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Protein

Tubulin alpha chain

Gene

TUB1

Organism
Colletotrichum orbiculare (strain 104-T / ATCC 96160 / CBS 514.97 / LARS 414 / MAFF 240422) (Cucumber anthracnose fungus) (Colletotrichum lagenarium)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei454Involved in polymerizationBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi142 – 148GTPSequence analysis7

GO - Molecular functioni

GO - Biological processi

Keywordsi

LigandGTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Tubulin alpha chain
Alternative name(s):
Alpha-tubulin
Gene namesi
Name:TUB1
ORF Names:Cob_05533
OrganismiColletotrichum orbiculare (strain 104-T / ATCC 96160 / CBS 514.97 / LARS 414 / MAFF 240422) (Cucumber anthracnose fungus) (Colletotrichum lagenarium)
Taxonomic identifieri1213857 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeGlomerellalesGlomerellaceaeColletotrichum
Proteomesi
  • UP000014480 Componenti: Unassembled WGS sequence

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000481741 – 454Tubulin alpha chainAdd BLAST454

Proteomic databases

PRIDEiQ9C413.

Interactioni

Subunit structurei

Dimer of alpha and beta chains. A typical microtubule is a hollow water-filled tube with an outer diameter of 25 nm and an inner diameter of 15 nM. Alpha-beta heterodimers associate head-to-tail to form protofilaments running lengthwise along the microtubule wall with the beta-tubulin subunit facing the microtubule plus end conferring a structural polarity. Microtubules usually have 13 protofilaments but different protofilament numbers can be found in some organisms and specialized cells.

Family & Domainsi

Sequence similaritiesi

Belongs to the tubulin family.Curated

Phylogenomic databases

OrthoDBiEOG092C2JRV.

Family and domain databases

Gene3Di3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.
InterProiView protein in InterPro
IPR002452. Alpha_tubulin.
IPR008280. Tub_FtsZ_C.
IPR000217. Tubulin.
IPR018316. Tubulin/FtsZ_2-layer-sand-dom.
IPR037103. Tubulin/FtsZ_C_sf.
IPR036525. Tubulin/FtsZ_GTPase_sf.
IPR017975. Tubulin_CS.
IPR003008. Tubulin_FtsZ_GTPase.
PANTHERiPTHR11588. PTHR11588. 1 hit.
PfamiView protein in Pfam
PF00091. Tubulin. 1 hit.
PF03953. Tubulin_C. 1 hit.
PRINTSiPR01162. ALPHATUBULIN.
PR01161. TUBULIN.
SMARTiView protein in SMART
SM00864. Tubulin. 1 hit.
SM00865. Tubulin_C. 1 hit.
SUPFAMiSSF52490. SSF52490. 1 hit.
SSF55307. SSF55307. 1 hit.
PROSITEiView protein in PROSITE
PS00227. TUBULIN. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9C413-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKGEILHLHL GQAGTQLGNS AWELYLLEHG LGHDGRPDPS AKDVVDGGSY
60 70 80 90 100
ETFFTETSNG KYVPRSLFVD LDPSPIDEIR TGGYRQLFHP ELLISGKEDA
110 120 130 140 150
ANNYARGHYT IGKEMVDNVI DRIRRVADNC HSLQGFLIFH SFGGGTGSGF
160 170 180 190 200
GALLLERLST EYGKKSKLEF AVYPAPRVST AVVEPYNAVL STHSTIENSD
210 220 230 240 250
CTFLVDNEAV YDICRRNLDI PRPSYDHLNR LIAQVVSSIT SSLRFDGALN
260 270 280 290 300
VDLNEFQTNL VPYPRIHYPL ISYAPVISAS KSAHESFKVQ ELTFQCFEPN
310 320 330 340 350
NQMVVCDPRN GKYMAVALLY RGDAVPRDCN AAIAALKAKS SFNLVEWCPT
360 370 380 390 400
GFKLGINYQK PMAVPAAPGD GGLAPVDRSV SMLSNTTAIA EAWSRLDHKF
410 420 430 440 450
DLMYSKRAFV HWYVGEGMEE GEFSEAREDL AALEKDYEEV AADSYEGDEG

EAEY
Length:454
Mass (Da):50,266
Last modified:September 18, 2013 - v2
Checksum:i6A685BFC14642AC0
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti279 – 280AS → GF in AAK11178 (PubMed:11686676).Curated2
Sequence conflicti291Missing in AAK11178 (PubMed:11686676).Curated1
Sequence conflicti389 – 390IA → MP in AAK11178 (PubMed:11686676).Curated2
Sequence conflicti395 – 398RLDH → KTGIT in AAK11178 (PubMed:11686676).Curated4
Sequence conflicti404 – 405YS → SA in AAK11178 (PubMed:11686676).Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF321052 Genomic DNA. Translation: AAK11178.1.
KB725738 Genomic DNA. Translation: ENH86182.1.

Genome annotation databases

EnsemblFungiiENH86182; ENH86182; Cob_05533.

Similar proteinsi

Entry informationi

Entry nameiTBA_COLOR
AccessioniPrimary (citable) accession number: Q9C413
Secondary accession number(s): N4VQM2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: September 18, 2013
Last modified: October 25, 2017
This is version 76 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families