ID A0A369GJ72_9HYPO Unreviewed; 1728 AA.
AC A0A369GJ72;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 08-NOV-2023, entry version 21.
DE RecName: Full=Tubulin gamma chain {ECO:0000256|ARBA:ARBA00018848};
DE AltName: Full=Gamma-tubulin {ECO:0000256|ARBA:ARBA00033229};
GN ORFNames=CP532_6332 {ECO:0000313|EMBL:RDA82595.1};
OS Ophiocordyceps camponoti-leonardi (nom. inval.).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX NCBI_TaxID=2039875 {ECO:0000313|EMBL:RDA82595.1, ECO:0000313|Proteomes:UP000252748};
RN [1] {ECO:0000313|EMBL:RDA82595.1, ECO:0000313|Proteomes:UP000252748}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCC 80369 {ECO:0000313|EMBL:RDA82595.1,
RC ECO:0000313|Proteomes:UP000252748};
RA Kobmoo N., Wichadakul D., Arnamnart N., Rodriguez De La Vega R.C.,
RA Luangsa-Ard J.-J., Giraud T.;
RT "A genome scan of diversifying selection in the zombie-ant fungus
RT Ophiocordyceps unilateralis complex supports a role of enterotoxins in
RT coevolution and host-specificity.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Tubulin is the major constituent of microtubules, a cylinder
CC consisting of laterally associated linear protofilaments composed of
CC alpha- and beta-tubulin heterodimers. Microtubules grow by the addition
CC of GTP-tubulin dimers to the microtubule end, where a stabilizing cap
CC forms. Below the cap, tubulin dimers are in GDP-bound state, owing to
CC GTPase activity of alpha-tubulin. {ECO:0000256|ARBA:ARBA00034296}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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: 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:RDA82595.1}.
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DR EMBL; PDHP01000298; RDA82595.1; -; Genomic_DNA.
DR STRING; 2039875.A0A369GJ72; -.
DR Proteomes; UP000252748; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IEA:InterPro.
DR GO; GO:0046907; P:intracellular transport; IEA:InterPro.
DR GO; GO:0007020; P:microtubule nucleation; IEA:InterPro.
DR CDD; cd02188; gamma_tubulin; 1.
DR CDD; cd13170; RanBD_NUP50; 1.
DR Gene3D; 1.10.287.600; Helix hairpin bin; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 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; IPR002454; Gamma_tubulin.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR000156; Ran_bind_dom.
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; PTHR11588; TUBULIN; 1.
DR PANTHER; PTHR11588:SF7; TUBULIN GAMMA CHAIN; 1.
DR Pfam; PF00638; Ran_BP1; 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; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF55307; Tubulin C-terminal domain-like; 1.
DR SUPFAM; SSF52490; Tubulin nucleotide-binding domain-like; 1.
DR PROSITE; PS50196; RANBD1; 1.
DR PROSITE; PS00227; TUBULIN; 1.
PE 3: Inferred from homology;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000252748}.
FT DOMAIN 1044..1126
FT /note="RanBD1"
FT /evidence="ECO:0000259|PROSITE:PS50196"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 258..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 370..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 475..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 524..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 604..853
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 874..1033
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1061..1082
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1705..1728
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..305
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..391
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..446
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..498
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 621..635
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 682..697
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 775..790
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 809..853
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 898..933
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 940..966
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 980..1023
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1061..1078
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1728 AA; 180010 MW; DC530BB202797AFA CRC64;
MVTFSLPADD EVAEAANGTP KPRPPLPFAK RSLVSSFSAK RNDTPYKPAP SRSLFGNQQD
ETPPAGGLSS SSIATARNIF SATTFADSPS STTFSPSLPQ SAMKRLFAPG STPEPNRLLR
AQATPRGMAA AASDKELFPM RIASPPPELT GEALSQKVPK DWNSKGSIYS DQFLGHLCPA
ELDDEQRRQF FCILDLRRLK YAANEIFSRK DWKLNVVNFA KEFEKSRSII LLRYGLYEFQ
TIKPSKAILQ KWRREHGLPQ SDEEEADGTP SRFASAKKRK ASDDFAKDPA ASAKGKRRAM
DVDEPEPETP AVAPSKNKRK ASLSVESPAK MQKAAPSSAK ALFEKIANKA TATQSPAATA
PGNLFAMAKP SGSSGSNLAR SVLTSGASQG GGPDAPQPGG NIFGYLSDAS SAKNSGVEAD
AESEGETGSD ETAKQRQKDK PTLDVAGADH GYKSSFAAAA NAATAADTAT ATQVSNPFMS
MGGNTSTGNS SVPGTRESTP GRSLFDRVTK GSDGYPMRAE AKAEVEAEKP QATIDNPTAP
LDQTWNPNTT PIKFAPAATQ SSSLFGNATS TTTNNTNNIF APKPAASSAN WATAAQHAPP
AKAPLFGAVA GQGGGQDGGE SDKENGSKRS KKTTPEAAKP AAAAPSSIFG EKTAAVGAQD
KPADAEPPKP ASLFGGQAAP SIFGSTPATT SSLFGASKAG AAASDSSAPA APAKPGFLFG
APSTVGGAKS ATASAAAAEP AASQPALFGF GAASRADSAK SSLETEAAAS KAAPSAGDKS
SSSGNAAGGS SLFGGSPMKQ DDPSPAKNPF AGGSTTSLFS FGAKPQGSTE SAPAFGSPSA
NSSAGHNVSF GAGAPSNTGG FNFNFTGGTT ASGSSSFVNP FAAQPSSDAA PKATGGGLFS
FDSSSAPSNP FQFGSSSGAN GSTSTSSGGS IFGQLGGGVS GPGGTSSNLS GGQSQASSQA
SGAVFGSSQP APAFGGVQPP AGGSSTTGTN SPLNFGGGGS SLATTPAVGT PEHWSQAEGT
TATSGGEPKE GEEDAQIRLA DVVDADEVVL HEVRAKALKF TSPREDKADS EEGKKAKAKS
PWTTQGVGPL RLLKHRVTGA VRLLLRTEPS GNVAVNRTVL PTVVYKADGK YVKVTTSTAE
GHGLETWMMQ NVAAFIAVFA GLAVAASADC PPPVPCLRRA DCTENINGCT VCKPECTVGG
RRCPPPVACL RRSDCTENIN GCTVCKPECT VGGAACPPPV ACLRRADCTE NVNGCTVCKP
ECRGEANREI ITIQAGQCGN SIGSQFWQQL CQEHGISQDG NLEDFATEGG DRKDVFYYQS
DDTRYIPRAI LIDLEPRVIN GIQTGPYRNI YNPENFYVGK NGMGAANNWG DGYQSGEAVC
EDIMEMIDRE ADGSDSLEGF MMLHSIAGGT GSGLGSFLLE RLNDRFPKKI IQTYSVFPDT
TNAGDVVVHP YNSILSMRRL TQNADSVVVL DNGALSHIAA DRLHVQEPSF QQTNQLVATV
MSASTTTLRY PGYMHNDLVS ILASLIPTPR CHFLMTAYTP FTGDQVEQAK TVRKTTVLDV
MRRLLQPKNR MVSTVPGKKS CYMSILNVIQ GEVDPTDVHK SLLRIRERRL ATFIPWGPAS
IQVALTKRSP YISASHRVSG LMLANHTSIA TLFKRILKQY DGMRKRNAFM EGYKKTAPFS
ENLDEFDEAR EVVAELIGEY EAAEGADYLN PDAGEKPSSS ADADKRMS
//