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Conserved domains on  [gi|426206890|emb|CCH50707|]
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yersinia adhesin (plasmid) [Yersinia pseudotuberculosis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LbR_YadA-like cd12820
YadA-like, left-handed beta-roll; This group contains the collagen-binding domain virulence ...
 125-239 6.63e-17

YadA-like, left-handed beta-roll; This group contains the collagen-binding domain virulence factor YadA an adhesion proteins of several Yersinia species, and related cell surface proteins, including Moraxella catarrhalis UspA-like proteins. The collagen-binding portion is found in the hydrophobic N-terminal region. YadA forms a matrix on the bacterial outer membrane, which mediates binding to collagen and epithelial cells. YadA inhibits the complement-activating pathway with the coating of the cell surface with factor H, which impedes C3b molecules. These domains form a left handed beta roll made up of a series of short repeated elements. UspA1 and UspA2 are part of a class of pathogenicity factors that act as cell surface adhesion molecules, in which N-terminal head and neck domains extend from the bacterial outer membrane. The UspA1 head domain of Moraxella catarrhalis, is formed from trimeric left-handed parallel beta-helices of 14-16 amino acid repeats. The UspA1 head domain connects to a neck region of large extended, charged loops that maybe be ligand binding, which is in turn connected to an extended coiled coil domain that tethers the head and neck region to the cell surface via a transmembrane region.


:

Pssm-ID: 240612 [Multi-domain]  Cd Length: 126  Bit Score: 76.77  E-value: 6.63e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426206890 125 GSIATGVNSVAIGPLSKALGDSAVTYGASSTAQ-KDGVAIGARASAS-DTGVAVGFNSKVDAQNSVAIGHSShvAADHGY 202
Cdd:cd12820    8 NNKASGENSTAFGYNNKASGDNSSAFGYGNKASgENSSAFGYNNKASgENSTAFGYGNKASGENSSAFGSNN--TASGNN 85

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 426206890 203 SIAIGDLSKTDRENSVSIGHESLNRQLTHLAAGTKDN 239
Cdd:cd12820   86 SSAFGYNNTASGENSTAFGNNSKASGENSTALGNGNK 122
YadA_anchor pfam03895
YadA-like membrane anchor domain; This region represents the C-terminal 120 amino acids of a ...
 373-432 7.82e-13

YadA-like membrane anchor domain; This region represents the C-terminal 120 amino acids of a family of surface-exposed bacterial proteins. YadA, an adhesin from Yersinia, was the first member of this family to be characterized. UspA2 from Moraxella was second. The Eib immunoglobulin-binding proteins from E. coli were third, followed by the DsrA proteins of Haemophilus ducreyi and others. These proteins are homologous at their C-terminal and have predicted signal sequences, but they diverge elsewhere. The C-terminal 9 amino acids, consisting of alternating hydrophobic amino acids ending in F or W, comprise a targeting motif for the outer membrane of the Gram negative cell envelope. This region is important for oligomerization.


:

Pssm-ID: 427576 [Multi-domain]  Cd Length: 60  Bit Score: 62.96  E-value: 7.82e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 426206890  373 FQPYGVGKVNFTAGVGGYRSSQALAIGSGYRVNESVALKAGVAYAGSSNVMYNASFNIEW 432
Cdd:pfam03895   1 PQPDRPGKFSVSVGVGTYKGESAVALGASARSNGNLVVKLGVSSSSGGSVGAGAGVGYQW 60
auto_Ata super family cl41274
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an ...
 95-351 1.71e-11

trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an architecture that consists of a long signal peptide, a repetitive passenger domain that varies in length from strain to strain, and a C-terminal domain of four transmembrane beta stands that forms one third of the pore for autotransporter activity and anchoring in the outer membrane.


The actual alignment was detected with superfamily member NF033481:

Pssm-ID: 411124 [Multi-domain]  Cd Length: 1862  Bit Score: 66.43  E-value: 1.71e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426206890   95 GLDARAKGIHSIAIGATAEAAKPAAVAVGAGSIATGVNSVAIGPLSKALGDSAVTYGASSTA-QKDGVAIGARA-SASDT 172
Cdd:NF033481  614 GEGAKATGNSSAAIGSGAQATGDNSAAIGKGAEATNENAAAVGGGAKATGKNAAAIGGGAIAdQENAVAVGQGAqSLVEG 693

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426206890  173 GVAVGFNSKVDAQNSVAIGHSShVAADHGYSIAIGDLSKTDRENSVSIGHESLNRQLTHLAAGTKDNDAVNVAQLKKEMA 252
Cdd:NF033481  694 GVALGARSKVEAKNSVALGQDA-VATEATGTSFLTNRDASQSNGVISVGSAGKERRITNVEDGSADSDAVTVRQLKNVDS 772

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426206890  253 ETLENARK-----ETLAQSNDVLDAAKKH-SNSVARTTLETAEEHANKKSAEALVSAKVyadSNSSHTLKTANSYTDVTV 326
Cdd:NF033481  773 RVNQNTSNigkntQNITNLNQKLDDTKTNlGNQITDTNKNLNDAKKDLGNQITDTNTKL---NTTKDQLTTQINDTKTEL 849

                         250       260
                  ....*....|....*....|....*
gi 426206890  327 SSSTKKAIRESNQYTDHKFSQLDNR 351
Cdd:NF033481  850 NNTIGNTKTELNTKIDNTKTELENK 874
 
Name Accession Description Interval E-value
LbR_YadA-like cd12820
YadA-like, left-handed beta-roll; This group contains the collagen-binding domain virulence ...
 125-239 6.63e-17

YadA-like, left-handed beta-roll; This group contains the collagen-binding domain virulence factor YadA an adhesion proteins of several Yersinia species, and related cell surface proteins, including Moraxella catarrhalis UspA-like proteins. The collagen-binding portion is found in the hydrophobic N-terminal region. YadA forms a matrix on the bacterial outer membrane, which mediates binding to collagen and epithelial cells. YadA inhibits the complement-activating pathway with the coating of the cell surface with factor H, which impedes C3b molecules. These domains form a left handed beta roll made up of a series of short repeated elements. UspA1 and UspA2 are part of a class of pathogenicity factors that act as cell surface adhesion molecules, in which N-terminal head and neck domains extend from the bacterial outer membrane. The UspA1 head domain of Moraxella catarrhalis, is formed from trimeric left-handed parallel beta-helices of 14-16 amino acid repeats. The UspA1 head domain connects to a neck region of large extended, charged loops that maybe be ligand binding, which is in turn connected to an extended coiled coil domain that tethers the head and neck region to the cell surface via a transmembrane region.


Pssm-ID: 240612 [Multi-domain]  Cd Length: 126  Bit Score: 76.77  E-value: 6.63e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426206890 125 GSIATGVNSVAIGPLSKALGDSAVTYGASSTAQ-KDGVAIGARASAS-DTGVAVGFNSKVDAQNSVAIGHSShvAADHGY 202
Cdd:cd12820    8 NNKASGENSTAFGYNNKASGDNSSAFGYGNKASgENSSAFGYNNKASgENSTAFGYGNKASGENSSAFGSNN--TASGNN 85

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 426206890 203 SIAIGDLSKTDRENSVSIGHESLNRQLTHLAAGTKDN 239
Cdd:cd12820   86 SSAFGYNNTASGENSTAFGNNSKASGENSTALGNGNK 122
YadA_anchor pfam03895
YadA-like membrane anchor domain; This region represents the C-terminal 120 amino acids of a ...
 373-432 7.82e-13

YadA-like membrane anchor domain; This region represents the C-terminal 120 amino acids of a family of surface-exposed bacterial proteins. YadA, an adhesin from Yersinia, was the first member of this family to be characterized. UspA2 from Moraxella was second. The Eib immunoglobulin-binding proteins from E. coli were third, followed by the DsrA proteins of Haemophilus ducreyi and others. These proteins are homologous at their C-terminal and have predicted signal sequences, but they diverge elsewhere. The C-terminal 9 amino acids, consisting of alternating hydrophobic amino acids ending in F or W, comprise a targeting motif for the outer membrane of the Gram negative cell envelope. This region is important for oligomerization.


Pssm-ID: 427576 [Multi-domain]  Cd Length: 60  Bit Score: 62.96  E-value: 7.82e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 426206890  373 FQPYGVGKVNFTAGVGGYRSSQALAIGSGYRVNESVALKAGVAYAGSSNVMYNASFNIEW 432
Cdd:pfam03895   1 PQPDRPGKFSVSVGVGTYKGESAVALGASARSNGNLVVKLGVSSSSGGSVGAGAGVGYQW 60
auto_Ata NF033481
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an ...
 95-351 1.71e-11

trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an architecture that consists of a long signal peptide, a repetitive passenger domain that varies in length from strain to strain, and a C-terminal domain of four transmembrane beta stands that forms one third of the pore for autotransporter activity and anchoring in the outer membrane.


Pssm-ID: 411124 [Multi-domain]  Cd Length: 1862  Bit Score: 66.43  E-value: 1.71e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426206890   95 GLDARAKGIHSIAIGATAEAAKPAAVAVGAGSIATGVNSVAIGPLSKALGDSAVTYGASSTA-QKDGVAIGARA-SASDT 172
Cdd:NF033481  614 GEGAKATGNSSAAIGSGAQATGDNSAAIGKGAEATNENAAAVGGGAKATGKNAAAIGGGAIAdQENAVAVGQGAqSLVEG 693

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426206890  173 GVAVGFNSKVDAQNSVAIGHSShVAADHGYSIAIGDLSKTDRENSVSIGHESLNRQLTHLAAGTKDNDAVNVAQLKKEMA 252
Cdd:NF033481  694 GVALGARSKVEAKNSVALGQDA-VATEATGTSFLTNRDASQSNGVISVGSAGKERRITNVEDGSADSDAVTVRQLKNVDS 772

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426206890  253 ETLENARK-----ETLAQSNDVLDAAKKH-SNSVARTTLETAEEHANKKSAEALVSAKVyadSNSSHTLKTANSYTDVTV 326
Cdd:NF033481  773 RVNQNTSNigkntQNITNLNQKLDDTKTNlGNQITDTNKNLNDAKKDLGNQITDTNTKL---NTTKDQLTTQINDTKTEL 849

                         250       260
                  ....*....|....*....|....*
gi 426206890  327 SSSTKKAIRESNQYTDHKFSQLDNR 351
Cdd:NF033481  850 NNTIGNTKTELNTKIDNTKTELENK 874
Hia COG5295
Autotransporter adhesin [Intracellular trafficking, secretion, and vesicular transport, ...
 125-258 9.35e-10

Autotransporter adhesin [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444098 [Multi-domain]  Cd Length: 785  Bit Score: 60.94  E-value: 9.35e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426206890 125 GSIATGVNSVAIGPLSKALGDSAVTYGASSTAQKDGVAIGARASASDTGVAVGFNSKVDAQNSVAIGHSSHVAADHgySI 204
Cdd:COG5295  567 NSVALGAGSVASGANSVSVGAAGAENVAAGATDTDAVNGGGAVATGDNSVAVGNNAQASGANSVALGAGATATANN--SV 644

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 426206890 205 AIGDLSKTDRENSVSIGHESLNRQLTHLAAGTKDNDAVNVAQLKKEMAETLENA 258
Cdd:COG5295  645 ALGAGSVADRANTVSVGSAGAERQITNVAAGTADTDAVNVSQLKAVNSSTDQRF 698
auto_Ata NF033481
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an ...
 96-248 4.57e-06

trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an architecture that consists of a long signal peptide, a repetitive passenger domain that varies in length from strain to strain, and a C-terminal domain of four transmembrane beta stands that forms one third of the pore for autotransporter activity and anchoring in the outer membrane.


Pssm-ID: 411124 [Multi-domain]  Cd Length: 1862  Bit Score: 49.09  E-value: 4.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426206890   96 LDARAKGIHSIAIGATAEAAKPAAVAVGAGSIATGVNSVAIGPLSKALGDSAVTYGASSTAQKDGvaigarasasdtGVA 175
Cdd:NF033481  235 MATKATGKDSIAFGGGAVATEENALAIGAFSESKGKKSVAIGTGAKAQKDNAVVIGDQAEASFEG------------GVA 302

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 426206890  176 VGFNSKVDAQNSVAIGHSSHVAADHGYSIAIGDLSKTdreNSVSIGHESLNRQLTHLAAGTKDNDAVNVAQLK 248
Cdd:NF033481  303 IGKGARSEAENSIALGKDSKASQATGESFLTKQSAPT---GVLSIGDIGTERRIQNVADGAADSDAATVRQLK 372
auto_Ata NF033481
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an ...
 126-237 8.19e-04

trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an architecture that consists of a long signal peptide, a repetitive passenger domain that varies in length from strain to strain, and a C-terminal domain of four transmembrane beta stands that forms one third of the pore for autotransporter activity and anchoring in the outer membrane.


Pssm-ID: 411124 [Multi-domain]  Cd Length: 1862  Bit Score: 42.16  E-value: 8.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426206890  126 SIATGVNSVAIGPLSKALGDSAVTYGASSTAQ-KDGVAIGARASASDTGV-AVGFNSKVDAQNSVAIGHSSH----VAAD 199
Cdd:NF033481  541 AVGTGAFSSAFGMTSKATGDASSAFGVMSNASgKGAAAFGAVAQATGDGAsAMGINSLASGTNSTAIGSGNKpgegAKAT 620

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 426206890  200 HGYSIAIGDLSKTDRENSVSIGH--ESLNRQLTHLAAGTK 237
Cdd:NF033481  621 GNSSAAIGSGAQATGDNSAAIGKgaEATNENAAAVGGGAK 660
VOMP_auto_Cterm NF033870
Vomp family autotransporter C-terminal domain; The Vomp (variably expressed outer-membrane ...
 315-402 1.55e-03

Vomp family autotransporter C-terminal domain; The Vomp (variably expressed outer-membrane proteins) family, as described in Bartonella, consists of autotransporter surface proteins including collagen-binding autotransporter adhesins VompA and VompC.


Pssm-ID: 411434 [Multi-domain]  Cd Length: 356  Bit Score: 40.54  E-value: 1.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426206890 315 LKTANSYTDVTVSSSTKKAI----RESNQYTDHKFSQLDNRLDKLDKRVDKGLASSAALNSLFQPYGVGKVNFTAGVGGY 390
Cdd:NF033870 234 LDDAKKYTDERIKNIVVDAIddavAEAKSYTDMKFEALNYSIEGVRKEARQAAAIGLAVSNLRYNDTPGKLSVAFGSGLW 313

                         90
                 ....*....|..
gi 426206890 391 RSSQALAIGSGY 402
Cdd:NF033870 314 RSQSAFAFGAGY 325
YadA_stalk pfam05662
Coiled stalk of trimeric autotransporter adhesin; This short motif is found in invasins and ...
 228-258 2.97e-03

Coiled stalk of trimeric autotransporter adhesin; This short motif is found in invasins and haemagglutinins, normally associated with (pfam05658).


Pssm-ID: 428572 [Multi-domain]  Cd Length: 43  Bit Score: 35.24  E-value: 2.97e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 426206890  228 QLTHLAAGTKDNDAVNVAQLKKEMAETLENA 258
Cdd:pfam05662   1 KITNVAAGTVSTDAVNGSQLYAVNQSVSNGA 31
PHA00430 PHA00430
tail fiber protein
 227-338 3.19e-03

tail fiber protein


Pssm-ID: 222790 [Multi-domain]  Cd Length: 568  Bit Score: 39.87  E-value: 3.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426206890 227 RQLTHLAAGTKDNDAVNVAQLkKEMAETLENARKETLaQSNDVLDAAKKHSNSV-----ARTTLETAEEHANKKSAEALV 301
Cdd:PHA00430 134 RRIVNLADAVDDGDAVPLGQI-KTWNQSAWNARNEAN-RSRNEADRARNQAERFnnesgASATNTKQWRSEADGSNSEAN 211

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 426206890 302 SAKVYADSNSSHTLKT------ANSYTDVTVSSSTKKAIRESN 338
Cdd:PHA00430 212 RFKGYADSMTSSVEAAkgqaesSSKEANTAGDYATKAAASASA 254
auto_Ata NF033481
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an ...
 142-242 4.72e-03

trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an architecture that consists of a long signal peptide, a repetitive passenger domain that varies in length from strain to strain, and a C-terminal domain of four transmembrane beta stands that forms one third of the pore for autotransporter activity and anchoring in the outer membrane.


Pssm-ID: 411124 [Multi-domain]  Cd Length: 1862  Bit Score: 39.46  E-value: 4.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426206890  142 ALGDSAVTYGA-SSTAQKDGVAIGARASASDTG-VAVGFNSKVDAQNSVAIGHSSHVAADHGY----SIAIGDLSKTDRE 215
Cdd:NF033481  396 ATGRNAIAVGVnASAAGREAMAIGGSAQAIGSGaIAMGSSSQTVGRGDVAIGRNASTQGAEGVnsnqSVAIGDQTKAIGD 475

                          90       100
                  ....*....|....*....|....*..
gi 426206890  216 NSVSIGHESLNRQLTHLAAGTKDNDAV 242
Cdd:NF033481  476 QSVAIGADVIAKGNSSVAIGGDDVDKI 502
auto_Ata NF033481
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an ...
 95-191 6.54e-03

trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an architecture that consists of a long signal peptide, a repetitive passenger domain that varies in length from strain to strain, and a C-terminal domain of four transmembrane beta stands that forms one third of the pore for autotransporter activity and anchoring in the outer membrane.


Pssm-ID: 411124 [Multi-domain]  Cd Length: 1862  Bit Score: 39.08  E-value: 6.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426206890   95 GLDARAKGIHSIAIGATAEAAKPAAVAVGAGSIATGVNSVAIGPLSKALGDSAVTYGASSTAQKDGVAIGARASA-SDTG 173
Cdd:NF033481  398 GRNAIAVGVNASAAGREAMAIGGSAQAIGSGAIAMGSSSQTVGRGDVAIGRNASTQGAEGVNSNQSVAIGDQTKAiGDQS 477

                          90
                  ....*....|....*...
gi 426206890  174 VAVGFNSKVDAQNSVAIG 191
Cdd:NF033481  478 VAIGADVIAKGNSSVAIG 495
auto_Ata NF033481
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an ...
 105-221 9.38e-03

trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an architecture that consists of a long signal peptide, a repetitive passenger domain that varies in length from strain to strain, and a C-terminal domain of four transmembrane beta stands that forms one third of the pore for autotransporter activity and anchoring in the outer membrane.


Pssm-ID: 411124 [Multi-domain]  Cd Length: 1862  Bit Score: 38.69  E-value: 9.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426206890  105 SIAIGATAEAAKPAAVAVGAGSIATGVNSVAIGPLSKALGDSAVTYGASSTAQKDG--------VAIGARASASDTGVAV 176
Cdd:NF033481  534 STAVGVQAVGTGAFSSAFGMTSKATGDASSAFGVMSNASGKGAAAFGAVAQATGDGasamginsLASGTNSTAIGSGNKP 613

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 426206890  177 GFNSKVDAQNSVAIGHSSHVAADHgySIAIGDLSKTDRENSVSIG 221
Cdd:NF033481  614 GEGAKATGNSSAAIGSGAQATGDN--SAAIGKGAEATNENAAAVG 656
 
Name Accession Description Interval E-value
LbR_YadA-like cd12820
YadA-like, left-handed beta-roll; This group contains the collagen-binding domain virulence ...
 125-239 6.63e-17

YadA-like, left-handed beta-roll; This group contains the collagen-binding domain virulence factor YadA an adhesion proteins of several Yersinia species, and related cell surface proteins, including Moraxella catarrhalis UspA-like proteins. The collagen-binding portion is found in the hydrophobic N-terminal region. YadA forms a matrix on the bacterial outer membrane, which mediates binding to collagen and epithelial cells. YadA inhibits the complement-activating pathway with the coating of the cell surface with factor H, which impedes C3b molecules. These domains form a left handed beta roll made up of a series of short repeated elements. UspA1 and UspA2 are part of a class of pathogenicity factors that act as cell surface adhesion molecules, in which N-terminal head and neck domains extend from the bacterial outer membrane. The UspA1 head domain of Moraxella catarrhalis, is formed from trimeric left-handed parallel beta-helices of 14-16 amino acid repeats. The UspA1 head domain connects to a neck region of large extended, charged loops that maybe be ligand binding, which is in turn connected to an extended coiled coil domain that tethers the head and neck region to the cell surface via a transmembrane region.


Pssm-ID: 240612 [Multi-domain]  Cd Length: 126  Bit Score: 76.77  E-value: 6.63e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426206890 125 GSIATGVNSVAIGPLSKALGDSAVTYGASSTAQ-KDGVAIGARASAS-DTGVAVGFNSKVDAQNSVAIGHSShvAADHGY 202
Cdd:cd12820    8 NNKASGENSTAFGYNNKASGDNSSAFGYGNKASgENSSAFGYNNKASgENSTAFGYGNKASGENSSAFGSNN--TASGNN 85

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 426206890 203 SIAIGDLSKTDRENSVSIGHESLNRQLTHLAAGTKDN 239
Cdd:cd12820   86 SSAFGYNNTASGENSTAFGNNSKASGENSTALGNGNK 122
LbR_YadA-like cd12820
YadA-like, left-handed beta-roll; This group contains the collagen-binding domain virulence ...
 95-224 9.35e-17

YadA-like, left-handed beta-roll; This group contains the collagen-binding domain virulence factor YadA an adhesion proteins of several Yersinia species, and related cell surface proteins, including Moraxella catarrhalis UspA-like proteins. The collagen-binding portion is found in the hydrophobic N-terminal region. YadA forms a matrix on the bacterial outer membrane, which mediates binding to collagen and epithelial cells. YadA inhibits the complement-activating pathway with the coating of the cell surface with factor H, which impedes C3b molecules. These domains form a left handed beta roll made up of a series of short repeated elements. UspA1 and UspA2 are part of a class of pathogenicity factors that act as cell surface adhesion molecules, in which N-terminal head and neck domains extend from the bacterial outer membrane. The UspA1 head domain of Moraxella catarrhalis, is formed from trimeric left-handed parallel beta-helices of 14-16 amino acid repeats. The UspA1 head domain connects to a neck region of large extended, charged loops that maybe be ligand binding, which is in turn connected to an extended coiled coil domain that tethers the head and neck region to the cell surface via a transmembrane region.


Pssm-ID: 240612 [Multi-domain]  Cd Length: 126  Bit Score: 75.99  E-value: 9.35e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426206890  95 GLDARAKGIHSIAIGAtaeaakpaavavgaGSIATGVNSVAIGPLSKALGDSAVTYGASSTAQKD-GVAIGARASASDTG 173
Cdd:cd12820    6 GYNNKASGENSTAFGY--------------NNKASGDNSSAFGYGNKASGENSSAFGYNNKASGEnSTAFGYGNKASGEN 71

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 426206890 174 -VAVGFNSKVDAQNSVAIGHSSHVAADhgYSIAIGDLSKTDRENSVSIGHES 224
Cdd:cd12820   72 sSAFGSNNTASGNNSSAFGYNNTASGE--NSTAFGNNSKASGENSTALGNGN 121
YadA_anchor pfam03895
YadA-like membrane anchor domain; This region represents the C-terminal 120 amino acids of a ...
 373-432 7.82e-13

YadA-like membrane anchor domain; This region represents the C-terminal 120 amino acids of a family of surface-exposed bacterial proteins. YadA, an adhesin from Yersinia, was the first member of this family to be characterized. UspA2 from Moraxella was second. The Eib immunoglobulin-binding proteins from E. coli were third, followed by the DsrA proteins of Haemophilus ducreyi and others. These proteins are homologous at their C-terminal and have predicted signal sequences, but they diverge elsewhere. The C-terminal 9 amino acids, consisting of alternating hydrophobic amino acids ending in F or W, comprise a targeting motif for the outer membrane of the Gram negative cell envelope. This region is important for oligomerization.


Pssm-ID: 427576 [Multi-domain]  Cd Length: 60  Bit Score: 62.96  E-value: 7.82e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 426206890  373 FQPYGVGKVNFTAGVGGYRSSQALAIGSGYRVNESVALKAGVAYAGSSNVMYNASFNIEW 432
Cdd:pfam03895   1 PQPDRPGKFSVSVGVGTYKGESAVALGASARSNGNLVVKLGVSSSSGGSVGAGAGVGYQW 60
LbR-like cd12813
Left-handed beta-roll, including virulence factors and various other proteins; This family ...
 125-207 2.38e-12

Left-handed beta-roll, including virulence factors and various other proteins; This family contains a variety of protein domains with a left-handed beta-roll structure including cell surface adhesion proteins, bacterial virulence factors, and ice-binding proteins, and other activities. UspA1 Head And Neck Domain and YadA of Yersinia are part of a class of pathogenicity factors that act as cell surface adhesion molecules, in which N-terminal head and neck domains extend from the bacterial outer membrane. The UspA1 head domain of Moraxella catarrhalis, is formed from trimeric beta-rolls of 14-16 amino acid repeats. The UspA1 head domain connects to a neck region of large extended, charged loops that maybe be ligand binding, which is in turn connected to an extended coiled coil domain that tethers the head and neck region to the cell surface via a transmembrane region. The collagen-binding domain virulence factor YadA an adhesion proteins of several Yersinia species, and related cell surface proteins. The collagen-binding portion is found in the hydrophobic N-terminal region. YadA forms a matrix on the bacterial outer membrane, which mediates binding to collagen and epithelial cells. YadA inhibits the complement-activating pathway with the coating of the cell surface with factor H, which impedes C3b molecules. The ice-binding protein of the grass Lolium perenne (LpIBP) discourages the recrystallization of ice. Ice-binding proteins produced by organisms to prevent the growing of ice are termed to anti-freeze proteins. LpIBP consists of an unusual left-handed beta roll. Ice-binding is mediated by a flat beta-sheet on one side of the helix. These domains form a left handed beta roll made up of a series of short repeated elements.


Pssm-ID: 240610 [Multi-domain]  Cd Length: 99  Bit Score: 62.95  E-value: 2.38e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426206890 125 GSIATGVNSVAIGPL-SKALGDSAVTYGASSTAQKDG-VAIGARASASD-TGVAVGFNSKVDAQNSVAIGHSSHVAADhg 201
Cdd:cd12813   16 GNVATGTDSTVIGGDnNSASGSNSTAVGGANTATGSNaVASGTNAIVTDdNAVASGNNNLASGSNSTALGGHSTVTGS-- 93


                 ....*.
gi 426206890 202 YSIAIG 207
Cdd:cd12813   94 NSAALG 99
auto_Ata NF033481
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an ...
 95-351 1.71e-11

trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an architecture that consists of a long signal peptide, a repetitive passenger domain that varies in length from strain to strain, and a C-terminal domain of four transmembrane beta stands that forms one third of the pore for autotransporter activity and anchoring in the outer membrane.


Pssm-ID: 411124 [Multi-domain]  Cd Length: 1862  Bit Score: 66.43  E-value: 1.71e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426206890   95 GLDARAKGIHSIAIGATAEAAKPAAVAVGAGSIATGVNSVAIGPLSKALGDSAVTYGASSTA-QKDGVAIGARA-SASDT 172
Cdd:NF033481  614 GEGAKATGNSSAAIGSGAQATGDNSAAIGKGAEATNENAAAVGGGAKATGKNAAAIGGGAIAdQENAVAVGQGAqSLVEG 693

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426206890  173 GVAVGFNSKVDAQNSVAIGHSShVAADHGYSIAIGDLSKTDRENSVSIGHESLNRQLTHLAAGTKDNDAVNVAQLKKEMA 252
Cdd:NF033481  694 GVALGARSKVEAKNSVALGQDA-VATEATGTSFLTNRDASQSNGVISVGSAGKERRITNVEDGSADSDAVTVRQLKNVDS 772

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426206890  253 ETLENARK-----ETLAQSNDVLDAAKKH-SNSVARTTLETAEEHANKKSAEALVSAKVyadSNSSHTLKTANSYTDVTV 326
Cdd:NF033481  773 RVNQNTSNigkntQNITNLNQKLDDTKTNlGNQITDTNKNLNDAKKDLGNQITDTNTKL---NTTKDQLTTQINDTKTEL 849

                         250       260
                  ....*....|....*....|....*
gi 426206890  327 SSSTKKAIRESNQYTDHKFSQLDNR 351
Cdd:NF033481  850 NNTIGNTKTELNTKIDNTKTELENK 874
LbR_YadA-like cd12820
YadA-like, left-handed beta-roll; This group contains the collagen-binding domain virulence ...
 95-199 5.94e-11

YadA-like, left-handed beta-roll; This group contains the collagen-binding domain virulence factor YadA an adhesion proteins of several Yersinia species, and related cell surface proteins, including Moraxella catarrhalis UspA-like proteins. The collagen-binding portion is found in the hydrophobic N-terminal region. YadA forms a matrix on the bacterial outer membrane, which mediates binding to collagen and epithelial cells. YadA inhibits the complement-activating pathway with the coating of the cell surface with factor H, which impedes C3b molecules. These domains form a left handed beta roll made up of a series of short repeated elements. UspA1 and UspA2 are part of a class of pathogenicity factors that act as cell surface adhesion molecules, in which N-terminal head and neck domains extend from the bacterial outer membrane. The UspA1 head domain of Moraxella catarrhalis, is formed from trimeric left-handed parallel beta-helices of 14-16 amino acid repeats. The UspA1 head domain connects to a neck region of large extended, charged loops that maybe be ligand binding, which is in turn connected to an extended coiled coil domain that tethers the head and neck region to the cell surface via a transmembrane region.


Pssm-ID: 240612 [Multi-domain]  Cd Length: 126  Bit Score: 59.82  E-value: 5.94e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426206890  95 GLDARAKGIHSIAIGAtaeaakpaavavgaGSIATGVNSVAIGPLSKALGDSAVTYGASSTAQKDG-VAIGARASASDTG 173
Cdd:cd12820   34 GYGNKASGENSSAFGY--------------NNKASGENSTAFGYGNKASGENSSAFGSNNTASGNNsSAFGYNNTASGEN 99

                         90       100
                 ....*....|....*....|....*..
gi 426206890 174 -VAVGFNSKVDAQNSVAIGHSSHVAAD 199
Cdd:cd12820  100 sTAFGNNSKASGENSTALGNGNKASGN 126
Hia COG5295
Autotransporter adhesin [Intracellular trafficking, secretion, and vesicular transport, ...
 125-258 9.35e-10

Autotransporter adhesin [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444098 [Multi-domain]  Cd Length: 785  Bit Score: 60.94  E-value: 9.35e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426206890 125 GSIATGVNSVAIGPLSKALGDSAVTYGASSTAQKDGVAIGARASASDTGVAVGFNSKVDAQNSVAIGHSSHVAADHgySI 204
Cdd:COG5295  567 NSVALGAGSVASGANSVSVGAAGAENVAAGATDTDAVNGGGAVATGDNSVAVGNNAQASGANSVALGAGATATANN--SV 644

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 426206890 205 AIGDLSKTDRENSVSIGHESLNRQLTHLAAGTKDNDAVNVAQLKKEMAETLENA 258
Cdd:COG5295  645 ALGAGSVADRANTVSVGSAGAERQITNVAAGTADTDAVNVSQLKAVNSSTDQRF 698
auto_Ata NF033481
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an ...
 96-248 4.57e-06

trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an architecture that consists of a long signal peptide, a repetitive passenger domain that varies in length from strain to strain, and a C-terminal domain of four transmembrane beta stands that forms one third of the pore for autotransporter activity and anchoring in the outer membrane.


Pssm-ID: 411124 [Multi-domain]  Cd Length: 1862  Bit Score: 49.09  E-value: 4.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426206890   96 LDARAKGIHSIAIGATAEAAKPAAVAVGAGSIATGVNSVAIGPLSKALGDSAVTYGASSTAQKDGvaigarasasdtGVA 175
Cdd:NF033481  235 MATKATGKDSIAFGGGAVATEENALAIGAFSESKGKKSVAIGTGAKAQKDNAVVIGDQAEASFEG------------GVA 302

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 426206890  176 VGFNSKVDAQNSVAIGHSSHVAADHGYSIAIGDLSKTdreNSVSIGHESLNRQLTHLAAGTKDNDAVNVAQLK 248
Cdd:NF033481  303 IGKGARSEAENSIALGKDSKASQATGESFLTKQSAPT---GVLSIGDIGTERRIQNVADGAADSDAATVRQLK 372
auto_Ata NF033481
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an ...
 126-237 8.19e-04

trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an architecture that consists of a long signal peptide, a repetitive passenger domain that varies in length from strain to strain, and a C-terminal domain of four transmembrane beta stands that forms one third of the pore for autotransporter activity and anchoring in the outer membrane.


Pssm-ID: 411124 [Multi-domain]  Cd Length: 1862  Bit Score: 42.16  E-value: 8.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426206890  126 SIATGVNSVAIGPLSKALGDSAVTYGASSTAQ-KDGVAIGARASASDTGV-AVGFNSKVDAQNSVAIGHSSH----VAAD 199
Cdd:NF033481  541 AVGTGAFSSAFGMTSKATGDASSAFGVMSNASgKGAAAFGAVAQATGDGAsAMGINSLASGTNSTAIGSGNKpgegAKAT 620

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 426206890  200 HGYSIAIGDLSKTDRENSVSIGH--ESLNRQLTHLAAGTK 237
Cdd:NF033481  621 GNSSAAIGSGAQATGDNSAAIGKgaEATNENAAAVGGGAK 660
VOMP_auto_Cterm NF033870
Vomp family autotransporter C-terminal domain; The Vomp (variably expressed outer-membrane ...
 315-402 1.55e-03

Vomp family autotransporter C-terminal domain; The Vomp (variably expressed outer-membrane proteins) family, as described in Bartonella, consists of autotransporter surface proteins including collagen-binding autotransporter adhesins VompA and VompC.


Pssm-ID: 411434 [Multi-domain]  Cd Length: 356  Bit Score: 40.54  E-value: 1.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426206890 315 LKTANSYTDVTVSSSTKKAI----RESNQYTDHKFSQLDNRLDKLDKRVDKGLASSAALNSLFQPYGVGKVNFTAGVGGY 390
Cdd:NF033870 234 LDDAKKYTDERIKNIVVDAIddavAEAKSYTDMKFEALNYSIEGVRKEARQAAAIGLAVSNLRYNDTPGKLSVAFGSGLW 313

                         90
                 ....*....|..
gi 426206890 391 RSSQALAIGSGY 402
Cdd:NF033870 314 RSQSAFAFGAGY 325
YadA_stalk pfam05662
Coiled stalk of trimeric autotransporter adhesin; This short motif is found in invasins and ...
 228-258 2.97e-03

Coiled stalk of trimeric autotransporter adhesin; This short motif is found in invasins and haemagglutinins, normally associated with (pfam05658).


Pssm-ID: 428572 [Multi-domain]  Cd Length: 43  Bit Score: 35.24  E-value: 2.97e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 426206890  228 QLTHLAAGTKDNDAVNVAQLKKEMAETLENA 258
Cdd:pfam05662   1 KITNVAAGTVSTDAVNGSQLYAVNQSVSNGA 31
PHA00430 PHA00430
tail fiber protein
 227-338 3.19e-03

tail fiber protein


Pssm-ID: 222790 [Multi-domain]  Cd Length: 568  Bit Score: 39.87  E-value: 3.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426206890 227 RQLTHLAAGTKDNDAVNVAQLkKEMAETLENARKETLaQSNDVLDAAKKHSNSV-----ARTTLETAEEHANKKSAEALV 301
Cdd:PHA00430 134 RRIVNLADAVDDGDAVPLGQI-KTWNQSAWNARNEAN-RSRNEADRARNQAERFnnesgASATNTKQWRSEADGSNSEAN 211

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 426206890 302 SAKVYADSNSSHTLKT------ANSYTDVTVSSSTKKAIRESN 338
Cdd:PHA00430 212 RFKGYADSMTSSVEAAkgqaesSSKEANTAGDYATKAAASASA 254
auto_Ata NF033481
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an ...
 142-242 4.72e-03

trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an architecture that consists of a long signal peptide, a repetitive passenger domain that varies in length from strain to strain, and a C-terminal domain of four transmembrane beta stands that forms one third of the pore for autotransporter activity and anchoring in the outer membrane.


Pssm-ID: 411124 [Multi-domain]  Cd Length: 1862  Bit Score: 39.46  E-value: 4.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426206890  142 ALGDSAVTYGA-SSTAQKDGVAIGARASASDTG-VAVGFNSKVDAQNSVAIGHSSHVAADHGY----SIAIGDLSKTDRE 215
Cdd:NF033481  396 ATGRNAIAVGVnASAAGREAMAIGGSAQAIGSGaIAMGSSSQTVGRGDVAIGRNASTQGAEGVnsnqSVAIGDQTKAIGD 475

                          90       100
                  ....*....|....*....|....*..
gi 426206890  216 NSVSIGHESLNRQLTHLAAGTKDNDAV 242
Cdd:NF033481  476 QSVAIGADVIAKGNSSVAIGGDDVDKI 502
auto_Ata NF033481
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an ...
 95-191 6.54e-03

trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an architecture that consists of a long signal peptide, a repetitive passenger domain that varies in length from strain to strain, and a C-terminal domain of four transmembrane beta stands that forms one third of the pore for autotransporter activity and anchoring in the outer membrane.


Pssm-ID: 411124 [Multi-domain]  Cd Length: 1862  Bit Score: 39.08  E-value: 6.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426206890   95 GLDARAKGIHSIAIGATAEAAKPAAVAVGAGSIATGVNSVAIGPLSKALGDSAVTYGASSTAQKDGVAIGARASA-SDTG 173
Cdd:NF033481  398 GRNAIAVGVNASAAGREAMAIGGSAQAIGSGAIAMGSSSQTVGRGDVAIGRNASTQGAEGVNSNQSVAIGDQTKAiGDQS 477

                          90
                  ....*....|....*...
gi 426206890  174 VAVGFNSKVDAQNSVAIG 191
Cdd:NF033481  478 VAIGADVIAKGNSSVAIG 495
auto_Ata NF033481
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an ...
 105-221 9.38e-03

trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an architecture that consists of a long signal peptide, a repetitive passenger domain that varies in length from strain to strain, and a C-terminal domain of four transmembrane beta stands that forms one third of the pore for autotransporter activity and anchoring in the outer membrane.


Pssm-ID: 411124 [Multi-domain]  Cd Length: 1862  Bit Score: 38.69  E-value: 9.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426206890  105 SIAIGATAEAAKPAAVAVGAGSIATGVNSVAIGPLSKALGDSAVTYGASSTAQKDG--------VAIGARASASDTGVAV 176
Cdd:NF033481  534 STAVGVQAVGTGAFSSAFGMTSKATGDASSAFGVMSNASGKGAAAFGAVAQATGDGasamginsLASGTNSTAIGSGNKP 613

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 426206890  177 GFNSKVDAQNSVAIGHSSHVAADHgySIAIGDLSKTDRENSVSIG 221
Cdd:NF033481  614 GEGAKATGNSSAAIGSGAQATGDN--SAAIGKGAEATNENAAAVG 656
 
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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