ID A0A371CW91_9APHY Unreviewed; 1145 AA.
AC A0A371CW91;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=C2 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=OH76DRAFT_1408962 {ECO:0000313|EMBL:RDX44545.1};
OS Polyporus brumalis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Polyporus.
OX NCBI_TaxID=139420 {ECO:0000313|EMBL:RDX44545.1, ECO:0000313|Proteomes:UP000256964};
RN [1] {ECO:0000313|EMBL:RDX44545.1, ECO:0000313|Proteomes:UP000256964}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRFM 1820 {ECO:0000313|EMBL:RDX44545.1,
RC ECO:0000313|Proteomes:UP000256964};
RX PubMed=30061923; DOI=10.1186/s13068-018-1198-5;
RA Miyauchi S., Rancon A., Drula E., Hage H., Chaduli D., Favel A., Grisel S.,
RA Henrissat B., Herpoel-Gimbert I., Ruiz-Duenas F.J., Chevret D., Hainaut M.,
RA Lin J., Wang M., Pangilinan J., Lipzen A., Lesage-Meessen L., Navarro D.,
RA Riley R., Grigoriev I.V., Zhou S., Raouche S., Rosso M.N.;
RT "Integrative visual omics of the white-rot fungus Polyporus brumalis
RT exposes the biotechnological potential of its oxidative enzymes for
RT delignifying raw plant biomass.";
RL Biotechnol. Biofuels 11:201-201(2018).
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DR EMBL; KZ857448; RDX44545.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A371CW91; -.
DR STRING; 139420.A0A371CW91; -.
DR Proteomes; UP000256964; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0061817; P:endoplasmic reticulum-plasma membrane tethering; IEA:InterPro.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR CDD; cd04041; C2A_fungal; 1.
DR CDD; cd04052; C2B_Tricalbin-like; 1.
DR CDD; cd21676; SMP_Mug190; 1.
DR Gene3D; 2.60.40.150; C2 domain; 2.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR037767; C2A_Mug190-like.
DR InterPro; IPR037765; C2B_Tricalbin.
DR InterPro; IPR031468; SMP_LBD.
DR PANTHER; PTHR47348; MEIOTICALLY UP-REGULATED GENE 190 PROTEIN; 1.
DR PANTHER; PTHR47348:SF3; MEIOTICALLY UP-REGULATED GENE 190 PROTEIN; 1.
DR Pfam; PF00168; C2; 2.
DR SMART; SM00239; C2; 2.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 2.
DR PROSITE; PS50004; C2; 2.
DR PROSITE; PS51847; SMP; 1.
PE 4: Predicted;
KW Lipid transport {ECO:0000256|ARBA:ARBA00023055};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000256964};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 198..431
FT /note="SMP-LTD"
FT /evidence="ECO:0000259|PROSITE:PS51847"
FT DOMAIN 429..555
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 614..758
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 1..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 645..681
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 987..1111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..89
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..669
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 987..1007
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1008..1024
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1036..1070
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1072..1108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1145 AA; 127221 MW; CF6CFF3E9F7EBE70 CRC64;
MTHKFTEPYS GKNPVPHIAT KLTSLVNPEK ATNAKAEQLQ DESVKREEKD TEKTADKLSK
GHVMHTTDPT TGEDLDIRNA DEDPDPRPQG ENVLHQPFPP PDWKEHRDHV LSITNSSTVY
ISGAFVTAFL VSTFFSSRIL RVLCLIPPAF LSFLLLFRIN KAAQGDFEQR VWHAERMRGL
AAGSDVDGDG KVTDDERTRE SAEWANAVIR GLWPIMNTDM FSSLLDMLED IMQSSVPRFI
HSVRVVDLGL GSNAGRITSI RSLPDARSRD TGEVKATDDS LRDMGIDGET IGPDDREALD
GDHVNLELSF AYQGLPSGRS AQSKAENIHL LIEFFVGIKN VTGIRVPVWV EVTGVVGTAR
ARLQLIPDPP FVKTTLVTLM GLPRITISVL PLSRMLPNMM NIPFISGFIS SALDTAAAEY
VAPKSLTLDL QQLISGDDIK KDTEAIGVIV VHIHRATGVK KMDTTDSSAD PYVTLTYSRL
EKPLYSTRII QGDCNPVFEE TAVLLVDVNT VKLRERLSFQ LWDSDRMSVD DMLGFAEIDI
VDLIRQRGKP VRRVSPLSSP DSKDRPGSLE YTVGYYGKLP PNKKLATDGS DPSLPDDLRQ
LPEFKDARAV ALNDLEAAVL VTAPDPEWPS GLLSVQVHEI RDLSVKTMGK ERKGSKGREG
EKGQDDGQQT EEEGEGLPSS YCTISLNDEL VYETRVKPIT SSPMFNAGTE RFVRDWRKAH
VAVTVKDSRM RENDAVLGTV FLKLSEVFVN ASEVTRCYSL EKGLGSGRIR ISLLFRPVEA
KLPPNLLGFD TGTLEIRDVS VQSQQIDLSK CEVRLKITTG EAEEKVSRKT AEQRDDKIVW
APDSPTKLPV RQRYAAALLI SFRDASGFKS SGRRALGVLW LRDLIDRAEG PVEVSLWRAK
DGDYSRLKLN YVPPDGDLSY WDSDKEKVER IGSVFLDLVF WPGFAKEHYE MLNGQGARKR
GSWDEYDRQK KAGFRDSIGE LAVKVPHDHK AQESHETQER DGAQPSPEKT DKTMTNGPVN
TQEGDNEDAS EDAEGHGTNT IVSADSVEVE SSAQSTRSGS EGGGEQEQES GNETDGSEKK
HGGIIGKAKE WRKHQKELHR DHRGIMQAKP MRTAEWIKDS VEDSAHAVKD RFKMKARHPD
VETEV
//
