ID A0A0J7L622_LASNI Unreviewed; 784 AA.
AC A0A0J7L622;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Tubulin beta-1 chain {ECO:0000313|EMBL:KMQ98061.1};
GN ORFNames=RF55_1586 {ECO:0000313|EMBL:KMQ98061.1};
OS Lasius niger (Black garden ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Formicinae; Lasius; Lasius.
OX NCBI_TaxID=67767 {ECO:0000313|EMBL:KMQ98061.1, ECO:0000313|Proteomes:UP000036403};
RN [1] {ECO:0000313|EMBL:KMQ98061.1, ECO:0000313|Proteomes:UP000036403}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Whole {ECO:0000313|EMBL:KMQ98061.1};
RA Konorov E.A., Nikitin M.A., Kirill M.V., Chang P.;
RT "Lasius niger genome sequencing.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
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:KMQ98061.1}.
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DR EMBL; LBMM01000557; KMQ98061.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J7L622; -.
DR STRING; 67767.A0A0J7L622; -.
DR PaxDb; 67767-A0A0J7L622; -.
DR OrthoDB; 3124041at2759; -.
DR Proteomes; UP000036403; Unassembled WGS sequence.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
DR CDD; cd02187; beta_tubulin; 1.
DR CDD; cd00195; UBCc; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 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 Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_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 InterPro; IPR000608; UBQ-conjugat_E2.
DR InterPro; IPR023313; UBQ-conjugating_AS.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR PANTHER; PTHR11588; TUBULIN; 1.
DR PANTHER; PTHR11588:SF429; TUBULIN BETA-1 CHAIN; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR Pfam; PF00091; Tubulin; 1.
DR Pfam; PF03953; Tubulin_C; 1.
DR Pfam; PF00179; UQ_con; 1.
DR PRINTS; PR00111; ABHYDROLASE.
DR PRINTS; PR01163; BETATUBULIN.
DR PRINTS; PR01161; TUBULIN.
DR SMART; SM00864; Tubulin; 1.
DR SMART; SM00865; Tubulin_C; 1.
DR SMART; SM00212; UBCc; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF55307; Tubulin C-terminal domain-like; 1.
DR SUPFAM; SSF52490; Tubulin nucleotide-binding domain-like; 1.
DR SUPFAM; SSF54495; UBC-like; 1.
DR PROSITE; PS00227; TUBULIN; 1.
DR PROSITE; PS00183; UBC_1; 1.
DR PROSITE; PS50127; UBC_2; 1.
PE 3: Inferred from homology;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000036403};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 31..184
FT /note="UBC core"
FT /evidence="ECO:0000259|PROSITE:PS50127"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 763..784
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 765..784
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 115
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10133"
SQ SEQUENCE 784 AA; 88812 MW; 69066943D75F3F9D CRC64;
MAQNVNPFSS TQNTPTKAAE EKQSLPKDNH AVSKRLQKEL MVLMMNTEQG VSAFPEGENL
FKWIGTITGP RDTVYAGLTY KLTLEFPHSY PYSAPIVRFA TPCFHPNVDT GGNICLDILK
DKWSALYDVR TILLSIQSLL SGTIWTDFKP QIENLNTDKL TIVAWDPPGY GKSRPPDRTF
PDDFFQRDAA WAHSLMQTLG YSKFSLIGWS NGGITSLLLA STYPESIRRM VVFGANAYIH
PDEAKIYENI RDIDKWSERM RTSMIQVYGE DYFRKTWSNW IDAKLRLYEK QNGNVCKEVL
SKIKCPTLII HGAKDAIVFP EHPTYLKQNI ANSNLHILEK GAHNLHLRYF EEFNNLFWEI
ISDEHGIDPT GTYHGDSDLQ LERINVYYNE ASGGKYVPRA ILVDLEPGTM DSVRSGPFGQ
IFRPDNFVFG QSGAGNNWAK GHYTEGAELV DSVLDVVRKE AESCDCLQGF QLTHSLGGGT
GSGMGTLLIS KIREEYPDRI MNTYSVVPSP KVSDTVVEPY NATLSVHQLV ENTDETYCID
NEALYDICFR TLKLSTPTYG DLNHLVSLTM SGVTTCLRFP GQLNADLRKL AVNMVPFPRL
HFFMPGFAPL TSRGSQQYRA LSVPELTQQM FDAKNMMAAC DPRHGRYLTV AAIFRGRMSM
KEVDEQMLNI QNKNSSYFVE WIPNNVKTAV CDIPPRGLKM SATFIGNSTA IQELFKRISE
QFTAMFRRKA FLHWYTGEGM DEMEFTEAES NMNDLVSEYQ QYQEATADED AEFDEEQEAE
VDEN
//
