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Database: UniProt
Entry: A0A194SA76_RHOGW
LinkDB: A0A194SA76_RHOGW
Original site: A0A194SA76_RHOGW 
ID   A0A194SA76_RHOGW        Unreviewed;      1078 AA.
AC   A0A194SA76;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=Branchpoint-bridging protein {ECO:0000256|ARBA:ARBA00017984};
GN   ORFNames=RHOBADRAFT_41619 {ECO:0000313|EMBL:KPV77623.1};
OS   Rhodotorula graminis (strain WP1).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX   NCBI_TaxID=578459 {ECO:0000313|EMBL:KPV77623.1, ECO:0000313|Proteomes:UP000053890};
RN   [1] {ECO:0000313|EMBL:KPV77623.1, ECO:0000313|Proteomes:UP000053890}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WP1 {ECO:0000313|EMBL:KPV77623.1,
RC   ECO:0000313|Proteomes:UP000053890};
RX   PubMed=26441909; DOI=10.3389/fmicb.2015.00978;
RA   Firrincieli A., Otillar R., Salamov A., Schmutz J., Khan Z., Redman R.S.,
RA   Fleck N.D., Lindquist E., Grigoriev I.V., Doty S.L.;
RT   "Genome sequence of the plant growth promoting endophytic yeast Rhodotorula
RT   graminis WP1.";
RL   Front. Microbiol. 6:978-978(2015).
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   -!- SIMILARITY: Belongs to the BBP/SF1 family.
CC       {ECO:0000256|ARBA:ARBA00010382}.
CC   -!- SIMILARITY: Belongs to the tubulin family.
CC       {ECO:0000256|ARBA:ARBA00009636}.
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DR   EMBL; KQ474074; KPV77623.1; -; Genomic_DNA.
DR   RefSeq; XP_018273672.1; XM_018413917.1.
DR   AlphaFoldDB; A0A194SA76; -.
DR   STRING; 578459.A0A194SA76; -.
DR   GeneID; 28974366; -.
DR   OrthoDB; 1397at2759; -.
DR   Proteomes; UP000053890; Unassembled WGS sequence.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   CDD; cd02187; beta_tubulin; 1.
DR   CDD; cd02395; KH-I_BBP; 1.
DR   Gene3D; 6.10.140.1790; -; 1.
DR   Gene3D; 1.10.287.600; Helix hairpin bin; 1.
DR   Gene3D; 3.30.1370.10; K Homology domain, type 1; 1.
DR   Gene3D; 3.30.1330.20; Tubulin/FtsZ, C-terminal domain; 1.
DR   Gene3D; 3.40.50.1440; Tubulin/FtsZ, GTPase domain; 2.
DR   Gene3D; 4.10.60.10; Zinc finger, CCHC-type; 1.
DR   InterPro; IPR013838; Beta-tubulin_BS.
DR   InterPro; IPR002453; Beta_tubulin.
DR   InterPro; IPR004087; KH_dom.
DR   InterPro; IPR004088; KH_dom_type_1.
DR   InterPro; IPR036612; KH_dom_type_1_sf.
DR   InterPro; IPR032570; SF1-HH.
DR   InterPro; IPR047086; SF1-HH_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; IPR003008; Tubulin_FtsZ_GTPase.
DR   InterPro; IPR001878; Znf_CCHC.
DR   InterPro; IPR036875; Znf_CCHC_sf.
DR   PANTHER; PTHR11588; TUBULIN; 1.
DR   PANTHER; PTHR11588:SF457; TUBULIN BETA CHAIN; 1.
DR   Pfam; PF00013; KH_1; 1.
DR   Pfam; PF16275; SF1-HH; 1.
DR   Pfam; PF00091; Tubulin; 1.
DR   Pfam; PF03953; Tubulin_C; 1.
DR   Pfam; PF00098; zf-CCHC; 2.
DR   PRINTS; PR01163; BETATUBULIN.
DR   PRINTS; PR01161; TUBULIN.
DR   SMART; SM00322; KH; 1.
DR   SMART; SM00864; Tubulin; 1.
DR   SMART; SM00865; Tubulin_C; 1.
DR   SMART; SM00343; ZnF_C2HC; 2.
DR   SUPFAM; SSF54791; Eukaryotic type KH-domain (KH-domain type I); 1.
DR   SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 1.
DR   SUPFAM; SSF55307; Tubulin C-terminal domain-like; 1.
DR   SUPFAM; SSF52490; Tubulin nucleotide-binding domain-like; 1.
DR   PROSITE; PS50084; KH_TYPE_1; 1.
DR   PROSITE; PS00228; TUBULIN_B_AUTOREG; 1.
DR   PROSITE; PS50158; ZF_CCHC; 2.
PE   3: Inferred from homology;
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00047};
KW   Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW   mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW   mRNA splicing {ECO:0000256|ARBA:ARBA00023187};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053890};
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00117};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT   DOMAIN          848..863
FT                   /note="CCHC-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50158"
FT   DOMAIN          873..888
FT                   /note="CCHC-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50158"
FT   REGION          424..625
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          651..681
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          756..786
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          888..919
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          935..1078
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        567..582
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        595..610
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        898..913
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        994..1019
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1078 AA;  114987 MW;  D4C8DFCF87B179E3 CRC64;
     MRELVTLQVG QAGNQVATSF WETVLKEHGL SNDGQLDPTA THLQTDRLDV FFAEAAKHKY
     VPRGLQIDLE PATLDAVKAS KLGGLFRPSG FINGSSGAGN NWAKGYYTEG AELVESIMDQ
     LHHETEACDS LQGFQMFPDR MLATYSVLPS PKVSETVVEP YNAILSYHQL IENADLVFAF
     DNEALYDILG RTLKVSNPTY PQLNGLIAKV MSGITTPLRF PGQLNSDLRK LATNMVPFPR
     LHFLTTSYAP LVSPAGATFN KLSVADLTQQ LLDPSHMMAA SDVRDGKFLT AAAYFRGENV
     SSAAVEEAMT GVQQKNASYF VEWIPHAVQT ALTSVPSRDS PLSATFVSNS TSVQGLLRRT
     HAQFASLFRR KAFLHWYTGE GMDELEFTEA ESNVIDLVAE YQQYQEAGID DDEEDEVGLE
     YEESARHHHH HHQQHPRHMY NRNSRQTGAN EAPLPPVRRW GGADGGGGGG GPPPPPPPHG
     GGGMRDGYGG GGYGNGGGGG GGGYGRDDRG PPPRDDFRSG PAPGGYGMRD ERGYEGSGGG
     GGGYDDRGRP RSRFDERPMP SSPYGGGSSA PAPPPPASAG LPPMPAAHGS ESPAAPTGER
     KRKSRWGDKS EDSAMPVAIT GGVQERDLET YAGASSSFPL QLRLDEIQRA LRTGQVVPPD
     GQRSPSPPPT YDGHGRRTNT REVRYRKRLE DERMRLVDRQ IKLDPNFRPP AEYIMAKRQS
     SGRPQDKVYI PVKEFPEINF FGLLVGPRGN SLKKMERESG ARISIRGKGS VKEGKGRPGH
     REEDENDELH CLISADTEEK VQGCVKLINS VIETAASVPE GQNDHKRNQL RELAALNGTL
     RDDENQVCQN CGGLGHRKYD CPEQKNWSAN IICRICGGAG HMARDCTQRR GPGFGGPGGG
     PPGFPPVPGP DGGPPSVAQQ FDSEYASLMA ELGETTAAPP MSGPGGGGAG GGPGGPGPMM
     GGAQGMQQEP RDEQGNKIPP WRIPSNWNPP MNMQFNRGPP PPPGQRPPPP PPPAPYGGGP
     PGQQMGGAGY GGYPQGNYGG GGGAPYGGGG YQQRGPPQGY GGGGGPPPGY GGGGGPGY
//
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