ID Q3SEG9_PARTE Unreviewed; 608 AA.
AC Q3SEG9;
DT 11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT 11-OCT-2005, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=Alpha tubulin,putative {ECO:0000313|EMBL:CAI38955.1};
GN Name=alphaPT11 {ECO:0000313|EMBL:CAI38955.1};
OS Paramecium tetraurelia.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX NCBI_TaxID=5888 {ECO:0000313|EMBL:CAI38955.1};
RN [1] {ECO:0000313|EMBL:CAI38955.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAI38955.1};
RA Genoscope;
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CAI38955.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAI38955.1};
RA Klotz C.;
RT "Paramecium tetraurelia alpha-tubulin-related protein genes.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00011747}.
CC -!- SIMILARITY: Belongs to the tubulin family.
CC {ECO:0000256|ARBA:ARBA00009636}.
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DR EMBL; CR932118; CAI38955.1; -; Genomic_DNA.
DR AlphaFoldDB; Q3SEG9; -.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
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; 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; IPR002452; Alpha_tubulin.
DR InterPro; IPR013838; Beta-tubulin_BS.
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; IPR003008; Tubulin_FtsZ_GTPase.
DR PANTHER; PTHR11588; TUBULIN; 1.
DR PANTHER; PTHR11588:SF239; TUBULIN ALPHA CHAIN; 1.
DR Pfam; PF00091; Tubulin; 1.
DR Pfam; PF03953; Tubulin_C; 1.
DR PRINTS; PR01162; ALPHATUBULIN.
DR PRINTS; PR01161; TUBULIN.
DR SUPFAM; SSF55307; Tubulin C-terminal domain-like; 1.
DR SUPFAM; SSF52490; Tubulin nucleotide-binding domain-like; 1.
DR PROSITE; PS00228; TUBULIN_B_AUTOREG; 1.
PE 3: Inferred from homology;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 3..167
FT /note="Tubulin/FtsZ GTPase"
FT /evidence="ECO:0000259|Pfam:PF00091"
FT DOMAIN 247..376
FT /note="Tubulin/FtsZ 2-layer sandwich"
FT /evidence="ECO:0000259|Pfam:PF03953"
FT REGION 420..608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..442
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..484
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..608
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 608 AA; 69342 MW; ECFCAD7DAA869999 CRC64;
MREILQFHVG QAGIQIGNTA WELLCLEHGI QPDGSAPSSQ NLQVLFSESQ TKANVPRAAF
FDDDPLTINS LNRGPLKKVL NQNLIKLFKD DASSIWASKK ITQYDEKDRS SRAADEIVRK
MLEAADAASA IIIYHSLAGG FGSGFTCKLL QLLNDETAKT TKLTVSINYL LNLLLNPIIQ
YSLCQHFQNC QISIFFMIML LYFETPNFSH LNYMIAQTIS SISQSIRFRG TKLVDFNDMR
TNLITTPKQQ FLWTSYSPFI YTDQQHLKKP NLQNITESLF DDNGHLLSFN RLTHKYLGSS
LFFKGDCPLP ELNYVIKQIK QSEEIRFAEG TQVAYQTCVS MAQPCTLPNY PFAKYSKTAC
MLAHSTGVLQ SFESLKKRFS TLYSKRAFVS WYVGQGLEEG QFSESNESLQ QIIELYKGKH
GDGKPIEVQP KTDRKQEYGY KKEKQAQQQP QVKKTQEVKK TQDVKKNQAP KASNQITTAR
VENNDYSEDA YDQRAPARAQ QKPLKLTTND QKQSNSAKPN RIQQEDDNIV NQPQQQEDDN
QINEPQEQED INQQAIQQYD EEPVQQQEDQ QQNQDDGFGE SNNQQPKQND QKGPQANQLN
AVENISFQ
//
