ID A0A1C1D1L5_9EURO Unreviewed; 1334 AA.
AC A0A1C1D1L5;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=C2 (Calcium/lipid-binding, CaLB) {ECO:0000313|EMBL:OCT54560.1};
GN ORFNames=CLCR_00761 {ECO:0000313|EMBL:OCT54560.1};
OS Cladophialophora carrionii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=86049 {ECO:0000313|EMBL:OCT54560.1, ECO:0000313|Proteomes:UP000094526};
RN [1] {ECO:0000313|Proteomes:UP000094526}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSF {ECO:0000313|Proteomes:UP000094526};
RA Teixeira M.M., Souza R.C., Almeida L.G., Vicente V.A., de Hoog S.,
RA Bocca A.L., de Almeida S.R., Vasconcelos A.T., Felipe M.S.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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:OCT54560.1}.
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DR EMBL; LGRB01000004; OCT54560.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C1D1L5; -.
DR STRING; 86049.A0A1C1D1L5; -.
DR VEuPathDB; FungiDB:CLCR_00761; -.
DR VEuPathDB; FungiDB:G647_10098; -.
DR eggNOG; KOG1012; Eukaryota.
DR Proteomes; UP000094526; 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:SF2; MEIOTICALLY UP-REGULATED 190 PROTEIN; 1.
DR PANTHER; PTHR47348; 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, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000094526};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 248..273
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 285..309
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 339..604
FT /note="SMP-LTD"
FT /evidence="ECO:0000259|PROSITE:PS51847"
FT DOMAIN 602..730
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 816..954
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 1..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 181..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 410..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 793..815
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 849..873
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1170..1232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1314..1334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..68
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..220
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1170..1190
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1191..1216
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1217..1232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1334 AA; 149124 MW; 4B066DAFA7A31CF2 CRC64;
MSSADELDPD SQRRTYQGPH SARHPIPTIQ KYKAERQELN NNQQDAEQAQ RDETDDSTYK
RAYHAAKGVL KGEDPPQSGH DPYRTQNRNV HTEGEERAAG GRERQQDGPE EGQNREEPQT
NGEQKTDEPG QSATEAVAGQ HDPRQKRKDM KHKKRSDGGR EVTDPVTHLP IVIRDSTHKD
LKSAGENIPG PGVDYRTRTG VDGATKSKEE HDTERRELQS SLDGMQKLFP PPKFEDVRDE
LARTYERAAM IGLSCIAVVI LLGQLLALVF DVGFYKKDAG WVSKVCALAF VLVPAVVAGS
VIVGVKGWLG KKVQTIWDDE VWDAARQEEL STTQAEDVVP ESVAWLNNLL SAVWPLINPD
LFTSISDMLE DVMQASLPKV VRMVSVDDLG QGSEAFRILG INWLPTGAAS QSVGSDGGLK
RPGKDEENDR TAAGQGQVDN GADDQGGGEA KSGDNTQDKQ QKEQEDQAIR EGMEAEQGDF
VNMELAFAYR ARSSGKSLTA KAKNAHLYLK FYLPGGIAVP VWVELRGIIG TMRLRLQLTP
DPPFFSLCTL TFMGQPQADM SCVPLSKHAL NLMDVPLISS FVQSSIDAAL AEYVAPKSLT
LDLKDMLVGD DFKKDTVTRG VVMIFIKSAQ GFKQGDGGVG PFQGSSDAYM TVSWGKFGKP
VSSTRIIVDD QEPNWSEWSH ILVTPEELNA DEKLRLQLWD SDKWTADDDL GRVEVDLKEL
MFGSKTKNKM CDREDRFKGE DSDEDMPGTL QWQVGYFEKT QITEQQLAKQ NADPNIRTVD
DLRKQVSDTA ERKLREATAH DESREIKQQK QEDYKEQEDA LVISSPPPDE YPSGIFSIQI
HNITGLEVQS LQKKDKNNAN DNREDEAEQS DDMPSSYATI ILNHQKIYRT RTKPKNAKPF
FNAGTERFVA DWKTAEVMVA VLDDREREDD AQLGMIYLPL RRVFQENSQV TQTYPLVGGI
GYGRARISMV WRSVELKLPK ELLGWSYGTL EIRCPVRSKD ARVHTNEEKS YSQHRIKLRT
NMMRAKMWPG SGDDVEWKPK GDKKSVFLAV RKRYSSPLII EFRKSSLGPD STPAFGVFWL
KDIPDEEEKA ITVKVWKGGK EAAHRATTSY GYSGMEENEQ PLGEIELTIK FWRGLSGYHK
SFADKSRNAD MRHVMEVLDT ANDEGQVEEF EGEYGGESQA SEDEDSENTD NEHGSEPSKK
NDRSRRKLRT HTNDDSSASD SDAGSTNSKN PIRAPAQMIS KPLSTASHLA GKVLDVNGHN
DPDDGDRGLR AQVRDYKDHH KQLHRKHRGV MQWRGARTVD WMAKKVKGIE GLGDRVVSRD
KDGDKSGGGV ETEV
//
