ID A0A3M7PCZ7_BRAPC Unreviewed; 410 AA.
AC A0A3M7PCZ7;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Tubulin beta chain {ECO:0000256|RuleBase:RU000352};
DE Flags: Fragment;
GN ORFNames=BpHYR1_024381 {ECO:0000313|EMBL:RMZ96918.1};
OS Brachionus plicatilis (Marine rotifer) (Brachionus muelleri).
OC Eukaryota; Metazoa; Spiralia; Gnathifera; Rotifera; Eurotatoria;
OC Monogononta; Pseudotrocha; Ploima; Brachionidae; Brachionus.
OX NCBI_TaxID=10195 {ECO:0000313|EMBL:RMZ96918.1, ECO:0000313|Proteomes:UP000276133};
RN [1] {ECO:0000313|EMBL:RMZ96918.1, ECO:0000313|Proteomes:UP000276133}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HYR1 {ECO:0000313|EMBL:RMZ96918.1};
RX PubMed=30375419; DOI=10.1038/s41598-018-34188-y;
RA Franch-Gras L., Hahn C., Garcia-Roger E.M., Carmona M.J., Serra M.,
RA Gomez A.;
RT "Genomic signatures of local adaptation to the degree of environmental
RT predictability in rotifers.";
RL Sci. Rep. 8:16051-16051(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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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 -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
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:RMZ96918.1}.
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DR EMBL; REGN01011776; RMZ96918.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M7PCZ7; -.
DR STRING; 10195.A0A3M7PCZ7; -.
DR Proteomes; UP000276133; 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 Hydrolase {ECO:0000313|EMBL:RMZ96918.1};
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:UP000276133}.
FT DOMAIN 13..210
FT /note="Tubulin/FtsZ GTPase"
FT /evidence="ECO:0000259|SMART:SM00864"
FT DOMAIN 212..349
FT /note="Tubulin/FtsZ 2-layer sandwich"
FT /evidence="ECO:0000259|SMART:SM00865"
FT REGION 391..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:RMZ96918.1"
SQ SEQUENCE 410 AA; 45991 MW; B556BE60E9D65F3C CRC64;
HNPSILKCRK NIDMVYFNEA TGGKYVPRCV LLDLEPGTMD SVRSGPFGQI FRPDNFVFGQ
SGAGNNWAKG HYTEGAELVD SVLDVIRKES EACDCLQGFQ LTHSLGGGTG SGMGTLLISK
IREEYPDRIM NTFSVVPSPK VSDTVVEPYN ATLSVHQLVE NTDETYCIDN EALYDICFRT
LKLTTPTYGD LNHLVSATMS GVTTCLRFPG QLNADLRKLA VNMVPFPRLH FFMPGFAPLT
SRGSQQYRSL TVPELTQQMF DAKNMMAACD PRHGRYLTVA TIFRGRMSMK EVDEQMLNVQ
NKNSSYFVEW IPNNVKTAVC DIPPRGLKMS ATFIGNSTAI QELFKRVSEQ FTAMFRRKAF
LHWYTGEGMD EMEFTEAESN MNDLVSEYQQ YQDATADEEG EAGEEEEIEA
//
