Superfamily : 55116 [ Formiminotransferase domain of formiminotransferase-cyclodeaminase. ]
Class : Alpha and beta proteins (a+b)
Fold : Ferredoxin-like
# of Members : 2
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  
d1qd1a1  (   2 )    sqlVeCvPnFSeGknqevIdaIsraVa----qTpgCvlldvdsgpstnRT
d1qd1a2  ( 181 )       flLaFNINLlstreqAhrIAldLreqggrLkkVqA-iGwyldeknlA
                         b  bb     aaaaaaaaaaa          bb bbbbb    bb

                             60        70        80        90        100 
d1qd1a1  (  48 )    vYtFvg-rPed--VVeGALnAAraAyqlIdMsrhhgehpRMGALDvCPFi
d1qd1a2  ( 233 )    QVsTnLldfevtGLhtVfeeTcreAqel--------------slpvvgSq
                    bbbbbb       aaaaaaaaaaaaaa                  bbbbb

                             110       120       130       140       150 
d1qd1a1  (  95 )    pvrgVtmdeCvrCAqaFGqrLAeelgVPVYLygeAArtagrqslpaLrag
d1qd1a2  ( 269 )    Lvg----lVplkALldAAafYcekenl-fll-----------qdehrIrl
                    bb        aaaaaaaaaaaaaaa                  aaaaa  

                             160       170       180       
d1qd1a1  ( 145 )    eyeaLpekLkqaewaPDfgpsafvpsWGATVAGArk   
d1qd1a2  ( 303 )    VvnrLgLdsla----------pFkpk-----erIieylv
                    aaaaa                                  

 

 

Domain IDNameFamilySourceDomainSTRING-DB
Formiminotransferase domain of formiminotransferase-cyclodeaminase.Formiminotransferase domain of formiminotransferase-cyclodeaminase.Pig (Sus scrofa) [TaxId: 9823]view
Formiminotransferase domain of formiminotransferase-cyclodeaminase.Formiminotransferase domain of formiminotransferase-cyclodeaminase.Pig (Sus scrofa) [TaxId: 9823]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
S Q L V E C V P N F S E G K N Q E V I D A I S R A V A - - - - Q T P G C V L L D V D S G P S T N R T V Y T F V G - R P E D - - V V E G A L N A A R A A Y Q L I D M S R H H G E H P R M G A L D V C P F I P V R G V T M D E C V R C A Q A F G Q R L A E E L G V P V Y L Y G E A A R T A G R Q S L P A L R A G E Y E A L P E K L K Q A E W A P D F G P S A F V P S W G A T V A G A R K - - -
- - - F L L A F N I N L L S T R E Q A H R I A L D L R E Q G G R L K K V Q A - I G W Y L D E K N L A Q V S T N L L D F E V T G L H T V F E E T C R E A Q E L - - - - - - - - - - - - - - S L P V V G S Q L V G - - - - L V P L K A L L D A A A F Y C E K E N L - F L L - - - - - - - - - - - Q D E H R I R L V V N R L G L D S L A - - - - - - - - - - P F K P K - - - - - E R I I E Y L V

 

 

 

 

 

Member Chain UniProtKB GO term
d1qd1a1 A P53603 GO:0005542
d1qd1a1 A P53603 GO:0016740
d1qd1a1 A P53603 GO:0005542
d1qd1a1 A P53603 GO:0016740
d1qd1a2 A P53603 GO:0005542
d1qd1a2 A P53603 GO:0016740
d1qd1a2 A P53603 GO:0005542
d1qd1a2 A P53603 GO:0016740