ID A0A176WLS3_MARPO Unreviewed; 475 AA.
AC A0A176WLS3;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 22-FEB-2023, entry version 19.
DE RecName: Full=Tubulin gamma chain {ECO:0000256|RuleBase:RU000352};
GN ORFNames=AXG93_3891s1020 {ECO:0000313|EMBL:OAE33989.1};
OS Marchantia polymorpha subsp. ruderalis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE33989.1, ECO:0000313|Proteomes:UP000077202};
RN [1] {ECO:0000313|EMBL:OAE33989.1, ECO:0000313|Proteomes:UP000077202}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Tak-1 and cv. Tak-2 {ECO:0000313|Proteomes:UP000077202};
RC TISSUE=Whole gametophyte {ECO:0000313|EMBL:OAE33989.1};
RA Honkanen S., Jones V.A., Morieri G., Champion C., Hetherington A.J.,
RA Kelly S., Saint-Marcoux D., Proust H., Prescott H., Dolan L.;
RT "Mechanisms controlling the formation of the plant cell surface in tip-
RT growing cells are functionally conserved among land plants.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Tubulin is the major constituent of microtubules. The gamma
CC chain is found at microtubule organizing centers (MTOC) such as the
CC spindle poles or the centrosome. {ECO:0000256|RuleBase:RU000352}.
CC -!- FUNCTION: Tubulin is the major constituent of microtubules. The gamma
CC chain is found at microtubule organizing centers (MTOC) such as the
CC spindle poles, suggesting that it is involved in the minus-end
CC nucleation of microtubule assembly. {ECO:0000256|ARBA:ARBA00002783}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center {ECO:0000256|ARBA:ARBA00004267}.
CC -!- SIMILARITY: Belongs to the tubulin family.
CC {ECO:0000256|ARBA:ARBA00009636, ECO:0000256|RuleBase:RU000352}.
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:OAE33989.1}.
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DR EMBL; LVLJ01000464; OAE33989.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A176WLS3; -.
DR OrthoDB; 5476567at2759; -.
DR Proteomes; UP000077202; 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-UniRule.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IEA:InterPro.
DR GO; GO:0007020; P:microtubule nucleation; IEA:InterPro.
DR CDD; cd02188; gamma_tubulin; 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 InterPro; IPR002454; Gamma_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 PANTHER; PTHR11588; TUBULIN; 1.
DR PANTHER; PTHR11588:SF7; TUBULIN GAMMA CHAIN; 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 GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|RuleBase:RU000352};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701, ECO:0000256|RuleBase:RU000352};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU000352};
KW Reference proteome {ECO:0000313|Proteomes:UP000077202}.
FT DOMAIN 48..247
FT /note="Tubulin/FtsZ GTPase"
FT /evidence="ECO:0000259|SMART:SM00864"
FT DOMAIN 249..395
FT /note="Tubulin/FtsZ 2-layer sandwich"
FT /evidence="ECO:0000259|SMART:SM00865"
SQ SEQUENCE 475 AA; 53316 MW; 0F7CF0E58A6B43D6 CRC64;
MPREIITLQV GQCGNQIGME FWKQLCLEHG ISKAGILEDF ATQGGDRKDV FFYQADDEHY
IPRALLLDLE PRVINSIQNS EYRNLYNHEN VFVADHGGGA GNNWASGYHQ GEQVEEDIMD
MIDREADGSD SLEGFVLCHS IAGGTGSGMG SYLLEALNDR YSKKLVQTYS VFPNQMETSD
VVVQPYNSLL TLKRLTLNAD CVVVLDNTAL NRIAVDRLHI PNPTFAQTNS LVSTVMSAST
TTLRYPGYMN NDLVGLVASL IPTPRCHFLM TGYTPLTVER QANAIRKTTV LDVMRRLLQA
KNIMVSSYAR TKDASQAKYI SILNIIQGEV DPTQVHKSLQ RIRERKLANF IEWGPASIQV
ALSRKSPYVQ TAHRVSGLML ASHTSIRHLF SKCISQYEKL RKKQAFLDNY RKFPMFADND
LSEFDESREI VQNLVDEYKA CESADYIKWG MEDRSKAMTG EGNATGSLDS RAPLL
//
