ID A0A167RHP8_CALVF Unreviewed; 850 AA.
AC A0A167RHP8;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Kinase-like protein {ECO:0000313|EMBL:KZP00919.1};
GN ORFNames=CALVIDRAFT_524625 {ECO:0000313|EMBL:KZP00919.1};
OS Calocera viscosa (strain TUFC12733).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Calocera.
OX NCBI_TaxID=1330018 {ECO:0000313|EMBL:KZP00919.1, ECO:0000313|Proteomes:UP000076738};
RN [1] {ECO:0000313|EMBL:KZP00919.1, ECO:0000313|Proteomes:UP000076738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TUFC12733 {ECO:0000313|EMBL:KZP00919.1,
RC ECO:0000313|Proteomes:UP000076738};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC -!- PATHWAY: Phospholipid metabolism. {ECO:0000256|ARBA:ARBA00025707}.
CC -!- SIMILARITY: Belongs to the choline/ethanolamine kinase family.
CC {ECO:0000256|ARBA:ARBA00038211}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KV417268; KZP00919.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A167RHP8; -.
DR STRING; 1330018.A0A167RHP8; -.
DR OrthoDB; 144299at2759; -.
DR Proteomes; UP000076738; Unassembled WGS sequence.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd05157; ETNK_euk; 1.
DR Gene3D; 3.90.1200.10; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR22603; CHOLINE/ETHANOALAMINE KINASE; 1.
DR PANTHER; PTHR22603:SF93; RE24176P; 1.
DR Pfam; PF01633; Choline_kinase; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000313|EMBL:KZP00919.1};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Reference proteome {ECO:0000313|Proteomes:UP000076738};
KW Transferase {ECO:0000313|EMBL:KZP00919.1};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT DOMAIN 615..656
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 457..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 528..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 575..595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 736..769
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..495
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..563
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 752..766
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 850 AA; 95034 MW; 047465D57A6E0FBD CRC64;
MSTPTLGPSL PLDLPTPPPL HLSNSYTSVI SLTSSYGDSR TWQRSESQTR WNVETEEDEP
ELQEYQLKDL PYSDVDLDPR KYRSESFATT LLSLFRTLRI PSWSSHRLSP SQVQLQKISG
ALTNAVFFVS YPQAPKPPTL VLRIYGPSSH ALISRPSELQ TLHILSSQYG IGPRVYGTFA
NGRVEQYFPS RTLTAPEVRD SQMSRWIGMR MKELHSVDLD RVVSDDVSVP GVWKNITSWL
APAREVLGLL DKAQLPPNHK WAAIVHDIDI RRFARDIASY RAFLSSRTPS LVFAHNDAQY
GNLLRLTKPP RTPSSSPLAG ATLPPQHQLI VVDFEYASPN PAAFDIGNHF HEWCFDYARR
VTTSWELESK HYPSLEERRN FYRAYLGHSA TEEQLEQLEK EVREWSPASH AMWAVWGIVQ
ARDDVVALGN QGASAEGGDF DYLRTTPIDK CLKEVPESKQ PGRKWALQPS RPSFKFAGPI
TPHSTTSSST IRPSSSPGLY IMMSSDDEYD EYFVDLPWDE VGKLLDAPVQ ASPPSSQQAS
SSRSDSTRLS SLLKLSSRKP SNNEFQSAAR LYGASGSAGA KRGRSPEPDS PGSSLKKMKL
YAQKVLKGFE EDYSCPICFD LIVGCHLTNP CGHSACGSCS TKWAANKTVP TCFACRAPMN
RTTPVIPGLL VDNVIEKQIN LLAENGDEEW QERGAKRKEW DQRKAAWAKE KSKQSANENV
VSNLRARRME MLRRAAHPQA PEVVSLSEDS ESDSQAEADP EDASDENGEV MAGAHRILEE
LRDIRRGIVR DHDILRYPRV SRRMLQIPVV DNPNDADYVP DTQNVASSNG NAAATGPVTR
MRFHFRAENP
//