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== Exemplos ==
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'''[[PA clan]]''' - Members share a [[chymotrypsin]]-like double [[β-barrel]] fold and similar [[proteolysis]] mechanisms but sequence identity of <10%. The clan contains both [[Cysteine protease|cysteine]] and [[serine proteases]] (different [[nucleophiles]]).<ref name=merops/><ref>{{cite journal|last=Bazan|first=JF|author2=Fletterick, RJ |title=Viral cysteine proteases are homologous to the trypsin-like family of serine proteases: structural and functional implications.|journal=Proceedings of the National Academy of Sciences of the United States of America|date=November 1988|volume=85|issue=21|pages=7872–6|pmid=3186696|doi=10.1073/pnas.85.21.7872|pmc=282299}}</ref> ▼
▲'''[[ Clan PA clan]]''' . -Os Membersseus sharemembros acomparten un pregamento de [[ chymotrypsinbarril beta]] -like doubledobre de tipo [[ β-barrelquimotripsina]] folde andmecanismos similarde [[ proteolysisproteólise]] mechanismssimilares, butpero sequencea identityidentidade ofde secuencia é <10%. TheO clan containscontén bothtanto [[ Cysteinecisteína protease |cysteine]] s andcoma [[ serineserin proteasesprotease]] s ( differentdiferentes [[ nucleophilesnucleófilo]] s).<ref name=merops/><ref>{{cite journal|last=Bazan|first=JF|author2=Fletterick, RJ |title=Viral cysteine proteases are homologous to the trypsin-like family of serine proteases: structural and functional implications.|journal=Proceedings of the National Academy of Sciences of the United States of America|date=November 1988|volume=85|issue=21|pages=7872–6|pmid=3186696|doi=10.1073/pnas.85.21.7872|pmc=282299}}</ref>
'''[[α/β hydrolase|α/β hydrolase superfamily]]''' - Members share an α/β sheet, containing 8 [[beta strand|strands]] connected by [[alpha helix|helices]] with [[catalytic triad]] residues in the same order,<ref>{{cite journal |author=Carr PD, Ollis DL |title=Alpha/beta hydrolase fold: an update |journal=Protein Pept. Lett. |volume=16 |issue=10 |pages=1137–48 |year=2009 |pmid=19508187 |doi= |url=}}</ref> activities include [[proteases]], [[lipases]], [[peroxidases]], [[esterases]], [[epoxide hydrolase]]s and [[dehalogenase]]s.<ref name="pmid10607665">{{cite journal |author=Nardini M, Dijkstra BW |title=Alpha/beta hydrolase fold enzymes: the family keeps growing |journal=Curr. Opin. Struct. Biol. |volume=9 |issue=6 |pages=732–7 |date=December 1999 |pmid=10607665 |doi= 10.1016/S0959-440X(99)00037-8|url=}}</ref> ▼
▲'''[[α/β hydrolasehidrolase| superfamilia da α/β hydrolase superfamilyhidrolase]]''' . -Os Membersseus sharemembros ancomparten unha folla α/β sheet, containingque contén 8 [[ betafebra strandbeta| strandsfebras]] connectedconectadas bypor [[ alphahélice helixalfa| heliceshélices alfa]] withcon residuos de [[ catalytictríada triadcatalítica]] residues insituados thena samemesma orderorde,<ref>{{cite journal |author=Carr PD, Ollis DL |title=Alpha/beta hydrolase fold: an update |journal=Protein Pept. Lett. |volume=16 |issue=10 |pages=1137–48 |year=2009 |pmid=19508187 |doi= |url=}}</ref> activities include [[proteases]], [[lipases]], [[peroxidases]], [[esterases]], [[epoxide hydrolase]]s and [[dehalogenase]]s.<ref name="pmid10607665">{{cite journal |author=Nardini M, Dijkstra BW |title=Alpha/beta hydrolase fold enzymes: the family keeps growing |journal=Curr. Opin. Struct. Biol. |volume=9 |issue=6 |pages=732–7 |date=December 1999 |pmid=10607665 |doi= 10.1016/S0959-440X(99)00037-8|url=}}</ref>
'''[[TIM barrel|TIM barrel superfamily]]''' - Members share a large α<sub>8</sub>β<sub>8</sub> barrel structure. It is one of the most common [[protein fold]]s and the [[Monophyly|monophylicity]] of this superfamily is still contested.<ref>{{cite journal|last=Nagano|first=N|author2=Orengo, CA |author3=Thornton, JM |title=One fold with many functions: the evolutionary relationships between TIM barrel families based on their sequences, structures and functions.|journal=Journal of Molecular Biology|date=Aug 30, 2002|volume=321|issue=5|pages=741–65|pmid=12206759|doi=10.1016/s0022-2836(02)00649-6}}</ref><ref>{{cite journal|last=Farber|first=G|title=An α/β-barrel full of evolutionary trouble|journal=Current Opinion in Structural Biology|year=1993|volume=3|issue=3|pages=409–412|url=http://www.sciencedirect.com/science/article/pii/S0959440X05801149|doi=10.1016/S0959-440X(05)80114-9}}</ref> ▼
▲'''[[ TIMBarril barrel|TIM |Superfamilia barrelde superfamilybarril TIM]]''' . -Os Membersseus sharemembros acomparten unha gran estrutura largede barril α<sub>8</sub>β<sub>8</sub> barrel structure. ItÉ isun onedos ofpregamentos theproteicos mostmáis commoncomúns, [[proteinpero fold]]s and thea [[ Monophyly|monophylicitymonofilia]] of thisdesta superfamilyfamilia isaínda stillse contesteddiscute.<ref>{{cite journal|last=Nagano|first=N|author2=Orengo, CA |author3=Thornton, JM |title=One fold with many functions: the evolutionary relationships between TIM barrel families based on their sequences, structures and functions.|journal=Journal of Molecular Biology|date=Aug 30, 2002|volume=321|issue=5|pages=741–65|pmid=12206759|doi=10.1016/s0022-2836(02)00649-6}}</ref><ref>{{cite journal|last=Farber|first=G|title=An α/β-barrel full of evolutionary trouble|journal=Current Opinion in Structural Biology|year=1993|volume=3|issue=3|pages=409–412|url=http://www.sciencedirect.com/science/article/pii/S0959440X05801149|doi=10.1016/S0959-440X(05)80114-9}}</ref>
'''[[Alkaline phosphatase|Alkaline phosphatase superfamily]]''' - Members share an αβα sandwich structure<ref>{{cite web|title=SCOP|url=http://scop.mrc-lmb.cam.ac.uk/scop/data/scop.b.d.bah.A.html|accessdate=28 May 2014}}</ref> as well as performing common [[enzyme promiscuity|promiscuous reactions]] by a common mechanism.<ref>{{cite journal|last=Mohamed|first=MF|author2=Hollfelder, F |title=Efficient, crosswise catalytic promiscuity among enzymes that catalyze phosphoryl transfer.|journal=Biochimica et Biophysica Acta|date=Jan 2013|volume=1834|issue=1|pages=417–24|pmid=22885024|doi=10.1016/j.bbapap.2012.07.015}}</ref> ▼
▲'''[[ AlkalineFosfatase phosphatasealcalina| AlkalineSuperfamilia phosphataseda superfamilyfosfatase alcalina]]''' . -Os Membersseus sharemembros ancomparten αβαunha estrutura en sandwich structureαβα<ref>{{cite web|title=SCOP|url=http://scop.mrc-lmb.cam.ac.uk/scop/data/scop.b.d.bah.A.html|accessdate=28 May 2014}}</ref> ase welltamén aslevan performinga commoncabo [[ enzymepromiscuidade promiscuityencimática| promiscuousreaccións reactionspromiscuas]] bycomúns apor un commonmecanismo mechanismsimilar.<ref>{{cite journal|last=Mohamed|first=MF|author2=Hollfelder, F |title=Efficient, crosswise catalytic promiscuity among enzymes that catalyze phosphoryl transfer.|journal=Biochimica et Biophysica Acta|date=Jan 2013|volume=1834|issue=1|pages=417–24|pmid=22885024|doi=10.1016/j.bbapap.2012.07.015}}</ref>
'''[[Immunoglobulin superfamily]]''' - Members share a sandwich-like structure of two [[beta sheet|sheets]] of antiparallel [[beta strand]]s ([[immunoglobulin fold|Ig-fold]]), and are involved in recognition, binding, and [[cell adhesion|adhesion]].<ref name="pmid7932691">{{cite journal | author = Bork P, Holm L, Sander C | title = The immunoglobulin fold. Structural classification, sequence patterns and common core | journal = J. Mol. Biol. | volume = 242 | issue = 4 | pages = 309–20 |date=September 1994 | pmid = 7932691 | doi = 10.1006/jmbi.1994.1582 | url = | issn = }}</ref><ref name="pmid8574878">{{cite journal | author = Brümmendorf T, Rathjen FG | title = Cell adhesion molecules 1: immunoglobulin superfamily | journal = Protein Profile | volume = 2 | issue = 9 | pages = 963–1108 | year = 1995 | pmid = 8574878 | doi = | url = | issn = }}</ref> ▼
▲'''[[ ImmunoglobulinSuperfamilia superfamilydas inmunoglobulinas]]''' . -Os Membersseus sharemembros acomparten unha estrutura de tipo sandwich -like structureformada ofpor twodíuas [[ betafolla sheetbeta| sheets]]follas ofde antiparallelfebras beta]] [[ betaantiparalelismo strand(bioquímica)|antiparalelas]] s ([[ immunoglobulinpregamento foldde inmunoglobulina| pregamento Ig -fold]]), ande areestán involvedimplicados inno recognitionrecoñecemento, bindingunión, ande [[ celladhesión adhesioncelular| adhesionadhesión]].<ref name="pmid7932691">{{cite journal | author = Bork P, Holm L, Sander C | title = The immunoglobulin fold. Structural classification, sequence patterns and common core | journal = J. Mol. Biol. | volume = 242 | issue = 4 | pages = 309–20 |date=September 1994 | pmid = 7932691 | doi = 10.1006/jmbi.1994.1582 | url = | issn = }}</ref><ref name="pmid8574878">{{cite journal | author = Brümmendorf T, Rathjen FG | title = Cell adhesion molecules 1: immunoglobulin superfamily | journal = Protein Profile | volume = 2 | issue = 9 | pages = 963–1108 | year = 1995 | pmid = 8574878 | doi = | url = | issn = }}</ref>
'''[[Globin|Globin superfamily]]''' - Members share an 8- helix globular [[globin fold]].<ref>{{cite book|last1=Branden|first1=Carl|last2=Tooze|first2=John|title=Introduction to protein structure|date=1999|publisher=Garland Pub.|location=New York|isbn=978-0815323051|edition=2nd}}</ref><ref>{{Cite journal ▼
▲'''[[ GlobinGlobina| GlobinSuperfamilia superfamilydas globinas]]''' . -Os Membersseus sharemembros ancomparten 8- helix globularun [[ globinpregamento foldde globina]] globular de 8 hélices.<ref>{{cite book|last1=Branden|first1=Carl|last2=Tooze|first2=John|title=Introduction to protein structure|date=1999|publisher=Garland Pub.|location=New York|isbn=978-0815323051|edition=2nd}}</ref><ref>{{Cite journal
| pmid = 2926816
| year = 1989
}}</ref>
'''[[RasSuperfamilia superfamilyRas]]'''. -Os Membersseus sharemembros acomparte commonun catalyticdomino G domaincatalítico ofcomún ade 6-strandfolla beta sheetde seis febras surroundedrodeada byde 5 alphahélices helicesalfa.<ref name="pmid11701921">{{cite journal | author = Vetter IR, Wittinghofer A | title = The guanine nucleotide-binding switch in three dimensions | journal = Science | volume = 294 | issue = 5545 | pages = 1299–304 |date=November 2001 | pmid = 11701921 | doi = 10.1126/science.1062023 | url = | issn = }}</ref>
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== Recursos sobre superfamilias de proteínas ==
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