ID A0A0V0VHX3_9BILA Unreviewed; 1202 AA.
AC A0A0V0VHX3;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Tubulin gamma-1 chain {ECO:0000313|EMBL:KRX62961.1};
DE Flags: Fragment;
GN ORFNames=T09_3044 {ECO:0000313|EMBL:KRX62961.1};
OS Trichinella sp. T9.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX62961.1, ECO:0000313|Proteomes:UP000054681};
RN [1] {ECO:0000313|EMBL:KRX62961.1, ECO:0000313|Proteomes:UP000054681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS409 {ECO:0000313|EMBL:KRX62961.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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:KRX62961.1}.
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DR EMBL; JYDN01000035; KRX62961.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0VHX3; -.
DR Proteomes; UP000054681; Unassembled WGS sequence.
DR GO; GO:0000930; C:gamma-tubulin complex; IEA:InterPro.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0043130; F:ubiquitin binding; IEA:InterPro.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IEA:InterPro.
DR GO; GO:0007020; P:microtubule nucleation; IEA:InterPro.
DR CDD; cd14279; CUE; 1.
DR CDD; cd02188; gamma_tubulin; 1.
DR Gene3D; 3.30.1370.110; -; 1.
DR Gene3D; 1.10.287.600; Helix hairpin bin; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; IPR003892; CUE.
DR InterPro; IPR013899; DUF1771.
DR InterPro; IPR002454; Gamma_tubulin.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR002625; Smr_dom.
DR InterPro; IPR036063; Smr_dom_sf.
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 PANTHER; PTHR46535; NEDD4-BINDING PROTEIN 2; 1.
DR PANTHER; PTHR46535:SF1; NEDD4-BINDING PROTEIN 2; 1.
DR Pfam; PF13671; AAA_33; 1.
DR Pfam; PF08590; DUF1771; 1.
DR Pfam; PF01713; Smr; 1.
DR Pfam; PF00091; Tubulin; 1.
DR Pfam; PF03953; Tubulin_C; 1.
DR PRINTS; PR01164; GAMMATUBULIN.
DR PRINTS; PR01161; TUBULIN.
DR SMART; SM01162; DUF1771; 1.
DR SMART; SM00463; SMR; 1.
DR SMART; SM00864; Tubulin; 1.
DR SMART; SM00865; Tubulin_C; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF160443; SMR domain-like; 1.
DR SUPFAM; SSF55307; Tubulin C-terminal domain-like; 1.
DR SUPFAM; SSF52490; Tubulin nucleotide-binding domain-like; 1.
DR PROSITE; PS51140; CUE; 1.
DR PROSITE; PS50828; SMR; 1.
DR PROSITE; PS00227; TUBULIN; 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:UP000054681}.
FT DOMAIN 497..541
FT /note="CUE"
FT /evidence="ECO:0000259|PROSITE:PS51140"
FT DOMAIN 651..725
FT /note="Smr"
FT /evidence="ECO:0000259|PROSITE:PS50828"
FT REGION 547..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1202
FT /evidence="ECO:0000313|EMBL:KRX62961.1"
SQ SEQUENCE 1202 AA; 135880 MW; F6E0F4327B99C8C6 CRC64;
MKKKSRFLSL KMTASYHKES SPTEVNFFMI RHALAANHKV FVILRGLPGS GKSTLARNLA
EMNNDSSIWC ADDYFVDSGG IYRFNPDQLE NAHNWCFAGA VSAIRKSQTL VIVDNTNIHR
WEMKRYVLSA YRAGYEIFFV EPDTKWKFDA AACFRRNSHG VPYFTIQRML DNYERNVTLE
DFLSPDFQVC DGKQPSSSTE NWFNTSEVKR EPSNLKGDGF EKRFSEFNIA SNSKAQANCL
SSVTVADVGL QVTEKLITLA STAHWRASDA CDGADEVHRS NERRVLRGRC KNGTDVEVDA
TRASAEDAHE MLYSCFPDLA RQDLDYIFSI CENDLQWTIN VLLDSAYDGN WKPDQLQLND
TPSIDQQEQQ HQVEAEPAGD LQALFTDDES YQCNFQISSE MAFQLQHLFG FVHPNISSDL
LMPHQLNVKM PLKLAFSLYQ CWANTQATMT ENSDENSTDF LYQEEVEFKN DENYASAVAT
EFETAWAPSA YHPDSLSSKM KLKCLYELFP DLNENFLESL FLSNNCQLSP TVEVICETMG
IPKPNLESLS VPSNSSSSTM NGTEFQSGLS SESSSTVADC KKLREEARNY QKNRIMNFQK
AQDAYRRGMK TVAWHYAQKG HLYHRKAKEA DQQAAEKIIE HYNTVHPINV VDLHGLHVSE
AISYVAKSLR RVIESTSLNE VKIITGQGSH STEGPRLKPA VLRYLKCRNL NFYESNPGMI
VVNLTIVEGN LGKMPREMIT VQLGQCGNQI GSEFWKTLCA EHGISPEGVL ENYAADTEDR
KDIYFYQADD EHYIPRAVLI DLEPRVIQSI LNSPYAKLYN PENIFLSKDG GGAGNNWTSG
FSQAYLISGE LVYEKIFDIL DREVENSDRL EGFVLCHSIA GGTGSGLGSY ILERFGDRFP
KKLIQTYSVF PNQDEASDVV VQPYNSLLTL KRLAQNSDCV VVLDNTALNR IAVERLHIDT
PSFSQINSLV STIMSASTST LRYPGYMDNN LLSLLSSLIP SLKLHFLITG YTPLTTDANV
TNIRKTSVMD VMRRLLQPEN MMVSNIPLKS KNAEHCYISI LNIIQGDVDP SSVQKSILRL
RERKLIQFIP WAPASVHVAL SQKSPFVQTA NRISGLMLAN HTAISALFER TQSQYEKLRK
KRAFLEQFKH EVIGENYEEL DSSLEVVQNL AEEYKVAATS NYLNFGLDKI VQSMPNTFEM
RR
//
