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Conserved domains on  [gi|1443436474|emb|SUW35271|]
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HlyD family secretion protein [Brucella melitensis]

Protein Classification

HlyD family secretion protein( domain architecture ID 11446287)

HlyD family secretion protein similar to Escherichia coli protein YhiI, Acinetobacter baumannii colistin resistance protein EmrA, and Burkholderia cepacia fusaric acid resistance protein FusE

Gene Ontology:  GO:0022857|GO:0016020|GO:0055085
TCDB:  3.A.1

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
1-340 4.27e-58

Multidrug resistance efflux pump EmrA [Defense mechanisms];


:

Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 191.03  E-value: 4.27e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443436474   1 MGFSRKQWIVAGAIVVLAAGGYYALQAMNGsglPDGIASGNGRVEAVEIDISTKSPGRIREIFANEGSFVKAGDVLARMD 80
Cdd:COG1566     1 MKALKKRRLLALVLLLLALGLALWAAGRNG---PDEPVTADGRVEARVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443436474  81 TDQLESQYRQAKAQLRRAEIGIDTAQSLVTQrQAEHAAAEATVAQREAQLDAAQRRLARSRQLSESRTVSQQVLDDDRAT 160
Cdd:COG1566    78 PTDLQAALAQAEAQLAAAEAQLARLEAELGA-EAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKGAVSQQELDEARAA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443436474 161 AQGAEAAVGAAKAQLAATDAAIGAaKAQVVDAQASVEAAKAAIAAIEADLRDATLTAPKPGRVQYRVAQPGEVLSAGGRV 240
Cdd:COG1566   157 LDAAQAQLEAAQAQLAQAQAGLRE-EEELAAAQAQVAQAEAALAQAELNLARTTIRAPVDGVVTNLNVEPGEVVSAGQPL 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443436474 241 LNLVDLSDVSMTFFLPTAQAGRVAIGADARIVLDAAPQYVIPAKVSFVADVAQFTPKTVESeEERQKLMFRVKAKIPqil 320
Cdd:COG1566   236 LTIVPLDDLWVEAYVPETDLGRVKPGQPVEVRVDAYPDRVFEGKVTSISPGAGFTSPPKNA-TGNVVQRYPVRIRLD--- 311
                         330       340
                  ....*....|....*....|
gi 1443436474 321 lQKYIQQVKTGLPGVAYVKL 340
Cdd:COG1566   312 -NPDPEPLRPGMSATVEIDT 330
 
Name Accession Description Interval E-value
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
1-340 4.27e-58

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 191.03  E-value: 4.27e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443436474   1 MGFSRKQWIVAGAIVVLAAGGYYALQAMNGsglPDGIASGNGRVEAVEIDISTKSPGRIREIFANEGSFVKAGDVLARMD 80
Cdd:COG1566     1 MKALKKRRLLALVLLLLALGLALWAAGRNG---PDEPVTADGRVEARVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443436474  81 TDQLESQYRQAKAQLRRAEIGIDTAQSLVTQrQAEHAAAEATVAQREAQLDAAQRRLARSRQLSESRTVSQQVLDDDRAT 160
Cdd:COG1566    78 PTDLQAALAQAEAQLAAAEAQLARLEAELGA-EAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKGAVSQQELDEARAA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443436474 161 AQGAEAAVGAAKAQLAATDAAIGAaKAQVVDAQASVEAAKAAIAAIEADLRDATLTAPKPGRVQYRVAQPGEVLSAGGRV 240
Cdd:COG1566   157 LDAAQAQLEAAQAQLAQAQAGLRE-EEELAAAQAQVAQAEAALAQAELNLARTTIRAPVDGVVTNLNVEPGEVVSAGQPL 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443436474 241 LNLVDLSDVSMTFFLPTAQAGRVAIGADARIVLDAAPQYVIPAKVSFVADVAQFTPKTVESeEERQKLMFRVKAKIPqil 320
Cdd:COG1566   236 LTIVPLDDLWVEAYVPETDLGRVKPGQPVEVRVDAYPDRVFEGKVTSISPGAGFTSPPKNA-TGNVVQRYPVRIRLD--- 311
                         330       340
                  ....*....|....*....|
gi 1443436474 321 lQKYIQQVKTGLPGVAYVKL 340
Cdd:COG1566   312 -NPDPEPLRPGMSATVEIDT 330
PRK03598 PRK03598
putative efflux pump membrane fusion protein; Provisional
4-311 3.59e-35

putative efflux pump membrane fusion protein; Provisional


Pssm-ID: 235136 [Multi-domain]  Cd Length: 331  Bit Score: 130.85  E-value: 3.59e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443436474   4 SRKQWIVAGAIVVLAAGG----YYALQAMNGSGLpdgiasgNGRVEAVEIDISTKSPGRIREIFANEGSFVKAGDVLARM 79
Cdd:PRK03598    2 KKKVVIGLAVVVLAAAVAggwwWYQSRQDNGLTL-------YGNVDIRTVNLGFRVGGRLASLAVDEGDAVKAGQVLGEL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443436474  80 DTDQLESQYRQAKAQLRRAEIGIDTAQSlvTQRQAEHAAAEATVAQREAQLDAAQRRLARSRQLSESRTVSQQVLDDDRA 159
Cdd:PRK03598   75 DAAPYENALMQAKANVSVAQAQLDLMLA--GYRDEEIAQARAAVKQAQAAYDYAQNFYNRQQGLWKSRTISANDLENARS 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443436474 160 TAQGAEAAVGAAKAQLAATDAAIGaaKAQVVDAQASVEAAKAAIAAIEADLRDATLTAPKPGRVQYRVAQPGEVLSAGGR 239
Cdd:PRK03598  153 SRDQAQATLKSAQDKLSQYREGNR--PQDIAQAKASLAQAQAALAQAELNLQDTELIAPSDGTILTRAVEPGTMLNAGST 230
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1443436474 240 VLNLVDLSDVSMTFFLPTAQAGRVAIGADARIVLDAAPQYVIPAKVSFVADVAQFTPKTVESEEERQKLMFR 311
Cdd:PRK03598  231 VFTLSLTRPVWVRAYVDERNLGQAQPGRKVLLYTDGRPDKPYHGQIGFVSPTAEFTPKTVETPDLRTDLVYR 302
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
37-296 1.29e-28

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: 113.29  E-value: 1.29e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443436474  37 IASGNGRVEAVEIDISTKSPGRIREIFANEGSFVKAGDVLARMDT-------DQLESQYRQAKAQLRRAEIGIDTAQSLV 109
Cdd:pfam00529   9 EAPGRVVVSGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPtdyqaalDSAEAQLAKAQAQVARLQAELDRLQALE 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443436474 110 ----------TQRQAEHAAAEATVAQREAQLDAAQRRLARSRQLSESRTVSQQVLDDDRATAQGAEAAVGAAKAQLAATD 179
Cdd:pfam00529  89 selaisrqdyDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQANLLATVAQLDQIY 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443436474 180 AAIGAA--------KAQVVDAQASVEAAKAAIAAIEADLRDATLTAPKPGRVQYRVAQP-GEVLSAGGRVLNLVDLSDVS 250
Cdd:pfam00529 169 VQITQSaaenqaevRSELSGAQLQIAEAEAELKLAKLDLERTEIRAPVDGTVAFLSVTVdGGTVSAGLRLMFVVPEDNLL 248
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1443436474 251 MTFFLPTAQAGRVAIGADARIVLDAAPQYVIPAKVSFVADVAQFTP 296
Cdd:pfam00529 249 VPGMFVETQLDQVRVGQPVLIPFDAFPQTKTGRFTGVVVGISPDTG 294
RND_mfp TIGR01730
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ...
42-292 1.33e-26

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: 107.79  E-value: 1.33e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443436474  42 GRVEAV-EIDISTKSPGRIREIFANEGSFVKAGDVLARMDTDQLESQYRQAKAQLRRAeigidtaqslvtqrqaehaaae 120
Cdd:TIGR01730  19 GSLEAVdEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAA---------------------- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443436474 121 atvaqrEAQLDAAQRRLARSRQLSESRTVSQQVLDDdrataqgaeaavgaakaqlaatdaaigaAKAQVVDAQASVEAAK 200
Cdd:TIGR01730  77 ------EAQLELAQRSFERAERLVKRNAVSQADLDD----------------------------AKAAVEAAQADLEAAK 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443436474 201 AAIAAIEADLRDATLTAPKPGRVQYRVAQPGEVLSAGGRVLNLVDLSDVSMTFFLPTAQAGRVAIGADARIVLDAAPQYV 280
Cdd:TIGR01730 123 ASLASAQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAGQTLATIVDLDPLEADFSVPERDLPQLRRGQTLTVELDALPGEE 202
                         250
                  ....*....|..
gi 1443436474 281 IPAKVSFVADVA 292
Cdd:TIGR01730 203 FKGKLRFIDPRV 214
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
44-79 9.40e-03

The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.


Pssm-ID: 133459 [Multi-domain]  Cd Length: 67  Bit Score: 34.31  E-value: 9.40e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1443436474  44 VEA--VEIDISTKSPGRIREIFANEGSFVKAGDVLARM 79
Cdd:cd06850    30 LEAmkMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
 
Name Accession Description Interval E-value
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
1-340 4.27e-58

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 191.03  E-value: 4.27e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443436474   1 MGFSRKQWIVAGAIVVLAAGGYYALQAMNGsglPDGIASGNGRVEAVEIDISTKSPGRIREIFANEGSFVKAGDVLARMD 80
Cdd:COG1566     1 MKALKKRRLLALVLLLLALGLALWAAGRNG---PDEPVTADGRVEARVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443436474  81 TDQLESQYRQAKAQLRRAEIGIDTAQSLVTQrQAEHAAAEATVAQREAQLDAAQRRLARSRQLSESRTVSQQVLDDDRAT 160
Cdd:COG1566    78 PTDLQAALAQAEAQLAAAEAQLARLEAELGA-EAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKGAVSQQELDEARAA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443436474 161 AQGAEAAVGAAKAQLAATDAAIGAaKAQVVDAQASVEAAKAAIAAIEADLRDATLTAPKPGRVQYRVAQPGEVLSAGGRV 240
Cdd:COG1566   157 LDAAQAQLEAAQAQLAQAQAGLRE-EEELAAAQAQVAQAEAALAQAELNLARTTIRAPVDGVVTNLNVEPGEVVSAGQPL 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443436474 241 LNLVDLSDVSMTFFLPTAQAGRVAIGADARIVLDAAPQYVIPAKVSFVADVAQFTPKTVESeEERQKLMFRVKAKIPqil 320
Cdd:COG1566   236 LTIVPLDDLWVEAYVPETDLGRVKPGQPVEVRVDAYPDRVFEGKVTSISPGAGFTSPPKNA-TGNVVQRYPVRIRLD--- 311
                         330       340
                  ....*....|....*....|
gi 1443436474 321 lQKYIQQVKTGLPGVAYVKL 340
Cdd:COG1566   312 -NPDPEPLRPGMSATVEIDT 330
PRK03598 PRK03598
putative efflux pump membrane fusion protein; Provisional
4-311 3.59e-35

putative efflux pump membrane fusion protein; Provisional


Pssm-ID: 235136 [Multi-domain]  Cd Length: 331  Bit Score: 130.85  E-value: 3.59e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443436474   4 SRKQWIVAGAIVVLAAGG----YYALQAMNGSGLpdgiasgNGRVEAVEIDISTKSPGRIREIFANEGSFVKAGDVLARM 79
Cdd:PRK03598    2 KKKVVIGLAVVVLAAAVAggwwWYQSRQDNGLTL-------YGNVDIRTVNLGFRVGGRLASLAVDEGDAVKAGQVLGEL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443436474  80 DTDQLESQYRQAKAQLRRAEIGIDTAQSlvTQRQAEHAAAEATVAQREAQLDAAQRRLARSRQLSESRTVSQQVLDDDRA 159
Cdd:PRK03598   75 DAAPYENALMQAKANVSVAQAQLDLMLA--GYRDEEIAQARAAVKQAQAAYDYAQNFYNRQQGLWKSRTISANDLENARS 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443436474 160 TAQGAEAAVGAAKAQLAATDAAIGaaKAQVVDAQASVEAAKAAIAAIEADLRDATLTAPKPGRVQYRVAQPGEVLSAGGR 239
Cdd:PRK03598  153 SRDQAQATLKSAQDKLSQYREGNR--PQDIAQAKASLAQAQAALAQAELNLQDTELIAPSDGTILTRAVEPGTMLNAGST 230
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1443436474 240 VLNLVDLSDVSMTFFLPTAQAGRVAIGADARIVLDAAPQYVIPAKVSFVADVAQFTPKTVESEEERQKLMFR 311
Cdd:PRK03598  231 VFTLSLTRPVWVRAYVDERNLGQAQPGRKVLLYTDGRPDKPYHGQIGFVSPTAEFTPKTVETPDLRTDLVYR 302
AcrA COG0845
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ...
39-292 5.87e-32

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: 122.36  E-value: 5.87e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443436474  39 SGNGRVEAV-EIDISTKSPGRIREIFANEGSFVKAGDVLARMDTDQLESQYRQAKAQLRRAEigidtaqslvtqrqaeha 117
Cdd:COG0845    13 EATGTVEARrEVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQ------------------ 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443436474 118 aaeatvaqreAQLDAAQRRLARSRQLSESRTVSQQVLDDdrataqgaeaavgaakaqlaatdaaigaAKAQVVDAQASVE 197
Cdd:COG0845    75 ----------AQLELAKAELERYKALLKKGAVSQQELDQ----------------------------AKAALDQAQAALA 116
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443436474 198 AAKAAIAAIEADLRDATLTAPKPGRVQYRVAQPGEVLSAGGRVLNLVDLSDVSMTFFLPTAQAGRVAIGADARIVLDAAP 277
Cdd:COG0845   117 AAQAALEQARANLAYTTIRAPFDGVVGERNVEPGQLVSAGTPLFTIADLDPLEVEFDVPESDLARLKVGQPVTVTLDAGP 196
                         250
                  ....*....|....*
gi 1443436474 278 QYVIPAKVSFVADVA 292
Cdd:COG0845   197 GKTFEGKVTFIDPAV 211
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
37-296 1.29e-28

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: 113.29  E-value: 1.29e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443436474  37 IASGNGRVEAVEIDISTKSPGRIREIFANEGSFVKAGDVLARMDT-------DQLESQYRQAKAQLRRAEIGIDTAQSLV 109
Cdd:pfam00529   9 EAPGRVVVSGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPtdyqaalDSAEAQLAKAQAQVARLQAELDRLQALE 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443436474 110 ----------TQRQAEHAAAEATVAQREAQLDAAQRRLARSRQLSESRTVSQQVLDDDRATAQGAEAAVGAAKAQLAATD 179
Cdd:pfam00529  89 selaisrqdyDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQANLLATVAQLDQIY 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443436474 180 AAIGAA--------KAQVVDAQASVEAAKAAIAAIEADLRDATLTAPKPGRVQYRVAQP-GEVLSAGGRVLNLVDLSDVS 250
Cdd:pfam00529 169 VQITQSaaenqaevRSELSGAQLQIAEAEAELKLAKLDLERTEIRAPVDGTVAFLSVTVdGGTVSAGLRLMFVVPEDNLL 248
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1443436474 251 MTFFLPTAQAGRVAIGADARIVLDAAPQYVIPAKVSFVADVAQFTP 296
Cdd:pfam00529 249 VPGMFVETQLDQVRVGQPVLIPFDAFPQTKTGRFTGVVVGISPDTG 294
RND_mfp TIGR01730
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ...
42-292 1.33e-26

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: 107.79  E-value: 1.33e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443436474  42 GRVEAV-EIDISTKSPGRIREIFANEGSFVKAGDVLARMDTDQLESQYRQAKAQLRRAeigidtaqslvtqrqaehaaae 120
Cdd:TIGR01730  19 GSLEAVdEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAA---------------------- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443436474 121 atvaqrEAQLDAAQRRLARSRQLSESRTVSQQVLDDdrataqgaeaavgaakaqlaatdaaigaAKAQVVDAQASVEAAK 200
Cdd:TIGR01730  77 ------EAQLELAQRSFERAERLVKRNAVSQADLDD----------------------------AKAAVEAAQADLEAAK 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443436474 201 AAIAAIEADLRDATLTAPKPGRVQYRVAQPGEVLSAGGRVLNLVDLSDVSMTFFLPTAQAGRVAIGADARIVLDAAPQYV 280
Cdd:TIGR01730 123 ASLASAQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAGQTLATIVDLDPLEADFSVPERDLPQLRRGQTLTVELDALPGEE 202
                         250
                  ....*....|..
gi 1443436474 281 IPAKVSFVADVA 292
Cdd:TIGR01730 203 FKGKLRFIDPRV 214
PRK10476 PRK10476
multidrug transporter subunit MdtN;
8-245 3.56e-15

multidrug transporter subunit MdtN;


Pssm-ID: 182488 [Multi-domain]  Cd Length: 346  Bit Score: 75.45  E-value: 3.56e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443436474   8 WIVAGAIVVLAAGGYYALQAMNgsglpdgiASGNGRVEAVEIDISTKSPGRIREIFANEGSFVKAGDVLARMDTDQLESQ 87
Cdd:PRK10476   16 LAIVALAIVALVFVIWRTDSAP--------STDDAYIDADVVHVASEVGGRIVELAVTENQAVKKGDLLFRIDPRPYELT 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443436474  88 YRQAKAQLRRAEIGIDTAQSLVTQRQAEHAAAEATVAQREAQLDAAQRRLARSRQLSESRTVSQQVLDDDRATAQGAEAA 167
Cdd:PRK10476   88 VAQAQADLALADAQIMTTQRSVDAERSNAASANEQVERARANAKLATRTLERLEPLLAKGYVSAQQVDQARTAQRDAEVS 167
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1443436474 168 VGAAKAQlaatDAAIGAAKAQVVDAQASVEAAKAAIAAIEADLRDATLTAPKPGRVQYRVAQPGEVLSAGGRVLNLVD 245
Cdd:PRK10476  168 LNQALLQ----AQAAAAAVGGVDALVAQRAAREAALAIAELHLEDTTVRAPFDGRVVGLKVSVGEFAAPMQPIFTLID 241
type_I_hlyD TIGR01843
type I secretion membrane fusion protein, HlyD family; Type I secretion is an ABC transport ...
8-333 4.18e-11

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: 63.88  E-value: 4.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443436474   8 WIVAGAIVVLAAGGYYALQamngsglpDGIASGNGRVEAVEIDISTKSP--GRIREIFANEGSFVKAGDVLARMDT---- 81
Cdd:TIGR01843   9 WLIAGLVVIFFLWAYFAPL--------DVVATATGKVVPSGNVKVVQHLegGIVREILVREGDRVKAGQVLVELDAtdve 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443436474  82 ---DQLESQYRQAKAQLRR--AEIG----------------------IDTAQSLVTQR----QAEHAAAEATVAQREAQL 130
Cdd:TIGR01843  81 adaAELESQVLRLEAEVARlrAEADsqaaiefpddllsaedpavpelIKGQQSLFESRkstlRAQLELILAQIKQLEAEL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443436474 131 DAAQRRLARSRQL--------------------SESRTVSQQV--------LDDDRATAQGAEAAVGAAKAQLAATDAA- 181
Cdd:TIGR01843 161 AGLQAQLQALRQQleviseelearrklkekglvSRLELLELEReraeaqgeLGRLEAELEVLKRQIDELQLERQQIEQTf 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443436474 182 IGAAKAQVVDAQASVEAAKAAIAAIEADLRDATLTAPKPGRVQ-YRVAQPGEVLSAGGRVLNLVDLSDVSM--TFFLPTA 258
Cdd:TIGR01843 241 REEVLEELTEAQARLAELRERLNKARDRLQRLIIRSPVDGTVQsLKVHTVGGVVQPGETLMEIVPEDDPLEieAKLSPKD 320
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1443436474 259 qAGRVAIGADARIVLDAAPQYVIPAkvsFVADVAQFTPKTVEsEEERQKLMFRVKAKIPqillQKYIQQVKTGLP 333
Cdd:TIGR01843 321 -IGFVHVGQPAEIKFSAFPYRRYGI---LNGKVKSISPDTFT-DERGGGPYYRVRISID----QNTLGIGPKGLE 386
HlyD_3 pfam13437
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ...
214-321 8.11e-10

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: 55.45  E-value: 8.11e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443436474 214 TLTAPKPGRVQYRVAQPGEVLSAGGRVLNLVDLSDVSMTFFLPTAQAGRVAIGADARIVLDAAPQYVIPAKVSFVADvaq 293
Cdd:pfam13437   1 TIRAPVDGVVAELNVEEGQVVQAGDPLATIVPPDRLLVEAFVPAADLGSLKKGQKVTLKLDPGSDYTLEGKVVRISP--- 77
                          90       100
                  ....*....|....*....|....*...
gi 1443436474 294 ftpkTVESEEERQKLMFRVKAKIPQILL 321
Cdd:pfam13437  78 ----TVDPDTGVIPVRVSIENPKTPIPL 101
heterocyst_DevB TIGR02971
ABC exporter membrane fusion protein, DevB family; Members of this protein family are found ...
58-277 1.40e-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: 58.68  E-value: 1.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443436474  58 RIREIFANEGSFVKAGDVLARMDT--------DQLESQYRQAKAQL--RRA-----EIGIDTAQSLVTQRQAEHAAAEAT 122
Cdd:TIGR02971  26 RIKKLLVAEGDRVQAGQVLAELDSrpertaelDVARTQLDEAKARLaqVRAgakkgEIAAQRAARAAAKLFKDVAAQQAT 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443436474 123 VAQREAQLDAAQRRLARSRQLSESRTVSQQVLD---------DDRATAQGAEAAVGAAKAQLAATDAAIGAAKAQVVDAQ 193
Cdd:TIGR02971 106 LNRLEAELETAQREVDRYRSLFRDGAVSASDLDskalklrtaEEELEEALASRSEQIDGARAALASLAEEVRETDVDLAQ 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443436474 194 ASVEAAKAAIAAIEADLRDATLTAPKPGRVQYRVAQPGEVLSAGGrVLNLVDLSDVSMTFFLPTAQAGRVAIGADARIVL 273
Cdd:TIGR02971 186 AEVKSALEAVQQAEALLELTYVKAPIDGRVLKIHAREGEVIGSEG-ILEMGDTSQMYAVAEVYETDINRVRVGQRATITS 264

                  ....
gi 1443436474 274 DAAP 277
Cdd:TIGR02971 265 TALS 268
HlyD_D23 pfam16576
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ...
42-298 5.63e-07

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: 49.81  E-value: 5.63e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443436474  42 GRVEAVE---IDISTKSPGRIREIFAN-EGSFVKAGDVLARMDTDQL---ESQYRQAKAQLRRAeigidTAQSLVtqrqa 114
Cdd:pfam16576  10 GRVAYDErrlAHVHARVEGWIEKLYVNaTGDPVKKGQPLAELYSPELvaaQQEYLLALRSGDAL-----SKSELL----- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443436474 115 ehAAAEatvaQREAQLDAAQRRLArsrQLSESRTVSQQVldddrataqgaeaavgaakaqlaatdaaigaakaqvvdaqa 194
Cdd:pfam16576  80 --RAAR----QRLRLLGMPEAQIA---ELERTGKVQPTV----------------------------------------- 109
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443436474 195 sveaakaaiaaieadlrdaTLTAPKPGRVQYRVAQPGEVLSAGGRVLNLVDLSDVSMTFFLPTAQAGRVAIGADARIVLD 274
Cdd:pfam16576 110 -------------------TVYAPISGVVTELNVREGMYVQPGDTLFTIADLSTVWVEADVPEQDLALVKVGQPAEVTLP 170
                         250       260
                  ....*....|....*....|....
gi 1443436474 275 AAPQYVIPAKVSFVADVAQftPKT 298
Cdd:pfam16576 171 ALPGKTFEGKVDYIYPTLD--PKT 192
PRK11556 PRK11556
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;
39-159 5.93e-07

MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;


Pssm-ID: 183194 [Multi-domain]  Cd Length: 415  Bit Score: 50.94  E-value: 5.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443436474  39 SGNGRVEAVE-IDISTKSPGRIREIFANEGSFVKAGDVLARMDTDQLESQYRQAKAQLrraeigidtaqslvtqrqaeha 117
Cdd:PRK11556   77 TGLGTVTAANtVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPRPFKVALAQAQGQL---------------------- 134
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1443436474 118 aaeatvAQREAQLDAAQRRLARSRQLSESRTVSQQVLDDDRA 159
Cdd:PRK11556  135 ------AKDQATLANARRDLARYQQLAKTNLVSRQELDAQQA 170
Biotin_lipoyl_2 pfam13533
Biotin-lipoyl like;
51-96 1.36e-06

Biotin-lipoyl like;


Pssm-ID: 433286  Cd Length: 50  Bit Score: 44.74  E-value: 1.36e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1443436474  51 ISTKSPGRIREIFANEGSFVKAGDVLARMDTDQLESQYRQAKAQLR 96
Cdd:pfam13533   5 IASPVSGKVVAVNVKEGQQVKKGDVLATLDSPELQLQLQQAEAQLA 50
PRK11578 PRK11578
macrolide transporter subunit MacA; Provisional
4-155 3.66e-05

macrolide transporter subunit MacA; Provisional


Pssm-ID: 183211 [Multi-domain]  Cd Length: 370  Bit Score: 45.15  E-value: 3.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443436474   4 SRKQWIVAgaIVVLAAGGYYALQAMNGSgLPD----GIASGN--------GRVEAV-EIDISTKSPGRIREIFANEGSFV 70
Cdd:PRK11578    7 VKKRYLIA--LVIVLAGGITLWRILNAP-VPTyqtlIVRPGDlqqsvlatGKLDALrKVDVGAQVSGQLKTLSVAIGDKV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443436474  71 KAGDVLARMDTDQLESQYRQAKAqlrraeigidTAQSLVTQRQaehaaaeatvaQREAQLDAAQRRLARSRQLSESRTVS 150
Cdd:PRK11578   84 KKDQLLGVIDPEQAENQIKEVEA----------TLMELRAQRQ-----------QAEAELKLARVTLSRQQRLAKTQAVS 142

                  ....*
gi 1443436474 151 QQVLD 155
Cdd:PRK11578  143 QQDLD 147
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
82-217 2.65e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.92  E-value: 2.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443436474  82 DQLESQYRQAKAQLRRAEIGIDTAQSLVTQRQAEHAAAEATVAQREAQLDAAQRRLARSRQLSESRTVSQQVLDDDRATA 161
Cdd:COG1196   256 EELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEEL 335
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1443436474 162 QGAEAAVGAAKAQLAATDAAIGAAKAQVVDAQASVEAAKAAIAAIEADLRDATLTA 217
Cdd:COG1196   336 EEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
Surf_Exclu_PgrA TIGR04320
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ...
80-134 8.00e-03

SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.


Pssm-ID: 275124 [Multi-domain]  Cd Length: 356  Bit Score: 37.78  E-value: 8.00e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1443436474  80 DTDQLESQYRQAKAQLRRAEIGIDTAQSLVTQRQAEHAAAEATVAQREAQLDAAQ 134
Cdd:TIGR04320 255 SLAALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQ 309
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
44-79 9.40e-03

The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.


Pssm-ID: 133459 [Multi-domain]  Cd Length: 67  Bit Score: 34.31  E-value: 9.40e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1443436474  44 VEA--VEIDISTKSPGRIREIFANEGSFVKAGDVLARM 79
Cdd:cd06850    30 LEAmkMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
 
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.
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