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}.
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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
//