ID A0A1Q9E0P4_SYMMI Unreviewed; 684 AA.
AC A0A1Q9E0P4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Tubulin delta chain {ECO:0000256|ARBA:ARBA00014184};
DE AltName: Full=Delta-tubulin {ECO:0000256|ARBA:ARBA00030594};
GN Name=TUBA {ECO:0000313|EMBL:OLQ00991.1};
GN ORFNames=AK812_SmicGene16292 {ECO:0000313|EMBL:OLQ00991.1};
OS Symbiodinium microadriaticum (Dinoflagellate) (Zooxanthella
OS microadriatica).
OC Eukaryota; Sar; Alveolata; Dinophyceae; Suessiales; Symbiodiniaceae;
OC Symbiodinium.
OX NCBI_TaxID=2951 {ECO:0000313|EMBL:OLQ00991.1, ECO:0000313|Proteomes:UP000186817};
RN [1] {ECO:0000313|EMBL:OLQ00991.1, ECO:0000313|Proteomes:UP000186817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP2467 {ECO:0000313|EMBL:OLQ00991.1,
RC ECO:0000313|Proteomes:UP000186817};
RA Aranda M., Li Y., Liew Y.J., Baumgarten S., Simakov O., Wilson M., Piel J.,
RA Ashoor H., Bougouffa S., Bajic V.B., Ryu T., Ravasi T., Bayer T.,
RA Micklem G., Kim H., Bhak J., Lajeunesse T.C., Voolstra C.R.;
RT "Genome analysis of coral dinoflagellate symbionts highlights evolutionary
RT adaptations to a symbiotic lifestyle.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBCELLULAR LOCATION: Cell projection, cilium
CC {ECO:0000256|ARBA:ARBA00004138}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome, centriole
CC {ECO:0000256|ARBA:ARBA00004114}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the tubulin family.
CC {ECO:0000256|ARBA:ARBA00009636}.
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:OLQ00991.1}.
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DR EMBL; LSRX01000308; OLQ00991.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q9E0P4; -.
DR OrthoDB; 1206011at2759; -.
DR Proteomes; UP000186817; Unassembled WGS sequence.
DR GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
DR GO; GO:0005929; C:cilium; IEA:UniProtKB-SubCell.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:InterPro.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:InterPro.
DR GO; GO:0030030; P:cell projection organization; IEA:UniProtKB-KW.
DR GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd02186; alpha_tubulin; 1.
DR CDD; cd02248; Peptidase_C1A; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 2.
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; 2.
DR InterPro; IPR002967; Delta_tubulin.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR025661; Pept_asp_AS.
DR InterPro; IPR000169; Pept_cys_AS.
DR InterPro; IPR025660; Pept_his_AS.
DR InterPro; IPR000668; Peptidase_C1A_C.
DR InterPro; IPR039417; Peptidase_C1A_papain-like.
DR InterPro; IPR013201; Prot_inhib_I29.
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; PF08246; Inhibitor_I29; 1.
DR Pfam; PF00112; Peptidase_C1; 2.
DR Pfam; PF00091; Tubulin; 1.
DR Pfam; PF03953; Tubulin_C; 1.
DR PRINTS; PR01224; DELTATUBULIN.
DR PRINTS; PR01161; TUBULIN.
DR SMART; SM00848; Inhibitor_I29; 1.
DR SMART; SM00645; Pept_C1; 1.
DR SMART; SM00864; Tubulin; 1.
DR SMART; SM00865; Tubulin_C; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 2.
DR SUPFAM; SSF55307; Tubulin C-terminal domain-like; 1.
DR SUPFAM; SSF52490; Tubulin nucleotide-binding domain-like; 1.
DR PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE 3: Inferred from homology;
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Cilium biogenesis/degradation {ECO:0000256|ARBA:ARBA00022794};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000186817};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..684
FT /note="Tubulin delta chain"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012344637"
FT DOMAIN 36..93
FT /note="Cathepsin propeptide inhibitor"
FT /evidence="ECO:0000259|SMART:SM00848"
FT DOMAIN 124..673
FT /note="Peptidase C1A papain C-terminal"
FT /evidence="ECO:0000259|SMART:SM00645"
FT DOMAIN 192..350
FT /note="Tubulin/FtsZ GTPase"
FT /evidence="ECO:0000259|SMART:SM00864"
FT DOMAIN 352..489
FT /note="Tubulin/FtsZ 2-layer sandwich"
FT /evidence="ECO:0000259|SMART:SM00865"
SQ SEQUENCE 684 AA; 75889 MW; B69E1456F49FE39E CRC64;
MAACSRTALL LCLAKTVASW TDASKPLTAE EVRNAFDGFK AFFRRDYADE DEEARRFSNF
QATMETVRQH NSDEQRTWDM GLNQFSDMTD AEFESQVLMA PQKCSATGSP SYQMPSPTVP
DSALEKKMDW RSYGVISEVK NQGSCGSCWA FSTAGCLEAH LAIKMRSTWK APRLSEQQLV
DCAQAPLLST PNASVFEAVR REPAVDLEPT VVDEVRTGTY RQLFHPEQLI SGKEDAANNF
ARGHYTIGKE IVDLVLDRIR LSVDYGKKSK ISFTVWCCPQ VATAVVEPYN TVLCVHSLLE
HTDVTIMYDN EALYDICRRN LDIERPTYTN LNRLIAQIIS SLTASLRFDG ALNVDITEFQ
TNLVPYPRIH FMLTSYAPVI SAEKAYHEQL SVAEITMSVF EPASMMVKCD PRHLAGGDVV
PKDVNAAVAT IKTKRTIQFV DWCPTGFKCG INYQPPTVVP GGDLAKVMRA CCMISNSTAI
AEVFSRIDHK FDLMYSKRAF VHHYVGEGME EGEFSEARED LAALEKDYEE VGIETAEGEG
EEGSNLTDGL HFEPRSAGIG VKVPGGSVNI TAGDEQALKR AIALVGPVSV AFQVASDFRH
YSSGVYSSKV CKSGPKDVNH AVLAIGYGKD RKSGKQYWLI KNSWDYDWGE EGFFKMEAFK
NMCGVADCMA YPDLGPRDPE SILV
//
