NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|493780405|ref|WP_006728820|]
View 

HlyD family type I secretion periplasmic adaptor subunit, partial [Agrobacterium albertimagni]

Protein Classification

putative HlyD family type I secretion protein( domain architecture ID 1000742)

putative HlyD family type I secretion protein similar to Escherichia coli hemolysin secretion protein D, an inner membrane protein involved in the transport of hemolysin A

Gene Ontology:  GO:0016020|GO:0005886|GO:0009306
TCDB:  8.A.1

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
CusB_dom_1 super family cl46872
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 24-434 3.98e-94

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.


The actual alignment was detected with superfamily member TIGR01843:

Pssm-ID: 481212 [Multi-domain]  Cd Length: 423  Bit Score: 289.99  E-value: 3.98e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405   24 LGATVLGLALTAGIGGWAAHAKLAGAVISQGELVVIGDTKQVQHVDGGTIVEIPVKIGSLVEKGDVVLRLDDTQLRIELG 103
Cdd:TIGR01843   5 RLITWLIAGLVVIFFLWAYFAPLDVVATATGKVVPSGNVKVVQHLEGGIVREILVREGDRVKAGQVLVELDATDVEADAA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405  104 IVTSQVAQLKAMMARLVAERDGLDVLSFEGLELS-------PEVKREEAkLFDENRVMRANQKQQIEMQISQLGNQIDGL 176
Cdd:TIGR01843  85 ELESQVLRLEAEVARLRAEADSQAAIEFPDDLLSaedpavpELIKGQQS-LFESRKSTLRAQLELILAQIKQLEAELAGL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405  177 REQEKANLAENELLAEELAMQEGLVQKGLAKAAELRGLRRQMVRIEGTIGDLLARVAEAEGQISELKVRLMSVDQTSRTE 256
Cdd:TIGR01843 164 QAQLQALRQQLEVISEELEARRKLKEKGLVSRLELLELERERAEAQGELGRLEAELEVLKRQIDELQLERQQIEQTFREE 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405  257 LQKEIVSVEARLTELEQRALQLTHRLDRTVVKAPESGTIYDLQAHTIGGVVAPGQVIMAIVPANSELNVHVKVAPTDIDR 336
Cdd:TIGR01843 244 VLEELTEAQARLAELRERLNKARDRLQRLIIRSPVDGTVQSLKVHTVGGVVQPGETLMEIVPEDDPLEIEAKLSPKDIGF 323

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405  337 VFVGQTARMRFTAFNRQTTPEIVGAVDIIPGATIVDKSTNLPFYKTSVTFSPSDLGDLATK--LTPGMPVEVYIETEERT 414
Cdd:TIGR01843 324 VHVGQPAEIKFSAFPYRRYGILNGKVKSISPDTFTDERGGGPYYRVRISIDQNTLGIGPKGleLSPGMPVTADIKTGERT 403

                         410       420
                  ....*....|....*....|
gi 493780405  415 VISFLAKPFTDQITRAFREE 434
Cdd:TIGR01843 404 VIEYLLKPITDSVQEALRER 423
 
Name Accession Description Interval E-value
type_I_hlyD TIGR01843
type I secretion membrane fusion protein, HlyD family; Type I secretion is an ABC transport ...
 24-434 3.98e-94

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: 289.99  E-value: 3.98e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405   24 LGATVLGLALTAGIGGWAAHAKLAGAVISQGELVVIGDTKQVQHVDGGTIVEIPVKIGSLVEKGDVVLRLDDTQLRIELG 103
Cdd:TIGR01843   5 RLITWLIAGLVVIFFLWAYFAPLDVVATATGKVVPSGNVKVVQHLEGGIVREILVREGDRVKAGQVLVELDATDVEADAA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405  104 IVTSQVAQLKAMMARLVAERDGLDVLSFEGLELS-------PEVKREEAkLFDENRVMRANQKQQIEMQISQLGNQIDGL 176
Cdd:TIGR01843  85 ELESQVLRLEAEVARLRAEADSQAAIEFPDDLLSaedpavpELIKGQQS-LFESRKSTLRAQLELILAQIKQLEAELAGL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405  177 REQEKANLAENELLAEELAMQEGLVQKGLAKAAELRGLRRQMVRIEGTIGDLLARVAEAEGQISELKVRLMSVDQTSRTE 256
Cdd:TIGR01843 164 QAQLQALRQQLEVISEELEARRKLKEKGLVSRLELLELERERAEAQGELGRLEAELEVLKRQIDELQLERQQIEQTFREE 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405  257 LQKEIVSVEARLTELEQRALQLTHRLDRTVVKAPESGTIYDLQAHTIGGVVAPGQVIMAIVPANSELNVHVKVAPTDIDR 336
Cdd:TIGR01843 244 VLEELTEAQARLAELRERLNKARDRLQRLIIRSPVDGTVQSLKVHTVGGVVQPGETLMEIVPEDDPLEIEAKLSPKDIGF 323

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405  337 VFVGQTARMRFTAFNRQTTPEIVGAVDIIPGATIVDKSTNLPFYKTSVTFSPSDLGDLATK--LTPGMPVEVYIETEERT 414
Cdd:TIGR01843 324 VHVGQPAEIKFSAFPYRRYGILNGKVKSISPDTFTDERGGGPYYRVRISIDQNTLGIGPKGleLSPGMPVTADIKTGERT 403

                         410       420
                  ....*....|....*....|
gi 493780405  415 VISFLAKPFTDQITRAFREE 434
Cdd:TIGR01843 404 VIEYLLKPITDSVQEALRER 423
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
17-411 1.23e-41

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 150.20  E-value: 1.23e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405  17 KGLKGRMLGATVLGLALTAGIGGWAAHAKLAGAVISQGelVVIGDTKQVQHVDGGTIVEIPVKIGSLVEKGDVVLRLDDT 96
Cdd:COG1566    2 KALKKRRLLALVLLLLALGLALWAAGRNGPDEPVTADG--RVEARVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405  97 QLRIELGIVTSQVAQLKAMMARLVAErdgldvlsfeglelspevkreeaklfdenrvmranqkqqiemqiSQLGNQIDGL 176
Cdd:COG1566   80 DLQAALAQAEAQLAAAEAQLARLEAE--------------------------------------------LGAEAEIAAA 115

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405 177 REQEKANLAENELLAEELAMQEGLVQKGLAKAAELRGLRRQMVRIEGTIGDLLARVAEAEGQISElkvrlmsvdqtsrte 256
Cdd:COG1566  116 EAQLAAAQAQLDLAQRELERYQALYKKGAVSQQELDEARAALDAAQAQLEAAQAQLAQAQAGLRE--------------- 180

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405 257 lQKEIVSVEARLTELEQRALQLTHRLDRTVVKAPESGTIYDLQAHtIGGVVAPGQVIMAIVPANSeLNVHVKVAPTDIDR 336
Cdd:COG1566  181 -EEELAAAQAQVAQAEAALAQAELNLARTTIRAPVDGVVTNLNVE-PGEVVSAGQPLLTIVPLDD-LWVEAYVPETDLGR 257

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493780405 337 VFVGQTARMRFTAFNRQTTPEIVGAV--DIIPGATIVDKSTNL-PFYKTSVTFSPSDLGdlatKLTPGMPVEVYIETE 411
Cdd:COG1566  258 VKPGQPVEVRVDAYPDRVFEGKVTSIspGAGFTSPPKNATGNVvQRYPVRIRLDNPDPE----PLRPGMSATVEIDTE 331
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 44-394 2.17e-41

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: 149.50  E-value: 2.17e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405   44 AKLAGAVISQGELVVIGDTKQVQHVDGGTIVEIPVKIGSLVEKGDVVLRLDDTQLRIELGIVTSQVAQLKAMMARLVAER 123
Cdd:pfam00529   2 APLTKGVEAPGRVVVSGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAEL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405  124 DGLDVLsfeglelspevkreeaklfdenRVMRANQKQQIEMQISQLgnqiDGLREQEKANLAENELLAEELAMQEGLVQK 203
Cdd:pfam00529  82 DRLQAL----------------------ESELAISRQDYDGATAQL----RAAQAAVKAAQAQLAQAQIDLARRRVLAPI 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405  204 GLAKAAELRGLRRQMvriegtiGDLLARVAEAEGQISELKVRLMSVDQTSRTELQKEIVSVEARLTELEQRALQLTHRLD 283
Cdd:pfam00529 136 GGISRESLVTAGALV-------AQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLE 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405  284 RTVVKAPESGTIYDLQAHTIGGVVAPGQVIMAIVPANSELnVHVKVAPTDIDRVFVGQTARMRFTAFNRQTTPEIVGAVD 363
Cdd:pfam00529 209 RTEIRAPVDGTVAFLSVTVDGGTVSAGLRLMFVVPEDNLL-VPGMFVETQLDQVRVGQPVLIPFDAFPQTKTGRFTGVVV 287

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 493780405  364 II----PGATIVDKSTNLPFYKTSVTFSPSDLGDL 394
Cdd:pfam00529 288 GIspdtGPVRVVVDKAQGPYYPLRIGLSAGALVRL 322
PRK10476 PRK10476
multidrug transporter subunit MdtN;
11-378 1.55e-05

multidrug transporter subunit MdtN;


Pssm-ID: 182488 [Multi-domain]  Cd Length: 346  Bit Score: 46.56  E-value: 1.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405  11 HVSLSGKGLKGRMLGATVLGLALTAGIG-GW--AAHAKLAGAVISqgelvviGDTKQVQHVDGGTIVEIPVKIGSLVEKG 87
Cdd:PRK10476   1 MESTPKKSPRKKLPALAIVALAIVALVFvIWrtDSAPSTDDAYID-------ADVVHVASEVGGRIVELAVTENQAVKKG 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405  88 DVVLRLDDTQLRIelgivtsQVAQLKAmmarlvaerdgldvlsfeGLELSpevkreEAKLFDENRVMRAnqkQQIEMQIS 167
Cdd:PRK10476  74 DLLFRIDPRPYEL-------TVAQAQA------------------DLALA------DAQIMTTQRSVDA---ERSNAASA 119

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405 168 QlgNQIdglrEQEKANLAeneLLAEELAMQEGLVQKGLAKAAELRGlrrqmvriegtigdllARVAEAEGQISELKVRLM 247
Cdd:PRK10476 120 N--EQV----ERARANAK---LATRTLERLEPLLAKGYVSAQQVDQ----------------ARTAQRDAEVSLNQALLQ 174

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405 248 SVDQTSR-TELQKEIVSVEARlteleQRALQLT-HRLDRTVVKAPESGTIYDLQAhTIGGVVAPGQVIMAIVpANSELNV 325
Cdd:PRK10476 175 AQAAAAAvGGVDALVAQRAAR-----EAALAIAeLHLEDTTVRAPFDGRVVGLKV-SVGEFAAPMQPIFTLI-DTDHWYA 247

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 493780405 326 HVKVAPTDIDRVFVGQTARMRfTAFNRQTTpeIVGAVDIIPGATIVDKSTNLP 378
Cdd:PRK10476 248 IANFRETDLKNIRVGDCATVY-SMIDRGRP--FEGKVDSIGWGVLPDDGGNVP 297
 
Name Accession Description Interval E-value
type_I_hlyD TIGR01843
type I secretion membrane fusion protein, HlyD family; Type I secretion is an ABC transport ...
 24-434 3.98e-94

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: 289.99  E-value: 3.98e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405   24 LGATVLGLALTAGIGGWAAHAKLAGAVISQGELVVIGDTKQVQHVDGGTIVEIPVKIGSLVEKGDVVLRLDDTQLRIELG 103
Cdd:TIGR01843   5 RLITWLIAGLVVIFFLWAYFAPLDVVATATGKVVPSGNVKVVQHLEGGIVREILVREGDRVKAGQVLVELDATDVEADAA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405  104 IVTSQVAQLKAMMARLVAERDGLDVLSFEGLELS-------PEVKREEAkLFDENRVMRANQKQQIEMQISQLGNQIDGL 176
Cdd:TIGR01843  85 ELESQVLRLEAEVARLRAEADSQAAIEFPDDLLSaedpavpELIKGQQS-LFESRKSTLRAQLELILAQIKQLEAELAGL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405  177 REQEKANLAENELLAEELAMQEGLVQKGLAKAAELRGLRRQMVRIEGTIGDLLARVAEAEGQISELKVRLMSVDQTSRTE 256
Cdd:TIGR01843 164 QAQLQALRQQLEVISEELEARRKLKEKGLVSRLELLELERERAEAQGELGRLEAELEVLKRQIDELQLERQQIEQTFREE 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405  257 LQKEIVSVEARLTELEQRALQLTHRLDRTVVKAPESGTIYDLQAHTIGGVVAPGQVIMAIVPANSELNVHVKVAPTDIDR 336
Cdd:TIGR01843 244 VLEELTEAQARLAELRERLNKARDRLQRLIIRSPVDGTVQSLKVHTVGGVVQPGETLMEIVPEDDPLEIEAKLSPKDIGF 323

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405  337 VFVGQTARMRFTAFNRQTTPEIVGAVDIIPGATIVDKSTNLPFYKTSVTFSPSDLGDLATK--LTPGMPVEVYIETEERT 414
Cdd:TIGR01843 324 VHVGQPAEIKFSAFPYRRYGILNGKVKSISPDTFTDERGGGPYYRVRISIDQNTLGIGPKGleLSPGMPVTADIKTGERT 403

                         410       420
                  ....*....|....*....|
gi 493780405  415 VISFLAKPFTDQITRAFREE 434
Cdd:TIGR01843 404 VIEYLLKPITDSVQEALRER 423
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
17-411 1.23e-41

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 150.20  E-value: 1.23e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405  17 KGLKGRMLGATVLGLALTAGIGGWAAHAKLAGAVISQGelVVIGDTKQVQHVDGGTIVEIPVKIGSLVEKGDVVLRLDDT 96
Cdd:COG1566    2 KALKKRRLLALVLLLLALGLALWAAGRNGPDEPVTADG--RVEARVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405  97 QLRIELGIVTSQVAQLKAMMARLVAErdgldvlsfeglelspevkreeaklfdenrvmranqkqqiemqiSQLGNQIDGL 176
Cdd:COG1566   80 DLQAALAQAEAQLAAAEAQLARLEAE--------------------------------------------LGAEAEIAAA 115

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405 177 REQEKANLAENELLAEELAMQEGLVQKGLAKAAELRGLRRQMVRIEGTIGDLLARVAEAEGQISElkvrlmsvdqtsrte 256
Cdd:COG1566  116 EAQLAAAQAQLDLAQRELERYQALYKKGAVSQQELDEARAALDAAQAQLEAAQAQLAQAQAGLRE--------------- 180

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405 257 lQKEIVSVEARLTELEQRALQLTHRLDRTVVKAPESGTIYDLQAHtIGGVVAPGQVIMAIVPANSeLNVHVKVAPTDIDR 336
Cdd:COG1566  181 -EEELAAAQAQVAQAEAALAQAELNLARTTIRAPVDGVVTNLNVE-PGEVVSAGQPLLTIVPLDD-LWVEAYVPETDLGR 257

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493780405 337 VFVGQTARMRFTAFNRQTTPEIVGAV--DIIPGATIVDKSTNL-PFYKTSVTFSPSDLGdlatKLTPGMPVEVYIETE 411
Cdd:COG1566  258 VKPGQPVEVRVDAYPDRVFEGKVTSIspGAGFTSPPKNATGNVvQRYPVRIRLDNPDPE----PLRPGMSATVEIDTE 331
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 44-394 2.17e-41

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: 149.50  E-value: 2.17e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405   44 AKLAGAVISQGELVVIGDTKQVQHVDGGTIVEIPVKIGSLVEKGDVVLRLDDTQLRIELGIVTSQVAQLKAMMARLVAER 123
Cdd:pfam00529   2 APLTKGVEAPGRVVVSGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAEL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405  124 DGLDVLsfeglelspevkreeaklfdenRVMRANQKQQIEMQISQLgnqiDGLREQEKANLAENELLAEELAMQEGLVQK 203
Cdd:pfam00529  82 DRLQAL----------------------ESELAISRQDYDGATAQL----RAAQAAVKAAQAQLAQAQIDLARRRVLAPI 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405  204 GLAKAAELRGLRRQMvriegtiGDLLARVAEAEGQISELKVRLMSVDQTSRTELQKEIVSVEARLTELEQRALQLTHRLD 283
Cdd:pfam00529 136 GGISRESLVTAGALV-------AQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLE 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405  284 RTVVKAPESGTIYDLQAHTIGGVVAPGQVIMAIVPANSELnVHVKVAPTDIDRVFVGQTARMRFTAFNRQTTPEIVGAVD 363
Cdd:pfam00529 209 RTEIRAPVDGTVAFLSVTVDGGTVSAGLRLMFVVPEDNLL-VPGMFVETQLDQVRVGQPVLIPFDAFPQTKTGRFTGVVV 287

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 493780405  364 II----PGATIVDKSTNLPFYKTSVTFSPSDLGDL 394
Cdd:pfam00529 288 GIspdtGPVRVVVDKAQGPYYPLRIGLSAGALVRL 322
AcrA COG0845
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ...
 227-413 5.43e-11

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: 63.42  E-value: 5.43e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405 227 DLLARVAEAEGQISELKVRLMSVDQT-------------SRTELQKEIVSV---EARLTELEQRALQLTHRLDRTVVKAP 290
Cdd:COG0845   58 DLQAALAQAQAQLAAAQAQLELAKAElerykallkkgavSQQELDQAKAALdqaQAALAAAQAALEQARANLAYTTIRAP 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405 291 ESGTIYDLQAhTIGGVVAPGQVIMAIVpANSELNVHVKVAPTDIDRVFVGQTARMRFTAFNRQTTPeivGAVDIIpgATI 370
Cdd:COG0845  138 FDGVVGERNV-EPGQLVSAGTPLFTIA-DLDPLEVEFDVPESDLARLKVGQPVTVTLDAGPGKTFE---GKVTFI--DPA 210

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 493780405 371 VDKSTNLpfYKTSVTFSPSDlgdlaTKLTPGMPVEVYIETEER 413
Cdd:COG0845  211 VDPATRT--VRVRAELPNPD-----GLLRPGMFVRVRIVLGER 246
HlyD_3 pfam13437
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ...
 286-369 3.79e-08

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: 51.21  E-value: 3.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405  286 VVKAPESGTIYDLQAhTIGGVVAPGQVIMAIVPANsELNVHVKVAPTDIDRVFVGQTARMRFTAFNRQTTPEIVGAVDII 365
Cdd:pfam13437   1 TIRAPVDGVVAELNV-EEGQVVQAGDPLATIVPPD-RLLVEAFVPAADLGSLKKGQKVTLKLDPGSDYTLEGKVVRISPT 78


                  ....
gi 493780405  366 PGAT 369
Cdd:pfam13437  79 VDPD 82
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
159-292 6.64e-08

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 54.92  E-value: 6.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405  159 KQQIEM--QISQLGNQIDGLREQekanLAENELLAEELAMQEGLVQKGLAKAaELRGLRRQMVRIEGTIGDLLARVAEAE 236
Cdd:COG4913   248 REQIELlePIRELAERYAAARER----LAELEYLRAALRLWFAQRRLELLEA-ELEELRAELARLEAELERLEARLDALR 322

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 493780405  237 GQISELKVRLMSVDQTSRTELQKEIVSVEARLTELEQRALQLTHRLDRTVVKAPES 292
Cdd:COG4913   323 EELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPAS 378
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 90-284 9.81e-07

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.09  E-value: 9.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405  90 VLRLDDTQLRIELgiVTSQVAQLKAMMARLVAERDGLDVlsfeglelspEVKREEAKLFDENRVMRANQKQ--QIEMQIS 167
Cdd:COG1196  231 LLKLRELEAELEE--LEAELEELEAELEELEAELAELEA----------ELEELRLELEELELELEEAQAEeyELLAELA 298

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405 168 QLGNQIDGLREQEKANLAENELLAEELA----MQEGLVQKGLAKAAELRGLRRQMVRIEGTIGDLLARVAEAEGQISElK 243
Cdd:COG1196  299 RLEQDIARLEERRRELEERLEELEEELAeleeELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE-A 377

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 493780405 244 VRLMSVDQTSRTELQKEIVSVEARLTELEQRALQLTHRLDR 284
Cdd:COG1196  378 EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER 418
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 154-284 2.39e-06

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: 48.38  E-value: 2.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405 154 MRANQKQQIEMQisQLGNQIDGLREQEKAnlaenelLAEELAMQEglvqkglakaAELRGLRRQMVRIEGTIGDLLARVA 233
Cdd:COG1579    2 MPEDLRALLDLQ--ELDSELDRLEHRLKE-------LPAELAELE----------DELAALEARLEAAKTELEDLEKEIK 62

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405 234 EAEGQISEL-------KVRLMSVdQTSR--TELQKEIVSVEARLTELEQRALQLTHRLDR 284
Cdd:COG1579   63 RLELEIEEVearikkyEEQLGNV-RNNKeyEALQKEIESLKRRISDLEDEILELMERIEE 121
RND_mfp TIGR01730
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ...
 229-413 3.09e-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: 48.85  E-value: 3.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405  229 LARVAEAEGQISELKV------RLMSVDQTSRTEL---QKEIVSVEARLTELEQRALQLTHRLDRTVVKAPESGTIYDLQ 299
Cdd:TIGR01730  70 LAQLAAAEAQLELAQRsferaeRLVKRNAVSQADLddaKAAVEAAQADLEAAKASLASAQLNLRYTEIRAPFDGTIGRRL 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405  300 AhTIGGVVAPGQVIMAIVpANSELNVHVKVAPTDIDRVFVGQTARMRFTAFNRQttpEIVGAVDIIpgATIVDKSTNLpf 379
Cdd:TIGR01730 150 V-EVGAYVTAGQTLATIV-DLDPLEADFSVPERDLPQLRRGQTLTVELDALPGE---EFKGKLRFI--DPRVDSGTGT-- 220

                         170       180       190
                  ....*....|....*....|....*....|....
gi 493780405  380 YKTSVTFSpsdlgDLATKLTPGMPVEVYIETEER 413
Cdd:TIGR01730 221 VRVRATFP-----NPDGRLLPGMFGRVTISLKVR 249
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
156-284 1.41e-05

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 47.32  E-value: 1.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405 156 ANQKQQIEMQISQLGNQIDGLREQEKANLAENELLAEELAMQEGLVQKgLAKAAELRGLRRQMVRIEGTIGDLLAR---- 231
Cdd:COG3206  211 SEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPE-LLQSPVIQQLRAQLAELEAELAELSARytpn 289

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 493780405 232 ---VAEAEGQISELKVRLMSVDQTSRTELQKEIVSVEARLTELEQRALQLTHRLDR 284
Cdd:COG3206  290 hpdVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAE 345
PRK10476 PRK10476
multidrug transporter subunit MdtN;
11-378 1.55e-05

multidrug transporter subunit MdtN;


Pssm-ID: 182488 [Multi-domain]  Cd Length: 346  Bit Score: 46.56  E-value: 1.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405  11 HVSLSGKGLKGRMLGATVLGLALTAGIG-GW--AAHAKLAGAVISqgelvviGDTKQVQHVDGGTIVEIPVKIGSLVEKG 87
Cdd:PRK10476   1 MESTPKKSPRKKLPALAIVALAIVALVFvIWrtDSAPSTDDAYID-------ADVVHVASEVGGRIVELAVTENQAVKKG 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405  88 DVVLRLDDTQLRIelgivtsQVAQLKAmmarlvaerdgldvlsfeGLELSpevkreEAKLFDENRVMRAnqkQQIEMQIS 167
Cdd:PRK10476  74 DLLFRIDPRPYEL-------TVAQAQA------------------DLALA------DAQIMTTQRSVDA---ERSNAASA 119

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405 168 QlgNQIdglrEQEKANLAeneLLAEELAMQEGLVQKGLAKAAELRGlrrqmvriegtigdllARVAEAEGQISELKVRLM 247
Cdd:PRK10476 120 N--EQV----ERARANAK---LATRTLERLEPLLAKGYVSAQQVDQ----------------ARTAQRDAEVSLNQALLQ 174

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405 248 SVDQTSR-TELQKEIVSVEARlteleQRALQLT-HRLDRTVVKAPESGTIYDLQAhTIGGVVAPGQVIMAIVpANSELNV 325
Cdd:PRK10476 175 AQAAAAAvGGVDALVAQRAAR-----EAALAIAeLHLEDTTVRAPFDGRVVGLKV-SVGEFAAPMQPIFTLI-DTDHWYA 247

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 493780405 326 HVKVAPTDIDRVFVGQTARMRfTAFNRQTTpeIVGAVDIIPGATIVDKSTNLP 378
Cdd:PRK10476 248 IANFRETDLKNIRVGDCATVY-SMIDRGRP--FEGKVDSIGWGVLPDDGGNVP 297
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
108-284 1.62e-05

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.22  E-value: 1.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405  108 QVAQLKAMMA---RLVAERDGLDVLSFEGLELSPEVKREEAKLFDENRVMRANQKQQIEMQISQLGNQIDGLREQE---K 181
Cdd:COG4913   250 QIELLEPIRElaeRYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELdelE 329

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405  182 ANLAEN-----ELLAEELAMQEGLVQKGLAKAAELRGLRRQM-VRIEGTIGDLLARVAEAEGQISELKVRLMSVDQ---- 251
Cdd:COG4913   330 AQIRGNggdrlEQLEREIERLERELEERERRRARLEALLAALgLPLPASAEEFAALRAEAAALLEALEEELEALEEalae 409

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 493780405  252 --TSRTELQKEIVSVEARLTELEQRALQLTHRLDR 284
Cdd:COG4913   410 aeAALRDLRRELRELEAEIASLERRKSNIPARLLA 444
heterocyst_DevB TIGR02971
ABC exporter membrane fusion protein, DevB family; Members of this protein family are found ...
 73-350 2.69e-05

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: 45.97  E-value: 2.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405   73 IVEIPVKIGSLVEKGDVVLRLDDTQLRI-ELGIVTSQVAQLKAMMARLVAERDGLDVLSFEGLELSPEVKREEAKLFDE- 150
Cdd:TIGR02971  27 IKKLLVAEGDRVQAGQVLAELDSRPERTaELDVARTQLDEAKARLAQVRAGAKKGEIAAQRAARAAAKLFKDVAAQQATl 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405  151 NRVMRANQKQQIEmqisqlgnqIDGLREQEKAN-LAENELLAEELAMQEGLVQKGLAKAAELRGLRRQMVRiegtigdlL 229
Cdd:TIGR02971 107 NRLEAELETAQRE---------VDRYRSLFRDGaVSASDLDSKALKLRTAEEELEEALASRSEQIDGARAA--------L 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405  230 ARVAEAegqISELKVRLMSVDQTSRTELQKeivsvearlteleqralQLTHRLDRTVVKAPESGTIydLQAHTIGGVVAP 309
Cdd:TIGR02971 170 ASLAEE---VRETDVDLAQAEVKSALEAVQ-----------------QAEALLELTYVKAPIDGRV--LKIHAREGEVIG 227

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 493780405  310 GQVIMAIvpANSELNVHV-KVAPTDIDRVFVGQTARMRFTAF 350
Cdd:TIGR02971 228 SEGILEM--GDTSQMYAVaEVYETDINRVRVGQRATITSTAL 267
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 96-254 3.32e-05

chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.21  E-value: 3.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405    96 TQLRIELGIVTSQVAQLKAMMARLVAERDGLDVLSFEGLELSPEVKREEAKLFDE------NRVMRANQKQQIEMQISQL 169
Cdd:TIGR02169  346 EEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREinelkrELDRLQEELQRLSEELADL 425

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405   170 GNQIDGLREQEKANLAENELLAEELAMQEGLVQKglaKAAELRGLRRQMVRIEGTIGDLLARVAEAEGQISELKVRLMSV 249
Cdd:TIGR02169  426 NAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQ---LAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARAS 502


                   ....*
gi 493780405   250 DQTSR 254
Cdd:TIGR02169  503 EERVR 507
HlyD_D23 pfam16576
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ...
 258-350 7.11e-05

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: 43.65  E-value: 7.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405  258 QKEIVSVEARL-----TELEQRALQLTHRLDRTV-VKAPESGTIYDLQAhTIGGVVAPGQVIMAIvpAN-SELNVHVKVA 330
Cdd:pfam16576  76 SELLRAARQRLrllgmPEAQIAELERTGKVQPTVtVYAPISGVVTELNV-REGMYVQPGDTLFTI--ADlSTVWVEADVP 152

                          90       100
                  ....*....|....*....|
gi 493780405  331 PTDIDRVFVGQTARMRFTAF 350
Cdd:pfam16576 153 EQDLALVKVGQPAEVTLPAL 172
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
158-285 9.85e-05

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.76  E-value: 9.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405 158 QKQQIEMQISQLGNQIDGLREQEKA--NLAENELLAEELAMQEGLVQKGLAKAAELRGLRRQMVRIEGTIGDLLARVAEA 235
Cdd:COG4717  103 ELEELEAELEELREELEKLEKLLQLlpLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEEL 182

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 493780405 236 EGQISELKVRLMSVDQTSRTELQKEIVSVEARLTELEQRALQLTHRLDRT 285
Cdd:COG4717  183 LEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL 232
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 101-289 2.65e-04

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 43.14  E-value: 2.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405  101 ELGIVTSQVAQLKAMMARLVAERDGLDVLSFEglELSPEVKREEAKLFDENRVMRANQKQQIEMQISQLGNQID------ 174
Cdd:pfam05622 243 ELRCAQLQQAELSQADALLSPSSDPGDNLAAE--IMPAEIREKLIRLQHENKMLRLGQEGSYRERLTELQQLLEdanrrk 320

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405  175 -GLREQEKANLAENELLAEELAMQEGLVQKGLAKAAELRGLRRQMvriegtiGDLLARVAEAEGQISELKVRLMSVDQTS 253
Cdd:pfam05622 321 nELETQNRLANQRILELQQQVEELQKALQEQGSKAEDSSLLKQKL-------EEHLEKLHEAQSELQKKKEQIEELEPKQ 393

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 493780405  254 RTELQKEIVSVEARLTELEQRALQLTHRLDRTVVKA 289
Cdd:pfam05622 394 DSNLAQKIDELQEALRKKDEDMKAMEERYKKYVEKA 429
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
 130-282 3.04e-04

Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.


Pssm-ID: 462900 [Multi-domain]  Cd Length: 305  Bit Score: 42.44  E-value: 3.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405  130 SFEGLELSPEVKREEAKLFDEnRVMRANQKQQIEMQISQLGNQIDGLREQEKANLAE-NELLAEELAMQEGLVQKGLAKA 208
Cdd:pfam09787  35 GVEGLDSSTALTLELEELRQE-RDLLREEIQKLRGQIQQLRTELQELEAQQQEEAESsREQLQELEEQLATERSARREAE 113

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493780405  209 AELRGLRRQMVRIE----GTIGDLLARVAEAEGQISELKVRLMSVDQTSRTElqkeivsvearlTELEQRALQLTHRL 282
Cdd:pfam09787 114 AELERLQEELRYLEeelrRSKATLQSRIKDREAEIEKLRNQLTSKSQSSSSQ------------SELENRLHQLTETL 179
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 97-283 3.30e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 3.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405  97 QLRIELGIVTSQVAQLKAMMARLVAERdgldvlsfEGLELSPEVKREEAKLFDENRVMRANQKQQIEMQISQLGNQIDGL 176
Cdd:COG1196  271 ELRLELEELELELEEAQAEEYELLAEL--------ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEEL 342

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405 177 REQEKANLAENELLAEELAMQEG----LVQKGLAKAAELRGLRRQMVRIEGTIGDLLARVAEAEGQISELKVRLMSVDQT 252
Cdd:COG1196  343 EEELEEAEEELEEAEAELAEAEEalleAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422

                        170       180       190
                 ....*....|....*....|....*....|.
gi 493780405 253 SRTELQKEIVSVEARLTELEQRALQLTHRLD 283
Cdd:COG1196  423 LEELEEALAELEEEEEEEEEALEEAAEEEAE 453
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 166-284 6.41e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.23  E-value: 6.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405 166 ISQLGNQIDGLREQ-----------EKANLAENELLA---EELAMQEGLVQKGLAKA-AELRGLRRQMVRIEGTIGDLLA 230
Cdd:COG1196  195 LGELERQLEPLERQaekaeryrelkEELKELEAELLLlklRELEAELEELEAELEELeAELEELEAELAELEAELEELRL 274

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 493780405 231 RVAEAEGQISELKVRLMSVDQtSRTELQKEIVSVEARLTELEQRALQLTHRLDR 284
Cdd:COG1196  275 ELEELELELEEAQAEEYELLA-ELARLEQDIARLEERRRELEERLEELEEELAE 327
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
108-282 7.74e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.82  E-value: 7.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405  108 QVAQLKAMMARLVAERDGLDVLSFEGL--ELSPEVKREEAKLfDENRVMRANQKQQIEM---QISQL-GNQIDGLREQEK 181
Cdd:COG4913   270 RLAELEYLRAALRLWFAQRRLELLEAEleELRAELARLEAEL-ERLEARLDALREELDEleaQIRGNgGDRLEQLEREIE 348

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405  182 ANLAENELLAEELAMQEGLVQK-GLAKAAELRGLRRQMVRIEGTIGDLLARVAEAEGQISELKVRLmSVDQTSRTELQKE 260
Cdd:COG4913   349 RLERELEERERRRARLEALLAAlGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAAL-RDLRRELRELEAE 427

                         170       180
                  ....*....|....*....|..
gi 493780405  261 IVSVEARLTELEQRALQLTHRL 282
Cdd:COG4913   428 IASLERRKSNIPARLLALRDAL 449
Biotin_lipoyl_2 pfam13533
Biotin-lipoyl like;
71-110 8.14e-04

Biotin-lipoyl like;


Pssm-ID: 433286  Cd Length: 50  Bit Score: 37.04  E-value: 8.14e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 493780405   71 GTIVEIPVKIGSLVEKGDVVLRLDDTQLRIELGIVTSQVA 110
Cdd:pfam13533  11 GKVVAVNVKEGQQVKKGDVLATLDSPELQLQLQQAEAQLA 50
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 111-284 9.76e-04

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: 41.58  E-value: 9.76e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405   111 QLKAMMARLVAERDGLDVLSFEGLELSPEVKREEAKLFDENR--VMRANQKQQIEMQISQLGNQIDGLRE-----QEKAN 183
Cdd:TIGR02168  797 ELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERrlEDLEEQIEELSEDIESLAAEIEELEElieelESELE 876

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405   184 LAENELLAEELAMQEGLVQKGlAKAAELRGLRRQMVRIEG-------TIGDLLARVAEAEGQISELKVRLMSVDQTSRTE 256
Cdd:TIGR02168  877 ALLNERASLEEALALLRSELE-ELSEELRELESKRSELRReleelreKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEE 955

                          170       180
                   ....*....|....*....|....*...
gi 493780405   257 LQKEIVSVEARLTELEQRALQLTHRLDR 284
Cdd:TIGR02168  956 AEALENKIEDDEEEARRRLKRLENKIKE 983
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 90-285 1.03e-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: 41.58  E-value: 1.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405    90 VLRLDDTQLRIELGIVTSQVAQLKAMMARLVAERDGLDV----LSFEGLELSPEVKREEAKLFDENRVMRA--NQKQQIE 163
Cdd:TIGR02168  229 LLVLRLEELREELEELQEELKEAEEELEELTAELQELEEkleeLRLEVSELEEEIEELQKELYALANEISRleQQKQILR 308

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405   164 MQISQLGNQIDGLREQEKANLAENELLAEELAMQEglvqkglAKAAELrglrrqmvriEGTIGDLLARVAEAEGQISELK 243
Cdd:TIGR02168  309 ERLANLERQLEELEAQLEELESKLDELAEELAELE-------EKLEEL----------KEELESLEAELEELEAELEELE 371

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 493780405   244 VRLMSVDQTSRT------ELQKEIVSVEARLTELEQRALQLTHRLDRT 285
Cdd:TIGR02168  372 SRLEELEEQLETlrskvaQLELQIASLNNEIERLEARLERLEDRRERL 419
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 58-275 1.38e-03

chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.21  E-value: 1.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405    58 VIGDTKQVQHVDGGTIVEIPVKI----GSLVEKGDVV---------LRLDDTQLRIELGIVTSQVAQLKAMMARLVAERD 124
Cdd:TIGR02169  619 VFGDTLVVEDIEAARRLMGKYRMvtleGELFEKSGAMtggsraprgGILFSRSEPAELQRLRERLEGLKRELSSLQSELR 698

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405   125 GLDVLSFEgleLSPEVKREEAKLFD-ENRVMRANQKQQIEMQ-ISQLGNQIDGLREQEKANLAENELLAEELA-MQEGLV 201
Cdd:TIGR02169  699 RIENRLDE---LSQELSDASRKIGEiEKEIEQLEQEEEKLKErLEELEEDLSSLEQEIENVKSELKELEARIEeLEEDLH 775

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405   202 QKGLAKAA--------ELRGLRRQMVRIEGTIGDLLARVAEAEGQISELKVRLMSVDQTS-------------RTELQKE 260
Cdd:TIGR02169  776 KLEEALNDlearlshsRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIqelqeqridlkeqIKSIEKE 855

                          250
                   ....*....|....*
gi 493780405   261 IVSVEARLTELEQRA 275
Cdd:TIGR02169  856 IENLNGKKEELEEEL 870
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 160-261 1.86e-03

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 40.44  E-value: 1.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405  160 QQIEMQISQLgnqidglrEQEKANL-AENELLAEELAMQEGLVQKGLAKAAELRGLRRQM-------VRIEGTIGDLLAR 231
Cdd:pfam05622  17 HELDQQVSLL--------QEEKNSLqQENKKLQERLDQLESGDDSGTPGGKKYLLLQKQLeqlqeenFRLETARDDYRIK 88

                          90       100       110
                  ....*....|....*....|....*....|...
gi 493780405  232 VAEAEGQISELKVR---LMSVDQTSRTeLQKEI 261
Cdd:pfam05622  89 CEELEKEVLELQHRneeLTSLAEEAQA-LKDEM 120
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
157-275 2.04e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.43  E-value: 2.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405 157 NQKQQIEMQISQLGNQIDGLREQEKaNLAE-----NEL------LAEELAMQEGLVQKGLAKAAELRGLRRQMVRIEGTI 225
Cdd:PRK03918 176 RRIERLEKFIKRTENIEELIKEKEK-ELEEvlreiNEIsselpeLREELEKLEKEVKELEELKEEIEELEKELESLEGSK 254

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 493780405 226 GDLLARVAEAEGQISELKVRLmsvdqtsrtelqKEIVSVEARLTELEQRA 275
Cdd:PRK03918 255 RKLEEKIRELEERIEELKKEI------------EELEEKVKELKELKEKA 292
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 156-246 3.37e-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: 39.36  E-value: 3.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405 156 ANQKQQIEMQISQLGNQIDGLREQEKANLAENELLAEELAMQEglvQKGLAKAAELRGLRRQMVRIEGTIGDLLARVAEA 235
Cdd:COG4942   19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALE---RRIAALARRIRALEQELAALEAELAELEKEIAEL 95

                         90
                 ....*....|.
gi 493780405 236 EGQISELKVRL 246
Cdd:COG4942   96 RAELEAQKEEL 106
PRK09039 PRK09039
peptidoglycan -binding protein;
167-246 4.08e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 39.18  E-value: 4.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405 167 SQLGNQIDGLREQEKANLAENELLAEELAMQEGLVQKGLAKAAELR----GLRRQMVRIEGTIGDLLARVAEAEGQISEL 242
Cdd:PRK09039  98 SRLQALLAELAGAGAAAEGRAGELAQELDSEKQVSARALAQVELLNqqiaALRRQLAALEAALDASEKRDRESQAKIADL 177


                 ....
gi 493780405 243 KVRL 246
Cdd:PRK09039 178 GRRL 181
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 139-277 4.14e-03

chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 39.67  E-value: 4.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405   139 EVKREEAKLFDENRVMRANQKQqIEMQISQLGNQIDGLREqEKANLAENELLAEELAMQEGLVqkglaKAAELRGLRRQM 218
Cdd:TIGR02169  167 EFDRKKEKALEELEEVEENIER-LDLIIDEKRQQLERLRR-EREKAERYQALLKEKREYEGYE-----LLKEKEALERQK 239

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 493780405   219 VRIEGTIGDLLARVAEAEGQISELKVRLMSVDQTsRTELQKEIvsveARLTELEQRALQ 277
Cdd:TIGR02169  240 EAIERQLASLEEELEKLTEEISELEKRLEEIEQL-LEELNKKI----KDLGEEEQLRVK 293
RND_mfp TIGR01730
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ...
 70-123 6.06e-03

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: 38.45  E-value: 6.06e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 493780405   70 GGTIVEIPVKIGSLVEKGDVVLRLDDTQLRIELGIVTSQVAQLKA--MMARLVAER 123
Cdd:TIGR01730  34 AGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAqlELAQRSFER 89
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
96-278 6.72e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.89  E-value: 6.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405  96 TQLRIELGIVTSQVAQLKAmmaRLVAERDGLDVLSFEGLELSPEVKR-----EEAKLFDENRVMRAN---QKQQIEMQIS 167
Cdd:PRK03918 241 EELEKELESLEGSKRKLEE---KIRELEERIEELKKEIEELEEKVKElkelkEKAEEYIKLSEFYEEyldELREIEKRLS 317

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405 168 QLGNQIDGLREQ-EKANLAENELlaEELAMQEGLVQKGLA----KAAELRGLRRQMVRIEGtigdLLARVAEAEgqISEL 242
Cdd:PRK03918 318 RLEEEINGIEERiKELEEKEERL--EELKKKLKELEKRLEeleeRHELYEEAKAKKEELER----LKKRLTGLT--PEKL 389

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 493780405 243 KVRLMSVdQTSRTELQKEIVSVEARLTELEQRALQL 278
Cdd:PRK03918 390 EKELEEL-EKAKEEIEEEISKITARIGELKKEIKEL 424
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
151-274 7.00e-03

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 38.84  E-value: 7.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405 151 NRVMRANQKQQIEMQISQLGNQIDGLREQ-----EKANLAENELlaEELAMQEGLV---QKGLAKAAELRGLRRQMVRIE 222
Cdd:COG3206  155 NALAEAYLEQNLELRREEARKALEFLEEQlpelrKELEEAEAAL--EEFRQKNGLVdlsEEAKLLLQQLSELESQLAEAR 232

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 493780405 223 GTIGDLLARVAEAEGQISELKVRLMSVDQTSR-TELQKEIVSVEARLTELEQR 274
Cdd:COG3206  233 AELAEAEARLAALRAQLGSGPDALPELLQSPViQQLRAQLAELEAELAELSAR 285
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
97-284 7.38e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 38.74  E-value: 7.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405   97 QLRIELGIVTSQVAQLKAMMARLVAERDGLDVLsfeglelspevkreEAKLFDENRVmranqkQQIEMQISQLGNQIDGL 176
Cdd:COG4913   621 ELEEELAEAEERLEALEAELDALQERREALQRL--------------AEYSWDEIDV------ASAEREIAELEAELERL 680

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405  177 REqekanlAENELlaEELAMQEGLVQkglakaAELRGLRRQMVRIEGTIGDLLARVAEAEGQISELKVRLMSVDQTSRTE 256
Cdd:COG4913   681 DA------SSDDL--AALEEQLEELE------AELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLE 746

                         170       180       190
                  ....*....|....*....|....*....|....
gi 493780405  257 LQKEIvsvEARLTELEQRAL------QLTHRLDR 284
Cdd:COG4913   747 LRALL---EERFAAALGDAVerelreNLEERIDA 777
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
91-282 7.70e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.60  E-value: 7.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405  91 LRLDDTQLRIELGIVTSQVAQLKAMMARLVAERDGLDVLSFEGL--ELSPEVKREEAKLFdENRVMRANQKQQIEMQISQ 168
Cdd:COG4717  328 LGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEiaALLAEAGVEDEEEL-RAALEQAEEYQELKEELEE 406

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405 169 LGNQIDGLREQEKANLAENELlaEELAmqeglvqkglakaAELRGLRRQMVRIEGTIGDLLARVAEAEGQISELKvrlms 248
Cdd:COG4717  407 LEEQLEELLGELEELLEALDE--EELE-------------EELEELEEELEELEEELEELREELAELEAELEQLE----- 466

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 493780405 249 vDQTSRTELQKEIVSVEARLTELEQR--ALQLTHRL 282
Cdd:COG4717  467 -EDGELAELLQELEELKAELRELAEEwaALKLALEL 501
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
210-284 8.30e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 38.69  E-value: 8.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493780405 210 ELRGLRRQMVRIEGTIGDLLARVAEAEGQISELKVRLMSVDQTSRTE---------LQKEIVSVEARLTELEQRALQLTH 280
Cdd:COG2433  414 EIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREirkdreisrLDREIERLERELEEERERIEELKR 493


                 ....
gi 493780405 281 RLDR 284
Cdd:COG2433  494 KLER 497
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH