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Database: UniProt
Entry: A0A2V3J2W4_9FLOR
LinkDB: A0A2V3J2W4_9FLOR
Original site: A0A2V3J2W4_9FLOR 
ID   A0A2V3J2W4_9FLOR        Unreviewed;       453 AA.
AC   A0A2V3J2W4;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=Tubulin beta chain {ECO:0000256|RuleBase:RU000352};
GN   ORFNames=BWQ96_01571 {ECO:0000313|EMBL:PXF48719.1};
OS   Gracilariopsis chorda.
OC   Eukaryota; Rhodophyta; Florideophyceae; Rhodymeniophycidae; Gracilariales;
OC   Gracilariaceae; Gracilariopsis.
OX   NCBI_TaxID=448386 {ECO:0000313|EMBL:PXF48719.1, ECO:0000313|Proteomes:UP000247409};
RN   [1] {ECO:0000313|EMBL:PXF48719.1, ECO:0000313|Proteomes:UP000247409}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SKKU-2015 {ECO:0000313|EMBL:PXF48719.1,
RC   ECO:0000313|Proteomes:UP000247409};
RC   TISSUE=Whole body {ECO:0000313|EMBL:PXF48719.1};
RX   PubMed=29688518; DOI=10.1093/molbev/msy081;
RA   Lee J., Yang E.C., Graf L., Yang J.H., Qiu H., Zel Zion U., Chan C.X.,
RA   Stephens T.G., Weber A.P.M., Boo G.H., Boo S.M., Kim K.M., Shin Y.,
RA   Jung M., Lee S.J., Yim H.S., Lee J.H., Bhattacharya D., Yoon H.S.;
RT   "Analysis of the draft genome of the red seaweed Gracilariopsis chorda
RT   provides insights into genome size evolution in Rhodophyta.";
RL   Mol. Biol. Evol. 0:0-0(2018).
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PXF48719.1}.
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DR   EMBL; NBIV01000012; PXF48719.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2V3J2W4; -.
DR   STRING; 448386.A0A2V3J2W4; -.
DR   Proteomes; UP000247409; Unassembled WGS sequence.
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; 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; 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.
PE   3: Inferred from homology;
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000247409}.
FT   DOMAIN          49..246
FT                   /note="Tubulin/FtsZ GTPase"
FT                   /evidence="ECO:0000259|SMART:SM00864"
FT   DOMAIN          248..385
FT                   /note="Tubulin/FtsZ 2-layer sandwich"
FT                   /evidence="ECO:0000259|SMART:SM00865"
FT   REGION          430..453
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        434..453
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   453 AA;  50438 MW;  9D1F6F1C23A66526 CRC64;
     MTRSIVSLQA GQCGNQVGAN FWEGISAEHG IDAEGAFAGD KPDQQLERIS VYYNESSNGR
     YVPRAAMVDL EPGVIDFIKN SSKGRLFRPD NFVYGQSGAG NNWAKGHYTE GAELVEMCLD
     VIRREAETCD VLQGFQVTHS LGGGTGSGMG TLLVSKIREE YPDRMMCTYS VLPSPKVSNT
     VVEPYNCTLS IHQLVENADA VFAIDNEALF NICQRSLNVD QPSYTHLNRL ISSVMSGITC
     SLRFPGQLNA DLRKLAVNLI PFPRLHFFAV GHAPLASPDS HSYRSLTVPE LAGQMFDRNN
     MMAEVDPREG RYLTAAVYFR GKVSTKEVED EMALMQSKNS AYFVEWIPHN IKTSVCDIPA
     KGEKISSAFI GNTTAIQSIF LRVGDQFRSM FKRKAFLHWY KGEGMDELEF TEAESNMADL
     VSEYQQYTDA TAEQPEEEFV DDYTNGVEDV EEE
//
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