GenomeNet

Database: UniProt
Entry: F8QQL4_AMPCA
LinkDB: F8QQL4_AMPCA
Original site: F8QQL4_AMPCA 
ID   F8QQL4_AMPCA            Unreviewed;       447 AA.
AC   F8QQL4;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   22-FEB-2023, entry version 51.
DE   RecName: Full=Tubulin beta chain {ECO:0000256|ARBA:ARBA00013288, ECO:0000256|RuleBase:RU000352};
GN   Name=bTub {ECO:0000313|EMBL:ADV03060.1};
OS   Amphidinium carterae (Dinoflagellate).
OC   Eukaryota; Sar; Alveolata; Dinophyceae; Amphidiniales; Amphidiniaceae;
OC   Amphidinium.
OX   NCBI_TaxID=2961 {ECO:0000313|EMBL:ADV03060.1};
RN   [1] {ECO:0000313|EMBL:ADV03060.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CCMP1314 {ECO:0000313|EMBL:ADV03060.1};
RX   PubMed=21629701; DOI=10.1371/journal.pone.0019933;
RA   Zhang H., Campbell D.A., Sturm N.R., Dungan C.F., Lin S.;
RT   "Spliced Leader RNAs, Mitochondrial Gene Frameshifts and Multi-Protein
RT   Phylogeny Expand Support for the Genus Perkinsus as a Unique Group of
RT   Alveolates.";
RL   PLoS ONE 6:E19933-E19933(2011).
CC   -!- FUNCTION: Tubulin is the major constituent of microtubules, a cylinder
CC       consisting of laterally associated linear protofilaments composed of
CC       alpha- and beta-tubulin heterodimers. Microtubules grow by the addition
CC       of GTP-tubulin dimers to the microtubule end, where a stabilizing cap
CC       forms. Below the cap, tubulin dimers are in GDP-bound state, owing to
CC       GTPase activity of alpha-tubulin. {ECO:0000256|RuleBase:RU000352}.
CC   -!- SUBUNIT: Dimer of alpha and beta chains. A typical microtubule is a
CC       hollow water-filled tube with an outer diameter of 25 nm and an inner
CC       diameter of 15 nM. Alpha-beta heterodimers associate head-to-tail to
CC       form protofilaments running lengthwise along the microtubule wall with
CC       the beta-tubulin subunit facing the microtubule plus end conferring a
CC       structural polarity. Microtubules usually have 13 protofilaments but
CC       different protofilament numbers can be found in some organisms and
CC       specialized cells. {ECO:0000256|RuleBase:RU000352}.
CC   -!- SIMILARITY: Belongs to the tubulin family.
CC       {ECO:0000256|ARBA:ARBA00009636, ECO:0000256|RuleBase:RU000352}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; GU373022; ADV03060.1; -; mRNA.
DR   AlphaFoldDB; F8QQL4; -.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:InterPro.
DR   GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
DR   CDD; cd02187; beta_tubulin; 1.
DR   Gene3D; 1.10.287.600; Helix hairpin bin; 1.
DR   Gene3D; 3.30.1330.20; Tubulin/FtsZ, C-terminal domain; 1.
DR   Gene3D; 3.40.50.1440; Tubulin/FtsZ, GTPase domain; 1.
DR   InterPro; IPR013838; Beta-tubulin_BS.
DR   InterPro; IPR002453; Beta_tubulin.
DR   InterPro; IPR008280; Tub_FtsZ_C.
DR   InterPro; IPR000217; Tubulin.
DR   InterPro; IPR037103; Tubulin/FtsZ-like_C.
DR   InterPro; IPR018316; Tubulin/FtsZ_2-layer-sand-dom.
DR   InterPro; IPR036525; Tubulin/FtsZ_GTPase_sf.
DR   InterPro; IPR023123; Tubulin_C.
DR   InterPro; IPR017975; Tubulin_CS.
DR   InterPro; IPR003008; Tubulin_FtsZ_GTPase.
DR   PANTHER; PTHR11588; TUBULIN; 1.
DR   PANTHER; PTHR11588:SF429; TUBULIN BETA-1 CHAIN-RELATED; 1.
DR   Pfam; PF00091; Tubulin; 1.
DR   Pfam; PF03953; Tubulin_C; 1.
DR   PRINTS; PR01163; BETATUBULIN.
DR   PRINTS; PR01161; TUBULIN.
DR   SMART; SM00864; Tubulin; 1.
DR   SMART; SM00865; Tubulin_C; 1.
DR   SUPFAM; SSF55307; Tubulin C-terminal domain-like; 1.
DR   SUPFAM; SSF52490; Tubulin nucleotide-binding domain-like; 1.
DR   PROSITE; PS00227; TUBULIN; 1.
DR   PROSITE; PS00228; TUBULIN_B_AUTOREG; 1.
PE   2: Evidence at transcript level;
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|RuleBase:RU000352};
KW   Microtubule {ECO:0000256|ARBA:ARBA00022701, ECO:0000256|RuleBase:RU000352};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU000352}.
FT   DOMAIN          47..244
FT                   /note="Tubulin/FtsZ GTPase"
FT                   /evidence="ECO:0000259|SMART:SM00864"
FT   DOMAIN          246..383
FT                   /note="Tubulin/FtsZ 2-layer sandwich"
FT                   /evidence="ECO:0000259|SMART:SM00865"
FT   REGION          423..447
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        428..447
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   447 AA;  50189 MW;  F311F7728A5F530A CRC64;
     MRELVHIQGG QCGNQIGAKF WEVISDEHGI DPTGTYHGDS DLQLERINVY YNEATGGRYV
     PRAVLMDLEP GTMDSVRAGP FGQLFRPDNF VFGQTGAGNN WAKGHYTEGA ELIDSVLDVV
     RKEAEGCDCL QGFQLCHSLG GGTGAGMGTL LISKVREEYP DRIMETFSII PSPKVSDTVV
     EPYNAVLSFH QLVENADECM LLDNEALYDI CFRTLKLTTP TYGDLNHLVS MAISGVTTCL
     RFPGQLNCDL RKIAVNLIPF PRLHFFMTGF APLTSRGSQQ YRALTVPELT QQMFDAKNMM
     CAADPRHGRY LTAAALFRGR MSTKEVDEQM LNVQNKNSSY FVEWIPNNMK CGVCDIPPKG
     LKMAVAFLGN TTAIQEMFKR VAEYFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS
     EYQQYQDATA EEEGEFDEEE GEYDMQP
//
DBGET integrated database retrieval system