ID K1VNU6_TRIAC Unreviewed; 1209 AA.
AC K1VNU6;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Phospholipid binding protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=A1Q2_07371 {ECO:0000313|EMBL:EKC98357.1};
OS Trichosporon asahii var. asahii (strain CBS 8904) (Yeast).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Trichosporonales; Trichosporonaceae; Trichosporon.
OX NCBI_TaxID=1220162 {ECO:0000313|EMBL:EKC98357.1, ECO:0000313|Proteomes:UP000006757};
RN [1] {ECO:0000313|EMBL:EKC98357.1, ECO:0000313|Proteomes:UP000006757}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 8904 {ECO:0000313|EMBL:EKC98357.1,
RC ECO:0000313|Proteomes:UP000006757};
RX PubMed=23193141; DOI=10.1128/EC.00264-12;
RA Yang R.Y., Li H.T., Zhu H., Zhou G.P., Wang M., Wang L.;
RT "Genome sequence of the Trichosporon asahii environmental strain CBS
RT 8904.";
RL Eukaryot. Cell 11:1586-1587(2012).
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:EKC98357.1}.
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DR EMBL; AMBO01000391; EKC98357.1; -; Genomic_DNA.
DR AlphaFoldDB; K1VNU6; -.
DR STRING; 1220162.K1VNU6; -.
DR eggNOG; ENOG502RAFH; Eukaryota.
DR HOGENOM; CLU_007858_0_0_1; -.
DR InParanoid; K1VNU6; -.
DR OMA; RAMIPPI; -.
DR OrthoDB; 164125at2759; -.
DR Proteomes; UP000006757; Unassembled WGS sequence.
DR CDD; cd13316; PH_Boi; 1.
DR CDD; cd09535; SAM_BOI-like_fungal; 1.
DR CDD; cd00174; SH3; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR12844; CONNECTOR ENCHANCER OF KINASE SUPPRESSOR OF RAS; 1.
DR PANTHER; PTHR12844:SF42; CONNECTOR ENHANCER OF KSR PROTEIN CNK; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF07647; SAM_2; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00233; PH; 1.
DR SMART; SM00454; SAM; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
DR PROSITE; PS50002; SH3; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000006757};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 1..63
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 590..654
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 869..966
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 63..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 149..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 211..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 450..588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 653..871
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 987..1097
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..85
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..243
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..304
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..377
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..495
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..534
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..574
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 675..718
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 735..789
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 790..811
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 828..860
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1049..1083
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1209 AA; 126896 MW; 2078BA6D3F21C729 CRC64;
MALVVTAVHT FVAEHDDELE FQAGDKITVI EKDEAFGDGW WRGRNTKGEE GLFPATYISE
SSAETTSAAA PPASTDAQSS AIAQQPAAPV DAGVAGADSA KGPNGLQDSA PATEPIPPTS
QQVPAAAAAV PGTVNGCCSG ANAPASVLPT SAPANGINGH ASEDEGRQRD SLLDESGAPR
SAVTTGAAAQ KPAGNVMGST IDDVQGALEE HIASSPSSTR GLKNFETDKK DGFESRDQTD
DEGGMGITSD ARARLAEQAK LANEERDRQA QRESGGVAGL IYSDESDDED DESHHSRRGS
GINGDRYHQQ HMGGGIARGN STTGSHGYGI SRPEQQLAPV TDADYSPPQQ QQQRLSQQQQ
QHQQQVPYQS QPAAYQRSPE PAQAATMPPV DHVASRSPGQ QAVETIPPVS HPEGPHSAAQ
SPEMHSGSTL PPGAAAAGTG ATIAGVTAAA ATAAAYRQGG APAEPSPPAS NDSRGAGSPA
LTPSARSSSL PSRSPLVGNA ALPPTPSPQK AAMAPLPSTG SAPGSVQGTP HTDAVEQLQP
ALPLPPTPNN ANLANSQSSQ APQSVQSPTS AHPVTPGTAA RMPKSPPNTW TVNEVVEWAH
SRGFDQSVCD KFIEHDISGD VLLELDANLL KELDIPQFGK RIRIAQAINE LRRPASHGSP
NSIPQGGVDQ GHGRNASMPP SSYTGSVYGG SNAAEDQQGW GGSHSRKVST TPSTQPIDES
RVADVHPHPA STPTHSHFAV VNNANGGTPQ HHHGTPSQTP HSSTIASSTQ RSSASTPASP
STTVVKRDSS SSLGHKKGKG SMDKSDRLSF FGRARKPAPA QPPGSHSSGP RLPFTKQTNT
MTADRPEKRM SSSNGTQAPI GGALQKIGKP DKTGYLKKRG ERYNTWKQRF FVLKGSHLYY
LKSENEDRVK GHIDLKGHRI IVDENTNPGN YGFRLVGPGN EKVHYFSWPE RTQIRDWMKA
LMKATIARDY SVPVTSSCNI PTIPLAEAQA LQPRPPSPSE REAVQRANRR ENANQLTPRD
ASVLMALDTT GSGGKLMSGH MSLMPSRPSR DTRRASTGRS SNGGRPISSV GAGRPNSTGR
PSIASYYPPD DDPNPQAADL MQWVNRTLPP QYPRVAHWPN SFVSGEVIFL IVKHLAGLEP
VPPVPASAFS PDQSGLANVD GLFAMMDIVI DAGIDSAGVS LNDIRAGDAH AITQLLQGVR
GWAAQRGFP
//
