NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1192940763|gb|OTP17876|]
View 

hypothetical protein A5825_002800 [Enterococcus gallinarum]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Cna_B pfam05738
Cna protein B-type domain; This domain is found in Staphylococcus aureus collagen-binding ...
 1491-1573 9.32e-30

Cna protein B-type domain; This domain is found in Staphylococcus aureus collagen-binding surface protein. The structure of the repetitive B-region has been solved and forms a beta sandwich structure.


:

Pssm-ID: 461726 [Multi-domain]  Cd Length: 88  Bit Score: 113.88  E-value: 9.32e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192940763 1491 ISGTKTWEDNDNQDGKRPKAITVRLLADGKEV-DSKEVTAETNWTYEFTGLDKY-KSGNEIRYTIQEVSVPEYSSEVEE- 1567
Cdd:pfam05738    1 VSVTKVWDDNNNQDGIRPESITVQLLANGQKVgVTKELTAANNWTYTFTDLPKYdENGKEITYTVEEDAVPGYTTTVDAk 80


                   ....*...
gi 1192940763 1568 --FDVTNT 1573
Cdd:pfam05738   81 dgFTITNT 88
Cna_B pfam05738
Cna protein B-type domain; This domain is found in Staphylococcus aureus collagen-binding ...
 1677-1759 1.05e-28

Cna protein B-type domain; This domain is found in Staphylococcus aureus collagen-binding surface protein. The structure of the repetitive B-region has been solved and forms a beta sandwich structure.


:

Pssm-ID: 461726 [Multi-domain]  Cd Length: 88  Bit Score: 111.18  E-value: 1.05e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192940763 1677 ISGTKIWDDNDNQDGKRPDVITVHLLK-GTEVVKTVKVTADNDWKYEFKNMPKF-ENGEKIQYSVAEDKVEDYSSSI--- 1751
Cdd:pfam05738    1 VSVTKVWDDNNNQDGIRPESITVQLLAnGQKVGVTKELTAANNWTYTFTDLPKYdENGKEITYTVEEDAVPGYTTTVdak 80


                   ....*...
gi 1192940763 1752 KGFDITNS 1759
Cdd:pfam05738   81 DGFTITNT 88
Cna_B pfam05738
Cna protein B-type domain; This domain is found in Staphylococcus aureus collagen-binding ...
 1394-1483 1.46e-26

Cna protein B-type domain; This domain is found in Staphylococcus aureus collagen-binding surface protein. The structure of the repetitive B-region has been solved and forms a beta sandwich structure.


:

Pssm-ID: 461726 [Multi-domain]  Cd Length: 88  Bit Score: 105.02  E-value: 1.46e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192940763 1394 VSVKKAWDDKDNQDGVRPESIKVQLYAGDKKVGEEVELNAANEWTTTWKDLDLKDK-GQTIDYTVKEVGETnGYKVEVtg 1472
Cdd:pfam05738    1 VSVTKVWDDNNNQDGIRPESITVQLLANGQKVGVTKELTAANNWTYTFTDLPKYDEnGKEITYTVEEDAVP-GYTTTV-- 77

                           90
                   ....*....|.
gi 1192940763 1473 NAKDGYTLTNS 1483
Cdd:pfam05738   78 DAKDGFTITNT 88
Cna_B pfam05738
Cna protein B-type domain; This domain is found in Staphylococcus aureus collagen-binding ...
 1581-1669 2.88e-26

Cna protein B-type domain; This domain is found in Staphylococcus aureus collagen-binding surface protein. The structure of the repetitive B-region has been solved and forms a beta sandwich structure.


:

Pssm-ID: 461726 [Multi-domain]  Cd Length: 88  Bit Score: 103.87  E-value: 2.88e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192940763 1581 VNVVKAWDDADNQDGVRPDQIKVVLVADGVVTDQVKTLNAANHWQASFADLDEY-KAGKKVTYEVQELAVEGYESVIsgD 1659
Cdd:pfam05738    1 VSVTKVWDDNNNQDGIRPESITVQLLANGQKVGVTKELTAANNWTYTFTDLPKYdENGKEITYTVEEDAVPGYTTTV--D 78

                           90
                   ....*....|
gi 1192940763 1660 ASKGFVITNS 1669
Cdd:pfam05738   79 AKDGFTITNT 88
Cna_B pfam05738
Cna protein B-type domain; This domain is found in Staphylococcus aureus collagen-binding ...
 1767-1843 2.23e-24

Cna protein B-type domain; This domain is found in Staphylococcus aureus collagen-binding surface protein. The structure of the repetitive B-region has been solved and forms a beta sandwich structure.


:

Pssm-ID: 461726 [Multi-domain]  Cd Length: 88  Bit Score: 98.47  E-value: 2.23e-24
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1192940763 1767 VNVTKVWKDDDDKTGVRPDSITFKLLADGKETGKTLKLSAKSNWQGSFEDLDVYN-NGEEINYTIEELQVKGYVSNIQ 1843
Cdd:pfam05738    1 VSVTKVWDDNNNQDGIRPESITVQLLANGQKVGVTKELTAANNWTYTFTDLPKYDeNGKEITYTVEEDAVPGYTTTVD 78
CollagenBindB cd00222
Repeat unit of collagen-binding protein domain B; The collagen-binding protein mediates ...
 1293-1387 5.44e-24

Repeat unit of collagen-binding protein domain B; The collagen-binding protein mediates bacterial adherence to collagen; the primary sequence has a non-repetitive, collagen-binding A region, followed by instances of this B region repetitive unit. The B region has one to four 23 kDa repeat units (B1-B4), which have been suggested to serve as 'stalks' that project the A region from the bacterial surface and thus facilitate bacterial adherence to collagen. Each B repeat unit has two highly similar domains (D1 and D2) placed side-by-side; both D1 and D2 are included in this model. They exhibit a unique inverse IgG-like domain fold.


:

Pssm-ID: 212461 [Multi-domain]  Cd Length: 92  Bit Score: 97.75  E-value: 5.44e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192940763 1293 VDIPIEKVWNDKDNQDGIRPVKVTVELHADGKASGKTVELNTENDWKASFKKLRKTDaSTKEEIKYTVKEVDPDkNYKSD 1372
Cdd:cd00222      1 TDITVTKTWDDDDNQDGKRPESITVQLLANGKETGDTVTLTASNDWTYTFTNLPKYD-ENGKEITYTVKEVPVP-GYTTT 78

                           90
                   ....*....|....*
gi 1192940763 1373 VTGTMtGGFKITNSY 1387
Cdd:cd00222     79 VTGDD-GGFTITNTH 92
ClfA COG4932
Clumping factor A-related surface protein, MSCRAMM (microbial surface components recognizing ...
 1056-1524 7.16e-16

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: 83.48  E-value: 7.16e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192940763 1056 TEESTKVVVSIGTGEGSKSSVNIVKVDADdNKTPLKGAELELwsVDKDGKKQQIVRSGVTNKKGELKFGNLRATNYLLVE 1135
Cdd:COG4932    244 NAGGTVTVTLKNTPKYTKGSVTVTKTDAD-TGEPLAGATFTL--TDADGNTVVTTTVTVTDADGSYTFTDLPPGTYTVTE 320

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192940763 1136 TKAPAGYTISDELKngkKIKLEADKEGQ-EVATLKIENAVPEISFNKVDI--KGKALAGAVFAIKNEDsryynglkadkt 1212
Cdd:COG4932    321 TKAPAGYDLDGEAV---KVTITAGQTTTvTVTNGNNEVKTGSVTLTKVDAddGEAPLAGAEFTLTDAD------------ 385

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192940763 1213 vkwaergeisADTKTALTSDENGKVTVKGLPVGEYQLVELSAPDGYEKSDKTIDFEVV-NKDGQIKLKDAIADVENEATQ 1291
Cdd:COG4932    386 ----------GTVVATITTDADGTASFKGLAPGTYTLTETKAPEGYTLDSTPITVTVTdGGTGAIDTITNERKKGSVQVT 455

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192940763 1292 FVDIPIEKVWNDKDNQDGIRPVKVTVELHADGK-ASGKTVELNTENDWKASFKKLRKTDASTKEEIKYTVKEVDPDKNYK 1370
Cdd:COG4932    456 KVDAPLAGATFTLTDADGTVVTLTTDADLAGATfEADGKVVTTTDASGKYTFKNLPPGTYTDAGGSATVITDDTDGTVGD 535

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192940763 1371 SDVTGTMTGGFKITNSYAPKKTEVSVKKAWDDKDNQDGVRPESIKVQLYAGDKKVGEEVELNAANEWTTTWKDLDLKDKG 1450
Cdd:COG4932    536 EATGTDPEVTVTGKSTTTTPDVALLTNLGTTEDALTSLAKTGDEVGKGLTLTTTTTVDTLDTNATEKTETVTVTAQLIGV 615

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1192940763 1451 QTIDYTvKEVGETNGYKVEVTGNAKDGYTLTNSHTPATVDISGTKTWEDNDNQDGKRPKAITVRLLADGKEVDS 1524
Cdd:COG4932    616 KTTKLT-DTTDPKGGTVEEATTTGGTANTGKTGTDLTDDTTVTSTTNTATSVEDTTDVDNKDAFTGGTEPGGTI 688
Collagen_bind super family cl37551
Collagen binding domain; The domain fold is a jelly-roll, composed of two antiparallel ...
 381-500 7.69e-15

Collagen binding domain; The domain fold is a jelly-roll, composed of two antiparallel beta-sheets and two short alpha-helices. A groove on beta-sheet I exhibited the best surface complementarity to the collagen. This site partially overlaps with the peptide sequence previously shown to be critical for collagen binding. Recombinant proteins containing single amino acid mutations designed to disrupt the surface of the putative binding site exhibited significantly lower affinities for collagen.


The actual alignment was detected with superfamily member pfam05737:

Pssm-ID: 283410 [Multi-domain]  Cd Length: 129  Bit Score: 72.78  E-value: 7.69e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192940763  381 SKVTWEVSINTNLETLNNATVTDPMPEGLNLTG--VKVYRQTVDKNGKVVSVDKDHPLIEGKDYTKDGNVIkfINDYAKT 458
Cdd:pfam05737   15 SLIHWTVRINYALQNIENAVLTDFIGEGQNLVFdsIEVYELNYKKDGEVVSGDKEYPLYQTIDLDTDNGFT--VTFGDTI 92

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1192940763  459 NDSFQLVYETTVKDSAIPAAggdvkFNNTATLKDDNTDEQSA 500
Cdd:pfam05737   93 DSAYIISYTTTITDGGKSQS-----YDNKATLNGDNIDTNEI 129
Collagen_bind super family cl37551
Collagen binding domain; The domain fold is a jelly-roll, composed of two antiparallel ...
 918-1047 3.73e-08

Collagen binding domain; The domain fold is a jelly-roll, composed of two antiparallel beta-sheets and two short alpha-helices. A groove on beta-sheet I exhibited the best surface complementarity to the collagen. This site partially overlaps with the peptide sequence previously shown to be critical for collagen binding. Recombinant proteins containing single amino acid mutations designed to disrupt the surface of the putative binding site exhibited significantly lower affinities for collagen.


The actual alignment was detected with superfamily member pfam05737:

Pssm-ID: 283410 [Multi-domain]  Cd Length: 129  Bit Score: 53.90  E-value: 3.73e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192940763  918 FVDKSGKQDPNNANYVTWAVTINPSQSTMSNVVITDTPSINQVLAEDSFAIYgtkvdqAGNITKDASVVLGKGKDYTVdi 997
Cdd:pfam05737    2 AIYKVGWVDAENNSLIHWTVRINYALQNIENAVLTDFIGEGQNLVFDSIEVY------ELNYKKDGEVVSGDKEYPLY-- 73

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1192940763  998 ETNNEIGQQVATIKMNGTIDKAYIMEYKALIMpENNGENTLTNKISIKGD 1047
Cdd:pfam05737   74 QTIDLDTDNGFTVTFGDTIDSAYIISYTTTIT-DGGKSQSYDNKATLNGD 122
Collagen_bind super family cl37551
Collagen binding domain; The domain fold is a jelly-roll, composed of two antiparallel ...
 784-901 2.52e-04

Collagen binding domain; The domain fold is a jelly-roll, composed of two antiparallel beta-sheets and two short alpha-helices. A groove on beta-sheet I exhibited the best surface complementarity to the collagen. This site partially overlaps with the peptide sequence previously shown to be critical for collagen binding. Recombinant proteins containing single amino acid mutations designed to disrupt the surface of the putative binding site exhibited significantly lower affinities for collagen.


The actual alignment was detected with superfamily member pfam05737:

Pssm-ID: 283410 [Multi-domain]  Cd Length: 129  Bit Score: 42.73  E-value: 2.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192940763  784 KGGAYNAQNK-HITWTTKVNYTQDALKGAMITDPIIGNQDYVDGSAKLYEVkiiangNVSRGAEVTNADIAYDSASKTVT 862
Cdd:pfam05737    5 KVGWVDAENNsLIHWTVRINYALQNIENAVLTDFIGEGQNLVFDSIEVYEL------NYKKDGEVVSGDKEYPLYQTIDL 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1192940763  863 AKLPDG--------NKAYDLVFETSLEGKVIDQsQYKNTATYKNGAT 901
Cdd:pfam05737   79 DTDNGFtvtfgdtiDSAYIISYTTTITDGGKSQ-SYDNKATLNGDNI 124
LPXTG_anchor TIGR01167
LPXTG-motif cell wall anchor domain; This model describes the LPXTG motif-containing region ...
 1885-1917 6.34e-04

LPXTG-motif cell wall anchor domain; This model describes the LPXTG motif-containing region found at the C-terminus of many surface proteins of Streptococcus and Streptomyces species. Cleavage between the Thr and Gly by sortase or a related enzyme leads to covalent anchoring at the new C-terminal Thr to the cell wall. Hits that do not lie at the C-terminus or are not found in Gram-positive bacteria are probably false-positive. A common feature of this proteins containing this domain appears to be a high proportion of charged and zwitterionic residues immediatedly upstream of the LPXTG motif. This model differs from other descriptions of the LPXTG region by including a portion of that upstream charged region. [Cell envelope, Other]


:

Pssm-ID: 273478 [Multi-domain]  Cd Length: 34  Bit Score: 39.00  E-value: 6.34e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1192940763 1885 PQTGETSDWFISMIGLLLIvtAGAIYLLKYKRR 1917
Cdd:TIGR01167    3 PKTGESGNSLLLLLGLLLL--GLGGLLLRKRKK 33
RrgB_K2N_iso_D2 TIGR04226
fimbrial isopeptide formation D2 domain; The Streptococcus Pneumoniae pilus backbone protein, ...
 658-739 7.10e-03

fimbrial isopeptide formation D2 domain; The Streptococcus Pneumoniae pilus backbone protein, RrgB, has three tandem domains with Lys-to-Asn isopeptide bonds, but these three regions are extremely divergent in sequence. This model represents the homology domain family of the D2 domain. It occurs just once in many surface proteins but up to twenty times in some pilin subunit proteins. Three of every four members have the typical Gram-positive C-terminal motif, LPXTG, although in many cases this motif may be involved in pilin subunit cross-linking rather than cell wall attachment. Proteins with this domain include fimbrial proteins with lectin-like adhesion functions, and the majority of characterized members are involved in surface adhesion to host structures.


:

Pssm-ID: 275067 [Multi-domain]  Cd Length: 124  Bit Score: 38.40  E-value: 7.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192940763  658 KINWTITInKFKYEMANWY---LEDTLSKNLTLDPDSIVLkeQGGKTLVKDIDYKVTmDGQKFKVEFLGD-LKKDTDKTY 733
Cdd:TIGR04226   22 EVTYTITT-TVPADIADYKsfvITDTLDDGLTYKGSVKVT--VDGKTLTVDTDYTVT-DGQTVTVTFTDAgLKKLAGKKI 97


                   ....*.
gi 1192940763  734 VLTYTT 739
Cdd:TIGR04226   98 TVTYTA 103
 
Name Accession Description Interval E-value
Cna_B pfam05738
Cna protein B-type domain; This domain is found in Staphylococcus aureus collagen-binding ...
 1491-1573 9.32e-30

Cna protein B-type domain; This domain is found in Staphylococcus aureus collagen-binding surface protein. The structure of the repetitive B-region has been solved and forms a beta sandwich structure.


Pssm-ID: 461726 [Multi-domain]  Cd Length: 88  Bit Score: 113.88  E-value: 9.32e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192940763 1491 ISGTKTWEDNDNQDGKRPKAITVRLLADGKEV-DSKEVTAETNWTYEFTGLDKY-KSGNEIRYTIQEVSVPEYSSEVEE- 1567
Cdd:pfam05738    1 VSVTKVWDDNNNQDGIRPESITVQLLANGQKVgVTKELTAANNWTYTFTDLPKYdENGKEITYTVEEDAVPGYTTTVDAk 80


                   ....*...
gi 1192940763 1568 --FDVTNT 1573
Cdd:pfam05738   81 dgFTITNT 88
Cna_B pfam05738
Cna protein B-type domain; This domain is found in Staphylococcus aureus collagen-binding ...
 1677-1759 1.05e-28

Cna protein B-type domain; This domain is found in Staphylococcus aureus collagen-binding surface protein. The structure of the repetitive B-region has been solved and forms a beta sandwich structure.


Pssm-ID: 461726 [Multi-domain]  Cd Length: 88  Bit Score: 111.18  E-value: 1.05e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192940763 1677 ISGTKIWDDNDNQDGKRPDVITVHLLK-GTEVVKTVKVTADNDWKYEFKNMPKF-ENGEKIQYSVAEDKVEDYSSSI--- 1751
Cdd:pfam05738    1 VSVTKVWDDNNNQDGIRPESITVQLLAnGQKVGVTKELTAANNWTYTFTDLPKYdENGKEITYTVEEDAVPGYTTTVdak 80


                   ....*...
gi 1192940763 1752 KGFDITNS 1759
Cdd:pfam05738   81 DGFTITNT 88
CollagenBindB cd00222
Repeat unit of collagen-binding protein domain B; The collagen-binding protein mediates ...
 1489-1574 2.72e-28

Repeat unit of collagen-binding protein domain B; The collagen-binding protein mediates bacterial adherence to collagen; the primary sequence has a non-repetitive, collagen-binding A region, followed by instances of this B region repetitive unit. The B region has one to four 23 kDa repeat units (B1-B4), which have been suggested to serve as 'stalks' that project the A region from the bacterial surface and thus facilitate bacterial adherence to collagen. Each B repeat unit has two highly similar domains (D1 and D2) placed side-by-side; both D1 and D2 are included in this model. They exhibit a unique inverse IgG-like domain fold.


Pssm-ID: 212461 [Multi-domain]  Cd Length: 92  Bit Score: 110.08  E-value: 2.72e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192940763 1489 VDISGTKTWEDNDNQDGKRPKAITVRLLADGKE-VDSKEVTAETNWTYEFTGLDKYKS-GNEIRYTIQEVSVPEYSSEV- 1565
Cdd:cd00222      1 TDITVTKTWDDDDNQDGKRPESITVQLLANGKEtGDTVTLTASNDWTYTFTNLPKYDEnGKEITYTVKEVPVPGYTTTVt 80

                           90
                   ....*....|..
gi 1192940763 1566 ---EEFDVTNTH 1574
Cdd:cd00222     81 gddGGFTITNTH 92
CollagenBindB cd00222
Repeat unit of collagen-binding protein domain B; The collagen-binding protein mediates ...
 1675-1760 5.16e-28

Repeat unit of collagen-binding protein domain B; The collagen-binding protein mediates bacterial adherence to collagen; the primary sequence has a non-repetitive, collagen-binding A region, followed by instances of this B region repetitive unit. The B region has one to four 23 kDa repeat units (B1-B4), which have been suggested to serve as 'stalks' that project the A region from the bacterial surface and thus facilitate bacterial adherence to collagen. Each B repeat unit has two highly similar domains (D1 and D2) placed side-by-side; both D1 and D2 are included in this model. They exhibit a unique inverse IgG-like domain fold.


Pssm-ID: 212461 [Multi-domain]  Cd Length: 92  Bit Score: 109.31  E-value: 5.16e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192940763 1675 VDISGTKIWDDNDNQDGKRPDVITVHLLK-GTEVVKTVKVTADNDWKYEFKNMPKF-ENGEKIQYSVAEDKVEDYSSSIK 1752
Cdd:cd00222      1 TDITVTKTWDDDDNQDGKRPESITVQLLAnGKETGDTVTLTASNDWTYTFTNLPKYdENGKEITYTVKEVPVPGYTTTVT 80

                           90
                   ....*....|..
gi 1192940763 1753 G----FDITNSH 1760
Cdd:cd00222     81 GddggFTITNTH 92
Cna_B pfam05738
Cna protein B-type domain; This domain is found in Staphylococcus aureus collagen-binding ...
 1394-1483 1.46e-26

Cna protein B-type domain; This domain is found in Staphylococcus aureus collagen-binding surface protein. The structure of the repetitive B-region has been solved and forms a beta sandwich structure.


Pssm-ID: 461726 [Multi-domain]  Cd Length: 88  Bit Score: 105.02  E-value: 1.46e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192940763 1394 VSVKKAWDDKDNQDGVRPESIKVQLYAGDKKVGEEVELNAANEWTTTWKDLDLKDK-GQTIDYTVKEVGETnGYKVEVtg 1472
Cdd:pfam05738    1 VSVTKVWDDNNNQDGIRPESITVQLLANGQKVGVTKELTAANNWTYTFTDLPKYDEnGKEITYTVEEDAVP-GYTTTV-- 77

                           90
                   ....*....|.
gi 1192940763 1473 NAKDGYTLTNS 1483
Cdd:pfam05738   78 DAKDGFTITNT 88
Cna_B pfam05738
Cna protein B-type domain; This domain is found in Staphylococcus aureus collagen-binding ...
 1581-1669 2.88e-26

Cna protein B-type domain; This domain is found in Staphylococcus aureus collagen-binding surface protein. The structure of the repetitive B-region has been solved and forms a beta sandwich structure.


Pssm-ID: 461726 [Multi-domain]  Cd Length: 88  Bit Score: 103.87  E-value: 2.88e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192940763 1581 VNVVKAWDDADNQDGVRPDQIKVVLVADGVVTDQVKTLNAANHWQASFADLDEY-KAGKKVTYEVQELAVEGYESVIsgD 1659
Cdd:pfam05738    1 VSVTKVWDDNNNQDGIRPESITVQLLANGQKVGVTKELTAANNWTYTFTDLPKYdENGKEITYTVEEDAVPGYTTTV--D 78

                           90
                   ....*....|
gi 1192940763 1660 ASKGFVITNS 1669
Cdd:pfam05738   79 AKDGFTITNT 88
CollagenBindB cd00222
Repeat unit of collagen-binding protein domain B; The collagen-binding protein mediates ...
 1392-1484 3.03e-26

Repeat unit of collagen-binding protein domain B; The collagen-binding protein mediates bacterial adherence to collagen; the primary sequence has a non-repetitive, collagen-binding A region, followed by instances of this B region repetitive unit. The B region has one to four 23 kDa repeat units (B1-B4), which have been suggested to serve as 'stalks' that project the A region from the bacterial surface and thus facilitate bacterial adherence to collagen. Each B repeat unit has two highly similar domains (D1 and D2) placed side-by-side; both D1 and D2 are included in this model. They exhibit a unique inverse IgG-like domain fold.


Pssm-ID: 212461 [Multi-domain]  Cd Length: 92  Bit Score: 104.30  E-value: 3.03e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192940763 1392 TEVSVKKAWDDKDNQDGVRPESIKVQLYAGDKKVGEEVELNAANEWTTTWKDLDLKD-KGQTIDYTVKEVgETNGYKVEV 1470
Cdd:cd00222      1 TDITVTKTWDDDDNQDGKRPESITVQLLANGKETGDTVTLTASNDWTYTFTNLPKYDeNGKEITYTVKEV-PVPGYTTTV 79

                           90
                   ....*....|....
gi 1192940763 1471 TGNAkDGYTLTNSH 1484
Cdd:cd00222     80 TGDD-GGFTITNTH 92
CollagenBindB cd00222
Repeat unit of collagen-binding protein domain B; The collagen-binding protein mediates ...
 1579-1670 2.14e-25

Repeat unit of collagen-binding protein domain B; The collagen-binding protein mediates bacterial adherence to collagen; the primary sequence has a non-repetitive, collagen-binding A region, followed by instances of this B region repetitive unit. The B region has one to four 23 kDa repeat units (B1-B4), which have been suggested to serve as 'stalks' that project the A region from the bacterial surface and thus facilitate bacterial adherence to collagen. Each B repeat unit has two highly similar domains (D1 and D2) placed side-by-side; both D1 and D2 are included in this model. They exhibit a unique inverse IgG-like domain fold.


Pssm-ID: 212461 [Multi-domain]  Cd Length: 92  Bit Score: 101.60  E-value: 2.14e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192940763 1579 TSVNVVKAWDDADNQDGVRPDQIKVVLVADGVVTDQVKTLNAANHWQASFADLDEYKA-GKKVTYEVQELAVEGYESVIS 1657
Cdd:cd00222      1 TDITVTKTWDDDDNQDGKRPESITVQLLANGKETGDTVTLTASNDWTYTFTNLPKYDEnGKEITYTVKEVPVPGYTTTVT 80

                           90
                   ....*....|...
gi 1192940763 1658 GDAsKGFVITNSH 1670
Cdd:cd00222     81 GDD-GGFTITNTH 92
Cna_B pfam05738
Cna protein B-type domain; This domain is found in Staphylococcus aureus collagen-binding ...
 1767-1843 2.23e-24

Cna protein B-type domain; This domain is found in Staphylococcus aureus collagen-binding surface protein. The structure of the repetitive B-region has been solved and forms a beta sandwich structure.


Pssm-ID: 461726 [Multi-domain]  Cd Length: 88  Bit Score: 98.47  E-value: 2.23e-24
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1192940763 1767 VNVTKVWKDDDDKTGVRPDSITFKLLADGKETGKTLKLSAKSNWQGSFEDLDVYN-NGEEINYTIEELQVKGYVSNIQ 1843
Cdd:pfam05738    1 VSVTKVWDDNNNQDGIRPESITVQLLANGQKVGVTKELTAANNWTYTFTDLPKYDeNGKEITYTVEEDAVPGYTTTVD 78
CollagenBindB cd00222
Repeat unit of collagen-binding protein domain B; The collagen-binding protein mediates ...
 1766-1857 2.92e-24

Repeat unit of collagen-binding protein domain B; The collagen-binding protein mediates bacterial adherence to collagen; the primary sequence has a non-repetitive, collagen-binding A region, followed by instances of this B region repetitive unit. The B region has one to four 23 kDa repeat units (B1-B4), which have been suggested to serve as 'stalks' that project the A region from the bacterial surface and thus facilitate bacterial adherence to collagen. Each B repeat unit has two highly similar domains (D1 and D2) placed side-by-side; both D1 and D2 are included in this model. They exhibit a unique inverse IgG-like domain fold.


Pssm-ID: 212461 [Multi-domain]  Cd Length: 92  Bit Score: 98.52  E-value: 2.92e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192940763 1766 NVNVTKVWKDDDDKTGVRPDSITFKLLADGKETGKTLKLSAKSNWQGSFEDLDVYN-NGEEINYTIEELQVKGYVSNIqk 1844
Cdd:cd00222      2 DITVTKTWDDDDNQDGKRPESITVQLLANGKETGDTVTLTASNDWTYTFTNLPKYDeNGKEITYTVKEVPVPGYTTTV-- 79

                           90
                   ....*....|...
gi 1192940763 1845 IGKTTTFVARNTL 1857
Cdd:cd00222     80 TGDDGGFTITNTH 92
CollagenBindB cd00222
Repeat unit of collagen-binding protein domain B; The collagen-binding protein mediates ...
 1293-1387 5.44e-24

Repeat unit of collagen-binding protein domain B; The collagen-binding protein mediates bacterial adherence to collagen; the primary sequence has a non-repetitive, collagen-binding A region, followed by instances of this B region repetitive unit. The B region has one to four 23 kDa repeat units (B1-B4), which have been suggested to serve as 'stalks' that project the A region from the bacterial surface and thus facilitate bacterial adherence to collagen. Each B repeat unit has two highly similar domains (D1 and D2) placed side-by-side; both D1 and D2 are included in this model. They exhibit a unique inverse IgG-like domain fold.


Pssm-ID: 212461 [Multi-domain]  Cd Length: 92  Bit Score: 97.75  E-value: 5.44e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192940763 1293 VDIPIEKVWNDKDNQDGIRPVKVTVELHADGKASGKTVELNTENDWKASFKKLRKTDaSTKEEIKYTVKEVDPDkNYKSD 1372
Cdd:cd00222      1 TDITVTKTWDDDDNQDGKRPESITVQLLANGKETGDTVTLTASNDWTYTFTNLPKYD-ENGKEITYTVKEVPVP-GYTTT 78

                           90
                   ....*....|....*
gi 1192940763 1373 VTGTMtGGFKITNSY 1387
Cdd:cd00222     79 VTGDD-GGFTITNTH 92
Cna_B pfam05738
Cna protein B-type domain; This domain is found in Staphylococcus aureus collagen-binding ...
 1295-1386 2.19e-22

Cna protein B-type domain; This domain is found in Staphylococcus aureus collagen-binding surface protein. The structure of the repetitive B-region has been solved and forms a beta sandwich structure.


Pssm-ID: 461726 [Multi-domain]  Cd Length: 88  Bit Score: 93.08  E-value: 2.19e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192940763 1295 IPIEKVWNDKDNQDGIRPVKVTVELHADGKASGKTVELNTENDWKASFKKLRKTDASTKeEIKYTVKEVDPDkNYKSDVt 1374
Cdd:pfam05738    1 VSVTKVWDDNNNQDGIRPESITVQLLANGQKVGVTKELTAANNWTYTFTDLPKYDENGK-EITYTVEEDAVP-GYTTTV- 77

                           90
                   ....*....|..
gi 1192940763 1375 gTMTGGFKITNS 1386
Cdd:pfam05738   78 -DAKDGFTITNT 88
ClfA COG4932
Clumping factor A-related surface protein, MSCRAMM (microbial surface components recognizing ...
 1056-1524 7.16e-16

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: 83.48  E-value: 7.16e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192940763 1056 TEESTKVVVSIGTGEGSKSSVNIVKVDADdNKTPLKGAELELwsVDKDGKKQQIVRSGVTNKKGELKFGNLRATNYLLVE 1135
Cdd:COG4932    244 NAGGTVTVTLKNTPKYTKGSVTVTKTDAD-TGEPLAGATFTL--TDADGNTVVTTTVTVTDADGSYTFTDLPPGTYTVTE 320

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192940763 1136 TKAPAGYTISDELKngkKIKLEADKEGQ-EVATLKIENAVPEISFNKVDI--KGKALAGAVFAIKNEDsryynglkadkt 1212
Cdd:COG4932    321 TKAPAGYDLDGEAV---KVTITAGQTTTvTVTNGNNEVKTGSVTLTKVDAddGEAPLAGAEFTLTDAD------------ 385

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192940763 1213 vkwaergeisADTKTALTSDENGKVTVKGLPVGEYQLVELSAPDGYEKSDKTIDFEVV-NKDGQIKLKDAIADVENEATQ 1291
Cdd:COG4932    386 ----------GTVVATITTDADGTASFKGLAPGTYTLTETKAPEGYTLDSTPITVTVTdGGTGAIDTITNERKKGSVQVT 455

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192940763 1292 FVDIPIEKVWNDKDNQDGIRPVKVTVELHADGK-ASGKTVELNTENDWKASFKKLRKTDASTKEEIKYTVKEVDPDKNYK 1370
Cdd:COG4932    456 KVDAPLAGATFTLTDADGTVVTLTTDADLAGATfEADGKVVTTTDASGKYTFKNLPPGTYTDAGGSATVITDDTDGTVGD 535

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192940763 1371 SDVTGTMTGGFKITNSYAPKKTEVSVKKAWDDKDNQDGVRPESIKVQLYAGDKKVGEEVELNAANEWTTTWKDLDLKDKG 1450
Cdd:COG4932    536 EATGTDPEVTVTGKSTTTTPDVALLTNLGTTEDALTSLAKTGDEVGKGLTLTTTTTVDTLDTNATEKTETVTVTAQLIGV 615

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1192940763 1451 QTIDYTvKEVGETNGYKVEVTGNAKDGYTLTNSHTPATVDISGTKTWEDNDNQDGKRPKAITVRLLADGKEVDS 1524
Cdd:COG4932    616 KTTKLT-DTTDPKGGTVEEATTTGGTANTGKTGTDLTDDTTVTSTTNTATSVEDTTDVDNKDAFTGGTEPGGTI 688
Collagen_bind pfam05737
Collagen binding domain; The domain fold is a jelly-roll, composed of two antiparallel ...
 381-500 7.69e-15

Collagen binding domain; The domain fold is a jelly-roll, composed of two antiparallel beta-sheets and two short alpha-helices. A groove on beta-sheet I exhibited the best surface complementarity to the collagen. This site partially overlaps with the peptide sequence previously shown to be critical for collagen binding. Recombinant proteins containing single amino acid mutations designed to disrupt the surface of the putative binding site exhibited significantly lower affinities for collagen.


Pssm-ID: 283410 [Multi-domain]  Cd Length: 129  Bit Score: 72.78  E-value: 7.69e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192940763  381 SKVTWEVSINTNLETLNNATVTDPMPEGLNLTG--VKVYRQTVDKNGKVVSVDKDHPLIEGKDYTKDGNVIkfINDYAKT 458
Cdd:pfam05737   15 SLIHWTVRINYALQNIENAVLTDFIGEGQNLVFdsIEVYELNYKKDGEVVSGDKEYPLYQTIDLDTDNGFT--VTFGDTI 92

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1192940763  459 NDSFQLVYETTVKDSAIPAAggdvkFNNTATLKDDNTDEQSA 500
Cdd:pfam05737   93 DSAYIISYTTTITDGGKSQS-----YDNKATLNGDNIDTNEI 129
SpaA pfam17802
Prealbumin-like fold domain; This entry contains a prealbumin-like domain from a wide variety ...
 1185-1273 1.18e-12

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: 64.53  E-value: 1.18e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192940763 1185 KGKALAGAVFAIKNEDsryynglkadktvkwaerGEISADTKTALTSDENGKVTVKGLPVGEYQLVELSAPDGYEKSDKT 1264
Cdd:pfam17802    2 TGKPLAGAEFTLYDAD------------------GTVDGKVVGTLTTDEDGKATFDGLPPGTYTLKETKAPDGYVLDDTP 63


                   ....*....
gi 1192940763 1265 IDFEVVNKD 1273
Cdd:pfam17802   64 IEFTVTEDG 72
Collagen_bind pfam05737
Collagen binding domain; The domain fold is a jelly-roll, composed of two antiparallel ...
 918-1047 3.73e-08

Collagen binding domain; The domain fold is a jelly-roll, composed of two antiparallel beta-sheets and two short alpha-helices. A groove on beta-sheet I exhibited the best surface complementarity to the collagen. This site partially overlaps with the peptide sequence previously shown to be critical for collagen binding. Recombinant proteins containing single amino acid mutations designed to disrupt the surface of the putative binding site exhibited significantly lower affinities for collagen.


Pssm-ID: 283410 [Multi-domain]  Cd Length: 129  Bit Score: 53.90  E-value: 3.73e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192940763  918 FVDKSGKQDPNNANYVTWAVTINPSQSTMSNVVITDTPSINQVLAEDSFAIYgtkvdqAGNITKDASVVLGKGKDYTVdi 997
Cdd:pfam05737    2 AIYKVGWVDAENNSLIHWTVRINYALQNIENAVLTDFIGEGQNLVFDSIEVY------ELNYKKDGEVVSGDKEYPLY-- 73

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1192940763  998 ETNNEIGQQVATIKMNGTIDKAYIMEYKALIMpENNGENTLTNKISIKGD 1047
Cdd:pfam05737   74 QTIDLDTDNGFTVTFGDTIDSAYIISYTTTIT-DGGKSQSYDNKATLNGD 122
iso_D2_wall_anc NF033902
SpaH/EbpB family LPXTG-anchored major pilin; Members of this family are pilin major subunits ...
 919-1179 4.26e-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: 58.23  E-value: 4.26e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192940763  919 VDKSGKQDPNNANYVTWAVTI------NPSQSTMSNVVITDTpsinqvlAEDSFAIYGTKVDQAGNITKDASVVLGKGKD 992
Cdd:NF033902   211 KDVTDAVGNGVGDTITYTITApvpkidANTLDDFKGFTVTDT-------LDTRLDEVAGVVKSVKVGGTGLTATLTVTTD 283

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192940763  993 YTVDieTNNEIGQQVATIKMNGTIDKAYIMEYKALIM----------PENNGENTLTNKISIK------GDGQKEVEGNT 1056
Cdd:NF033902   284 YTVT--TDGLTADQKVTVTFTEAGLAKLAAAKNVKVTvtfktkvtktAKGGTNGEITNKAGLIpnnpgpNTPEPTTPGTP 361

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192940763 1057 EESTKVVVSIGTgegskssVNIVKVDADDNKTPLKGAELELWSVDKDGKKQQIVRSG---------------------VT 1115
Cdd:NF033902   362 DPTPTVKTYFGK-------LKIKKVDADDTSKKLKGAEFKVYACEADAAAACVNAIGingkttfttgadgtvsidglhVT 434

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1192940763 1116 NKKGELKFGNLRATNYLLVETKAPAGYTISDELKNGKKIKLEADKEGQEVATLKIENAVPEISF 1179
Cdd:NF033902   435 DLEDGASVKAAAGKDYCLVETKAPAGYVLPPKPVEVTVVKVTVTAATTADVKNTVVNNKKTVPN 498
Collagen_bind pfam05737
Collagen binding domain; The domain fold is a jelly-roll, composed of two antiparallel ...
 784-901 2.52e-04

Collagen binding domain; The domain fold is a jelly-roll, composed of two antiparallel beta-sheets and two short alpha-helices. A groove on beta-sheet I exhibited the best surface complementarity to the collagen. This site partially overlaps with the peptide sequence previously shown to be critical for collagen binding. Recombinant proteins containing single amino acid mutations designed to disrupt the surface of the putative binding site exhibited significantly lower affinities for collagen.


Pssm-ID: 283410 [Multi-domain]  Cd Length: 129  Bit Score: 42.73  E-value: 2.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192940763  784 KGGAYNAQNK-HITWTTKVNYTQDALKGAMITDPIIGNQDYVDGSAKLYEVkiiangNVSRGAEVTNADIAYDSASKTVT 862
Cdd:pfam05737    5 KVGWVDAENNsLIHWTVRINYALQNIENAVLTDFIGEGQNLVFDSIEVYEL------NYKKDGEVVSGDKEYPLYQTIDL 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1192940763  863 AKLPDG--------NKAYDLVFETSLEGKVIDQsQYKNTATYKNGAT 901
Cdd:pfam05737   79 DTDNGFtvtfgdtiDSAYIISYTTTITDGGKSQ-SYDNKATLNGDNI 124
LPXTG_anchor TIGR01167
LPXTG-motif cell wall anchor domain; This model describes the LPXTG motif-containing region ...
 1885-1917 6.34e-04

LPXTG-motif cell wall anchor domain; This model describes the LPXTG motif-containing region found at the C-terminus of many surface proteins of Streptococcus and Streptomyces species. Cleavage between the Thr and Gly by sortase or a related enzyme leads to covalent anchoring at the new C-terminal Thr to the cell wall. Hits that do not lie at the C-terminus or are not found in Gram-positive bacteria are probably false-positive. A common feature of this proteins containing this domain appears to be a high proportion of charged and zwitterionic residues immediatedly upstream of the LPXTG motif. This model differs from other descriptions of the LPXTG region by including a portion of that upstream charged region. [Cell envelope, Other]


Pssm-ID: 273478 [Multi-domain]  Cd Length: 34  Bit Score: 39.00  E-value: 6.34e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1192940763 1885 PQTGETSDWFISMIGLLLIvtAGAIYLLKYKRR 1917
Cdd:TIGR01167    3 PKTGESGNSLLLLLGLLLL--GLGGLLLRKRKK 33
iso_D2_wall_anc NF033902
SpaH/EbpB family LPXTG-anchored major pilin; Members of this family are pilin major subunits ...
 1177-1290 2.71e-03

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: 42.44  E-value: 2.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192940763 1177 ISFNKVD--IKGKALAGAVFAIknedsryyngLKADKTVKWAERGEISADTKTALTSDENGKVTVKGLPVGEYQ------ 1248
Cdd:NF033902   374 LKIKKVDadDTSKKLKGAEFKV----------YACEADAAAACVNAIGINGKTTFTTGADGTVSIDGLHVTDLEdgasvk 443

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1192940763 1249 --------LVELSAPDGYEKSDKTIDFEVVNKDgqiKLKDAIADVENEAT 1290
Cdd:NF033902   444 aaagkdycLVETKAPAGYVLPPKPVEVTVVKVT---VTAATTADVKNTVV 490
RrgB_K2N_iso_D2 TIGR04226
fimbrial isopeptide formation D2 domain; The Streptococcus Pneumoniae pilus backbone protein, ...
 658-739 7.10e-03

fimbrial isopeptide formation D2 domain; The Streptococcus Pneumoniae pilus backbone protein, RrgB, has three tandem domains with Lys-to-Asn isopeptide bonds, but these three regions are extremely divergent in sequence. This model represents the homology domain family of the D2 domain. It occurs just once in many surface proteins but up to twenty times in some pilin subunit proteins. Three of every four members have the typical Gram-positive C-terminal motif, LPXTG, although in many cases this motif may be involved in pilin subunit cross-linking rather than cell wall attachment. Proteins with this domain include fimbrial proteins with lectin-like adhesion functions, and the majority of characterized members are involved in surface adhesion to host structures.


Pssm-ID: 275067 [Multi-domain]  Cd Length: 124  Bit Score: 38.40  E-value: 7.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192940763  658 KINWTITInKFKYEMANWY---LEDTLSKNLTLDPDSIVLkeQGGKTLVKDIDYKVTmDGQKFKVEFLGD-LKKDTDKTY 733
Cdd:TIGR04226   22 EVTYTITT-TVPADIADYKsfvITDTLDDGLTYKGSVKVT--VDGKTLTVDTDYTVT-DGQTVTVTFTDAgLKKLAGKKI 97


                   ....*.
gi 1192940763  734 VLTYTT 739
Cdd:TIGR04226   98 TVTYTA 103
 
Name Accession Description Interval E-value
Cna_B pfam05738
Cna protein B-type domain; This domain is found in Staphylococcus aureus collagen-binding ...
 1491-1573 9.32e-30

Cna protein B-type domain; This domain is found in Staphylococcus aureus collagen-binding surface protein. The structure of the repetitive B-region has been solved and forms a beta sandwich structure.


Pssm-ID: 461726 [Multi-domain]  Cd Length: 88  Bit Score: 113.88  E-value: 9.32e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192940763 1491 ISGTKTWEDNDNQDGKRPKAITVRLLADGKEV-DSKEVTAETNWTYEFTGLDKY-KSGNEIRYTIQEVSVPEYSSEVEE- 1567
Cdd:pfam05738    1 VSVTKVWDDNNNQDGIRPESITVQLLANGQKVgVTKELTAANNWTYTFTDLPKYdENGKEITYTVEEDAVPGYTTTVDAk 80


                   ....*...
gi 1192940763 1568 --FDVTNT 1573
Cdd:pfam05738   81 dgFTITNT 88
Cna_B pfam05738
Cna protein B-type domain; This domain is found in Staphylococcus aureus collagen-binding ...
 1677-1759 1.05e-28

Cna protein B-type domain; This domain is found in Staphylococcus aureus collagen-binding surface protein. The structure of the repetitive B-region has been solved and forms a beta sandwich structure.


Pssm-ID: 461726 [Multi-domain]  Cd Length: 88  Bit Score: 111.18  E-value: 1.05e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192940763 1677 ISGTKIWDDNDNQDGKRPDVITVHLLK-GTEVVKTVKVTADNDWKYEFKNMPKF-ENGEKIQYSVAEDKVEDYSSSI--- 1751
Cdd:pfam05738    1 VSVTKVWDDNNNQDGIRPESITVQLLAnGQKVGVTKELTAANNWTYTFTDLPKYdENGKEITYTVEEDAVPGYTTTVdak 80


                   ....*...
gi 1192940763 1752 KGFDITNS 1759
Cdd:pfam05738   81 DGFTITNT 88
CollagenBindB cd00222
Repeat unit of collagen-binding protein domain B; The collagen-binding protein mediates ...
 1489-1574 2.72e-28

Repeat unit of collagen-binding protein domain B; The collagen-binding protein mediates bacterial adherence to collagen; the primary sequence has a non-repetitive, collagen-binding A region, followed by instances of this B region repetitive unit. The B region has one to four 23 kDa repeat units (B1-B4), which have been suggested to serve as 'stalks' that project the A region from the bacterial surface and thus facilitate bacterial adherence to collagen. Each B repeat unit has two highly similar domains (D1 and D2) placed side-by-side; both D1 and D2 are included in this model. They exhibit a unique inverse IgG-like domain fold.


Pssm-ID: 212461 [Multi-domain]  Cd Length: 92  Bit Score: 110.08  E-value: 2.72e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192940763 1489 VDISGTKTWEDNDNQDGKRPKAITVRLLADGKE-VDSKEVTAETNWTYEFTGLDKYKS-GNEIRYTIQEVSVPEYSSEV- 1565
Cdd:cd00222      1 TDITVTKTWDDDDNQDGKRPESITVQLLANGKEtGDTVTLTASNDWTYTFTNLPKYDEnGKEITYTVKEVPVPGYTTTVt 80

                           90
                   ....*....|..
gi 1192940763 1566 ---EEFDVTNTH 1574
Cdd:cd00222     81 gddGGFTITNTH 92
CollagenBindB cd00222
Repeat unit of collagen-binding protein domain B; The collagen-binding protein mediates ...
 1675-1760 5.16e-28

Repeat unit of collagen-binding protein domain B; The collagen-binding protein mediates bacterial adherence to collagen; the primary sequence has a non-repetitive, collagen-binding A region, followed by instances of this B region repetitive unit. The B region has one to four 23 kDa repeat units (B1-B4), which have been suggested to serve as 'stalks' that project the A region from the bacterial surface and thus facilitate bacterial adherence to collagen. Each B repeat unit has two highly similar domains (D1 and D2) placed side-by-side; both D1 and D2 are included in this model. They exhibit a unique inverse IgG-like domain fold.


Pssm-ID: 212461 [Multi-domain]  Cd Length: 92  Bit Score: 109.31  E-value: 5.16e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192940763 1675 VDISGTKIWDDNDNQDGKRPDVITVHLLK-GTEVVKTVKVTADNDWKYEFKNMPKF-ENGEKIQYSVAEDKVEDYSSSIK 1752
Cdd:cd00222      1 TDITVTKTWDDDDNQDGKRPESITVQLLAnGKETGDTVTLTASNDWTYTFTNLPKYdENGKEITYTVKEVPVPGYTTTVT 80

                           90
                   ....*....|..
gi 1192940763 1753 G----FDITNSH 1760
Cdd:cd00222     81 GddggFTITNTH 92
Cna_B pfam05738
Cna protein B-type domain; This domain is found in Staphylococcus aureus collagen-binding ...
 1394-1483 1.46e-26

Cna protein B-type domain; This domain is found in Staphylococcus aureus collagen-binding surface protein. The structure of the repetitive B-region has been solved and forms a beta sandwich structure.


Pssm-ID: 461726 [Multi-domain]  Cd Length: 88  Bit Score: 105.02  E-value: 1.46e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192940763 1394 VSVKKAWDDKDNQDGVRPESIKVQLYAGDKKVGEEVELNAANEWTTTWKDLDLKDK-GQTIDYTVKEVGETnGYKVEVtg 1472
Cdd:pfam05738    1 VSVTKVWDDNNNQDGIRPESITVQLLANGQKVGVTKELTAANNWTYTFTDLPKYDEnGKEITYTVEEDAVP-GYTTTV-- 77

                           90
                   ....*....|.
gi 1192940763 1473 NAKDGYTLTNS 1483
Cdd:pfam05738   78 DAKDGFTITNT 88
Cna_B pfam05738
Cna protein B-type domain; This domain is found in Staphylococcus aureus collagen-binding ...
 1581-1669 2.88e-26

Cna protein B-type domain; This domain is found in Staphylococcus aureus collagen-binding surface protein. The structure of the repetitive B-region has been solved and forms a beta sandwich structure.


Pssm-ID: 461726 [Multi-domain]  Cd Length: 88  Bit Score: 103.87  E-value: 2.88e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192940763 1581 VNVVKAWDDADNQDGVRPDQIKVVLVADGVVTDQVKTLNAANHWQASFADLDEY-KAGKKVTYEVQELAVEGYESVIsgD 1659
Cdd:pfam05738    1 VSVTKVWDDNNNQDGIRPESITVQLLANGQKVGVTKELTAANNWTYTFTDLPKYdENGKEITYTVEEDAVPGYTTTV--D 78

                           90
                   ....*....|
gi 1192940763 1660 ASKGFVITNS 1669
Cdd:pfam05738   79 AKDGFTITNT 88
CollagenBindB cd00222
Repeat unit of collagen-binding protein domain B; The collagen-binding protein mediates ...
 1392-1484 3.03e-26

Repeat unit of collagen-binding protein domain B; The collagen-binding protein mediates bacterial adherence to collagen; the primary sequence has a non-repetitive, collagen-binding A region, followed by instances of this B region repetitive unit. The B region has one to four 23 kDa repeat units (B1-B4), which have been suggested to serve as 'stalks' that project the A region from the bacterial surface and thus facilitate bacterial adherence to collagen. Each B repeat unit has two highly similar domains (D1 and D2) placed side-by-side; both D1 and D2 are included in this model. They exhibit a unique inverse IgG-like domain fold.


Pssm-ID: 212461 [Multi-domain]  Cd Length: 92  Bit Score: 104.30  E-value: 3.03e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192940763 1392 TEVSVKKAWDDKDNQDGVRPESIKVQLYAGDKKVGEEVELNAANEWTTTWKDLDLKD-KGQTIDYTVKEVgETNGYKVEV 1470
Cdd:cd00222      1 TDITVTKTWDDDDNQDGKRPESITVQLLANGKETGDTVTLTASNDWTYTFTNLPKYDeNGKEITYTVKEV-PVPGYTTTV 79

                           90
                   ....*....|....
gi 1192940763 1471 TGNAkDGYTLTNSH 1484
Cdd:cd00222     80 TGDD-GGFTITNTH 92
CollagenBindB cd00222
Repeat unit of collagen-binding protein domain B; The collagen-binding protein mediates ...
 1579-1670 2.14e-25

Repeat unit of collagen-binding protein domain B; The collagen-binding protein mediates bacterial adherence to collagen; the primary sequence has a non-repetitive, collagen-binding A region, followed by instances of this B region repetitive unit. The B region has one to four 23 kDa repeat units (B1-B4), which have been suggested to serve as 'stalks' that project the A region from the bacterial surface and thus facilitate bacterial adherence to collagen. Each B repeat unit has two highly similar domains (D1 and D2) placed side-by-side; both D1 and D2 are included in this model. They exhibit a unique inverse IgG-like domain fold.


Pssm-ID: 212461 [Multi-domain]  Cd Length: 92  Bit Score: 101.60  E-value: 2.14e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192940763 1579 TSVNVVKAWDDADNQDGVRPDQIKVVLVADGVVTDQVKTLNAANHWQASFADLDEYKA-GKKVTYEVQELAVEGYESVIS 1657
Cdd:cd00222      1 TDITVTKTWDDDDNQDGKRPESITVQLLANGKETGDTVTLTASNDWTYTFTNLPKYDEnGKEITYTVKEVPVPGYTTTVT 80

                           90
                   ....*....|...
gi 1192940763 1658 GDAsKGFVITNSH 1670
Cdd:cd00222     81 GDD-GGFTITNTH 92
Cna_B pfam05738
Cna protein B-type domain; This domain is found in Staphylococcus aureus collagen-binding ...
 1767-1843 2.23e-24

Cna protein B-type domain; This domain is found in Staphylococcus aureus collagen-binding surface protein. The structure of the repetitive B-region has been solved and forms a beta sandwich structure.


Pssm-ID: 461726 [Multi-domain]  Cd Length: 88  Bit Score: 98.47  E-value: 2.23e-24
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1192940763 1767 VNVTKVWKDDDDKTGVRPDSITFKLLADGKETGKTLKLSAKSNWQGSFEDLDVYN-NGEEINYTIEELQVKGYVSNIQ 1843
Cdd:pfam05738    1 VSVTKVWDDNNNQDGIRPESITVQLLANGQKVGVTKELTAANNWTYTFTDLPKYDeNGKEITYTVEEDAVPGYTTTVD 78
CollagenBindB cd00222
Repeat unit of collagen-binding protein domain B; The collagen-binding protein mediates ...
 1766-1857 2.92e-24

Repeat unit of collagen-binding protein domain B; The collagen-binding protein mediates bacterial adherence to collagen; the primary sequence has a non-repetitive, collagen-binding A region, followed by instances of this B region repetitive unit. The B region has one to four 23 kDa repeat units (B1-B4), which have been suggested to serve as 'stalks' that project the A region from the bacterial surface and thus facilitate bacterial adherence to collagen. Each B repeat unit has two highly similar domains (D1 and D2) placed side-by-side; both D1 and D2 are included in this model. They exhibit a unique inverse IgG-like domain fold.


Pssm-ID: 212461 [Multi-domain]  Cd Length: 92  Bit Score: 98.52  E-value: 2.92e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192940763 1766 NVNVTKVWKDDDDKTGVRPDSITFKLLADGKETGKTLKLSAKSNWQGSFEDLDVYN-NGEEINYTIEELQVKGYVSNIqk 1844
Cdd:cd00222      2 DITVTKTWDDDDNQDGKRPESITVQLLANGKETGDTVTLTASNDWTYTFTNLPKYDeNGKEITYTVKEVPVPGYTTTV-- 79

                           90
                   ....*....|...
gi 1192940763 1845 IGKTTTFVARNTL 1857
Cdd:cd00222     80 TGDDGGFTITNTH 92
CollagenBindB cd00222
Repeat unit of collagen-binding protein domain B; The collagen-binding protein mediates ...
 1293-1387 5.44e-24

Repeat unit of collagen-binding protein domain B; The collagen-binding protein mediates bacterial adherence to collagen; the primary sequence has a non-repetitive, collagen-binding A region, followed by instances of this B region repetitive unit. The B region has one to four 23 kDa repeat units (B1-B4), which have been suggested to serve as 'stalks' that project the A region from the bacterial surface and thus facilitate bacterial adherence to collagen. Each B repeat unit has two highly similar domains (D1 and D2) placed side-by-side; both D1 and D2 are included in this model. They exhibit a unique inverse IgG-like domain fold.


Pssm-ID: 212461 [Multi-domain]  Cd Length: 92  Bit Score: 97.75  E-value: 5.44e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192940763 1293 VDIPIEKVWNDKDNQDGIRPVKVTVELHADGKASGKTVELNTENDWKASFKKLRKTDaSTKEEIKYTVKEVDPDkNYKSD 1372
Cdd:cd00222      1 TDITVTKTWDDDDNQDGKRPESITVQLLANGKETGDTVTLTASNDWTYTFTNLPKYD-ENGKEITYTVKEVPVP-GYTTT 78

                           90
                   ....*....|....*
gi 1192940763 1373 VTGTMtGGFKITNSY 1387
Cdd:cd00222     79 VTGDD-GGFTITNTH 92
Cna_B pfam05738
Cna protein B-type domain; This domain is found in Staphylococcus aureus collagen-binding ...
 1295-1386 2.19e-22

Cna protein B-type domain; This domain is found in Staphylococcus aureus collagen-binding surface protein. The structure of the repetitive B-region has been solved and forms a beta sandwich structure.


Pssm-ID: 461726 [Multi-domain]  Cd Length: 88  Bit Score: 93.08  E-value: 2.19e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192940763 1295 IPIEKVWNDKDNQDGIRPVKVTVELHADGKASGKTVELNTENDWKASFKKLRKTDASTKeEIKYTVKEVDPDkNYKSDVt 1374
Cdd:pfam05738    1 VSVTKVWDDNNNQDGIRPESITVQLLANGQKVGVTKELTAANNWTYTFTDLPKYDENGK-EITYTVEEDAVP-GYTTTV- 77

                           90
                   ....*....|..
gi 1192940763 1375 gTMTGGFKITNS 1386
Cdd:pfam05738   78 -DAKDGFTITNT 88
ClfA COG4932
Clumping factor A-related surface protein, MSCRAMM (microbial surface components recognizing ...
 1056-1524 7.16e-16

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: 83.48  E-value: 7.16e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192940763 1056 TEESTKVVVSIGTGEGSKSSVNIVKVDADdNKTPLKGAELELwsVDKDGKKQQIVRSGVTNKKGELKFGNLRATNYLLVE 1135
Cdd:COG4932    244 NAGGTVTVTLKNTPKYTKGSVTVTKTDAD-TGEPLAGATFTL--TDADGNTVVTTTVTVTDADGSYTFTDLPPGTYTVTE 320

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192940763 1136 TKAPAGYTISDELKngkKIKLEADKEGQ-EVATLKIENAVPEISFNKVDI--KGKALAGAVFAIKNEDsryynglkadkt 1212
Cdd:COG4932    321 TKAPAGYDLDGEAV---KVTITAGQTTTvTVTNGNNEVKTGSVTLTKVDAddGEAPLAGAEFTLTDAD------------ 385

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192940763 1213 vkwaergeisADTKTALTSDENGKVTVKGLPVGEYQLVELSAPDGYEKSDKTIDFEVV-NKDGQIKLKDAIADVENEATQ 1291
Cdd:COG4932    386 ----------GTVVATITTDADGTASFKGLAPGTYTLTETKAPEGYTLDSTPITVTVTdGGTGAIDTITNERKKGSVQVT 455

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192940763 1292 FVDIPIEKVWNDKDNQDGIRPVKVTVELHADGK-ASGKTVELNTENDWKASFKKLRKTDASTKEEIKYTVKEVDPDKNYK 1370
Cdd:COG4932    456 KVDAPLAGATFTLTDADGTVVTLTTDADLAGATfEADGKVVTTTDASGKYTFKNLPPGTYTDAGGSATVITDDTDGTVGD 535

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192940763 1371 SDVTGTMTGGFKITNSYAPKKTEVSVKKAWDDKDNQDGVRPESIKVQLYAGDKKVGEEVELNAANEWTTTWKDLDLKDKG 1450
Cdd:COG4932    536 EATGTDPEVTVTGKSTTTTPDVALLTNLGTTEDALTSLAKTGDEVGKGLTLTTTTTVDTLDTNATEKTETVTVTAQLIGV 615

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1192940763 1451 QTIDYTvKEVGETNGYKVEVTGNAKDGYTLTNSHTPATVDISGTKTWEDNDNQDGKRPKAITVRLLADGKEVDS 1524
Cdd:COG4932    616 KTTKLT-DTTDPKGGTVEEATTTGGTANTGKTGTDLTDDTTVTSTTNTATSVEDTTDVDNKDAFTGGTEPGGTI 688
Collagen_bind pfam05737
Collagen binding domain; The domain fold is a jelly-roll, composed of two antiparallel ...
 381-500 7.69e-15

Collagen binding domain; The domain fold is a jelly-roll, composed of two antiparallel beta-sheets and two short alpha-helices. A groove on beta-sheet I exhibited the best surface complementarity to the collagen. This site partially overlaps with the peptide sequence previously shown to be critical for collagen binding. Recombinant proteins containing single amino acid mutations designed to disrupt the surface of the putative binding site exhibited significantly lower affinities for collagen.


Pssm-ID: 283410 [Multi-domain]  Cd Length: 129  Bit Score: 72.78  E-value: 7.69e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192940763  381 SKVTWEVSINTNLETLNNATVTDPMPEGLNLTG--VKVYRQTVDKNGKVVSVDKDHPLIEGKDYTKDGNVIkfINDYAKT 458
Cdd:pfam05737   15 SLIHWTVRINYALQNIENAVLTDFIGEGQNLVFdsIEVYELNYKKDGEVVSGDKEYPLYQTIDLDTDNGFT--VTFGDTI 92

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1192940763  459 NDSFQLVYETTVKDSAIPAAggdvkFNNTATLKDDNTDEQSA 500
Cdd:pfam05737   93 DSAYIISYTTTITDGGKSQS-----YDNKATLNGDNIDTNEI 129
ClfA COG4932
Clumping factor A-related surface protein, MSCRAMM (microbial surface components recognizing ...
 908-1622 2.21e-14

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: 78.86  E-value: 2.21e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192940763  908 ATVNVKHGNVFVDKSGKQDPNNANYVTWAVTINPSQSTMSNVVITDTPSINQVLAEDSFAIYGTKVDQAGNITKDASVVL 987
Cdd:COG4932      2 VGAKGAGTGVGTVIVEGAGSGSLVAVTTGAVLGLALGSTGGTAGSAAAINSAPATGTATGTSAGATAVIVIAAGLTATPT 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192940763  988 GKGKDYTVDIETNNEIGQQVATIKMNGTIDKayimEYKALIMPENNGENTLTNKISIKGDGQKEVEGNTEESTKVVVSIG 1067
Cdd:COG4932     82 ETASGLGGDATVTTTANVAKVTNGAAANLTV----NADGTASNAGTLAKGAETATGNLDGDAGDVTVTAAATDGVNDVDG 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192940763 1068 TGEGSKSSVNIVKVDADDNKTPLKGAELELWsvDKDGKKqqiVRSGVTNKKGELKFGNLRATNYLLVETKAPAGYTISDE 1147
Cdd:COG4932    158 NGASVTDSVTLKKVDDGDTGKPLPGATFTLY--DSDGTL---VKTVTTDADGKYTFTDLPPGTYTLTETKAPEGYVLDTK 232

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192940763 1148 LKNGKKIKLEADKEGQEVATLKIENAVPE--ISFNKVDIK-GKALAGAVFAIKNEDsryynglkadktvkwaerGEISAD 1224
Cdd:COG4932    233 DPTGATITVTVNAGGTVTVTLKNTPKYTKgsVTVTKTDADtGEPLAGATFTLTDAD------------------GNTVVT 294

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192940763 1225 TKTALTsDENGKVTVKGLPVGEYQLVELSAPDGYEKSDKTIDFEVVNKDGQiklkDAIADVENEATQFVDIPIEKVwNDK 1304
Cdd:COG4932    295 TTVTVT-DADGSYTFTDLPPGTYTVTETKAPAGYDLDGEAVKVTITAGQTT----TVTVTNGNNEVKTGSVTLTKV-DAD 368

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192940763 1305 DNQDGIRPVKVTVElhadgKASGKTV-ELNTENDWKASFKKLRKTDastkeeikYTVKEVDPDKNYKSDVT--------G 1375
Cdd:COG4932    369 DGEAPLAGAEFTLT-----DADGTVVaTITTDADGTASFKGLAPGT--------YTLTETKAPEGYTLDSTpitvtvtdG 435

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192940763 1376 TMTGGFKITNSYAPKKTEVSVKKAWDDKDNQDGVRPESIKVQLYAGDKKVGEEVELNAANEWTTTWKDLDLKDKGQTIDY 1455
Cdd:COG4932    436 GTGAIDTITNERKKGSVQVTKVDAPLAGATFTLTDADGTVVTLTTDADLAGATFEADGKVVTTTDASGKYTFKNLPPGTY 515

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192940763 1456 TVKEVGETNGYKVEVTGNAKDGYTLTNSHTPATVDISGTKTWEDNDNQDGKRPKAITVRLLADGKEVDSKEVTAETNWTY 1535
Cdd:COG4932    516 TDAGGSATVITDDTDGTVGDEATGTDPEVTVTGKSTTTTPDVALLTNLGTTEDALTSLAKTGDEVGKGLTLTTTTTVDTL 595

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192940763 1536 EFTGLDKYKSGNEIRYTIQEVSVPEYSSEVEEFDVTNTHTPGKTSVNVVKAWDDADNQDGVRPDQIKVVLVADGVVTDQV 1615
Cdd:COG4932    596 DTNATEKTETVTVTAQLIGVKTTKLTDTTDPKGGTVEEATTTGGTANTGKTGTDLTDDTTVTSTTNTATSVEDTTDVDNK 675


                   ....*..
gi 1192940763 1616 KTLNAAN 1622
Cdd:COG4932    676 DAFTGGT 682
SpaA pfam17802
Prealbumin-like fold domain; This entry contains a prealbumin-like domain from a wide variety ...
 1185-1273 1.18e-12

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: 64.53  E-value: 1.18e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192940763 1185 KGKALAGAVFAIKNEDsryynglkadktvkwaerGEISADTKTALTSDENGKVTVKGLPVGEYQLVELSAPDGYEKSDKT 1264
Cdd:pfam17802    2 TGKPLAGAEFTLYDAD------------------GTVDGKVVGTLTTDEDGKATFDGLPPGTYTLKETKAPDGYVLDDTP 63


                   ....*....
gi 1192940763 1265 IDFEVVNKD 1273
Cdd:pfam17802   64 IEFTVTEDG 72
SpaA pfam17802
Prealbumin-like fold domain; This entry contains a prealbumin-like domain from a wide variety ...
 1085-1147 8.80e-10

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: 56.44  E-value: 8.80e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1192940763 1085 DNKTPLKGAELELWSVDkDGKKQQIVRSGVTNKKGELKFGNLRATNYLLVETKAPAGYTISDE 1147
Cdd:pfam17802    1 DTGKPLAGAEFTLYDAD-GTVDGKVVGTLTTDEDGKATFDGLPPGTYTLKETKAPDGYVLDDT 62
Collagen_bind pfam05737
Collagen binding domain; The domain fold is a jelly-roll, composed of two antiparallel ...
 918-1047 3.73e-08

Collagen binding domain; The domain fold is a jelly-roll, composed of two antiparallel beta-sheets and two short alpha-helices. A groove on beta-sheet I exhibited the best surface complementarity to the collagen. This site partially overlaps with the peptide sequence previously shown to be critical for collagen binding. Recombinant proteins containing single amino acid mutations designed to disrupt the surface of the putative binding site exhibited significantly lower affinities for collagen.


Pssm-ID: 283410 [Multi-domain]  Cd Length: 129  Bit Score: 53.90  E-value: 3.73e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192940763  918 FVDKSGKQDPNNANYVTWAVTINPSQSTMSNVVITDTPSINQVLAEDSFAIYgtkvdqAGNITKDASVVLGKGKDYTVdi 997
Cdd:pfam05737    2 AIYKVGWVDAENNSLIHWTVRINYALQNIENAVLTDFIGEGQNLVFDSIEVY------ELNYKKDGEVVSGDKEYPLY-- 73

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1192940763  998 ETNNEIGQQVATIKMNGTIDKAYIMEYKALIMpENNGENTLTNKISIKGD 1047
Cdd:pfam05737   74 QTIDLDTDNGFTVTFGDTIDSAYIISYTTTIT-DGGKSQSYDNKATLNGD 122
iso_D2_wall_anc NF033902
SpaH/EbpB family LPXTG-anchored major pilin; Members of this family are pilin major subunits ...
 919-1179 4.26e-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: 58.23  E-value: 4.26e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192940763  919 VDKSGKQDPNNANYVTWAVTI------NPSQSTMSNVVITDTpsinqvlAEDSFAIYGTKVDQAGNITKDASVVLGKGKD 992
Cdd:NF033902   211 KDVTDAVGNGVGDTITYTITApvpkidANTLDDFKGFTVTDT-------LDTRLDEVAGVVKSVKVGGTGLTATLTVTTD 283

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192940763  993 YTVDieTNNEIGQQVATIKMNGTIDKAYIMEYKALIM----------PENNGENTLTNKISIK------GDGQKEVEGNT 1056
Cdd:NF033902   284 YTVT--TDGLTADQKVTVTFTEAGLAKLAAAKNVKVTvtfktkvtktAKGGTNGEITNKAGLIpnnpgpNTPEPTTPGTP 361

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192940763 1057 EESTKVVVSIGTgegskssVNIVKVDADDNKTPLKGAELELWSVDKDGKKQQIVRSG---------------------VT 1115
Cdd:NF033902   362 DPTPTVKTYFGK-------LKIKKVDADDTSKKLKGAEFKVYACEADAAAACVNAIGingkttfttgadgtvsidglhVT 434

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1192940763 1116 NKKGELKFGNLRATNYLLVETKAPAGYTISDELKNGKKIKLEADKEGQEVATLKIENAVPEISF 1179
Cdd:NF033902   435 DLEDGASVKAAAGKDYCLVETKAPAGYVLPPKPVEVTVVKVTVTAATTADVKNTVVNNKKTVPN 498
Collagen_bind pfam05737
Collagen binding domain; The domain fold is a jelly-roll, composed of two antiparallel ...
 784-901 2.52e-04

Collagen binding domain; The domain fold is a jelly-roll, composed of two antiparallel beta-sheets and two short alpha-helices. A groove on beta-sheet I exhibited the best surface complementarity to the collagen. This site partially overlaps with the peptide sequence previously shown to be critical for collagen binding. Recombinant proteins containing single amino acid mutations designed to disrupt the surface of the putative binding site exhibited significantly lower affinities for collagen.


Pssm-ID: 283410 [Multi-domain]  Cd Length: 129  Bit Score: 42.73  E-value: 2.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192940763  784 KGGAYNAQNK-HITWTTKVNYTQDALKGAMITDPIIGNQDYVDGSAKLYEVkiiangNVSRGAEVTNADIAYDSASKTVT 862
Cdd:pfam05737    5 KVGWVDAENNsLIHWTVRINYALQNIENAVLTDFIGEGQNLVFDSIEVYEL------NYKKDGEVVSGDKEYPLYQTIDL 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1192940763  863 AKLPDG--------NKAYDLVFETSLEGKVIDQsQYKNTATYKNGAT 901
Cdd:pfam05737   79 DTDNGFtvtfgdtiDSAYIISYTTTITDGGKSQ-SYDNKATLNGDNI 124
LPXTG_anchor TIGR01167
LPXTG-motif cell wall anchor domain; This model describes the LPXTG motif-containing region ...
 1885-1917 6.34e-04

LPXTG-motif cell wall anchor domain; This model describes the LPXTG motif-containing region found at the C-terminus of many surface proteins of Streptococcus and Streptomyces species. Cleavage between the Thr and Gly by sortase or a related enzyme leads to covalent anchoring at the new C-terminal Thr to the cell wall. Hits that do not lie at the C-terminus or are not found in Gram-positive bacteria are probably false-positive. A common feature of this proteins containing this domain appears to be a high proportion of charged and zwitterionic residues immediatedly upstream of the LPXTG motif. This model differs from other descriptions of the LPXTG region by including a portion of that upstream charged region. [Cell envelope, Other]


Pssm-ID: 273478 [Multi-domain]  Cd Length: 34  Bit Score: 39.00  E-value: 6.34e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1192940763 1885 PQTGETSDWFISMIGLLLIvtAGAIYLLKYKRR 1917
Cdd:TIGR01167    3 PKTGESGNSLLLLLGLLLL--GLGGLLLRKRKK 33
iso_D2_wall_anc NF033902
SpaH/EbpB family LPXTG-anchored major pilin; Members of this family are pilin major subunits ...
 1177-1290 2.71e-03

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: 42.44  E-value: 2.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192940763 1177 ISFNKVD--IKGKALAGAVFAIknedsryyngLKADKTVKWAERGEISADTKTALTSDENGKVTVKGLPVGEYQ------ 1248
Cdd:NF033902   374 LKIKKVDadDTSKKLKGAEFKV----------YACEADAAAACVNAIGINGKTTFTTGADGTVSIDGLHVTDLEdgasvk 443

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1192940763 1249 --------LVELSAPDGYEKSDKTIDFEVVNKDgqiKLKDAIADVENEAT 1290
Cdd:NF033902   444 aaagkdycLVETKAPAGYVLPPKPVEVTVVKVT---VTAATTADVKNTVV 490
RrgB_K2N_iso_D2 TIGR04226
fimbrial isopeptide formation D2 domain; The Streptococcus Pneumoniae pilus backbone protein, ...
 658-739 7.10e-03

fimbrial isopeptide formation D2 domain; The Streptococcus Pneumoniae pilus backbone protein, RrgB, has three tandem domains with Lys-to-Asn isopeptide bonds, but these three regions are extremely divergent in sequence. This model represents the homology domain family of the D2 domain. It occurs just once in many surface proteins but up to twenty times in some pilin subunit proteins. Three of every four members have the typical Gram-positive C-terminal motif, LPXTG, although in many cases this motif may be involved in pilin subunit cross-linking rather than cell wall attachment. Proteins with this domain include fimbrial proteins with lectin-like adhesion functions, and the majority of characterized members are involved in surface adhesion to host structures.


Pssm-ID: 275067 [Multi-domain]  Cd Length: 124  Bit Score: 38.40  E-value: 7.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1192940763  658 KINWTITInKFKYEMANWY---LEDTLSKNLTLDPDSIVLkeQGGKTLVKDIDYKVTmDGQKFKVEFLGD-LKKDTDKTY 733
Cdd:TIGR04226   22 EVTYTITT-TVPADIADYKsfvITDTLDDGLTYKGSVKVT--VDGKTLTVDTDYTVT-DGQTVTVTFTDAgLKKLAGKKI 97


                   ....*.
gi 1192940763  734 VLTYTT 739
Cdd:TIGR04226   98 TVTYTA 103
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH