NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2214743833|ref|WP_242977900|]
View 

HlyD family efflux transporter periplasmic adaptor subunit, partial [Clostridium perfringens]

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 ...
 28-496 3.00e-37

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: 141.69  E-value: 3.00e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214743833  28 IFLYIIIALIVTFFIWSWFSEKEIIVKVNGVVRPDNEIQAISNIVQGEVESIKMKNGESVSKGEVLFKIKSTelgdkknQ 107
Cdd:TIGR01843   6 LITWLIAGLVVIFFLWAYFAPLDVVATATGKVVPSGNVKVVQHLEGGIVREILVREGDRVKAGQVLVELDAT-------D 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214743833 108 VEEQIKYINTDNENLE----KLNKSINDNTNYFENNDKEKEYYYKFQsyeagnKVSLEETNNISSSKDNLNNEKDGLkil 183
Cdd:TIGR01843  79 VEADAAELESQVLRLEaevaRLRAEADSQAAIEFPDDLLSAEDPAVP------ELIKGQQSLFESRKSTLRAQLELI--- 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214743833 184 sksisenknlnkegsvySSQYESYASSKAMIQNKTDQLENSKKALNEQIEAnnkeKNNLSDenskaiiddknKQINNQIS 263
Cdd:TIGR01843 150 -----------------LAQIKQLEAELAGLQAQLQALRQQLEVISEELEA----RRKLKE-----------KGLVSRLE 197

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214743833 264 QIDLEiknnnEQLDKLKSDtLAQIKGSIDKINQNLNKLESNLSSLDES--SNISKEKNKT-TFLAQIEEKINmnnqkkke 340
Cdd:TIGR01843 198 LLELE-----RERAEAQGE-LGRLEAELEVLKRQIDELQLERQQIEQTfrEEVLEELTEAqARLAELRERLN-------- 263

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214743833 341 leENKKQIEQSIekcsVKAPSDGKL-NINANLEKGVIlQTGAIVASIIPNSDTYRVELMIPTKDIANIKVSEDVKYSFEA 419
Cdd:TIGR01843 264 --KARDRLQRLI----IRSPVDGTVqSLKVHTVGGVV-QPGETLMEIVPEDDPLEIEAKLSPKDIGFVHVGQPAEIKFSA 336

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2214743833 420 LPYREYGFLEGKIENLSPDSKVDSEKGISFFTGEGSLNSNRLYS-NKGEEsfIKPGMMCEARIITRKEKMLYYLLEKI 496
Cdd:TIGR01843 337 FPYRRYGILNGKVKSISPDTFTDERGGGPYYRVRISIDQNTLGIgPKGLE--LSPGMPVTADIKTGERTVIEYLLKPI 412
 
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 ...
 28-496 3.00e-37

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: 141.69  E-value: 3.00e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214743833  28 IFLYIIIALIVTFFIWSWFSEKEIIVKVNGVVRPDNEIQAISNIVQGEVESIKMKNGESVSKGEVLFKIKSTelgdkknQ 107
Cdd:TIGR01843   6 LITWLIAGLVVIFFLWAYFAPLDVVATATGKVVPSGNVKVVQHLEGGIVREILVREGDRVKAGQVLVELDAT-------D 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214743833 108 VEEQIKYINTDNENLE----KLNKSINDNTNYFENNDKEKEYYYKFQsyeagnKVSLEETNNISSSKDNLNNEKDGLkil 183
Cdd:TIGR01843  79 VEADAAELESQVLRLEaevaRLRAEADSQAAIEFPDDLLSAEDPAVP------ELIKGQQSLFESRKSTLRAQLELI--- 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214743833 184 sksisenknlnkegsvySSQYESYASSKAMIQNKTDQLENSKKALNEQIEAnnkeKNNLSDenskaiiddknKQINNQIS 263
Cdd:TIGR01843 150 -----------------LAQIKQLEAELAGLQAQLQALRQQLEVISEELEA----RRKLKE-----------KGLVSRLE 197

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214743833 264 QIDLEiknnnEQLDKLKSDtLAQIKGSIDKINQNLNKLESNLSSLDES--SNISKEKNKT-TFLAQIEEKINmnnqkkke 340
Cdd:TIGR01843 198 LLELE-----RERAEAQGE-LGRLEAELEVLKRQIDELQLERQQIEQTfrEEVLEELTEAqARLAELRERLN-------- 263

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214743833 341 leENKKQIEQSIekcsVKAPSDGKL-NINANLEKGVIlQTGAIVASIIPNSDTYRVELMIPTKDIANIKVSEDVKYSFEA 419
Cdd:TIGR01843 264 --KARDRLQRLI----IRSPVDGTVqSLKVHTVGGVV-QPGETLMEIVPEDDPLEIEAKLSPKDIGFVHVGQPAEIKFSA 336

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2214743833 420 LPYREYGFLEGKIENLSPDSKVDSEKGISFFTGEGSLNSNRLYS-NKGEEsfIKPGMMCEARIITRKEKMLYYLLEKI 496
Cdd:TIGR01843 337 FPYRRYGILNGKVKSISPDTFTDERGGGPYYRVRISIDQNTLGIgPKGLE--LSPGMPVTADIKTGERTVIEYLLKPI 412
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
23-484 2.99e-23

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 100.51  E-value: 2.99e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214743833  23 NKLMFIFLYIIIALIVTFFIWSWFSE---KEIIVKVNGVVRPDneIQAISNIVQGEVESIKMKNGESVSKGEVLFKIKST 99
Cdd:COG1566     2 KALKKRRLLALVLLLLALGLALWAAGrngPDEPVTADGRVEAR--VVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214743833 100 ELGDKKNQVEEQIKYINTDNENLEKlnksindntnyfenndkekeyyykfqsyeagnkvSLEETNNISSSKDNLNNEKDG 179
Cdd:COG1566    80 DLQAALAQAEAQLAAAEAQLARLEA----------------------------------ELGAEAEIAAAEAQLAAAQAQ 125

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214743833 180 LKILSKSISENKNLNKEGSVYSSQYESyasskamIQNKTDQLENSKKALNEQIEANNKEKNNLsdenskaiiddknkqin 259
Cdd:COG1566   126 LDLAQRELERYQALYKKGAVSQQELDE-------ARAALDAAQAQLEAAQAQLAQAQAGLREE----------------- 181

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214743833 260 NQISQIDLEIKNNNEQLDklksdtlaqikgsidkinqnlnklesnlssldessniskeknkttflaqieekinmnnqkkk 339
Cdd:COG1566   182 EELAAAQAQVAQAEAALA-------------------------------------------------------------- 199

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214743833 340 eleenkkQIEQSIEKCSVKAPSDGKLNiNANLEKGVILQTGAIVASIIPNSDTYrVELMIPTKDIANIKVSEDVKYSFEA 419
Cdd:COG1566   200 -------QAELNLARTTIRAPVDGVVT-NLNVEPGEVVSAGQPLLTIVPLDDLW-VEAYVPETDLGRVKPGQPVEVRVDA 270

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2214743833 420 LPYREYgflEGKIENLSPDSkvdsekgiSFFTGEGSLNSN-------RLYSNKGEESFIKPGMMCEARIITR 484
Cdd:COG1566   271 YPDRVF---EGKVTSISPGA--------GFTSPPKNATGNvvqrypvRIRLDNPDPEPLRPGMSATVEIDTE 331
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 219-439 6.44e-10

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: 60.51  E-value: 6.44e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214743833 219 DQLENSKKALNEQIEANNKEKNNL-SDENSKAIIDDKNKQINNQISQIDLEIKNNNEQLDKLKSD-----TLAQIKG--- 289
Cdd:pfam00529  61 DSAEAQLAKAQAQVARLQAELDRLqALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDlarrrVLAPIGGisr 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214743833 290 -SIDKINQNLNKLESNL-SSLDESSNISKEK--NKTTFLAQIEEKINMNNQKKKELEENKKQIEQSIEKCSVKAPSDGKL 365
Cdd:pfam00529 141 eSLVTAGALVAQAQANLlATVAQLDQIYVQItqSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLERTEIRAPVDGTV 220

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2214743833 366 -NINANLEKGVIlQTGAIVASIIPNSDTYrVELMIPTKDIANIKVSEDVKYSFEALPYREYGFLEGKIENLSPDS 439
Cdd:pfam00529 221 aFLSVTVDGGTV-SAGLRLMFVVPEDNLL-VPGMFVETQLDQVRVGQPVLIPFDAFPQTKTGRFTGVVVGISPDT 293
PTZ00121 PTZ00121
MAEBL; Provisional
 77-312 2.99e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.06  E-value: 2.99e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214743833   77 ESIKMKNGESVSKGEVLFKIKSTELGDKKNQVEEQIKYINTDNENLEKLNKSINDNTNYFENNDKEKEYYYKFQSYEAGN 156
Cdd:PTZ00121  1711 EAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDE 1790

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214743833  157 KVSLEETNNISSSKDNLNNEKDGLKilsksiSENKNLNKEGSVYSSQYESYASSKAMIQNKTDQLENSKKALNEQ----- 231
Cdd:PTZ00121  1791 KRRMEVDKKIKDIFDNFANIIEGGK------EGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNEngedg 1864

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214743833  232 -IEAN-NKEKNNLSDENSKAIIDDKNKQINN-----QISQIDLEIKNNNEQLDKLKSDTLaqIKGSIDKINQNLNKL-ES 303
Cdd:PTZ00121  1865 nKEADfNKEKDLKEDDEEEIEEADEIEKIDKddierEIPNNNMAGKNNDIIDDKLDKDEY--IKRDAEETREEIIKIsKK 1942


                   ....*....
gi 2214743833  304 NLSSLDESS 312
Cdd:PTZ00121  1943 DMCINDFSS 1951
 
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 ...
 28-496 3.00e-37

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: 141.69  E-value: 3.00e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214743833  28 IFLYIIIALIVTFFIWSWFSEKEIIVKVNGVVRPDNEIQAISNIVQGEVESIKMKNGESVSKGEVLFKIKSTelgdkknQ 107
Cdd:TIGR01843   6 LITWLIAGLVVIFFLWAYFAPLDVVATATGKVVPSGNVKVVQHLEGGIVREILVREGDRVKAGQVLVELDAT-------D 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214743833 108 VEEQIKYINTDNENLE----KLNKSINDNTNYFENNDKEKEYYYKFQsyeagnKVSLEETNNISSSKDNLNNEKDGLkil 183
Cdd:TIGR01843  79 VEADAAELESQVLRLEaevaRLRAEADSQAAIEFPDDLLSAEDPAVP------ELIKGQQSLFESRKSTLRAQLELI--- 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214743833 184 sksisenknlnkegsvySSQYESYASSKAMIQNKTDQLENSKKALNEQIEAnnkeKNNLSDenskaiiddknKQINNQIS 263
Cdd:TIGR01843 150 -----------------LAQIKQLEAELAGLQAQLQALRQQLEVISEELEA----RRKLKE-----------KGLVSRLE 197

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214743833 264 QIDLEiknnnEQLDKLKSDtLAQIKGSIDKINQNLNKLESNLSSLDES--SNISKEKNKT-TFLAQIEEKINmnnqkkke 340
Cdd:TIGR01843 198 LLELE-----RERAEAQGE-LGRLEAELEVLKRQIDELQLERQQIEQTfrEEVLEELTEAqARLAELRERLN-------- 263

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214743833 341 leENKKQIEQSIekcsVKAPSDGKL-NINANLEKGVIlQTGAIVASIIPNSDTYRVELMIPTKDIANIKVSEDVKYSFEA 419
Cdd:TIGR01843 264 --KARDRLQRLI----IRSPVDGTVqSLKVHTVGGVV-QPGETLMEIVPEDDPLEIEAKLSPKDIGFVHVGQPAEIKFSA 336

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2214743833 420 LPYREYGFLEGKIENLSPDSKVDSEKGISFFTGEGSLNSNRLYS-NKGEEsfIKPGMMCEARIITRKEKMLYYLLEKI 496
Cdd:TIGR01843 337 FPYRRYGILNGKVKSISPDTFTDERGGGPYYRVRISIDQNTLGIgPKGLE--LSPGMPVTADIKTGERTVIEYLLKPI 412
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
23-484 2.99e-23

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 100.51  E-value: 2.99e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214743833  23 NKLMFIFLYIIIALIVTFFIWSWFSE---KEIIVKVNGVVRPDneIQAISNIVQGEVESIKMKNGESVSKGEVLFKIKST 99
Cdd:COG1566     2 KALKKRRLLALVLLLLALGLALWAAGrngPDEPVTADGRVEAR--VVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214743833 100 ELGDKKNQVEEQIKYINTDNENLEKlnksindntnyfenndkekeyyykfqsyeagnkvSLEETNNISSSKDNLNNEKDG 179
Cdd:COG1566    80 DLQAALAQAEAQLAAAEAQLARLEA----------------------------------ELGAEAEIAAAEAQLAAAQAQ 125

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214743833 180 LKILSKSISENKNLNKEGSVYSSQYESyasskamIQNKTDQLENSKKALNEQIEANNKEKNNLsdenskaiiddknkqin 259
Cdd:COG1566   126 LDLAQRELERYQALYKKGAVSQQELDE-------ARAALDAAQAQLEAAQAQLAQAQAGLREE----------------- 181

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214743833 260 NQISQIDLEIKNNNEQLDklksdtlaqikgsidkinqnlnklesnlssldessniskeknkttflaqieekinmnnqkkk 339
Cdd:COG1566   182 EELAAAQAQVAQAEAALA-------------------------------------------------------------- 199

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214743833 340 eleenkkQIEQSIEKCSVKAPSDGKLNiNANLEKGVILQTGAIVASIIPNSDTYrVELMIPTKDIANIKVSEDVKYSFEA 419
Cdd:COG1566   200 -------QAELNLARTTIRAPVDGVVT-NLNVEPGEVVSAGQPLLTIVPLDDLW-VEAYVPETDLGRVKPGQPVEVRVDA 270

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2214743833 420 LPYREYgflEGKIENLSPDSkvdsekgiSFFTGEGSLNSN-------RLYSNKGEESFIKPGMMCEARIITR 484
Cdd:COG1566   271 YPDRVF---EGKVTSISPGA--------GFTSPPKNATGNvvqrypvRIRLDNPDPEPLRPGMSATVEIDTE 331
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 219-439 6.44e-10

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: 60.51  E-value: 6.44e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214743833 219 DQLENSKKALNEQIEANNKEKNNL-SDENSKAIIDDKNKQINNQISQIDLEIKNNNEQLDKLKSD-----TLAQIKG--- 289
Cdd:pfam00529  61 DSAEAQLAKAQAQVARLQAELDRLqALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDlarrrVLAPIGGisr 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214743833 290 -SIDKINQNLNKLESNL-SSLDESSNISKEK--NKTTFLAQIEEKINMNNQKKKELEENKKQIEQSIEKCSVKAPSDGKL 365
Cdd:pfam00529 141 eSLVTAGALVAQAQANLlATVAQLDQIYVQItqSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLERTEIRAPVDGTV 220

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2214743833 366 -NINANLEKGVIlQTGAIVASIIPNSDTYrVELMIPTKDIANIKVSEDVKYSFEALPYREYGFLEGKIENLSPDS 439
Cdd:pfam00529 221 aFLSVTVDGGTV-SAGLRLMFVVPEDNLL-VPGMFVETQLDQVRVGQPVLIPFDAFPQTKTGRFTGVVVGISPDT 293
AcrA COG0845
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ...
 347-487 1.78e-08

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: 56.11  E-value: 1.78e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214743833 347 QIEQSIEKCSVKAPSDGKLnINANLEKGVILQTGAIVASIIpNSDTYRVELMIPTKDIANIKVSEDVKYSFEALPYREYg 426
Cdd:COG0845   124 QARANLAYTTIRAPFDGVV-GERNVEPGQLVSAGTPLFTIA-DLDPLEVEFDVPESDLARLKVGQPVTVTLDAGPGKTF- 200

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2214743833 427 flEGKIENLSPdsKVDSEKGisFFTGEGSL-NSNRLysnkgeesfIKPGMMCEARIITRKEK 487
Cdd:COG0845   201 --EGKVTFIDP--AVDPATR--TVRVRAELpNPDGL---------LRPGMFVRVRIVLGERE 247
HlyD_3 pfam13437
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ...
 357-440 3.53e-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: 3.53e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214743833 357 VKAPSDGKLNInANLEKGVILQTGAIVASIIPnSDTYRVELMIPTKDIANIKvsEDVKYSFEALPYREYGfLEGKIENLS 436
Cdd:pfam13437   2 IRAPVDGVVAE-LNVEEGQVVQAGDPLATIVP-PDRLLVEAFVPAADLGSLK--KGQKVTLKLDPGSDYT-LEGKVVRIS 76


                  ....
gi 2214743833 437 PDSK 440
Cdd:pfam13437  77 PTVD 80
Biotin_lipoyl_2 pfam13533
Biotin-lipoyl like;
66-113 8.47e-07

Biotin-lipoyl like;


Pssm-ID: 433286  Cd Length: 50  Bit Score: 45.90  E-value: 8.47e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2214743833  66 QAISNIVQGEVESIKMKNGESVSKGEVLFKIKSTELGDKKNQVEEQIK 113
Cdd:pfam13533   3 VKIASPVSGKVVAVNVKEGQQVKKGDVLATLDSPELQLQLQQAEAQLA 50
AcrA COG0845
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ...
 50-101 1.01e-05

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: 47.63  E-value: 1.01e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2214743833  50 EIIVKVNGVVRPDNEIQaISNIVQGEVESIKMKNGESVSKGEVLFKIKSTEL 101
Cdd:COG0845     9 PETVEATGTVEARREVE-VRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDL 59
PTZ00121 PTZ00121
MAEBL; Provisional
 77-312 2.99e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.06  E-value: 2.99e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214743833   77 ESIKMKNGESVSKGEVLFKIKSTELGDKKNQVEEQIKYINTDNENLEKLNKSINDNTNYFENNDKEKEYYYKFQSYEAGN 156
Cdd:PTZ00121  1711 EAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDE 1790

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214743833  157 KVSLEETNNISSSKDNLNNEKDGLKilsksiSENKNLNKEGSVYSSQYESYASSKAMIQNKTDQLENSKKALNEQ----- 231
Cdd:PTZ00121  1791 KRRMEVDKKIKDIFDNFANIIEGGK------EGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNEngedg 1864

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214743833  232 -IEAN-NKEKNNLSDENSKAIIDDKNKQINN-----QISQIDLEIKNNNEQLDKLKSDTLaqIKGSIDKINQNLNKL-ES 303
Cdd:PTZ00121  1865 nKEADfNKEKDLKEDDEEEIEEADEIEKIDKddierEIPNNNMAGKNNDIIDDKLDKDEY--IKRDAEETREEIIKIsKK 1942


                   ....*....
gi 2214743833  304 NLSSLDESS 312
Cdd:PTZ00121  1943 DMCINDFSS 1951
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 97-331 1.37e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 41.54  E-value: 1.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214743833  97 KSTELGDKKNQVEEQIKYINTDNENLEKLNKSINDNTNYFENNDK-EKEYYYKFQSYEAGNKVSLEETNNISSSKDNLNN 175
Cdd:TIGR04523 361 KQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKlNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNS 440

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214743833 176 EKDGLK----ILSKSISENKNLNKEGSVYSSQYE-SYASSKAMIQNKTDQLENSKKALNEQIEANNKEKNNLSDENSK-A 249
Cdd:TIGR04523 441 EIKDLTnqdsVKELIIKNLDNTRESLETQLKVLSrSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKiS 520

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214743833 250 IIDDKNKQINNQISQIDLEIKNNNEQLDKLKSD-TLAQIKGSIDKINQNLNKLESNLSSLDESSN------ISKEKNKTT 322
Cdd:TIGR04523 521 SLKEKIEKLESEKKEKESKISDLEDELNKDDFElKKENLEKEIDEKNKEIEELKQTQKSLKKKQEekqeliDQKEKEKKD 600


                  ....*....
gi 2214743833 323 FLAQIEEKI 331
Cdd:TIGR04523 601 LIKEIEEKE 609
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 97-332 1.68e-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: 41.20  E-value: 1.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214743833   97 KSTELGDKKNQVEEQIKYINTDNENLEKLNKSINDNTNYFENNDKEKEYYYKFQSYEAGNKVSLEETnnISSSKDNLNNE 176
Cdd:TIGR02168  724 LSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ--IEQLKEELKAL 801

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214743833  177 KDGLKILSKsisENKNLNKEGSVYSSQYESYASSKAMIQNKTDQLENSKKALNEQIEANNKEKNNLSDENSKaiIDDKNK 256
Cdd:TIGR02168  802 REALDELRA---ELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE--LESELE 876

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2214743833  257 QINNQISQIDLEIKNNNEQLDKLkSDTLAQIKGSIDKINQNLNKLESNLSSLDEssNISKEKNKttfLAQIEEKIN 332
Cdd:TIGR02168  877 ALLNERASLEEALALLRSELEEL-SEELRELESKRSELRRELEELREKLAQLEL--RLEGLEVR---IDNLQERLS 946
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 94-333 2.33e-03

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 40.81  E-value: 2.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214743833   94 FKIKSTELGDKKNQVEEQIKYINTdnenLEKLNKSINDNTNYFENNDKEKEYY-YKFQSYEAGNKVSLEETN----NISS 168
Cdd:TIGR01612  936 FHNKQNILKEILNKNIDTIKESNL----IEKSYKDKFDNTLIDKINELDKAFKdASLNDYEAKNNELIKYFNdlkaNLGK 1011

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214743833  169 SKDNL------NNEKDGLKILSKSISENKNL-NKEGSVYSSQYESYASSKAMIQNKTDQL-ENSKKALNEQIEANNKEKN 240
Cdd:TIGR01612 1012 NKENMlyhqfdEKEKATNDIEQKIEDANKNIpNIEIAIHTSIYNIIDEIEKEIGKNIELLnKEILEEAEINITNFNEIKE 1091

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214743833  241 NLSDENSKAIIDDKNKQINNQISQIDLEIKNNNEQLDKlKSDTLAQIKGS----IDKINQNLNKLESNLSSLDESSNISK 316
Cdd:TIGR01612 1092 KLKHYNFDDFGKEENIKYADEINKIKDDIKNLDQKIDH-HIKALEEIKKKsenyIDEIKAQINDLEDVADKAISNDDPEE 1170

                          250
                   ....*....|....*...
gi 2214743833  317 -EKNKTTFLAQIEEKINM 333
Cdd:TIGR01612 1171 iEKKIENIVTKIDKKKNI 1188
AccB COG0511
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ...
 30-97 2.67e-03

Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440277 [Multi-domain]  Cd Length: 136  Bit Score: 37.95  E-value: 2.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214743833  30 LYIIIALIVTFFIWSWFSEKEIIVKVNGVVRPD------------NEIQAIsniVQGEVESIKMKNGESVSKGEVLFKIK 97
Cdd:COG0511    60 GGAVKSPMVGTFYRAPSPGAKPFVKVGDKVKAGdtlciieamkmmNEIEAP---VSGTVVEILVENGQPVEYGQPLFVIE 136
PRK11281 PRK11281
mechanosensitive channel MscK;
224-309 3.84e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 39.89  E-value: 3.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214743833  224 SKKALNEQIEANNKEKNNlsDENSKAIIDD----------------KNKQINNQISQIDLEIKNNNEQLDKLKSD----- 282
Cdd:PRK11281    37 TEADVQAQLDALNKQKLL--EAEDKLVQQDleqtlalldkidrqkeETEQLKQQLAQAPAKLRQAQAELEALKDDndeet 114

                           90       100       110
                   ....*....|....*....|....*....|....
gi 2214743833  283 -------TLAQIKGSIDKINQNLNKLESNLSSLD 309
Cdd:PRK11281   115 retlstlSLRQLESRLAQTLDQLQNAQNDLAEYN 148
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
171-384 8.15e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.98  E-value: 8.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214743833 171 DNLNNEKDGL-----KILSKSISENKNLNKEGSVYSSQYESYAsskamiqnktdQLENSKKALNEQIEANNKEKNNLSDE 245
Cdd:COG4717    49 ERLEKEADELfkpqgRKPELNLKELKELEEELKEAEEKEEEYA-----------ELQEELEELEEELEELEAELEELREE 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214743833 246 NSKAIIDDKNKQINNQISQIDLEIKNNNEQLDKLKS--DTLAQIKGSIDKINQNLNKLESNLSSLDESSNISKEKNKTTF 323
Cdd:COG4717   118 LEKLEKLLQLLPLYQELEALEAELAELPERLEELEErlEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDL 197

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2214743833 324 LAQIEE---KINMNNQKKKELEENKKQIEQSIEKCSVKAPSDGKLNINANLeKGVILQTGAIVA 384
Cdd:COG4717   198 AEELEElqqRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEA-RLLLLIAAALLA 260
PRK09282 PRK09282
pyruvate carboxylase subunit B; Validated
 63-97 8.60e-03

pyruvate carboxylase subunit B; Validated


Pssm-ID: 236449 [Multi-domain]  Cd Length: 592  Bit Score: 38.67  E-value: 8.60e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2214743833  63 NEIQAIsniVQGEVESIKMKNGESVSKGEVLFKIK 97
Cdd:PRK09282  560 NEIQAP---VDGTVKEILVKEGDRVNPGDVLMEIE 591
 
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