|
Name |
Accession |
Description |
Interval |
E-value |
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
38-399 |
9.83e-36 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 134.02 E-value: 9.83e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624114703 38 FMAGLVLMIFLVWGEYTKRSTVKGQLIPDKG-----LVQVYTTTAGVIIEKYVSEGQAVKAGDMLYKISTTRhtdagnvq 112
Cdd:COG1566 9 LLALVLLLLALGLALWAAGRNGPDEPVTADGrvearVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTD-------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624114703 113 siidkeltFKRQLiehEITRTKQAQAAEKRNIANTIERLQVDMDKLQAQIELQTHQVAIAKETLTRYEFAMQSEAVSKQE 192
Cdd:COG1566 81 --------LQAAL---AQAEAQLAAAEAQLARLEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKGAVSQQE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624114703 193 LESQTMAYNTQLNSLTALEREKEMIAKQIKEQTiALSRLEHEhrttLLQYERTLsdnksDSIQNQANDTlIIKAQVDGVA 272
Cdd:COG1566 150 LDEARAALDAAQAQLEAAQAQLAQAQAGLREEE-ELAAAQAQ----VAQAEAAL-----AQAELNLART-TIRAPVDGVV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624114703 273 SVAHADVGQFVDSSQSLVSTLPNDSyLIAVMYVPSRAIGFVKTDDEVLLRYVAYPYQKFghaKGRIISVAktahagqnlP 352
Cdd:COG1566 219 TNLNVEPGEVVSAGQPLLTIVPLDD-LWVEAYVPETDLGRVKPGQPVEVRVDAYPDRVF---EGKVTSIS---------P 285
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2624114703 353 TIGTVSATEQIAN--EPMYVIKAYLDKQTitaygkELPLAVGMTLEGDV 399
Cdd:COG1566 286 GAGFTSPPKNATGnvVQRYPVRIRLDNPD------PEPLRPGMSATVEI 328
|
|
| type_I_hlyD |
TIGR01843 |
type I secretion membrane fusion protein, HlyD family; Type I secretion is an ABC transport ... |
38-415 |
1.84e-27 |
|
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: 113.18 E-value: 1.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624114703 38 FMAGLVLmIFLVWGEYTKRSTV---KGQLIPD--KGLVQVYTTtaGVIIEKYVSEGQAVKAGDMLYKISTTR-------- 104
Cdd:TIGR01843 10 LIAGLVV-IFFLWAYFAPLDVVataTGKVVPSgnVKVVQHLEG--GIVREILVREGDRVKAGQVLVELDATDveadaael 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624114703 105 -------HTDAGNVQSIIDKELTFK-------------RQLIEHE---ITRTKQAQAAEKRNIANTIERLQVDMDKLQAQ 161
Cdd:TIGR01843 87 esqvlrlEAEVARLRAEADSQAAIEfpddllsaedpavPELIKGQqslFESRKSTLRAQLELILAQIKQLEAELAGLQAQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624114703 162 IELQTHQVAIAKETLTRYEFAMQSEAVSKQ---ELESQTMAYNTQLNSLTA----LEREKEMIAKQIkEQTIALSRLE-- 232
Cdd:TIGR01843 167 LQALRQQLEVISEELEARRKLKEKGLVSRLellELERERAEAQGELGRLEAelevLKRQIDELQLER-QQIEQTFREEvl 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624114703 233 ---HEHRTTLLQYERTLSDNKSdsiQNQAndtLIIKAQVDG-VASVAHADVGQFVDSSQSLVSTLPNDSYLIAVMYVPSR 308
Cdd:TIGR01843 246 eelTEAQARLAELRERLNKARD---RLQR---LIIRSPVDGtVQSLKVHTVGGVVQPGETLMEIVPEDDPLEIEAKLSPK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624114703 309 AIGFVKTDDEVLLRYVAYPYQKFGHAKGRIISVAKTahagqnlptigtvSATEQIANEPMYVIKAYLDKQTITAYGKELP 388
Cdd:TIGR01843 320 DIGFVHVGQPAEIKFSAFPYRRYGILNGKVKSISPD-------------TFTDERGGGPYYRVRISIDQNTLGIGPKGLE 386
|
410 420
....*....|....*....|....*..
gi 2624114703 389 LAVGMTLEGDVMHETRKLYEWVLEPLY 415
Cdd:TIGR01843 387 LSPGMPVTADIKTGERTVIEYLLKPIT 413
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
50-345 |
1.25e-26 |
|
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: 109.05 E-value: 1.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624114703 50 WGEYTKRSTVKGQLIPDKGLVQVYTTTAGVIIEKYVSEGQAVKAGDMLYKISTTRHTdaGNVQSIIDKELTFKRQLIEHE 129
Cdd:pfam00529 1 LAPLTKGVEAPGRVVVSGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQ--AALDSAEAQLAKAQAQVARLQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624114703 130 ITRTK-QAQAAEKRNIANTIERLQVDMDKLQAQIELQTHQVAIAKETLTRYEFAMQSEAVSKQELESQTMAYNTQLNSLT 208
Cdd:pfam00529 79 AELDRlQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQANLL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624114703 209 ALEREKEMIAKQIKEQTIALSRLEhehRTTLLQYERTLSDNKSDSIQNQANDT-LIIKAQVDG-VASVAHADVGQFVDSS 286
Cdd:pfam00529 159 ATVAQLDQIYVQITQSAAENQAEV---RSELSGAQLQIAEAEAELKLAKLDLErTEIRAPVDGtVAFLSVTVDGGTVSAG 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2624114703 287 QSLVSTLPNDSYLIAVMYVPSRaIGFVKTDDEVLLRYVAYPYQKFGHAKGRIISVAKTA 345
Cdd:pfam00529 236 LRLMFVVPEDNLLVPGMFVETQ-LDQVRVGQPVLIPFDAFPQTKTGRFTGVVVGISPDT 293
|
|
| PRK10476 |
PRK10476 |
multidrug transporter subunit MdtN; |
40-301 |
9.02e-05 |
|
multidrug transporter subunit MdtN;
Pssm-ID: 182488 [Multi-domain] Cd Length: 346 Bit Score: 44.25 E-value: 9.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624114703 40 AGLVLMIFLVWGEYTKRSTVKGQLipDKGLVQVYTTTAGVIIEKYVSEGQAVKAGDMLYKIS------TTRHTDAGnvQS 113
Cdd:PRK10476 21 LAIVALVFVIWRTDSAPSTDDAYI--DADVVHVASEVGGRIVELAVTENQAVKKGDLLFRIDprpyelTVAQAQAD--LA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624114703 114 IIDKELTFKRQLIEHEITRTKQAQAAEKRNIAN------TIERLQvdmdKLQAQIELQTHQVAIAKEtltryefAMQSEA 187
Cdd:PRK10476 97 LADAQIMTTQRSVDAERSNAASANEQVERARANaklatrTLERLE----PLLAKGYVSAQQVDQART-------AQRDAE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624114703 188 VSKQELESQTMAyntqlnSLTALEREKEMIAkQIKEQTIALSRLEHEHRTTllqyertlsdnksdsiqnqandtlIIKAQ 267
Cdd:PRK10476 166 VSLNQALLQAQA------AAAAVGGVDALVA-QRAAREAALAIAELHLEDT------------------------TVRAP 214
|
250 260 270
....*....|....*....|....*....|....*.
gi 2624114703 268 VDGVASVAHADVGQFVDSSQSLVsTLPNDS--YLIA 301
Cdd:PRK10476 215 FDGRVVGLKVSVGEFAAPMQPIF-TLIDTDhwYAIA 249
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
38-399 |
9.83e-36 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 134.02 E-value: 9.83e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624114703 38 FMAGLVLMIFLVWGEYTKRSTVKGQLIPDKG-----LVQVYTTTAGVIIEKYVSEGQAVKAGDMLYKISTTRhtdagnvq 112
Cdd:COG1566 9 LLALVLLLLALGLALWAAGRNGPDEPVTADGrvearVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTD-------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624114703 113 siidkeltFKRQLiehEITRTKQAQAAEKRNIANTIERLQVDMDKLQAQIELQTHQVAIAKETLTRYEFAMQSEAVSKQE 192
Cdd:COG1566 81 --------LQAAL---AQAEAQLAAAEAQLARLEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKGAVSQQE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624114703 193 LESQTMAYNTQLNSLTALEREKEMIAKQIKEQTiALSRLEHEhrttLLQYERTLsdnksDSIQNQANDTlIIKAQVDGVA 272
Cdd:COG1566 150 LDEARAALDAAQAQLEAAQAQLAQAQAGLREEE-ELAAAQAQ----VAQAEAAL-----AQAELNLART-TIRAPVDGVV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624114703 273 SVAHADVGQFVDSSQSLVSTLPNDSyLIAVMYVPSRAIGFVKTDDEVLLRYVAYPYQKFghaKGRIISVAktahagqnlP 352
Cdd:COG1566 219 TNLNVEPGEVVSAGQPLLTIVPLDD-LWVEAYVPETDLGRVKPGQPVEVRVDAYPDRVF---EGKVTSIS---------P 285
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2624114703 353 TIGTVSATEQIAN--EPMYVIKAYLDKQTitaygkELPLAVGMTLEGDV 399
Cdd:COG1566 286 GAGFTSPPKNATGnvVQRYPVRIRLDNPD------PEPLRPGMSATVEI 328
|
|
| type_I_hlyD |
TIGR01843 |
type I secretion membrane fusion protein, HlyD family; Type I secretion is an ABC transport ... |
38-415 |
1.84e-27 |
|
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: 113.18 E-value: 1.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624114703 38 FMAGLVLmIFLVWGEYTKRSTV---KGQLIPD--KGLVQVYTTtaGVIIEKYVSEGQAVKAGDMLYKISTTR-------- 104
Cdd:TIGR01843 10 LIAGLVV-IFFLWAYFAPLDVVataTGKVVPSgnVKVVQHLEG--GIVREILVREGDRVKAGQVLVELDATDveadaael 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624114703 105 -------HTDAGNVQSIIDKELTFK-------------RQLIEHE---ITRTKQAQAAEKRNIANTIERLQVDMDKLQAQ 161
Cdd:TIGR01843 87 esqvlrlEAEVARLRAEADSQAAIEfpddllsaedpavPELIKGQqslFESRKSTLRAQLELILAQIKQLEAELAGLQAQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624114703 162 IELQTHQVAIAKETLTRYEFAMQSEAVSKQ---ELESQTMAYNTQLNSLTA----LEREKEMIAKQIkEQTIALSRLE-- 232
Cdd:TIGR01843 167 LQALRQQLEVISEELEARRKLKEKGLVSRLellELERERAEAQGELGRLEAelevLKRQIDELQLER-QQIEQTFREEvl 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624114703 233 ---HEHRTTLLQYERTLSDNKSdsiQNQAndtLIIKAQVDG-VASVAHADVGQFVDSSQSLVSTLPNDSYLIAVMYVPSR 308
Cdd:TIGR01843 246 eelTEAQARLAELRERLNKARD---RLQR---LIIRSPVDGtVQSLKVHTVGGVVQPGETLMEIVPEDDPLEIEAKLSPK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624114703 309 AIGFVKTDDEVLLRYVAYPYQKFGHAKGRIISVAKTahagqnlptigtvSATEQIANEPMYVIKAYLDKQTITAYGKELP 388
Cdd:TIGR01843 320 DIGFVHVGQPAEIKFSAFPYRRYGILNGKVKSISPD-------------TFTDERGGGPYYRVRISIDQNTLGIGPKGLE 386
|
410 420
....*....|....*....|....*..
gi 2624114703 389 LAVGMTLEGDVMHETRKLYEWVLEPLY 415
Cdd:TIGR01843 387 LSPGMPVTADIKTGERTVIEYLLKPIT 413
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
50-345 |
1.25e-26 |
|
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: 109.05 E-value: 1.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624114703 50 WGEYTKRSTVKGQLIPDKGLVQVYTTTAGVIIEKYVSEGQAVKAGDMLYKISTTRHTdaGNVQSIIDKELTFKRQLIEHE 129
Cdd:pfam00529 1 LAPLTKGVEAPGRVVVSGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQ--AALDSAEAQLAKAQAQVARLQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624114703 130 ITRTK-QAQAAEKRNIANTIERLQVDMDKLQAQIELQTHQVAIAKETLTRYEFAMQSEAVSKQELESQTMAYNTQLNSLT 208
Cdd:pfam00529 79 AELDRlQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQANLL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624114703 209 ALEREKEMIAKQIKEQTIALSRLEhehRTTLLQYERTLSDNKSDSIQNQANDT-LIIKAQVDG-VASVAHADVGQFVDSS 286
Cdd:pfam00529 159 ATVAQLDQIYVQITQSAAENQAEV---RSELSGAQLQIAEAEAELKLAKLDLErTEIRAPVDGtVAFLSVTVDGGTVSAG 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2624114703 287 QSLVSTLPNDSYLIAVMYVPSRaIGFVKTDDEVLLRYVAYPYQKFGHAKGRIISVAKTA 345
Cdd:pfam00529 236 LRLMFVVPEDNLLVPGMFVETQ-LDQVRVGQPVLIPFDAFPQTKTGRFTGVVVGISPDT 293
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
51-370 |
1.20e-15 |
|
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: 77.29 E-value: 1.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624114703 51 GEYTKRSTVKGQLIPDKgLVQVYTTTAGVIIEKYVSEGQAVKAGDMLYKISTTRhtdagnvqsiidkeltfkrqliehei 130
Cdd:COG0845 6 GDVPETVEATGTVEARR-EVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPD-------------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624114703 131 trtkqaqaaekrniantierLQVDMDKLQAQIELQTHQVAIAKETLTRYEFAMQSEAVSKQELESQTMAYNTQLNSLTAL 210
Cdd:COG0845 59 --------------------LQAALAQAQAQLAAAQAQLELAKAELERYKALLKKGAVSQQELDQAKAALDQAQAALAAA 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624114703 211 ErekemiaKQIKEQTIALSRLEhehrttllqyertlsdnksdsiqnqandtliIKAQVDGVASVAHADVGQFVDSSQSLV 290
Cdd:COG0845 119 Q-------AALEQARANLAYTT-------------------------------IRAPFDGVVGERNVEPGQLVSAGTPLF 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624114703 291 sTLPNDSYLIAVMYVPSRAIGFVKTDDEVLLRYVAYPYQKFghaKGRIISVAKTAHagqnlPTIGTVSATEQIANEP--- 367
Cdd:COG0845 161 -TIADLDPLEVEFDVPESDLARLKVGQPVTVTLDAGPGKTF---EGKVTFIDPAVD-----PATRTVRVRAELPNPDgll 231
|
....*.
gi 2624114703 368 ---MYV 370
Cdd:COG0845 232 rpgMFV 237
|
|
| heterocyst_DevB |
TIGR02971 |
ABC exporter membrane fusion protein, DevB family; Members of this protein family are found ... |
58-286 |
8.37e-09 |
|
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: 56.76 E-value: 8.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624114703 58 TVKGQLIPDKGLVQVYTTTAGV---IIEKYVSEGQAVKAGDMLyKISTTRHTDAGNVQSIIDKELTFKRQLIEHEITRTK 134
Cdd:TIGR02971 2 TALGRLEPEGEVVAVAAPSSGGtdrIKKLLVAEGDRVQAGQVL-AELDSRPERTAELDVARTQLDEAKARLAQVRAGAKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624114703 135 QAQAAEKRNIANtiERLQVDMDKLQAQIELQTHQVAIAKETLTRYEFAMQSEAVSKQELESQTMAYNTQLNSLTALEREK 214
Cdd:TIGR02971 81 GEIAAQRAARAA--AKLFKDVAAQQATLNRLEAELETAQREVDRYRSLFRDGAVSASDLDSKALKLRTAEEELEEALASR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2624114703 215 EmiaKQIKEQTIALSRLEHEHRTTLLQYERT-LSDNKSDSIQNQANDTL-IIKAQVDGVASVAHADVGQFVDSS 286
Cdd:TIGR02971 159 S---EQIDGARAALASLAEEVRETDVDLAQAeVKSALEAVQQAEALLELtYVKAPIDGRVLKIHAREGEVIGSE 229
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
58-342 |
5.92e-06 |
|
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: 47.69 E-value: 5.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624114703 58 TVKGQLIPDKGlVQVYTTTAGVIIEKYVSEGQAVKAGDMLYKISTTRhtdagnvqsiidkeltfkrqlieheitrtkqAQ 137
Cdd:TIGR01730 16 TFPGSLEAVDE-ADLAAEVAGKITKISVREGQKVKKGQVLARLDDDD-------------------------------YQ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624114703 138 AAEKRNIANtierlqvdMDKLQAQIELqthqvaiAKETLTRYEFAMQSEAVSKQELESQTMAYNtqlnsltalerekemi 217
Cdd:TIGR01730 64 LALQAALAQ--------LAAAEAQLEL-------AQRSFERAERLVKRNAVSQADLDDAKAAVE---------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624114703 218 akqikeqtiALSRLEHEHRTTLLQYERTLSDNKsdsiqnqandtliIKAQVDGVASVAHADVGQFVDSSQSLVsTLPNDS 297
Cdd:TIGR01730 113 ---------AAQADLEAAKASLASAQLNLRYTE-------------IRAPFDGTIGRRLVEVGAYVTAGQTLA-TIVDLD 169
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2624114703 298 YLIAVMYVPSRAIGFVKTDDEVLLRYVAYPYQKFghaKGRIISVA 342
Cdd:TIGR01730 170 PLEADFSVPERDLPQLRRGQTLTVELDALPGEEF---KGKLRFID 211
|
|
| HlyD_3 |
pfam13437 |
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ... |
264-350 |
7.04e-06 |
|
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: 44.66 E-value: 7.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624114703 264 IKAQVDGVASVAHADVGQFVDSSQSLVSTLPNDSyLIAVMYVPSRAIGFVKTDDEVLLRYVAYPYQKFghaKGRIISVAK 343
Cdd:pfam13437 2 IRAPVDGVVAELNVEEGQVVQAGDPLATIVPPDR-LLVEAFVPAADLGSLKKGQKVTLKLDPGSDYTL---EGKVVRISP 77
|
....*..
gi 2624114703 344 TAHAGQN 350
Cdd:pfam13437 78 TVDPDTG 84
|
|
| PRK10476 |
PRK10476 |
multidrug transporter subunit MdtN; |
40-301 |
9.02e-05 |
|
multidrug transporter subunit MdtN;
Pssm-ID: 182488 [Multi-domain] Cd Length: 346 Bit Score: 44.25 E-value: 9.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624114703 40 AGLVLMIFLVWGEYTKRSTVKGQLipDKGLVQVYTTTAGVIIEKYVSEGQAVKAGDMLYKIS------TTRHTDAGnvQS 113
Cdd:PRK10476 21 LAIVALVFVIWRTDSAPSTDDAYI--DADVVHVASEVGGRIVELAVTENQAVKKGDLLFRIDprpyelTVAQAQAD--LA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624114703 114 IIDKELTFKRQLIEHEITRTKQAQAAEKRNIAN------TIERLQvdmdKLQAQIELQTHQVAIAKEtltryefAMQSEA 187
Cdd:PRK10476 97 LADAQIMTTQRSVDAERSNAASANEQVERARANaklatrTLERLE----PLLAKGYVSAQQVDQART-------AQRDAE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624114703 188 VSKQELESQTMAyntqlnSLTALEREKEMIAkQIKEQTIALSRLEHEHRTTllqyertlsdnksdsiqnqandtlIIKAQ 267
Cdd:PRK10476 166 VSLNQALLQAQA------AAAAVGGVDALVA-QRAAREAALAIAELHLEDT------------------------TVRAP 214
|
250 260 270
....*....|....*....|....*....|....*.
gi 2624114703 268 VDGVASVAHADVGQFVDSSQSLVsTLPNDS--YLIA 301
Cdd:PRK10476 215 FDGRVVGLKVSVGEFAAPMQPIF-TLIDTDhwYAIA 249
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
122-232 |
1.92e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 43.57 E-value: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624114703 122 KRQLIEHEITRTKQAQAAEKRNiANTIERlqvdmdklqaqiELQTHQVAIAKETLTRY---EFAMQSEAVSKQELESQTM 198
Cdd:pfam17380 493 RRKILEKELEERKQAMIEEERK-RKLLEK------------EMEERQKAIYEEERRREaeeERRKQQEMEERRRIQEQMR 559
|
90 100 110
....*....|....*....|....*....|....
gi 2624114703 199 AYNTQLNSLTALEREKEMIaKQIKEQTIALSRLE 232
Cdd:pfam17380 560 KATEERSRLEAMEREREMM-RQIVESEKARAEYE 592
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
129-267 |
1.85e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.69 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624114703 129 EITRTKQAQAAEKRNIANTIERLQVDMDKLQAQIELQTHQVAIAKETLTRYEFAM----QSEAVSKQELESQTMAYNTQL 204
Cdd:COG1196 299 RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELeeaeAELAEAEEALLEAEAELAEAE 378
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2624114703 205 NSLTALEREKEMIAKQIKEQTIALSRLEHEHRTTLLQYERTLSDNKSDSIQNQANDTLIIKAQ 267
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE 441
|
|
| HlyD_D23 |
pfam16576 |
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ... |
70-101 |
2.40e-03 |
|
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: 39.03 E-value: 2.40e-03
10 20 30
....*....|....*....|....*....|..
gi 2624114703 70 VQVYTTTAGVIIEKYVSEGQAVKAGDMLYKIS 101
Cdd:pfam16576 109 VTVYAPISGVVTELNVREGMYVQPGDTLFTIA 140
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
125-250 |
2.48e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 40.20 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624114703 125 LIEHEITrTKQAQAAEKRNIANTIERLQVDMDKLQAQIEL--QTHQVAiAKETLTRYEFAMQSEAVSKQ------ELESQ 196
Cdd:PRK04778 297 ILEREVK-ARKYVEKNSDTLPDFLEHAKEQNKELKEEIDRvkQSYTLN-ESELESVRQLEKQLESLEKQydeiteRIAEQ 374
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2624114703 197 TMAYNTQLNSLTALEREKEMIAKQ---IKEQTIALSRLEHEHRTTLLQYERTLSDNK 250
Cdd:PRK04778 375 EIAYSELQEELEEILKQLEEIEKEqekLSEMLQGLRKDELEAREKLERYRNKLHEIK 431
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
88-275 |
3.59e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 39.63 E-value: 3.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624114703 88 GQAVKAGDMLYKISTTRHTDA---GNVQSIIDKELTFKRQLIEheitRTKQAQAAEKRNIANTIERLQVDMDKLQAQIEL 164
Cdd:pfam05667 285 SGSSTTDTGLTKGSRFTHTEKlqfTNEAPAATSSPPTKVETEE----ELQQQREEELEELQEQLEDLESSIQELEKEIKK 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624114703 165 QTHQVAIAKETLTRYEfamQSEAVSKQELESQTMAYNTQLNSLTALEREKEMIaKQIKEQTIALSRLEHEHRTTLLQYER 244
Cdd:pfam05667 361 LESSIKQVEEELEELK---EQNEELEKQYKVKKKTLDLLPDAEENIAKLQALV-DASAQRLVELAGQWEKHRVPLIEEYR 436
|
170 180 190
....*....|....*....|....*....|....
gi 2624114703 245 TLSD---NKSDSIQNQANDTLIIKAQVDGVASVA 275
Cdd:pfam05667 437 ALKEaksNKEDESQRKLEEIKELREKIKEVAEEA 470
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
116-244 |
3.72e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.53 E-value: 3.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624114703 116 DKELTFKRQLIEHEI---TRTKQAQAAEKRNIANTIERLQVDMDKLQAQIELQTHQVAIAKETLTRYEFAMQSEAVSKQE 192
Cdd:COG1196 234 LRELEAELEELEAELeelEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE 313
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2624114703 193 LESQTMAYNTQlnsLTALEREKEMIAKQIKEQTIALSRLEHEHRTTLLQYER 244
Cdd:COG1196 314 LEERLEELEEE---LAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
89-235 |
4.10e-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: 39.65 E-value: 4.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624114703 89 QAVKAGDMLYKISTTRHTDAGNVQSIIDKELTFKRQLIEHEITRTKQAQAAEKRNIANtIERLQVDMDKLQAQIELQTHQ 168
Cdd:TIGR02168 726 RQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAE-IEELEAQIEQLKEELKALREA 804
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2624114703 169 VAIAKETLTRyefamqseavSKQELESQTMAYNTQLNSLTALEREKEMIAKQIKEQTIALSRLEHEH 235
Cdd:TIGR02168 805 LDELRAELTL----------LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEI 861
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
117-250 |
9.46e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 38.41 E-value: 9.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624114703 117 KELTFKRQLIEHEITRTKQAQAAEKRNIANTIERL-QVDMDKLQAQIELQTHQVAIAKETltryefaMQSEAVSKQELES 195
Cdd:TIGR00618 268 RIEELRAQEAVLEETQERINRARKAAPLAAHIKAVtQIEQQAQRIHTELQSKMRSRAKLL-------MKRAAHVKQQSSI 340
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2624114703 196 QtmaynTQLNSLTALEREKEMIAKQIKEQTIALSRLEHEHrtTLLQYERTLSDNK 250
Cdd:TIGR00618 341 E-----EQRRLLQTLHSQEIHIRDAHEVATSIREISCQQH--TLTQHIHTLQQQK 388
|
|
| |
