ID A0A1B7P5V7_9EURO Unreviewed; 1119 AA.
AC A0A1B7P5V7;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Tubulin gamma chain {ECO:0000256|ARBA:ARBA00018848};
DE AltName: Full=Gamma-tubulin {ECO:0000256|ARBA:ARBA00033229};
GN ORFNames=ACJ72_01216 {ECO:0000313|EMBL:OAX84410.1};
OS Emergomyces africanus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Emergomyces.
OX NCBI_TaxID=1955775 {ECO:0000313|EMBL:OAX84410.1, ECO:0000313|Proteomes:UP000091918};
RN [1] {ECO:0000313|EMBL:OAX84410.1, ECO:0000313|Proteomes:UP000091918}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 136260 {ECO:0000313|EMBL:OAX84410.1,
RC ECO:0000313|Proteomes:UP000091918};
RA Cuomo C.A., Schwartz I.S., Kenyon C., de Hoog G.S., Govender N.P.,
RA Botha A., Moreno L., de Vries M., Munoz J.F., Stielow J.B.;
RT "Emmonsia species relationships and genome sequence.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the tellurite-resistance/dicarboxylate
CC transporter (TDT) family. {ECO:0000256|ARBA:ARBA00008566}.
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:OAX84410.1}.
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DR EMBL; LGUA01000078; OAX84410.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B7P5V7; -.
DR STRING; 1658172.A0A1B7P5V7; -.
DR OrthoDB; 5476567at2759; -.
DR Proteomes; UP000091918; 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:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0036361; F:racemase activity, acting on amino acids and derivatives; IEA:InterPro.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IEA:InterPro.
DR GO; GO:0007020; P:microtubule nucleation; IEA:InterPro.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR CDD; cd02188; gamma_tubulin; 1.
DR CDD; cd09318; TDT_SSU1; 1.
DR Gene3D; 3.40.50.12500; -; 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; 1.
DR Gene3D; 1.50.10.150; Voltage-dependent anion channel; 1.
DR InterPro; IPR015942; Asp/Glu/hydantoin_racemase.
DR InterPro; IPR002454; Gamma_tubulin.
DR InterPro; IPR004695; SLAC1/Mae1/Ssu1/TehA.
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; IPR038665; Voltage-dep_anion_channel_sf.
DR PANTHER; PTHR31686; -; 1.
DR PANTHER; PTHR31686:SF1; SULFITE EFFLUX PUMP SSU1; 1.
DR Pfam; PF01177; Asp_Glu_race; 1.
DR Pfam; PF03595; SLAC1; 1.
DR Pfam; PF00091; Tubulin; 1.
DR Pfam; PF03953; Tubulin_C; 1.
DR PRINTS; PR01164; GAMMATUBULIN.
DR PRINTS; PR01161; TUBULIN.
DR SMART; SM00864; Tubulin; 1.
DR SMART; SM00865; Tubulin_C; 1.
DR SUPFAM; SSF55307; Tubulin C-terminal domain-like; 1.
DR SUPFAM; SSF52490; Tubulin nucleotide-binding domain-like; 1.
DR PROSITE; PS00227; TUBULIN; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000091918};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 81..99
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 105..130
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 150..174
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 180..206
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 218..237
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 249..273
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 285..308
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 328..349
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 361..378
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 715..913
FT /note="Tubulin/FtsZ GTPase"
FT /evidence="ECO:0000259|SMART:SM00864"
FT DOMAIN 915..1059
FT /note="Tubulin/FtsZ 2-layer sandwich"
FT /evidence="ECO:0000259|SMART:SM00865"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..58
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1119 AA; 122331 MW; 332CB03DA554B756 CRC64;
MLQDRNETHP SGNTNSAHSS EETGVGSGDN ISPNGNENKI GEAVGEDQSR DPEGQLSDDE
YEELAKNDQG WRKIVRNFTP SWFTINMGTG IVSILLFGLP YNGEWLYWIS VGIFGLNVLL
FSIFLTISIL RYALWPEIWG VMLLHPLQSL FLGTFPMALS TIVSMIALVC SPVWGSWVQI
VAWALWIANS LIAVACAVSF PFLLMIPGKP SDLPSMTAVW LLPVVSTIVS ASAGAVVSEN
LPSPQLSLWT IIASYILWGL GMLFSMIILA VYFQRLAIHK LPPKSVIVST CIPLGPMGQG
GFVILRLGAA ARKFFPLNNT LDPAAGGVFY SLGFMIALVL WGFGLLWLLF AITAIAQCKR
IPFSMGWWAS IFPLGVYANC TIQMSKEMPS QFFKVLSTCF RLTSVSSPSQ GVTSLGPDGE
TISGIPSINC SDDSLLSALH CLPHLKPLIP RYDAFLVACY SVHPLVGMLK ELIDIARAEE
RPESRKKYVT GIFEASVSKC ISLIRSTSCS SAFSSSLSSS ADAGDSLGTA ECKSSFGIIS
TGDVWKEIFV RAVPDLLRRT VDFGMNDNVS LESMFAGVET TGLSALELHT SRAEEVNRRL
ARATERLING AERQVAAICL GCAGMAGMDK AVRQGCKRAL GAVEGEKVVI VDGVVAGVEE
LVNVCKSGGM EIITIQAGQC GNNVGSQFWQ QLCVEHGINK DGNLAEFATE GGDRKDVFFY
QSDDTRYIPR AILLDLEPRV LNTIQTGAYR NIYNPENFFI GRQGIGAGNN WAAGYAAGEI
VQEEVFDMID READGSDSLE GFMLLHSIAG GTGSGLGSFI LERMNDRFPK KLIQTYSVFP
DTQAADVVVN PYNSLLAMRR LTQNADSVVV VDNGALSRIA ADRLHVQEPS FQQTNQLVST
VMSASTTTLR YPGYMHNDLV SILANLIPDP RTRFLITSYT PFTGDNVEQA KTVRKTTVLD
VMRRLLQPKN RMVSITPSKS SCYISIFNII QGEAAQTDVD KSILRIRERR LATFIPWGPA
SIHVAVPKRS PYLPNTHRVS GLMLANHTSV ATLFKRIVSQ YDRLRKRNAF LEQYKKEAPF
ADGLGEFDEA RTVVMDLIGE YESAERPDYA GGGTDVEEN
//
