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Database: UniProt
Entry: A0A369GJ72_9HYPO
LinkDB: A0A369GJ72_9HYPO
Original site: A0A369GJ72_9HYPO 
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
//
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