BASE   PART 1   PART 2  
Superfamily : 49401 [ Bacterial adhesins ]
Class : All beta proteins
Fold : Common fold of diphtheria toxin/transcription factors/cytochrome f
# of Members : 5
Superposed Structure
solvent inaccessible: UPPER CASE X
solvent accesible: lower case x
alpha helix: red x
beta strand: blue x
3 - 10 helix: maroon x
hydrogen bond to main chain amide: bold x
hydrogen bond to mainchain carbonyl: underline x
disulphide bond: cedilla
positive phi: italic x
 
                             10        20        30        40        50  
d1n67a2  ( 370 )      ekygkfynLSIKGtIdqidktnntYrQTIyVNPsGdnViaPvLTgNlk
d1zk5a-  (   1 )                       aVsf-igs-teNdVgpsqgsysstnlpfvY-
d4x5pa-  (   1 )              FaÇktangtaipi-gGgsanvyvnla-pvvnvgqnlvvd-
d4z3ga1  (   0 )    awnnivFYSlgdvnsyqggnvvitqrpqFitsWrp--giAt-vtwnqçng
d5ihwa2  ( 424 )      qdpmvhgdSNIQSifTkldedkqtIeQQIYVNplkksAtnTkVdIAGS
                                bbb    bb      bbbbbb      bb    bbb  

                             60        70        80        90        100 
d1n67a2  ( 418 )    p--------ntdSNAlIdqqnTsIkVykVdna-ad-LsesyfV-npenfe
d1zk5a-  (  34 )    --tghnIGyq-nanVWIsggfÇVGLdGkVdlpv--vgsld----------
d4x5pa-  (  38 )    --lstqifÇh-ndypeti-tDyvtlqrGsAy-------------------
d4z3ga1  (  47 )    pe----fAdgswaYyrey-iAWvvFpkkvmtkngyplf--ievhnkgsWs
d5ihwa2  ( 472 )    qVddyGniklgngsTiIdq-nTeIkVykVn-s-dqqLpqsNrIydfsqYe
                           b              bbbbbbb                     

                             110       120       130       140       150 
d1n67a2  ( 457 )    dvtnsV--nitfp----npnQYkVeFntpddqIt---tPYiVvVnGhIdp
d1zk5a-  (  70 )    -------gqsIYGLteeVGLlIwMGdtnysrGtaMsgnswenVfsGwçVg
d4x5pa-  (  65 )    ------------ggvlsnFsgtvkYsg-----ssypFpttsetprvvYns
d4z3ga1  (  90 )    eentgdn------------------------------dSyFFlkgykwdq
d5ihwa2  ( 519 )    dVtsqFdnkksfs-----nnvAtLdFg----dIn---sAyIIkVvSkYtp
                                        bbbbb       b       bbbbbbbb  

                             160       170       180       190       200 
d1n67a2  ( 498 )    ns--------------k--gdLALrSTLYGynsn------iiWrSMSWDN
d1zk5a-  ( 113 )    n---------------yvstQGLSVhVrPVilnssaqysVqk-tsIGsIr
d4x5pa-  (  98 )    r-----------------tdkpWpvalyltPvssAggvAikagsliAvli
d4z3ga1  ( 110 )    rafdtanlçqkpgettrltekfddiiFkvalpadlplgdysvtipYtSGi
d5ihwa2  ( 557 )    ts--------------dgeldIAQGTsMrTtdky------gyynyAGysn
                                         b  bbbbbbb            bbbbbbb

                             210       220       230       240 
d1n67a2  ( 526 )    evafnngsgsgdgidkpvvPeqPdepgeiepiPe      
d1zk5a-  ( 149 )    Mrpy-ngssag-----------svqttVnFsL-npFtLnd
d4x5pa-  ( 131 )    lrqtnnynsdd------------fqFvWniyAnndvvvpt
d4z3ga1  ( 160 )    qrHFAsyl---gArfkipynvAktlpreneMlFlFknigg
d5ihwa2  ( 587 )    fivts                                   
                    bbb
 

 

Domain IDNameFamilySourceDomainSTRING-DB
Clumping factor AFibrinogen-binding domainStaphylococcus aureus [TaxId: 1280]view
automated matchesF17c-type adhesinEscherichia coli [TaxId: 562]view
Mannose-specific adhesin FimH, N-terminal domainPilus subunitsEscherichia coli [TaxId: 83333]view
automated matchesPapG adhesin receptor-binding domainEscherichia coli [TaxId: 562]view
automated matchesautomated matchesStaphylococcus aureus [TaxId: 282459]view

 

No outliers

FeatureDownload
Superfamily
Distance Matrix
Conserved Interactions
Cusp Results
Alistat - Alignment Statistics
SMotif - Conserved Structural Motifs
MeanRMS
PCSSE Details
Absolutely Conserved Residues
Highly Conserved Residues

 

10 20 30 40 50 60 70 80 90 100 110 120 130 140 150 160 170 180 190 200 210 220 230 240
- - E K Y G K F Y N L S I K G T I D Q I D K T N N T Y R Q T I Y V N P S G D N V I A P V L T G N L K P - - - - - - - - N T D S N A L I D Q Q N T S I K V Y K V D N A - A D - L S E S Y F V - N P E N F E D V T N S V - - N I T F P - - - - N P N Q Y K V E F N T P D D Q I T - - - T P Y I V V V N G H I D P N S - - - - - - - - - - - - - - K - - G D L A L R S T L Y G Y N S N - - - - - - I I W R S M S W D N E V A F N N G S G S G D G I D K P V V P E Q P D E P G E I E P I P E - - - - - -
- - - - - - - - - - - - - - - - - - - A V S F - I G S - T E N D V G P S Q G S Y S S T N L P F V Y - - - T G H N I G Y Q - N A N V W I S G G F C V G L D G K V D L P V - - V G S L D - - - - - - - - - - - - - - - - - G Q S I Y G L T E E V G L L I W M G D T N Y S R G T A M S G N S W E N V F S G W C V G N - - - - - - - - - - - - - - - Y V S T Q G L S V H V R P V I L N S S A Q Y S V Q K - T S I G S I R M R P Y - N G S S A G - - - - - - - - - - - S V Q T T V N F S L - N P F T L N D
- - - - - - - - - - F A C K T A N G T A I P I - G G G S A N V Y V N L A - P V V N V G Q N L V V D - - - L S T Q I F C H - N D Y P E T I - T D Y V T L Q R G S A Y - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - G G V L S N F S G T V K Y S G - - - - - S S Y P F P T T S E T P R V V Y N S R - - - - - - - - - - - - - - - - - T D K P W P V A L Y L T P V S S A G G V A I K A G S L I A V L I L R Q T N N Y N S D D - - - - - - - - - - - - F Q F V W N I Y A N N D V V V P T
A W N N I V F Y S L G D V N S Y Q G G N V V I T Q R P Q F I T S W R P - - G I A T - V T W N Q C N G P E - - - - F A D G S W A Y Y R E Y - I A W V V F P K K V M T K N G Y P L F - - I E V H N K G S W S E E N T G D N - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - D S Y F F L K G Y K W D Q R A F D T A N L C Q K P G E T T R L T E K F D D I I F K V A L P A D L P L G D Y S V T I P Y T S G I Q R H F A S Y L - - - G A R F K I P Y N V A K T L P R E N E M L F L F K N I G G
- - Q D P M V H G D S N I Q S I F T K L D E D K Q T I E Q Q I Y V N P L K K S A T N T K V D I A G S Q V D D Y G N I K L G N G S T I I D Q - N T E I K V Y K V N - S - D Q Q L P Q S N R I Y D F S Q Y E D V T S Q F D N K K S F S - - - - - N N V A T L D F G - - - - D I N - - - S A Y I I K V V S K Y T P T S - - - - - - - - - - - - - - D G E L D I A Q G T S M R T T D K Y - - - - - - G Y Y N Y A G Y S N F I V T S - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - -

 

 

 

 

 

Member Chain UniProtKB GO term
d1n67a2 A Q53653 GO:0005618
d1n67a2 A Q53653 GO:0007155
d1n67a2 A Q53653 GO:0005618
d1n67a2 A Q53653 GO:0007155
d1n67a2 A Q53653 GO:0005618
d1n67a2 A Q53653 GO:0007155
d1n67a2 A Q53653 GO:0005618
d1n67a2 A Q53653 GO:0007155
 
Contact: Prof. R. Sowdhamini - mini@ncbs.res.in