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
//