ID I6LDI6_PHYDR Unreviewed; 312 AA.
AC I6LDI6;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Tubulin beta chain {ECO:0000256|RuleBase:RU000352};
DE Flags: Fragment;
OS Phytophthora drechsleri.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4794 {ECO:0000313|EMBL:AAW63441.1};
RN [1] {ECO:0000313|EMBL:AAW63441.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SCRP232 {ECO:0000313|EMBL:AAW63441.1};
RX PubMed=20943142;
RA Mostowfizadeh-Ghalamfarsa R., Panabieres F., Banihashemi Z., Cook D.E.L.;
RT "Phylogenetic relationship of Phytophthora cryptogea Pethybr. & Laff and P.
RT drechsleri Tucker.";
RL Fungal Biol. 114:325-339(2010).
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; AY659488; AAW63441.1; -; Genomic_DNA.
DR AlphaFoldDB; I6LDI6; -.
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}.
FT DOMAIN 1..140
FT /note="Tubulin/FtsZ GTPase"
FT /evidence="ECO:0000259|SMART:SM00864"
FT DOMAIN 142..279
FT /note="Tubulin/FtsZ 2-layer sandwich"
FT /evidence="ECO:0000259|SMART:SM00865"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAW63441.1"
FT NON_TER 312
FT /evidence="ECO:0000313|EMBL:AAW63441.1"
SQ SEQUENCE 312 AA; 35068 MW; FBB7B333B3DC1415 CRC64;
HYTEGAELID SVLDVVRKEA ESCDCLQGFQ ITHSLGGGTG SGMGTLLISK IREEYPDRIM
CTYSVCPSPK VSDTVVEPYN ATLSVHQLVE NADEVMCLDN EALYDICFRT LKLTTPTYGD
LNHLVCAAMS GITTCLRFPG QLNSDLRKLA VNLIPFPRLH FFMIGFAPLT SRGSQQYRAL
TVPELTQQQF DAKNMMCAAD PRHGRYLTAA CMFRGRMSTK EVDEQMLNVQ NKNSSYFVEW
IPNNIKASVC DIPPKGLKMS TTFIGNSTAI QEMFKRVSEQ FTAMFRRKAF LHWYTGEGMD
EMEFTEAESN MS
//
