsqyregnrpqdIAQAKASLAQAQAALAQAELNL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296743 182 DYTQIVAPMAGEVTQITTLQGqTVIAAQQApnILTLADMSTMLVKAQVSEADVIHLKPGQKAWFTVLGDPQTRYEGVLKD 261
Cdd:PRK03598 202 QDTELIAPSDGTILTRAVEPG-TMLNAGST--VFTLSLTRPVWVRAYVDERNLGQAQPGRKVLLYTDGRPDKPYHGQIGF 278
|
....*.
gi 823296743 262 ILPTPE 267
Cdd:PRK03598 279 VSPTAE 284
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
43-235 |
1.51e-18 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 85.17 E-value: 1.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296743 43 PGELQQNVLATGKLDALRKVD-VGAQVSGQLKTLSVEIGDKVKKGQLLGVIDPEQAQNQIREVEAKLMELRAQRAQAQAE 121
Cdd:pfam00529 1 LAPLTKGVEAPGRVVVSGNAKaVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296743 122 RNlaqitltRQQALAKTQAISKQDLDTAATELavKQAQigtidAQIKRNQASLDTAKTNLDYTQIVAPMAGEVTQITTLQ 201
Cdd:pfam00529 81 LD-------RLQALESELAISRQDYDGATAQL--RAAQ-----AAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTA 146
|
170 180 190
....*....|....*....|....*....|....
gi 823296743 202 GQTVIAAQQAPNIlTLADMSTMLVKAQVSEADVI 235
Cdd:pfam00529 147 GALVAQAQANLLA-TVAQLDQIYVQITQSAAENQ 179
|
|
| PRK09859 |
PRK09859 |
multidrug transporter subunit MdtE; |
31-363 |
7.19e-18 |
|
multidrug transporter subunit MdtE;
Pssm-ID: 137559 [Multi-domain] Cd Length: 385 Bit Score: 84.00 E-value: 7.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296743 31 APVPQYQTLIVRPGELQQNVLATGKLDALRKVDVGAQVSGQLKTLSVEIGDKVKKGQLLGVIDPEQAQnqireveAKLME 110
Cdd:PRK09859 31 AMTPEVGVVTLSPGSVNVLSELPGRTVPYEVAEIRPQVGGIIIKRNFIEGDKVNQGDSLYQIDPAPLQ-------AELNS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296743 111 LRAQRAQAQAERNLAQITLTRQQALAKTQAISKQDLDTAATelavkqaQIGTIDAQIKRNQASLDTAKTNLDYTQIVAPM 190
Cdd:PRK09859 104 AKGSLAKALSTASNARITFNRQASLLKTNYVSRQDYDTART-------QLNEAEANVTVAKAAVEQATINLQYANVTSPI 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296743 191 AGeVTQITTLQGQTVIAAQQAPNILTLADMSTMLV------------KAQVSEADVIHLKPGQKAWFTVLGDPQTRYEGV 258
Cdd:PRK09859 177 TG-VSGKSSVTVGALVTANQADSLVTVQRLDPIYVdltqsvqdflrmKEEVASGQIKQVQGSTPVQLNLENGKRYSQTGT 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296743 259 LKDILPTPEKVNDAIFYYARFevPNPQGVLRLDMTAQVHIQLTGVKNVLTVPLSALGESAGDNRYKVKVLRNGETREREV 338
Cdd:PRK09859 256 LKFSDPTVDETTGSVTLRAIF--PNPNGDLLPGMYVTALVDEGSRQNVLLVPQEGVTHNAQGKATALILDKDDVVQLREI 333
|
330 340
....*....|....*....|....*
gi 823296743 339 VIGARNDTDVVVVKGLEEGEEVVTS 363
Cdd:PRK09859 334 EASKAIGDQWVVTSGLQAGDRVIVS 358
|
|
| PRK15030 |
PRK15030 |
multidrug efflux RND transporter periplasmic adaptor subunit AcrA; |
33-363 |
3.76e-17 |
|
multidrug efflux RND transporter periplasmic adaptor subunit AcrA;
Pssm-ID: 184990 [Multi-domain] Cd Length: 397 Bit Score: 82.07 E-value: 3.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296743 33 VPQYQTLIVRPGELQQNVLATGKLDALRKVDVGAQVSGQLKTLSVEIGDKVKKGQLLGVIDPEQAQNQIREVEAKLmelr 112
Cdd:PRK15030 37 MPAVGVVTVKTEPLQITTELPGRTSAYRIAEVRPQVSGIILKRNFKEGSDIEAGVSLYQIDPATYQATYDSAKGDL---- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296743 113 aqrAQAQAERNLAQITLTRQQALAKTQAISKQDLDTAATElaVKQAqigtiDAQIKRNQASLDTAKTNLDYTQIVAPMAG 192
Cdd:PRK15030 113 ---AKAQAAANIAQLTVNRYQKLLGTQYISKQEYDQALAD--AQQA-----NAAVTAAKAAVETARINLAYTKVTSPISG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296743 193 EVTQITTLQGqTVIAAQQAPNILTLADMSTMLVKAQVSEADVIHLK----------PGQKAWFTVLGDPQTRY--EGVLK 260
Cdd:PRK15030 183 RIGKSNVTEG-ALVQNGQATALATVQQLDPIYVDVTQSSNDFLRLKqelangtlkqENGKAKVSLITSDGIKFpqDGTLE 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296743 261 DILPTPEKVNDAIFYYARFevPNPQGVLRLDMTAQVHIQLTGVKNVLTVPLSALGESAGDNRYKVKVLRNGETREREVVI 340
Cdd:PRK15030 262 FSDVTVDQTTGSITLRAIF--PNPDHTLLPGMFVRARLEEGLNPNAILVPQQGVTRTPRGDATVLVVGADDKVETRPIVA 339
|
330 340
....*....|....*....|...
gi 823296743 341 GARNDTDVVVVKGLEEGEEVVTS 363
Cdd:PRK15030 340 SQAIGDKWLVTEGLKAGDRVVIS 362
|
|
| HlyD_D23 |
pfam16576 |
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ... |
45-294 |
6.27e-17 |
|
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and 3 of the membrane-fusion proteins CusB and HlyD, which forms a barrel-sandwich. CusB and HlyD proteins are membrane fusion proteins of the CusCFBA copper efflux system in E.coli and related bacteria. The whole molecule hinges between D2 and D3. Efflux systems of this resistance-nodulation-division group - RND - have been developed to excrete poisonous metal ions, and in E.coli the only one that deals with silver and copper is the CusA transporter. The transporter CusA works in conjunction with a periplasmic component that is a membrane fusion protein, eg CusB, and an outer-membrane channel component CusC in a CusABC complex driven by import of protons.
Pssm-ID: 435440 [Multi-domain] Cd Length: 214 Bit Score: 78.70 E-value: 6.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296743 45 ELQQNVLATGKL--DALRKVDVGAQVSGQLKTLSV-EIGDKVKKGQLLGVID-PEQAQnqireveaklmelraqraqAQA 120
Cdd:pfam16576 1 PLSRTIRAVGRVayDERRLAHVHARVEGWIEKLYVnATGDPVKKGQPLAELYsPELVA-------------------AQQ 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296743 121 ERnlaqitltrQQALAKTQAISKQDLDTAATE----LAVKQAQIgtidAQIKRNQasldTAKTNLDytqIVAPMAGEVTQ 196
Cdd:pfam16576 62 EY---------LLALRSGDALSKSELLRAARQrlrlLGMPEAQI----AELERTG----KVQPTVT---VYAPISGVVTE 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296743 197 ITTLQGQTVIAAQqapNILTLADMSTMLVKAQVSEADVIHLKPGQKAWFTVLGDPQTRYEGVLKDILPTPEKVNDAIfyY 276
Cdd:pfam16576 122 LNVREGMYVQPGD---TLFTIADLSTVWVEADVPEQDLALVKVGQPAEVTLPALPGKTFEGKVDYIYPTLDPKTRTV--R 196
|
250
....*....|....*...
gi 823296743 277 ARFEVPNPQGVLRLDMTA 294
Cdd:pfam16576 197 VRIELPNPDGRLKPGMFA 214
|
|
| PRK09578 |
PRK09578 |
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit; |
30-363 |
1.62e-15 |
|
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 169982 [Multi-domain] Cd Length: 385 Bit Score: 77.14 E-value: 1.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296743 30 NAPVPQYQTLIVRPGELQQNVLATGKLDALRKVDVGAQVSGQLKTLSVEIGDKVKKGQLLGVIDPEQaqnqireVEAKLM 109
Cdd:PRK09578 32 AAAPREATVVTVRPTSVPMTVELPGRLDAYRQAEVRARVAGIVTARTYEEGQEVKQGAVLFRIDPAP-------LKAARD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296743 110 ELRAQRAQAQAERNLAQITLTRQQALAKTQAISKQDLDTAATElaVKQAQigtidAQIKRNQASLDTAKTNLDYTQIVAP 189
Cdd:PRK09578 105 AAAGALAKAEAAHLAALDKRRRYDDLVRDRAVSERDYTEAVAD--ERQAK-----AAVASAKAELARAQLQLDYATVTAP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296743 190 MAGEVTQITTLQGQTViaAQQAPNILTLAD-MSTMLVKAQVSEADVIHLKPGQKA-WFTVLGDPQTRYEGVLKDILPTPE 267
Cdd:PRK09578 178 IDGRARRALVTEGALV--GQDQATPLTTVEqLDPIYVNFSQPAADVEALRRAVKSgRATGIAQQDVAVTLVRADGSEYPL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296743 268 K------------VNDAIFYYARFevPNPQGVLRLDMTAQVHIQLTGVKNVLTVPLSALGESAGdnRYKVKVL-RNGETR 334
Cdd:PRK09578 256 KgkllfsdlavdpTTDTVAMRALF--PNPERELLPGAYVRIALDRAVNPRAILVPRDALLRTAD--SASVKVVgQNGKVR 331
|
330 340
....*....|....*....|....*....
gi 823296743 335 EREVVIGARNDTDVVVVKGLEEGEEVVTS 363
Cdd:PRK09578 332 DVEVEADQMSGRDWIVTRGLAGGERVIVD 360
|
|
| heterocyst_DevB |
TIGR02971 |
ABC exporter membrane fusion protein, DevB family; Members of this protein family are found ... |
72-249 |
3.49e-13 |
|
ABC exporter membrane fusion protein, DevB family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. DevB from Anabaena sp. strain PCC 7120 is partially characterized as a membrane fusion protein of the DevBCA ABC exporter, probably a glycolipid exporter, required for heterocyst formation. Most Cyanobacteria have one member only, but Nostoc sp. PCC 7120 has seven members.
Pssm-ID: 213754 [Multi-domain] Cd Length: 327 Bit Score: 69.47 E-value: 3.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296743 72 LKTLSVEIGDKVKKGQLLGVIDP--------EQAQNQIREVEAKLMELRAQRAQAQ------------------------ 119
Cdd:TIGR02971 27 IKKLLVAEGDRVQAGQVLAELDSrpertaelDVARTQLDEAKARLAQVRAGAKKGEiaaqraaraaaklfkdvaaqqatl 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296743 120 ----AERNLAQITLTRQQALAKTQAISKQDLD------------------------------TAATELAVKQAQIGTIDA 165
Cdd:TIGR02971 107 nrleAELETAQREVDRYRSLFRDGAVSASDLDskalklrtaeeeleealasrseqidgaraaLASLAEEVRETDVDLAQA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296743 166 QIKRNQASLDTAKTNLDYTQIVAPMAGEVTQITTLQGQTViaaqQAPNILTLADMSTMLVKAQVSEADVIHLKPGQKAWF 245
Cdd:TIGR02971 187 EVKSALEAVQQAEALLELTYVKAPIDGRVLKIHAREGEVI----GSEGILEMGDTSQMYAVAEVYETDINRVRVGQRATI 262
|
....
gi 823296743 246 TVLG 249
Cdd:TIGR02971 263 TSTA 266
|
|
| HlyD_3 |
pfam13437 |
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ... |
186-289 |
5.52e-12 |
|
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator HlyD proteins.
Pssm-ID: 433206 [Multi-domain] Cd Length: 104 Bit Score: 61.61 E-value: 5.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296743 186 IVAPMAGEVTQITTLQGQtVIAAQQapNILTLADMSTMLVKAQVSEADVIHLKPGQKAWFTVLGDPQTRYEGVLKDILPT 265
Cdd:pfam13437 2 IRAPVDGVVAELNVEEGQ-VVQAGD--PLATIVPPDRLLVEAFVPAADLGSLKKGQKVTLKLDPGSDYTLEGKVVRISPT 78
|
90 100
....*....|....*....|....
gi 823296743 266 PEKVNDAIFYYARFEVPNPQGVLR 289
Cdd:pfam13437 79 VDPDTGVIPVRVSIENPKTPIPLL 102
|
|
| PRK10559 |
PRK10559 |
p-hydroxybenzoic acid efflux pump subunit AaeA; |
62-258 |
1.09e-09 |
|
p-hydroxybenzoic acid efflux pump subunit AaeA;
Pssm-ID: 182548 [Multi-domain] Cd Length: 310 Bit Score: 58.98 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296743 62 VDVGAQVSGQLKTLSVEIGDKVKKGQLLGVIDPEQAQNQIREVEAklmELRAQRAQAQAERNLAQitltRQQALAkTQAI 141
Cdd:PRK10559 48 VAIAPDVSGLITQVNVHDNQLVKKGQVLFTIDQPRYQKALAEAEA---DVAYYQVLAQEKRREAG----RRNRLG-VQAM 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296743 142 SKQDLDTAATELAvkqaqigTIDAQIKRNQASLDTAKTNLDYTQIVAPMAGEVTQITTLQGQTVIAAQQApniLTLADMS 221
Cdd:PRK10559 120 SREEIDQANNVLQ-------TVLHQLAKAQATRDLAKLDLERTVIRAPADGWVTNLNVYTGEFITRGSTA---VALVKQN 189
|
170 180 190
....*....|....*....|....*....|....*..
gi 823296743 222 TMLVKAQVSEADVIHLKPGQKAWFTVLGDPQTRYEGV 258
Cdd:PRK10559 190 SFYVLAYMEETKLEGVRPGYRAEITPLGSNKVLKGTV 226
|
|
| PRK15136 |
PRK15136 |
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA; |
61-250 |
3.41e-08 |
|
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;
Pssm-ID: 185090 [Multi-domain] Cd Length: 390 Bit Score: 54.70 E-value: 3.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296743 61 KVDVGAQVSGQLKTLSVEIGDKVKKGQLLGVIDP-------EQAQ----NQIREVEAKLM---ELRAQRAQAQAERNLAQ 126
Cdd:PRK15136 61 QVQIMSQVSGSVTKVWADNTDFVKEGDVLVTLDPtdaeqafEKAKtalaNSVRQTHQLMInskQYQANIELQKTALAQAQ 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296743 127 ITLTRQQALAKTQAISKQDLDTAATELAVKQAQIGTIDAQIKRNQAS-LDT-----------------AKTNLDYTQIVA 188
Cdd:PRK15136 141 SDLNRRVPLGNANLIGREELQHARDAVASAQAQLDVAIQQYNANQAMiLNTpledqpavqqaatevrnAWLALQRTKIVS 220
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 823296743 189 PMAGEVTQITTLQGqtviaAQQAPN--ILTLADMSTMLVKAQVSEADVIHLKPGQKAwfTVLGD 250
Cdd:PRK15136 221 PMTGYVSRRSVQVG-----AQISPTtpLMAVVPATNLWVDANFKETQLANMRIGQPA--TITSD 277
|
|
| type_I_hlyD |
TIGR01843 |
type I secretion membrane fusion protein, HlyD family; Type I secretion is an ABC transport ... |
44-307 |
3.10e-06 |
|
type I secretion membrane fusion protein, HlyD family; Type I secretion is an ABC transport process that exports proteins, without cleavage of any signal sequence, from the cytosol to extracellular medium across both inner and outer membranes. The secretion signal is found in the C-terminus of the transported protein. This model represents the adaptor protein between the ATP-binding cassette (ABC) protein of the inner membrane and the outer membrane protein, and is called the membrane fusion protein. This model selects a subfamily closely related to HlyD; it is defined narrowly and excludes, for example, colicin V secretion protein CvaA and multidrug efflux proteins. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 130902 [Multi-domain] Cd Length: 423 Bit Score: 48.85 E-value: 3.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296743 44 GELQQNVLATGKLDAL--RKVdVGAQVSGQLKTLSVEIGDKVKKGQLLGVIDPEQAQNQIREVEAKLMELRAQRAQAQAE 121
Cdd:TIGR01843 25 APLDVVATATGKVVPSgnVKV-VQHLEGGIVREILVREGDRVKAGQVLVELDATDVEADAAELESQVLRLEAEVARLRAE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296743 122 RN--------------------------------------------LAQI------------------------------ 127
Cdd:TIGR01843 104 ADsqaaiefpddllsaedpavpelikgqqslfesrkstlraqleliLAQIkqleaelaglqaqlqalrqqleviseelea 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296743 128 --------------TLTRQQALAKTQ---AISKQDLDTAATELAVKQAQIGTIDAQIKRN-QASLDTAKTNL-DYTQ--- 185
Cdd:TIGR01843 184 rrklkekglvsrleLLELERERAEAQgelGRLEAELEVLKRQIDELQLERQQIEQTFREEvLEELTEAQARLaELRErln 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296743 186 ----------IVAPMAGEVTQIT-TLQGQTVIAAQQAPNILTLADmsTMLVKAQVSEADVIHLKPGQKAWFTVLGDPQTR 254
Cdd:TIGR01843 264 kardrlqrliIRSPVDGTVQSLKvHTVGGVVQPGETLMEIVPEDD--PLEIEAKLSPKDIGFVHVGQPAEIKFSAFPYRR 341
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 823296743 255 Y---EGVLKDILP--TPEKVNDAIFYYARFEVPNPQGVLRLD-------MTAQVHIQlTGVKNVL 307
Cdd:TIGR01843 342 YgilNGKVKSISPdtFTDERGGGPYYRVRISIDQNTLGIGPKglelspgMPVTADIK-TGERTVI 405
|
|
| Biotin_lipoyl_2 |
pfam13533 |
Biotin-lipoyl like; |
60-108 |
3.92e-06 |
|
Biotin-lipoyl like;
Pssm-ID: 433286 Cd Length: 50 Bit Score: 43.59 E-value: 3.92e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 823296743 60 RKVDVGAQVSGQLKTLSVEIGDKVKKGQLLGVIDPEQAQNQIREVEAKL 108
Cdd:pfam13533 1 PVVKIASPVSGKVVAVNVKEGQQVKKGDVLATLDSPELQLQLQQAEAQL 49
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
95-208 |
4.68e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 4.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296743 95 EQAQNQIREVEAKLMELRAQRAQAQAErnlaqitltRQQALAKTQAISKQDLDTAATELAVKQAQIGTIDAQIKRNQASL 174
Cdd:COG4717 152 EERLEELRELEEELEELEAELAELQEE---------LEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEEL 222
|
90 100 110
....*....|....*....|....*....|....
gi 823296743 175 DTAKTNLDYTQIVAPMAGEVTQITTLQGQTVIAA 208
Cdd:COG4717 223 EELEEELEQLENELEAAALEERLKEARLLLLIAA 256
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
88-182 |
7.10e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.29 E-value: 7.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296743 88 LLGVIDPEQAQNQIREVEAKLMELRAQRAQAQAErnLAQITLTRQQALAKTQAISKQdLDTAATELAVKQAQIGTIDAQI 167
Cdd:COG4942 9 LLLALAAAAQADAAAEAEAELEQLQQEIAELEKE--LAALKKEEKALLKQLAALERR-IAALARRIRALEQELAALEAEL 85
|
90
....*....|....*
gi 823296743 168 KRNQASLDTAKTNLD 182
Cdd:COG4942 86 AELEKEIAELRAELE 100
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
95-182 |
8.12e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.46 E-value: 8.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296743 95 EQAQNQIREVEAKLMELRAQRAQAQAERNLAQ----------ITLTRQQALAKTQAIS-KQDLDTAATELAVKQAQIGTI 163
Cdd:COG1196 256 EELEAELAELEAELEELRLELEELELELEEAQaeeyellaelARLEQDIARLEERRRElEERLEELEEELAELEEELEEL 335
|
90
....*....|....*....
gi 823296743 164 DAQIKRNQASLDTAKTNLD 182
Cdd:COG1196 336 EEELEELEEELEEAEEELE 354
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
95-188 |
1.52e-03 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 40.22 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296743 95 EQAQNQIREVEAKLMELRAQR----AQAQAERNLAQI-TLTRQQALAKTQ-AISKQDLDTAATELAVKQAQIGTIDAQIK 168
Cdd:COG3524 187 ERAEERLRDAREALLAFRNRNgildPEATAEALLQLIaTLEGQLAELEAElAALRSYLSPNSPQVRQLRRRIAALEKQIA 266
|
90 100
....*....|....*....|
gi 823296743 169 RNQASLDTAKTNLDYTQIVA 188
Cdd:COG3524 267 AERARLTGASGGDSLASLLA 286
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
93-182 |
2.30e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 39.04 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296743 93 DPEQAQNQ-IREVEAKLMELRAQRAQAQAERNLAQITLTRQQALAKT------QAISKQDLD---TAATELAVKQAQIGT 162
Cdd:COG1842 23 DPEKMLDQaIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKweekarLALEKGREDlarEALERKAELEAQAEA 102
|
90 100
....*....|....*....|
gi 823296743 163 IDAQIKRNQASLDTAKTNLD 182
Cdd:COG1842 103 LEAQLAQLEEQVEKLKEALR 122
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
103-186 |
2.51e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.14 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296743 103 EVEAKLMELRAQRAQAQAERNLAQitlTRQQALAKTQAISKQDLDTAATELAVKQAQIGTIDAQIKRNQASLDTAKTNLD 182
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELE---DELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKE 90
|
....
gi 823296743 183 YTQI 186
Cdd:COG1579 91 YEAL 94
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
92-203 |
4.31e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.13 E-value: 4.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296743 92 IDPEQAQNQIREVEAKLMELRAQRAQ-AQAERNLAQItltrqqalaktqaisKQDLDTAATELAVKQAQIGTIDAQIKRN 170
Cdd:COG4913 661 IDVASAEREIAELEAELERLDASSDDlAALEEQLEEL---------------EAELEELEEELDELKGEIGRLEKELEQA 725
|
90 100 110
....*....|....*....|....*....|...
gi 823296743 171 QASLDTAKTNLDYtqivAPMAGEVTQITTLQGQ 203
Cdd:COG4913 726 EEELDELQDRLEA----AEDLARLELRALLEER 754
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
57-175 |
6.16e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 38.21 E-value: 6.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296743 57 DALRKVDVGAQVSGQLKTLSV-----EIGDKVKKGQLLGVIDPEQaQNQIREVEAKLMELRAQRAQAQAERNLAQITLTR 131
Cdd:COG4942 104 EELAELLRALYRLGRQPPLALllspeDFLDAVRRLQYLKYLAPAR-REQAEELRADLAELAALRAELEAERAELEALLAE 182
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 823296743 132 QQALAKTQAISKQDLDTAATELAVKQAQIGTIDAQIKRNQASLD 175
Cdd:COG4942 183 LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE 226
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
95-181 |
6.53e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 38.50 E-value: 6.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296743 95 EQAQNQIREVEAKLMELRAQRAQAQAERNLAQitlTRQQALAKTQAISKQDLDTAATELAVKQAQIGTIDAQIKRNQASL 174
Cdd:TIGR02168 256 EELTAELQELEEKLEELRLEVSELEEEIEELQ---KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKL 332
|
....*..
gi 823296743 175 DTAKTNL 181
Cdd:TIGR02168 333 DELAEEL 339
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
35-92 |
9.97e-03 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 38.20 E-value: 9.97e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 823296743 35 QYQTLIVRPGELQQNVLATGKLDALRKVDVGAQVSGQLKTLSVEIGDKVKKGQLLGVI 92
Cdd:PRK12999 1050 QPREVQVRDRSVKSTVAAREKADPGNPGHVGAPMPGSVVTVLVKEGDEVKAGDPLAVI 1107
|
|
| |
