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Conserved domains on  [gi|880898064|ref|WP_048669907|]
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SpaA isopeptide-forming pilin-related protein, partial [Enterococcus sp. 255_ESPC]

Protein Classification

collagen binding domain-containing protein( domain architecture ID 1004465)

collagen binding domain-containing protein is a surface anchored protein that may function as an adhesin

Gene Ontology:  GO:0005518
PubMed:  16362049|9334749

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ClfA COG4932
Clumping factor A-related surface protein, MSCRAMM (microbial surface components recognizing ...
 339-568 2.71e-38

Clumping factor A-related surface protein, MSCRAMM (microbial surface components recognizing adhesive matrix molecules) family, DEv-IgG fold [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 443959 [Multi-domain]  Cd Length: 689  Bit Score: 150.51  E-value: 2.71e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880898064 339 RGGVVLEKIDAVTAKVLEGAVFKVVNTKTQQVVQETLT-TNQAGQIRLAGLEAGQYAFIETKAPTGYKLDATPVPFEIKL 417
Cdd:COG4932  261 KGSVTVTKTDADTGEPLAGATFTLTDADGNTVVTTTVTvTDADGSYTFTDLPPGTYTVTETKAPAGYDLDGEAVKVTITA 340

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880898064 418 EQTQTIRLKKE-NTRLENQLKVEKVDENNEVKRLAGAEFSLYDQKNNLIEKGVTNENGELLFSNLSPdGEYYLVETKAPN 496
Cdd:COG4932  341 GQTTTVTVTNGnNEVKTGSVTLTKVDADDGEAPLAGAEFTLTDADGTVVATITTDADGTASFKGLAP-GTYTLTETKAPE 419

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 880898064 497 GYELDETKHPISFAGKADyTLTYRVKNKqqVQIGSIKIVKQDkeskKRLTGAEFQWKDTvTGKTGIVTVGTD 568
Cdd:COG4932  420 GYTLDSTPITVTVTDGGT-GAIDTITNE--RKKGSVQVTKVD----APLAGATFTLTDA-DGTVVTLTTDAD 483
SpaA pfam17802
Prealbumin-like fold domain; This entry contains a prealbumin-like domain from a wide variety ...
 540-603 1.91e-11

Prealbumin-like fold domain; This entry contains a prealbumin-like domain from a wide variety of bacterial surface proteins. This entry corresponds to domain 1 and domain 3 of SpaA from Corynebacterium diphtheriae. Some members of this family contain an isopeptide bond.


:

Pssm-ID: 465513 [Multi-domain]  Cd Length: 72  Bit Score: 59.91  E-value: 1.91e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 880898064  540 ESKKRLTGAEFQWKD----TVTGKTGIVTVGTDGMVTIPNLAVNrTYELTETKAPAGYVLDKTVHKVT 603
Cdd:pfam17802   1 DTGKPLAGAEFTLYDadgtVDGKVVGTLTTDEDGKATFDGLPPG-TYTLKETKAPDGYVLDDTPIEFT 67
 
Name Accession Description Interval E-value
ClfA COG4932
Clumping factor A-related surface protein, MSCRAMM (microbial surface components recognizing ...
 339-568 2.71e-38

Clumping factor A-related surface protein, MSCRAMM (microbial surface components recognizing adhesive matrix molecules) family, DEv-IgG fold [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443959 [Multi-domain]  Cd Length: 689  Bit Score: 150.51  E-value: 2.71e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880898064 339 RGGVVLEKIDAVTAKVLEGAVFKVVNTKTQQVVQETLT-TNQAGQIRLAGLEAGQYAFIETKAPTGYKLDATPVPFEIKL 417
Cdd:COG4932  261 KGSVTVTKTDADTGEPLAGATFTLTDADGNTVVTTTVTvTDADGSYTFTDLPPGTYTVTETKAPAGYDLDGEAVKVTITA 340

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880898064 418 EQTQTIRLKKE-NTRLENQLKVEKVDENNEVKRLAGAEFSLYDQKNNLIEKGVTNENGELLFSNLSPdGEYYLVETKAPN 496
Cdd:COG4932  341 GQTTTVTVTNGnNEVKTGSVTLTKVDADDGEAPLAGAEFTLTDADGTVVATITTDADGTASFKGLAP-GTYTLTETKAPE 419

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 880898064 497 GYELDETKHPISFAGKADyTLTYRVKNKqqVQIGSIKIVKQDkeskKRLTGAEFQWKDTvTGKTGIVTVGTD 568
Cdd:COG4932  420 GYTLDSTPITVTVTDGGT-GAIDTITNE--RKKGSVQVTKVD----APLAGATFTLTDA-DGTVVTLTTDAD 483
SpaA pfam17802
Prealbumin-like fold domain; This entry contains a prealbumin-like domain from a wide variety ...
 448-507 9.62e-16

Prealbumin-like fold domain; This entry contains a prealbumin-like domain from a wide variety of bacterial surface proteins. This entry corresponds to domain 1 and domain 3 of SpaA from Corynebacterium diphtheriae. Some members of this family contain an isopeptide bond.


Pssm-ID: 465513 [Multi-domain]  Cd Length: 72  Bit Score: 71.85  E-value: 9.62e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 880898064  448 KRLAGAEFSLYD----QKNNLIEKGVTNENGELLFSNLSPdGEYYLVETKAPNGYELDETKHPI 507
Cdd:pfam17802   4 KPLAGAEFTLYDadgtVDGKVVGTLTTDEDGKATFDGLPP-GTYTLKETKAPDGYVLDDTPIEF 66
SpaA pfam17802
Prealbumin-like fold domain; This entry contains a prealbumin-like domain from a wide variety ...
 540-603 1.91e-11

Prealbumin-like fold domain; This entry contains a prealbumin-like domain from a wide variety of bacterial surface proteins. This entry corresponds to domain 1 and domain 3 of SpaA from Corynebacterium diphtheriae. Some members of this family contain an isopeptide bond.


Pssm-ID: 465513 [Multi-domain]  Cd Length: 72  Bit Score: 59.91  E-value: 1.91e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 880898064  540 ESKKRLTGAEFQWKD----TVTGKTGIVTVGTDGMVTIPNLAVNrTYELTETKAPAGYVLDKTVHKVT 603
Cdd:pfam17802   1 DTGKPLAGAEFTLYDadgtVDGKVVGTLTTDEDGKATFDGLPPG-TYTLKETKAPDGYVLDDTPIEFT 67
iso_D2_wall_anc NF033902
SpaH/EbpB family LPXTG-anchored major pilin; Members of this family are pilin major subunits ...
 435-534 2.70e-08

SpaH/EbpB family LPXTG-anchored major pilin; Members of this family are pilin major subunits whose structure includes an LPXTG motif-containing signal (see TIGR01167) near the C-terminus, for processing by sortases. Most contain a recognizable D2-type fimbrial isopeptide formation domain (see TIGR04226), in which Lys-to-Asn isopeptide bond formation provides additional structural integrity to support adhesion despite shear. For proper members of this subfamily, lengths fall typically in the range of 460 to 640 amino acids in length. Many members of this family contribute to the virulence of certain Gram-positive pathogens, including SpaA, SpaD, and SpaH from Corynebacterium diphtheriae, and EbpB and EbpC from Enterococcus faecalis.


Pssm-ID: 468234 [Multi-domain]  Cd Length: 533  Bit Score: 56.69  E-value: 2.70e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880898064 435 QLKVEKVDENNEVKRLAGAEFSLY------------DQKNNLIEKGVTNENGELLFSNLSPDG-------------EYYL 489
Cdd:NF033902 373 KLKIKKVDADDTSKKLKGAEFKVYaceadaaaacvnAIGINGKTTFTTGADGTVSIDGLHVTDledgasvkaaagkDYCL 452

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 880898064 490 VETKAPNGYELDETKHP-ISFAGKADYTLTYRVKNKQQVQIGSIKI 534
Cdd:NF033902 453 VETKAPAGYVLPPKPVEvTVVKVTVTAATTADVKNTVVNNKKTVPN 498
iso_D2_wall_anc NF033902
SpaH/EbpB family LPXTG-anchored major pilin; Members of this family are pilin major subunits ...
 522-603 5.23e-08

SpaH/EbpB family LPXTG-anchored major pilin; Members of this family are pilin major subunits whose structure includes an LPXTG motif-containing signal (see TIGR01167) near the C-terminus, for processing by sortases. Most contain a recognizable D2-type fimbrial isopeptide formation domain (see TIGR04226), in which Lys-to-Asn isopeptide bond formation provides additional structural integrity to support adhesion despite shear. For proper members of this subfamily, lengths fall typically in the range of 460 to 640 amino acids in length. Many members of this family contribute to the virulence of certain Gram-positive pathogens, including SpaA, SpaD, and SpaH from Corynebacterium diphtheriae, and EbpB and EbpC from Enterococcus faecalis.


Pssm-ID: 468234 [Multi-domain]  Cd Length: 533  Bit Score: 55.92  E-value: 5.23e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880898064 522 KNKQQVQIGSIKIVKQDKE-SKKRLTGAEFQ------------WKDTVTGKTGIVTVGTDGMVTIPNLAVN--------- 579
Cdd:NF033902 364 TPTVKTYFGKLKIKKVDADdTSKKLKGAEFKvyaceadaaaacVNAIGINGKTTFTTGADGTVSIDGLHVTdledgasvk 443

                         90       100
                 ....*....|....*....|....*...
gi 880898064 580 ----RTYELTETKAPAGYVLDKTVHKVT 603
Cdd:NF033902 444 aaagKDYCLVETKAPAGYVLPPKPVEVT 471
pilus_ancill_1 NF033396
pilus ancillary protein 1;
320-540 4.34e-04

pilus ancillary protein 1;


Pssm-ID: 380246 [Multi-domain]  Cd Length: 737  Bit Score: 43.34  E-value: 4.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880898064 320 WEDDDIAYITADESSDGTGRGGvvleKIDAVTAKVLEGAVFKVVNTKTQQVVQETLTTNQagqiRLAGLEAGQYAFiETK 399
Cdd:NF033396 171 WYYSDSSQINPDELFKSEAKSN----KINDQQLGLMREALSELIDPNLGEKYSNKTPSGY----RLNIFESHDKSF-QNL 241

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880898064 400 APTGYKLDATPVPFE---IKLEQTQTIrlkkentrlenqlkVEKVDENNEVKRLAGAEFSLYDQKNNLIEKGV--TNENG 474
Cdd:NF033396 242 LSAEYVPDTPPKPGEeppAKTEKTSVI--------------IRKYAEGDYSKLLEGATLKLTQIEGSGFQEKIfqSNSSG 307

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 880898064 475 ELLfsnLSPDGEYYLVETKAPNGYELDEtkhPISFagkadytltyRVKNKQQ--VQIGSIKIVKQDKE 540
Cdd:NF033396 308 ETV---ELPNGTYTLTETKSPDGYKIAE---PIKF----------RVKNGKVfiVQKDGSQVENPNKE 359
 
Name Accession Description Interval E-value
ClfA COG4932
Clumping factor A-related surface protein, MSCRAMM (microbial surface components recognizing ...
 339-568 2.71e-38

Clumping factor A-related surface protein, MSCRAMM (microbial surface components recognizing adhesive matrix molecules) family, DEv-IgG fold [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443959 [Multi-domain]  Cd Length: 689  Bit Score: 150.51  E-value: 2.71e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880898064 339 RGGVVLEKIDAVTAKVLEGAVFKVVNTKTQQVVQETLT-TNQAGQIRLAGLEAGQYAFIETKAPTGYKLDATPVPFEIKL 417
Cdd:COG4932  261 KGSVTVTKTDADTGEPLAGATFTLTDADGNTVVTTTVTvTDADGSYTFTDLPPGTYTVTETKAPAGYDLDGEAVKVTITA 340

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880898064 418 EQTQTIRLKKE-NTRLENQLKVEKVDENNEVKRLAGAEFSLYDQKNNLIEKGVTNENGELLFSNLSPdGEYYLVETKAPN 496
Cdd:COG4932  341 GQTTTVTVTNGnNEVKTGSVTLTKVDADDGEAPLAGAEFTLTDADGTVVATITTDADGTASFKGLAP-GTYTLTETKAPE 419

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 880898064 497 GYELDETKHPISFAGKADyTLTYRVKNKqqVQIGSIKIVKQDkeskKRLTGAEFQWKDTvTGKTGIVTVGTD 568
Cdd:COG4932  420 GYTLDSTPITVTVTDGGT-GAIDTITNE--RKKGSVQVTKVD----APLAGATFTLTDA-DGTVVTLTTDAD 483
ClfA COG4932
Clumping factor A-related surface protein, MSCRAMM (microbial surface components recognizing ...
 271-603 3.17e-29

Clumping factor A-related surface protein, MSCRAMM (microbial surface components recognizing adhesive matrix molecules) family, DEv-IgG fold [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443959 [Multi-domain]  Cd Length: 689  Bit Score: 123.16  E-value: 3.17e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880898064 271 GIPTATGSYLSNKNAYYIYLETIPNENIPSDAVLSNYTYMRISSEGFDAWEDDDIAYITADESSDGTGrggvvleKIDAV 350
Cdd:COG4932    7 AGTGVGTVIVEGAGSGSLVAVTTGAVLGLALGSTGGTAGSAAAINSAPATGTATGTSAGATAVIVIAA-------GLTAT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880898064 351 TAKVLEGAVFKVVNTKTQQVVQETLTTNQAGQIRLAGLEAGQYAFIETKAPTGYKLDATPVPFEIKLEQTQTIRL-KKEN 429
Cdd:COG4932   80 PTETASGLGGDATVTTTANVAKVTNGAAANLTVNADGTASNAGTLAKGAETATGNLDGDAGDVTVTAAATDGVNDvDGNG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880898064 430 TRLENQLKVEKVDENNEVKRLAGAEFSLYDQKNNLIEKGVTNENGELLFSNLsPDGEYYLVETKAPNGYELDETKHPISF 509
Cdd:COG4932  160 ASVTDSVTLKKVDDGDTGKPLPGATFTLYDSDGTLVKTVTTDADGKYTFTDL-PPGTYTLTETKAPEGYVLDTKDPTGAT 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880898064 510 AG---KADYTLTYRVKNKQQVQIGSIKIVKQDKESKKRLTGAEFQWKD---TVTGKTGIVTVGTDGMVTIPNLAVNrTYE 583
Cdd:COG4932  239 ITvtvNAGGTVTVTLKNTPKYTKGSVTVTKTDADTGEPLAGATFTLTDadgNTVVTTTVTVTDADGSYTFTDLPPG-TYT 317

                        330       340
                 ....*....|....*....|
gi 880898064 584 LTETKAPAGYVLDKTVHKVT 603
Cdd:COG4932  318 VTETKAPAGYDLDGEAVKVT 337
SpaA pfam17802
Prealbumin-like fold domain; This entry contains a prealbumin-like domain from a wide variety ...
 448-507 9.62e-16

Prealbumin-like fold domain; This entry contains a prealbumin-like domain from a wide variety of bacterial surface proteins. This entry corresponds to domain 1 and domain 3 of SpaA from Corynebacterium diphtheriae. Some members of this family contain an isopeptide bond.


Pssm-ID: 465513 [Multi-domain]  Cd Length: 72  Bit Score: 71.85  E-value: 9.62e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 880898064  448 KRLAGAEFSLYD----QKNNLIEKGVTNENGELLFSNLSPdGEYYLVETKAPNGYELDETKHPI 507
Cdd:pfam17802   4 KPLAGAEFTLYDadgtVDGKVVGTLTTDEDGKATFDGLPP-GTYTLKETKAPDGYVLDDTPIEF 66
SpaA pfam17802
Prealbumin-like fold domain; This entry contains a prealbumin-like domain from a wide variety ...
 350-416 5.09e-14

Prealbumin-like fold domain; This entry contains a prealbumin-like domain from a wide variety of bacterial surface proteins. This entry corresponds to domain 1 and domain 3 of SpaA from Corynebacterium diphtheriae. Some members of this family contain an isopeptide bond.


Pssm-ID: 465513 [Multi-domain]  Cd Length: 72  Bit Score: 67.23  E-value: 5.09e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 880898064  350 VTAKVLEGAVFKV--VNTKTQQVVQETLTTNQAGQIRLAGLEAGQYAFIETKAPTGYKLDATPVPFEIK 416
Cdd:pfam17802   1 DTGKPLAGAEFTLydADGTVDGKVVGTLTTDEDGKATFDGLPPGTYTLKETKAPDGYVLDDTPIEFTVT 69
SpaA pfam17802
Prealbumin-like fold domain; This entry contains a prealbumin-like domain from a wide variety ...
 540-603 1.91e-11

Prealbumin-like fold domain; This entry contains a prealbumin-like domain from a wide variety of bacterial surface proteins. This entry corresponds to domain 1 and domain 3 of SpaA from Corynebacterium diphtheriae. Some members of this family contain an isopeptide bond.


Pssm-ID: 465513 [Multi-domain]  Cd Length: 72  Bit Score: 59.91  E-value: 1.91e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 880898064  540 ESKKRLTGAEFQWKD----TVTGKTGIVTVGTDGMVTIPNLAVNrTYELTETKAPAGYVLDKTVHKVT 603
Cdd:pfam17802   1 DTGKPLAGAEFTLYDadgtVDGKVVGTLTTDEDGKATFDGLPPG-TYTLKETKAPDGYVLDDTPIEFT 67
iso_D2_wall_anc NF033902
SpaH/EbpB family LPXTG-anchored major pilin; Members of this family are pilin major subunits ...
 435-534 2.70e-08

SpaH/EbpB family LPXTG-anchored major pilin; Members of this family are pilin major subunits whose structure includes an LPXTG motif-containing signal (see TIGR01167) near the C-terminus, for processing by sortases. Most contain a recognizable D2-type fimbrial isopeptide formation domain (see TIGR04226), in which Lys-to-Asn isopeptide bond formation provides additional structural integrity to support adhesion despite shear. For proper members of this subfamily, lengths fall typically in the range of 460 to 640 amino acids in length. Many members of this family contribute to the virulence of certain Gram-positive pathogens, including SpaA, SpaD, and SpaH from Corynebacterium diphtheriae, and EbpB and EbpC from Enterococcus faecalis.


Pssm-ID: 468234 [Multi-domain]  Cd Length: 533  Bit Score: 56.69  E-value: 2.70e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880898064 435 QLKVEKVDENNEVKRLAGAEFSLY------------DQKNNLIEKGVTNENGELLFSNLSPDG-------------EYYL 489
Cdd:NF033902 373 KLKIKKVDADDTSKKLKGAEFKVYaceadaaaacvnAIGINGKTTFTTGADGTVSIDGLHVTDledgasvkaaagkDYCL 452

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 880898064 490 VETKAPNGYELDETKHP-ISFAGKADYTLTYRVKNKQQVQIGSIKI 534
Cdd:NF033902 453 VETKAPAGYVLPPKPVEvTVVKVTVTAATTADVKNTVVNNKKTVPN 498
iso_D2_wall_anc NF033902
SpaH/EbpB family LPXTG-anchored major pilin; Members of this family are pilin major subunits ...
 522-603 5.23e-08

SpaH/EbpB family LPXTG-anchored major pilin; Members of this family are pilin major subunits whose structure includes an LPXTG motif-containing signal (see TIGR01167) near the C-terminus, for processing by sortases. Most contain a recognizable D2-type fimbrial isopeptide formation domain (see TIGR04226), in which Lys-to-Asn isopeptide bond formation provides additional structural integrity to support adhesion despite shear. For proper members of this subfamily, lengths fall typically in the range of 460 to 640 amino acids in length. Many members of this family contribute to the virulence of certain Gram-positive pathogens, including SpaA, SpaD, and SpaH from Corynebacterium diphtheriae, and EbpB and EbpC from Enterococcus faecalis.


Pssm-ID: 468234 [Multi-domain]  Cd Length: 533  Bit Score: 55.92  E-value: 5.23e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880898064 522 KNKQQVQIGSIKIVKQDKE-SKKRLTGAEFQ------------WKDTVTGKTGIVTVGTDGMVTIPNLAVN--------- 579
Cdd:NF033902 364 TPTVKTYFGKLKIKKVDADdTSKKLKGAEFKvyaceadaaaacVNAIGINGKTTFTTGADGTVSIDGLHVTdledgasvk 443

                         90       100
                 ....*....|....*....|....*...
gi 880898064 580 ----RTYELTETKAPAGYVLDKTVHKVT 603
Cdd:NF033902 444 aaagKDYCLVETKAPAGYVLPPKPVEVT 471
SdrD_B pfam17210
SdrD B-like domain; This family corresponds to the B-like domain from the SdrD protein. This ...
 451-499 7.02e-05

SdrD B-like domain; This family corresponds to the B-like domain from the SdrD protein. This domain has three calcium binding sites within a greek key beta sandwich fold.


Pssm-ID: 435789 [Multi-domain]  Cd Length: 112  Bit Score: 42.20  E-value: 7.02e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 880898064  451 AGAEFSLYDQKNNLIEKGVTNENGELLFSNLSPdGEYYlVETKAPNGYE 499
Cdd:pfam17210  25 SGVTVTLYDANGTVVGTTTTDANGKYLFTNLAP-GTYY-VEFTAPAGYT 71
pilus_ancill_1 NF033396
pilus ancillary protein 1;
320-540 4.34e-04

pilus ancillary protein 1;


Pssm-ID: 380246 [Multi-domain]  Cd Length: 737  Bit Score: 43.34  E-value: 4.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880898064 320 WEDDDIAYITADESSDGTGRGGvvleKIDAVTAKVLEGAVFKVVNTKTQQVVQETLTTNQagqiRLAGLEAGQYAFiETK 399
Cdd:NF033396 171 WYYSDSSQINPDELFKSEAKSN----KINDQQLGLMREALSELIDPNLGEKYSNKTPSGY----RLNIFESHDKSF-QNL 241

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880898064 400 APTGYKLDATPVPFE---IKLEQTQTIrlkkentrlenqlkVEKVDENNEVKRLAGAEFSLYDQKNNLIEKGV--TNENG 474
Cdd:NF033396 242 LSAEYVPDTPPKPGEeppAKTEKTSVI--------------IRKYAEGDYSKLLEGATLKLTQIEGSGFQEKIfqSNSSG 307

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 880898064 475 ELLfsnLSPDGEYYLVETKAPNGYELDEtkhPISFagkadytltyRVKNKQQ--VQIGSIKIVKQDKE 540
Cdd:NF033396 308 ETV---ELPNGTYTLTETKSPDGYKIAE---PIKF----------RVKNGKVfiVQKDGSQVENPNKE 359
 
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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