ID A0A1V2L9F8_CYBFA Unreviewed; 1354 AA.
AC A0A1V2L9F8;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Sporulation-specific protein 1 {ECO:0000313|EMBL:ONH68547.1};
GN ORFNames=BON22_1628 {ECO:0000313|EMBL:ONH68547.1};
OS Cyberlindnera fabianii (Yeast) (Hansenula fabianii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Cyberlindnera.
OX NCBI_TaxID=36022 {ECO:0000313|EMBL:ONH68547.1, ECO:0000313|Proteomes:UP000189513};
RN [1] {ECO:0000313|Proteomes:UP000189513}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=65 {ECO:0000313|Proteomes:UP000189513};
RX PubMed=28385833; DOI=10.1128/genomeA.00064-17;
RA van Rijswijck I.M.H., Derks M.F.L., Abee T., de Ridder D., Smid E.J.;
RT "Genome sequences of Cyberlindnera fabianii 65, Pichia kudriavzevii 129,
RT and Saccharomyces cerevisiae 131 isolated from fermented masau fruits in
RT Zimbabwe.";
RL Genome Announc. 5:E00064-E00064(2017).
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:ONH68547.1}.
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DR EMBL; MPUK01000002; ONH68547.1; -; Genomic_DNA.
DR STRING; 36022.A0A1V2L9F8; -.
DR VEuPathDB; FungiDB:BON22_1628; -.
DR OrthoDB; 152877at2759; -.
DR Proteomes; UP000189513; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005096; F:GTPase activator activity; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR CDD; cd08204; ArfGap; 1.
DR CDD; cd00821; PH; 1.
DR CDD; cd06609; STKc_MST3_like; 1.
DR Gene3D; 1.10.220.150; Arf GTPase activating protein; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR037278; ARFGAP/RecO.
DR InterPro; IPR001164; ArfGAP_dom.
DR InterPro; IPR038508; ArfGAP_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR PANTHER; PTHR48012:SF10; SERINE_THREONINE-PROTEIN KINASE KIC1; 1.
DR PANTHER; PTHR48012; STERILE20-LIKE KINASE, ISOFORM B-RELATED; 1.
DR Pfam; PF01412; ArfGap; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00105; ArfGap; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF57863; ArfGap/RecO-like zinc finger; 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50115; ARFGAP; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00288};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000189513};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00288};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00288}.
FT DOMAIN 437..537
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 578..703
FT /note="Arf-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50115"
FT DOMAIN 879..1132
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 386..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1197..1243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1259..1284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1259..1279
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 908
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1354 AA; 153116 MW; F997CE7BC4BAF41E CRC64;
MNLVLPKTKP LATFTQNERS TEHPFLLNCL SSDTITVSFK VNPDVLSDFD KIESDSFTIY
PNLVLKIFDS EYNAIKYASL ASKLIMTTSD EKTTMDPSVI VITKNKDEFK TTLSLNGLLR
YGKTYITLMG GKEEIFKTMV YIEKDDTVAD SSLENATYKD ALFPFPPDGA EFRELLANLE
ERSTKLRQLL KTSIKKAQAL DEATRHLALV RSGFSSTLSE IASYSRDIEN PLMFDIINDL
IPIMTEKSTL DIEESNALTR NIITPLTLIY NSDIKLLSNK RRLFYDQTKE FYSSASKEYY
TDYDILKSQV SFELNRYDYF QYLNEFRNGH SVRNLLYNFS LYLESYDKKL FAPNANENIS
KSHFYYQNFF KYKGAQQRMR NALATTTDPK DLPSIGNSPF PQAPASSPAY STATNSRPKT
PDSSVDFSTM SADNTGTLSK SGILMTLGGK NKSGWHKQQV VISDNILSEY IDWRENHEVL
RNNPVDLTFS CIKTVDTLRD RKYCIEVITP SNVKRLFQAE SEVERESWVQ ALTAAASLKA
KENQYNRPRS VSSDSFRTKR SSMRVEHLSA HQEHDPDVDN LSIVRDVDVS NQLCCDCGSL
EQVEWISLNL LVVVCIDCSG VHRSLGSHVS KIRSLTLDTK SFRSKEMNTL LYHVSNKFAN
SYYQGALSHN EKLSPKASDQ ERREYITNKY VKKMFLLEEP SFHANESLIK GVHSANVPLV
LKALAYGANV KMVVIKDVRG EKKEISLFEY SLTHCHGTPS EPIFDVSLLL YLNNAPCGGK
VAPVLELNDF QKKFWGTKIS SPVNSPATSA EKSATLEKTE PKNILRSHSM LLRKGSTIQK
ATPATDDHQP ASVEKKDRTN RVTLYLSSMD DANELSRQYE INECVGKGNF GDVYKAVEKR
SRKVVAVKVI DLEDSEDEIN VLIQEISFLS QMRSRNITQY FEALVVDVKL WIVMEYCGGG
SCAELLKCHK SLSEEVTGFV IRETLKGLRY LHKEGKVHRD IKAANILLTE QGEVKLADFG
VSGQITATKA RKNTFVGTPF WMAPEIITRK TGYNQKVDIW SLGITTIELV TGSPPFADQE
PMKVLFEIPN NSPPRLEGDQ FSDIIKEFVK LCLQKNEKKR PTSKVLLATR FMRVSRKCSS
LVQLIREKNE WFSQRRTPQK RPRHRLEENI YTKGESSFRW NFTASPVTPI TYQTNNAGDS
SPDCQLSSDI VPETPLTSPE PQQLLNFDDD SPNPMQLGRT NESSSDSIES VVLQNHGAIS
GQLSEPSQGA ISSPVRQGRM RTGPSRDVDY LNEVILYCFK RVQKRAVDPD TRAAVSTLAG
IFRKTELNYP GLCEAFSSEI RVRMLSLHDT KDNT
//
