ID A0A068RZM0_9FUNG Unreviewed; 867 AA.
AC A0A068RZM0;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=FYVE-type domain-containing protein {ECO:0000259|PROSITE:PS50178};
GN ORFNames=LCOR_06371.1 {ECO:0000313|EMBL:CDH55205.1};
OS Lichtheimia corymbifera JMRC:FSU:9682.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Lichtheimiaceae; Lichtheimia.
OX NCBI_TaxID=1263082 {ECO:0000313|EMBL:CDH55205.1, ECO:0000313|Proteomes:UP000027586};
RN [1] {ECO:0000313|EMBL:CDH55205.1, ECO:0000313|Proteomes:UP000027586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JMRC:FSU:9682 {ECO:0000313|Proteomes:UP000027586};
RA Schwartze V.U., Winter S., Shelest E., Marcet-Houben M., Horn F.,
RA Wehner S., Hoffmann K., Riege K., Sammeth M., Nowrousian M., Valiante V.,
RA Linde J., Jacobsen I.D., Marz M., Brakhage A.A., Gabaldon T., Bocker S.,
RA Voigt K.;
RT "Gene expansion shapes genome architecture in the human pathogen
RT Lichtheimia corymbifera: an evolutionary genomics analysis in the ancient
RT terrestrial Mucorales (Mucoromycotina).";
RL Submitted (AUG-2013) 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:CDH55205.1}.
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DR EMBL; CBTN010000028; CDH55205.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A068RZM0; -.
DR STRING; 1263082.A0A068RZM0; -.
DR VEuPathDB; FungiDB:LCOR_06371.1; -.
DR OrthoDB; 38671at2759; -.
DR Proteomes; UP000027586; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd15760; FYVE_scVPS27p_like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR47794; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 27; 1.
DR PANTHER; PTHR47794:SF1; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 27; 1.
DR Pfam; PF01363; FYVE; 1.
DR SMART; SM00064; FYVE; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000027586};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT DOMAIN 802..856
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 53..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 307..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 456..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 538..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 634..696
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 8..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..279
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..371
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..392
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..426
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..500
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 867 AA; 96171 MW; A7771ED74CAA15E3 CRC64;
MMNYSRRKRC DSISSTQSAM TIEPEVSRRR SLRNVPSLSA MIKSTSLRSL DPDQASIVST
HTSTSTSRHN MTRRQSLTRA TASSLAKMVN FSSTTTDEQQ QQQSKPSRFN KLLKKRSSQE
RPPSQLPTKG KKDNNHVSSL PSPPTTPLPT ATANKRRWSP FRSPRNSTSG QDTPPMPTSP
SISTMAATQL HHHSTEENDD GTLLMGERPP QLPPIEQDQQ GFMLDLKASD STRSSNKSIS
SSTTTANRRR SMPPSAALVT PSSSINRKRH STGTAFAQQA AAAIPSASVS LARGSSNNKP
KCEACLRREA RRASSSDTAE VSKNKEEGVA CEIKEHKEIN KLTTKTTAKN DEDEDEKETV
QSHDLDSKHQ QQEVAFQETN AHEEHANHEM DEDEQDDKEM DAVEINKDDN ETIISSLSSK
QETEYTTAGG DALVEEQDKL QDVVVAHVGS NDDDLMVEDM QNNLGPAESH AQEEQVSNTK
EHQAVVSMQQ QQQQQDIVTT PVDPPSPPSL NDNDSIDALV VEELSISHPT ALHFISDEQQ
DNSSSHDQVD IQPSPPPTST HSDSTIASEE NPTTTTTQHQ DVQQQQPIVS MATSSSSSLA
IMQPIASRAA LVPSTAEQSL VRLIASCMAH ADKLEALANE VSRSEYRVSQ LLQQHQALIQ
SLDAREHRYM MHVQTYQQLL ASQTRMLNEL EQLQGRLSSA PLSCWHPPSP WWATLAPHNG
GSIITQQKNN LGHTTDIVVA GTCVAHNPPQ HLMLTNDAHQ STIYHHYLLH IGHDERSVKF
VLCPPDQWVP DEHADACQEA HCDTHFNLFN RRHHCRSCGH IVCNKHSQNR LPLFEPLNRD
KGEWARVCDA CFYRLLDRNT SSLTTPS
//
