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Conserved domains on  [gi|1173391209|ref|WP_081244576|]
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trimeric autotransporter actin-nucleating factor BimA [Burkholderia mallei]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BimA_second NF040983
trimeric autotransporter actin-nucleating factor BimA; This HMM describes BimA (Burkholderia ...
 1-376 0e+00

trimeric autotransporter actin-nucleating factor BimA; This HMM describes BimA (Burkholderia intracellular motility A), WP_004266405.1-like proteins in Burkholderia mallei or B. pseudomallei. The term BimA has also been used for WP_011205626.1-like homologs that have a very different N-terminal half.


:

Pssm-ID: 468913 [Multi-domain]  Cd Length: 382  Bit Score: 572.62  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173391209   1 MVLYIRMKYHRFPRSHAQQDTGRAASTVPFQRFAHLLCSSIAPLALGFSTDALAIGQAESTAFNAVIDQIKKGDFKLKPV 80
Cdd:NF040983    1 MVLYIRMKYHRFPRSHAQQDTGRAASTVPFQRFAHLLCSSIAPLALGFSTDALAIEQAESTAFNAVIDQIKKGDFKLKPV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173391209  81 GDRTLPNKVPPPPPP------PPPPPPPPPPSPPPPSPPPPSPPPPSPPPPSPPPPTTTPPTTTPPTTTTPTPSMHPIQP 154
Cdd:NF040983   81 GDRTLPNKVPPPPPPppppppPPPTPPPPPPPPPPPPPPSPPPPPPPSPPPSPPPPTTTPPTRTTPSTTTPTPSMHPIQP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173391209 155 TQLPSIPNATPTSGSATNVTINFNSTGASAMGTNSIALDFHARAKDSDSLASGRLAHASGPRSTAIGAEANASGQNTVAL 234
Cdd:NF040983  161 TQLPSIPNATPTSGSATNVTINFNSTGASAMGTNSIALDFHARAKDSDSLASGRLAHASGPRSTAIGAEANASGQNTVAL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173391209 235 GAGSIADRNNTVSVGRHGDERQIVHVAAGTQATDAVNVGQLNLAMSNANAYTNQRIGDLQQSITDTARDAYSGVAAATAL 314
Cdd:NF040983  241 GAGSIADRNNTVSVGRHGDERQIVHVAAGTQATDAVNVGQLNLAMSNANAYTNQRIGDLQQSITDTARDAYSGVAAATAL 320

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1173391209 315 TMIPDVDRDKRVSIGVGGAVYKGHRAVALGGTARINENLKVRAGVAMSAGGNAVGIGMSWQW 376
Cdd:NF040983  321 TMIPDVDRDKRVSIGVGGAVYKGHRAVALGGTARINENLKVRAGVAMSAGGNAVGIGMSWQW 382
 
Name Accession Description Interval E-value
BimA_second NF040983
trimeric autotransporter actin-nucleating factor BimA; This HMM describes BimA (Burkholderia ...
 1-376 0e+00

trimeric autotransporter actin-nucleating factor BimA; This HMM describes BimA (Burkholderia intracellular motility A), WP_004266405.1-like proteins in Burkholderia mallei or B. pseudomallei. The term BimA has also been used for WP_011205626.1-like homologs that have a very different N-terminal half.


Pssm-ID: 468913 [Multi-domain]  Cd Length: 382  Bit Score: 572.62  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173391209   1 MVLYIRMKYHRFPRSHAQQDTGRAASTVPFQRFAHLLCSSIAPLALGFSTDALAIGQAESTAFNAVIDQIKKGDFKLKPV 80
Cdd:NF040983    1 MVLYIRMKYHRFPRSHAQQDTGRAASTVPFQRFAHLLCSSIAPLALGFSTDALAIEQAESTAFNAVIDQIKKGDFKLKPV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173391209  81 GDRTLPNKVPPPPPP------PPPPPPPPPPSPPPPSPPPPSPPPPSPPPPSPPPPTTTPPTTTPPTTTTPTPSMHPIQP 154
Cdd:NF040983   81 GDRTLPNKVPPPPPPppppppPPPTPPPPPPPPPPPPPPSPPPPPPPSPPPSPPPPTTTPPTRTTPSTTTPTPSMHPIQP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173391209 155 TQLPSIPNATPTSGSATNVTINFNSTGASAMGTNSIALDFHARAKDSDSLASGRLAHASGPRSTAIGAEANASGQNTVAL 234
Cdd:NF040983  161 TQLPSIPNATPTSGSATNVTINFNSTGASAMGTNSIALDFHARAKDSDSLASGRLAHASGPRSTAIGAEANASGQNTVAL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173391209 235 GAGSIADRNNTVSVGRHGDERQIVHVAAGTQATDAVNVGQLNLAMSNANAYTNQRIGDLQQSITDTARDAYSGVAAATAL 314
Cdd:NF040983  241 GAGSIADRNNTVSVGRHGDERQIVHVAAGTQATDAVNVGQLNLAMSNANAYTNQRIGDLQQSITDTARDAYSGVAAATAL 320

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1173391209 315 TMIPDVDRDKRVSIGVGGAVYKGHRAVALGGTARINENLKVRAGVAMSAGGNAVGIGMSWQW 376
Cdd:NF040983  321 TMIPDVDRDKRVSIGVGGAVYKGHRAVALGGTARINENLKVRAGVAMSAGGNAVGIGMSWQW 382
BimA_first NF040984
trimeric autotransporter actin-nucleating factor BimA; BimA (B. pseudomallei intracellular ...
 117-376 5.21e-76

trimeric autotransporter actin-nucleating factor BimA; BimA (B. pseudomallei intracellular motility protein A) is a trimeric autotransporter, homologous in its C-terminal half to a number of trimeric autotransporter adhesins. It is a virulence factor that nucleates actin, so that actin polymerization can drive escape by B. pseudomallei out of one cell and into a neighboring cell. HMM NF040983 describes a homolog with similar activity but substantial difference in sequence architecture in the N-terminal region.


Pssm-ID: 468914 [Multi-domain]  Cd Length: 517  Bit Score: 244.01  E-value: 5.21e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173391209 117 PPPPSPPPPSPPPPTTTPPTTTPPTTTTPTPSMH-------------------------------------------PIQ 153
Cdd:NF040984  152 DANGDFSGRSAMPIEMAANAALRSLKKNPGDAGHaapaylpaerigqlrekvrrtiealesnrppkpqprstppqstPPK 231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173391209 154 PTQLPSIPN---------------------------ATPT------------------------------------SGSA 170
Cdd:NF040984  232 PTQHPTAPNpnapdastpdastppdastpdasapdaSAPSrpapapragtgapaasaatrapafanrvrkpnpampAASS 311

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173391209 171 TNVTINFNSTGASAMGTNSIALDFHARAKDSDSLASGRLAHASGPRSTAIGAEANASGQNTVALGAGSIADRNNTVSVGR 250
Cdd:NF040984  312 HAIASDFASSNAFAIGDDSTAVGAQAIAFSEQSIAIGSRAIAAGARSIAVGTDATAAAPDSVALGSGSIAEREGTVSVGR 391

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173391209 251 HGDERQIVHVAAGTQATDAVNVGQLNLAMSNANAYTNQRIGDLQQSITDTARDAYSGVAAATALTMIPDVDRDKRVSIGV 330
Cdd:NF040984  392 DGHERQITHVASGTEPTDAVNVTQLRAAMSNANAYTNQRIGDLQQSITDTARDAYSGVAAATALTMIPDVDRDKRVSIGV 471

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1173391209 331 GGAVYKGHRAVALGGTARINENLKVRAGVAMSAGGNAVGIGMSWQW 376
Cdd:NF040984  472 GGAVYKGHRAVALGGTARINENLKVRAGVAMSAGGNAVGIGMSWQW 517
Hia COG5295
Autotransporter adhesin [Intracellular trafficking, secretion, and vesicular transport, ...
 162-375 1.13e-20

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


Pssm-ID: 444098 [Multi-domain]  Cd Length: 785  Bit Score: 93.68  E-value: 1.13e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173391209 162 NATPTSGSATNVTINFNSTGASAMGTNSIALDFHARAKDSDSLASGRLAHASGPRSTAIGAEANASGQNTVALGAGSIAD 241
Cdd:COG5295   574 GSVASGANSVSVGAAGAENVAAGATDTDAVNGGGAVATGDNSVAVGNNAQASGANSVALGAGATATANNSVALGAGSVAD 653

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173391209 242 RNNTVSVGRHGDERQIVHVAAGTQATDAVNVGQLNlamsNANAYTNQRIGDLQQSITDTARDAYSGVAAATALTMIPDVD 321
Cdd:COG5295   654 RANTVSVGSAGAERQITNVAAGTADTDAVNVSQLK----AVNSSTDQRFNQLSNRINRVDKRARAGIASAMAMASLPQAY 729

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1173391209 322 RDKRVSIGVGGAVYKGHRAVALGGTARI-NENLKVRAGVAMSAGGN-AVGIGMSWQ 375
Cdd:COG5295   730 APGKSAVAAGVGTYRGQSAVAVGYSAVSdNGKWTVKLGGSANSQGNvGAGAGVGYQ 785
YadA_anchor pfam03895
YadA-like membrane anchor domain; This region represents the C-terminal 120 amino acids of a ...
 318-376 7.35e-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: 7.35e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173391209 318 PDVDRDKRVSIGVGGAVYKGHRAVALGGTARINENLKVRAGVA-MSAGGNAVGIGMSWQW 376
Cdd:pfam03895   1 PQPDRPGKFSVSVGVGTYKGESAVALGASARSNGNLVVKLGVSsSSGGSVGAGAGVGYQW 60
LbR_YadA-like cd12820
YadA-like, left-handed beta-roll; This group contains the collagen-binding domain virulence ...
 180-250 4.62e-10

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: 56.73  E-value: 4.62e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1173391209 180 TGASAMGTNSIALDFHARAKDSDSLASGRLAHASGPRSTAIGAEANASGQNTVALGAGSIADRNNTVSVGR 250
Cdd:cd12820    49 YNNKASGENSTAFGYGNKASGENSSAFGSNNTASGNNSSAFGYNNTASGENSTAFGNNSKASGENSTALGN 119
auto_Ata NF033481
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an ...
 181-274 2.43e-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: 49.86  E-value: 2.43e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173391209  181 GASAMGTNSIALDFHARAKDSDSLASGRLAHASGPRSTAIGAEANASGQNTVALGAGSIADRNNTVSVGRHGDERQIVHV 260
Cdd:NF033481   616 GAKATGNSSAAIGSGAQATGDNSAAIGKGAEATNENAAAVGGGAKATGKNAAAIGGGAIADQENAVAVGQGAQSLVEGGV 695

                           90
                   ....*....|....*...
gi 1173391209  261 AAG----TQATDAVNVGQ 274
Cdd:NF033481   696 ALGarskVEAKNSVALGQ 713
auto_Ata NF033481
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an ...
 170-303 2.56e-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: 49.86  E-value: 2.56e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173391209  170 ATNVTINFNSTGASAMGTNSIALDFHARAKDSDSLASGRLAHASGPRSTAIGAEANASGQNTVALGAGSIA--------- 240
Cdd:NF033481   647 ATNENAAAVGGGAKATGKNAAAIGGGAIADQENAVAVGQGAQSLVEGGVALGARSKVEAKNSVALGQDAVAteatgtsfl 726

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1173391209  241 ------DRNNTVSVGRHGDERQIVHVAAGTQATDAVNVGQLNLAMSNANAYTN------QRIGDLQQSITDTARD 303
Cdd:NF033481   727 tnrdasQSNGVISVGSAGKERRITNVEDGSADSDAVTVRQLKNVDSRVNQNTSnigkntQNITNLNQKLDDTKTN 801
auto_Ata NF033481
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an ...
 158-375 6.04e-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: 6.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173391209  158 PSIPNATPTSGSATNVTINFNSTGASamGTNSIALDFHARAKDSDSLASGRLAHASGPRSTAIGAEANASGQNTVALGAG 237
Cdd:NF033481   215 PDIENADPVAGQAGAAYQPKMATKAT--GKDSIAFGGGAVATEENALAIGAFSESKGKKSVAIGTGAKAQKDNAVVIGDQ 292

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173391209  238 SIADRNNTVSVGRHGDERQIVHVAAGTQATDAVNVGQLNLAMSNA--------NAYTNQRIGDLQQSITDTARDAYSGVA 309
Cdd:NF033481   293 AEASFEGGVAIGKGARSEAENSIALGKDSKASQATGESFLTKQSAptgvlsigDIGTERRIQNVADGAADSDAATVRQLK 372

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1173391209  310 AATALTMIPDVDRDKRVSIGVGGAVYKGHRAVALGGTARINENLKVrAGVAMSAGGNAVGIGMSWQ 375
Cdd:NF033481   373 AARTHYVSINDNGQQGGNFENDGATGRNAIAVGVNASAAGREAMAI-GGSAQAIGSGAIAMGSSSQ 437
auto_Ata NF033481
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an ...
 160-291 6.14e-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: 6.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173391209  160 IPNATPTSGSATNVTINFNSTGASAMGTNSIALDFH-------------ARAKDSDSLASGRLAHASGPRSTAIGAEANA 226
Cdd:NF033481   568 MSNASGKGAAAFGAVAQATGDGASAMGINSLASGTNstaigsgnkpgegAKATGNSSAAIGSGAQATGDNSAAIGKGAEA 647

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1173391209  227 SGQNTVALGAGSIADRNNTVSVGRHGDERQIVHVAAGTQATDAVNVGQLNLAMSNANAYTNQRIG 291
Cdd:NF033481   648 TNENAAAVGGGAKATGKNAAAIGGGAIADQENAVAVGQGAQSLVEGGVALGARSKVEAKNSVALG 712
VOMP_auto_Cterm NF033870
Vomp family autotransporter C-terminal domain; The Vomp (variably expressed outer-membrane ...
 245-371 9.16e-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: 37.84  E-value: 9.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173391209 245 TVSVGRHGDERQIVHVAAG---TQATDAVNVGQL--------NLAMSNANAYTNQRIGD--------------------- 292
Cdd:NF033870  189 TLVGGDESEPVVIDNVADGkieKGSKEAVNGGQLhdyteeqmKIVLDDAKKYTDERIKNivvdaiddavaeaksytdmkf 268

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173391209 293 --LQQSITDTARDAYSGVAAATALTMIPDVDRDKRVSIGVGGAVYKGHRAVALgGTARINENLKVRAGVAMSAGGNAVGI 370
Cdd:NF033870  269 eaLNYSIEGVRKEARQAAAIGLAVSNLRYNDTPGKLSVAFGSGLWRSQSAFAF-GAGYTSEDGKIRSNLSATSSGGHWGI 347


                  .
gi 1173391209 371 G 371
Cdd:NF033870  348 G 348
 
Name Accession Description Interval E-value
BimA_second NF040983
trimeric autotransporter actin-nucleating factor BimA; This HMM describes BimA (Burkholderia ...
 1-376 0e+00

trimeric autotransporter actin-nucleating factor BimA; This HMM describes BimA (Burkholderia intracellular motility A), WP_004266405.1-like proteins in Burkholderia mallei or B. pseudomallei. The term BimA has also been used for WP_011205626.1-like homologs that have a very different N-terminal half.


Pssm-ID: 468913 [Multi-domain]  Cd Length: 382  Bit Score: 572.62  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173391209   1 MVLYIRMKYHRFPRSHAQQDTGRAASTVPFQRFAHLLCSSIAPLALGFSTDALAIGQAESTAFNAVIDQIKKGDFKLKPV 80
Cdd:NF040983    1 MVLYIRMKYHRFPRSHAQQDTGRAASTVPFQRFAHLLCSSIAPLALGFSTDALAIEQAESTAFNAVIDQIKKGDFKLKPV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173391209  81 GDRTLPNKVPPPPPP------PPPPPPPPPPSPPPPSPPPPSPPPPSPPPPSPPPPTTTPPTTTPPTTTTPTPSMHPIQP 154
Cdd:NF040983   81 GDRTLPNKVPPPPPPppppppPPPTPPPPPPPPPPPPPPSPPPPPPPSPPPSPPPPTTTPPTRTTPSTTTPTPSMHPIQP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173391209 155 TQLPSIPNATPTSGSATNVTINFNSTGASAMGTNSIALDFHARAKDSDSLASGRLAHASGPRSTAIGAEANASGQNTVAL 234
Cdd:NF040983  161 TQLPSIPNATPTSGSATNVTINFNSTGASAMGTNSIALDFHARAKDSDSLASGRLAHASGPRSTAIGAEANASGQNTVAL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173391209 235 GAGSIADRNNTVSVGRHGDERQIVHVAAGTQATDAVNVGQLNLAMSNANAYTNQRIGDLQQSITDTARDAYSGVAAATAL 314
Cdd:NF040983  241 GAGSIADRNNTVSVGRHGDERQIVHVAAGTQATDAVNVGQLNLAMSNANAYTNQRIGDLQQSITDTARDAYSGVAAATAL 320

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1173391209 315 TMIPDVDRDKRVSIGVGGAVYKGHRAVALGGTARINENLKVRAGVAMSAGGNAVGIGMSWQW 376
Cdd:NF040983  321 TMIPDVDRDKRVSIGVGGAVYKGHRAVALGGTARINENLKVRAGVAMSAGGNAVGIGMSWQW 382
BimA_first NF040984
trimeric autotransporter actin-nucleating factor BimA; BimA (B. pseudomallei intracellular ...
 117-376 5.21e-76

trimeric autotransporter actin-nucleating factor BimA; BimA (B. pseudomallei intracellular motility protein A) is a trimeric autotransporter, homologous in its C-terminal half to a number of trimeric autotransporter adhesins. It is a virulence factor that nucleates actin, so that actin polymerization can drive escape by B. pseudomallei out of one cell and into a neighboring cell. HMM NF040983 describes a homolog with similar activity but substantial difference in sequence architecture in the N-terminal region.


Pssm-ID: 468914 [Multi-domain]  Cd Length: 517  Bit Score: 244.01  E-value: 5.21e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173391209 117 PPPPSPPPPSPPPPTTTPPTTTPPTTTTPTPSMH-------------------------------------------PIQ 153
Cdd:NF040984  152 DANGDFSGRSAMPIEMAANAALRSLKKNPGDAGHaapaylpaerigqlrekvrrtiealesnrppkpqprstppqstPPK 231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173391209 154 PTQLPSIPN---------------------------ATPT------------------------------------SGSA 170
Cdd:NF040984  232 PTQHPTAPNpnapdastpdastppdastpdasapdaSAPSrpapapragtgapaasaatrapafanrvrkpnpampAASS 311

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173391209 171 TNVTINFNSTGASAMGTNSIALDFHARAKDSDSLASGRLAHASGPRSTAIGAEANASGQNTVALGAGSIADRNNTVSVGR 250
Cdd:NF040984  312 HAIASDFASSNAFAIGDDSTAVGAQAIAFSEQSIAIGSRAIAAGARSIAVGTDATAAAPDSVALGSGSIAEREGTVSVGR 391

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173391209 251 HGDERQIVHVAAGTQATDAVNVGQLNLAMSNANAYTNQRIGDLQQSITDTARDAYSGVAAATALTMIPDVDRDKRVSIGV 330
Cdd:NF040984  392 DGHERQITHVASGTEPTDAVNVTQLRAAMSNANAYTNQRIGDLQQSITDTARDAYSGVAAATALTMIPDVDRDKRVSIGV 471

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1173391209 331 GGAVYKGHRAVALGGTARINENLKVRAGVAMSAGGNAVGIGMSWQW 376
Cdd:NF040984  472 GGAVYKGHRAVALGGTARINENLKVRAGVAMSAGGNAVGIGMSWQW 517
Hia COG5295
Autotransporter adhesin [Intracellular trafficking, secretion, and vesicular transport, ...
 162-375 1.13e-20

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


Pssm-ID: 444098 [Multi-domain]  Cd Length: 785  Bit Score: 93.68  E-value: 1.13e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173391209 162 NATPTSGSATNVTINFNSTGASAMGTNSIALDFHARAKDSDSLASGRLAHASGPRSTAIGAEANASGQNTVALGAGSIAD 241
Cdd:COG5295   574 GSVASGANSVSVGAAGAENVAAGATDTDAVNGGGAVATGDNSVAVGNNAQASGANSVALGAGATATANNSVALGAGSVAD 653

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173391209 242 RNNTVSVGRHGDERQIVHVAAGTQATDAVNVGQLNlamsNANAYTNQRIGDLQQSITDTARDAYSGVAAATALTMIPDVD 321
Cdd:COG5295   654 RANTVSVGSAGAERQITNVAAGTADTDAVNVSQLK----AVNSSTDQRFNQLSNRINRVDKRARAGIASAMAMASLPQAY 729

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1173391209 322 RDKRVSIGVGGAVYKGHRAVALGGTARI-NENLKVRAGVAMSAGGN-AVGIGMSWQ 375
Cdd:COG5295   730 APGKSAVAAGVGTYRGQSAVAVGYSAVSdNGKWTVKLGGSANSQGNvGAGAGVGYQ 785
YadA_anchor pfam03895
YadA-like membrane anchor domain; This region represents the C-terminal 120 amino acids of a ...
 318-376 7.35e-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: 7.35e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173391209 318 PDVDRDKRVSIGVGGAVYKGHRAVALGGTARINENLKVRAGVA-MSAGGNAVGIGMSWQW 376
Cdd:pfam03895   1 PQPDRPGKFSVSVGVGTYKGESAVALGASARSNGNLVVKLGVSsSSGGSVGAGAGVGYQW 60
LbR_YadA-like cd12820
YadA-like, left-handed beta-roll; This group contains the collagen-binding domain virulence ...
 180-250 4.62e-10

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: 56.73  E-value: 4.62e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1173391209 180 TGASAMGTNSIALDFHARAKDSDSLASGRLAHASGPRSTAIGAEANASGQNTVALGAGSIADRNNTVSVGR 250
Cdd:cd12820    49 YNNKASGENSTAFGYGNKASGENSSAFGSNNTASGNNSSAFGYNNTASGENSTAFGNNSKASGENSTALGN 119
LbR_YadA-like cd12820
YadA-like, left-handed beta-roll; This group contains the collagen-binding domain virulence ...
 181-250 2.58e-09

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: 54.81  E-value: 2.58e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173391209 181 GASAMGTNSIALDFHARAKDSDSLASGRLAHASGPRSTAIGAEANASGQNTVALGAGSIADRNNTVSVGR 250
Cdd:cd12820     8 NNKASGENSTAFGYNNKASGDNSSAFGYGNKASGENSSAFGYNNKASGENSTAFGYGNKASGENSSAFGS 77
LbR_YadA-like cd12820
YadA-like, left-handed beta-roll; This group contains the collagen-binding domain virulence ...
 180-243 1.07e-08

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: 52.88  E-value: 1.07e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1173391209 180 TGASAMGTNSIALDFHARAKDSDSLASGRLAHASGPRSTAIGAEANASGQNTVALGAGSIADRN 243
Cdd:cd12820    63 YGNKASGENSSAFGSNNTASGNNSSAFGYNNTASGENSTAFGNNSKASGENSTALGNGNKASGN 126
YadA_stalk pfam05662
Coiled stalk of trimeric autotransporter adhesin; This short motif is found in invasins and ...
 256-291 2.03e-07

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: 46.80  E-value: 2.03e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1173391209 256 QIVHVAAGTQATDAVNVGQLNLAMSNANAYTNQRIG 291
Cdd:pfam05662   1 KITNVAAGTVSTDAVNGSQLYAVNQSVSNGANNVTS 36
LbR_YadA-like cd12820
YadA-like, left-handed beta-roll; This group contains the collagen-binding domain virulence ...
 181-249 2.91e-07

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: 49.03  E-value: 2.91e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1173391209 181 GASAMGTNSIALDFHARAKDSDSLASGRLAHASGPRSTAIGAEANASGQNTVALGAGSIADRNNTVSVG 249
Cdd:cd12820    22 NNKASGDNSSAFGYGNKASGENSSAFGYNNKASGENSTAFGYGNKASGENSSAFGSNNTASGNNSSAFG 90
auto_Ata NF033481
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an ...
 181-274 2.43e-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: 49.86  E-value: 2.43e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173391209  181 GASAMGTNSIALDFHARAKDSDSLASGRLAHASGPRSTAIGAEANASGQNTVALGAGSIADRNNTVSVGRHGDERQIVHV 260
Cdd:NF033481   616 GAKATGNSSAAIGSGAQATGDNSAAIGKGAEATNENAAAVGGGAKATGKNAAAIGGGAIADQENAVAVGQGAQSLVEGGV 695

                           90
                   ....*....|....*...
gi 1173391209  261 AAG----TQATDAVNVGQ 274
Cdd:NF033481   696 ALGarskVEAKNSVALGQ 713
auto_Ata NF033481
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an ...
 170-303 2.56e-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: 49.86  E-value: 2.56e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173391209  170 ATNVTINFNSTGASAMGTNSIALDFHARAKDSDSLASGRLAHASGPRSTAIGAEANASGQNTVALGAGSIA--------- 240
Cdd:NF033481   647 ATNENAAAVGGGAKATGKNAAAIGGGAIADQENAVAVGQGAQSLVEGGVALGARSKVEAKNSVALGQDAVAteatgtsfl 726

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1173391209  241 ------DRNNTVSVGRHGDERQIVHVAAGTQATDAVNVGQLNLAMSNANAYTN------QRIGDLQQSITDTARD 303
Cdd:NF033481   727 tnrdasQSNGVISVGSAGKERRITNVEDGSADSDAVTVRQLKNVDSRVNQNTSnigkntQNITNLNQKLDDTKTN 801
YadA_head pfam05658
YadA head domain repeat (2 copies); This entry represents two copies of a fourteen residue ...
 212-238 5.12e-04

YadA head domain repeat (2 copies); This entry represents two copies of a fourteen residue repeat that makes up the head domain of bacterial haemagglutinins and invasins.


Pssm-ID: 461707 [Multi-domain]  Cd Length: 27  Bit Score: 36.84  E-value: 5.12e-04
                          10        20
                  ....*....|....*....|....*..
gi 1173391209 212 ASGPRSTAIGAEANASGQNTVALGAGS 238
Cdd:pfam05658   1 ASGTNSTAIGTNATASGDNSVAIGANA 27
auto_Ata NF033481
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an ...
 158-375 6.04e-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: 6.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173391209  158 PSIPNATPTSGSATNVTINFNSTGASamGTNSIALDFHARAKDSDSLASGRLAHASGPRSTAIGAEANASGQNTVALGAG 237
Cdd:NF033481   215 PDIENADPVAGQAGAAYQPKMATKAT--GKDSIAFGGGAVATEENALAIGAFSESKGKKSVAIGTGAKAQKDNAVVIGDQ 292

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173391209  238 SIADRNNTVSVGRHGDERQIVHVAAGTQATDAVNVGQLNLAMSNA--------NAYTNQRIGDLQQSITDTARDAYSGVA 309
Cdd:NF033481   293 AEASFEGGVAIGKGARSEAENSIALGKDSKASQATGESFLTKQSAptgvlsigDIGTERRIQNVADGAADSDAATVRQLK 372

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1173391209  310 AATALTMIPDVDRDKRVSIGVGGAVYKGHRAVALGGTARINENLKVrAGVAMSAGGNAVGIGMSWQ 375
Cdd:NF033481   373 AARTHYVSINDNGQQGGNFENDGATGRNAIAVGVNASAAGREAMAI-GGSAQAIGSGAIAMGSSSQ 437
auto_Ata NF033481
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an ...
 160-291 6.14e-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: 6.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173391209  160 IPNATPTSGSATNVTINFNSTGASAMGTNSIALDFH-------------ARAKDSDSLASGRLAHASGPRSTAIGAEANA 226
Cdd:NF033481   568 MSNASGKGAAAFGAVAQATGDGASAMGINSLASGTNstaigsgnkpgegAKATGNSSAAIGSGAQATGDNSAAIGKGAEA 647

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1173391209  227 SGQNTVALGAGSIADRNNTVSVGRHGDERQIVHVAAGTQATDAVNVGQLNLAMSNANAYTNQRIG 291
Cdd:NF033481   648 TNENAAAVGGGAKATGKNAAAIGGGAIADQENAVAVGQGAQSLVEGGVALGARSKVEAKNSVALG 712
VOMP_auto_Cterm NF033870
Vomp family autotransporter C-terminal domain; The Vomp (variably expressed outer-membrane ...
 245-371 9.16e-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: 37.84  E-value: 9.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173391209 245 TVSVGRHGDERQIVHVAAG---TQATDAVNVGQL--------NLAMSNANAYTNQRIGD--------------------- 292
Cdd:NF033870  189 TLVGGDESEPVVIDNVADGkieKGSKEAVNGGQLhdyteeqmKIVLDDAKKYTDERIKNivvdaiddavaeaksytdmkf 268

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173391209 293 --LQQSITDTARDAYSGVAAATALTMIPDVDRDKRVSIGVGGAVYKGHRAVALgGTARINENLKVRAGVAMSAGGNAVGI 370
Cdd:NF033870  269 eaLNYSIEGVRKEARQAAAIGLAVSNLRYNDTPGKLSVAFGSGLWRSQSAFAF-GAGYTSEDGKIRSNLSATSSGGHWGI 347


                  .
gi 1173391209 371 G 371
Cdd:NF033870  348 G 348
 
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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