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Database: UniProt
Entry: A0A091R6E6_MERNU
LinkDB: A0A091R6E6_MERNU
Original site: A0A091R6E6_MERNU 
ID   A0A091R6E6_MERNU        Unreviewed;       259 AA.
AC   A0A091R6E6;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Tubulin alpha chain {ECO:0000256|RuleBase:RU000352};
DE   Flags: Fragment;
GN   ORFNames=N331_05964 {ECO:0000313|EMBL:KFQ34802.1};
OS   Merops nubicus (Northern carmine bee-eater).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Coraciiformes; Meropidae; Merops.
OX   NCBI_TaxID=57421 {ECO:0000313|EMBL:KFQ34802.1, ECO:0000313|Proteomes:UP000052967};
RN   [1] {ECO:0000313|EMBL:KFQ34802.1, ECO:0000313|Proteomes:UP000052967}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N331 {ECO:0000313|EMBL:KFQ34802.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC         Evidence={ECO:0000256|ARBA:ARBA00001702};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC         Evidence={ECO:0000256|ARBA:ARBA00001702};
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; KK713443; KFQ34802.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091R6E6; -.
DR   Proteomes; UP000052967; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:InterPro.
DR   GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
DR   Gene3D; 3.40.50.1440; Tubulin/FtsZ, GTPase domain; 1.
DR   InterPro; IPR002452; Alpha_tubulin.
DR   InterPro; IPR000217; Tubulin.
DR   InterPro; IPR036525; Tubulin/FtsZ_GTPase_sf.
DR   InterPro; IPR017975; Tubulin_CS.
DR   InterPro; IPR003008; Tubulin_FtsZ_GTPase.
DR   PANTHER; PTHR11588; TUBULIN; 1.
DR   PANTHER; PTHR11588:SF278; TUBULIN ALPHA CHAIN-LIKE 3; 1.
DR   Pfam; PF00091; Tubulin; 1.
DR   PRINTS; PR01162; ALPHATUBULIN.
DR   PRINTS; PR01161; TUBULIN.
DR   SMART; SM00864; Tubulin; 1.
DR   SUPFAM; SSF52490; Tubulin nucleotide-binding domain-like; 1.
DR   PROSITE; PS00227; TUBULIN; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|RuleBase:RU000352};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
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:UP000052967}.
FT   DOMAIN          48..240
FT                   /note="Tubulin/FtsZ GTPase"
FT                   /evidence="ECO:0000259|SMART:SM00864"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFQ34802.1"
FT   NON_TER         259
FT                   /evidence="ECO:0000313|EMBL:KFQ34802.1"
SQ   SEQUENCE   259 AA;  28475 MW;  ED04776F66647951 CRC64;
     RECISVHIGQ AGVQMGNSCW ELYCLEHGIE PDGIISSSAS SGQTDSSFGT FFSESGSGKY
     VPRAIFIDLE PSVIDGIRTG TYRTLFHPEQ LISGKEDAAN NYARGHYTIG KEIIDPVVDR
     ARKMTEQCSG LQGFLVFHSF GGGTGSGFTS LLMERLSVEY SKKSKLEFSV YPAPQGDPST
     SILTTHTTLE HSDCSFMVDN EAIYDICNRN LDIERPTYTN LNRLIGQIVS SITASLRFDG
     ALNVDLTEFQ TNLVPYPRI
//
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