ID A0A197K3W9_9FUNG Unreviewed; 1356 AA.
AC A0A197K3W9;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=FYVE-type domain-containing protein {ECO:0000259|PROSITE:PS50178};
GN ORFNames=K457DRAFT_17635 {ECO:0000313|EMBL:OAQ31149.1};
OS Linnemannia elongata AG-77.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mortierellomycotina;
OC Mortierellomycetes; Mortierellales; Mortierellaceae; Linnemannia.
OX NCBI_TaxID=1314771 {ECO:0000313|EMBL:OAQ31149.1, ECO:0000313|Proteomes:UP000078512};
RN [1] {ECO:0000313|EMBL:OAQ31149.1, ECO:0000313|Proteomes:UP000078512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AG-77 {ECO:0000313|EMBL:OAQ31149.1,
RC ECO:0000313|Proteomes:UP000078512};
RG DOE Joint Genome Institute;
RA Uehling J., Gryganskyi A., Hameed K., Tschaplinski T., Misztal P., Wu S.,
RA Desiro A., Vande Pol N., Du Z.-Y., Zienkiewicz A., Zienkiewicz K.,
RA Morin E., Tisserant E., Splivallo R., Hainaut M., Henrissat B., Ohm R.,
RA Kuo A., Yan J., Lipzen A., Nolan M., Labutti K., Barry K., Goldstein A.,
RA Labbe J., Schadt C., Tuskan G., Grigoriev I., Martin F., Vilgalys R.,
RA Bonito G.;
RT "Genome sequencing reveals origins of a unique bacterial endosymbiosis in
RT the earliest lineages of terrestrial Fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KV442031; OAQ31149.1; -; Genomic_DNA.
DR STRING; 1314771.A0A197K3W9; -.
DR OrthoDB; 1388046at2759; -.
DR Proteomes; UP000078512; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd15737; FYVE2_Vac1p_like; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR011993; PH-like_dom_sf.
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; PTHR12673; FACIOGENITAL DYSPLASIA PROTEIN; 1.
DR PANTHER; PTHR12673:SF159; RAC GUANINE NUCLEOTIDE EXCHANGE FACTOR JJ; 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:UP000078512};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT DOMAIN 990..1066
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT REGION 1..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 435..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 901..946
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1069..1090
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1127..1146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1209..1230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1289..1356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1178..1205
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..94
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 903..917
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 923..946
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1320..1342
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1356 AA; 142755 MW; BF0E388471FC5B49 CRC64;
MSSQAPPSPS TAPTTAATTI TTTTAEANAT IRSSPTSATV RSNMPSKLMS ISTKTIFTTT
TTTTTTPNNE DQPSSSSASV SSPSSSNSPG SLSPATPAAE MMHTGPDPLP ATALITTPPS
VDNNNDIFVT PFAQMDNNST KDEATSSDTE TLEAGVTATL HKKDSGTSMG SSVVSSPIDS
RPSSQTALRK ADDTSCPTSP TEPAPAPTTT TTTGTRRFSQ SDTPSMISPA GRVLTRPLST
SKLSSIPLTA PHILPNQRYA GFNLAAFGQL SPSSSTAAAM TISRADSLAF LNSNSSAGSS
PNPYFGNSAA AMKAGGSGGA STPNSLMEGI MLPSSSGVTR TTMCGSDAIS LLDLDDSHND
IVMIDSNGNS SGSAVVGPAT VVETMASASA IVSNNHASAS HHHTLGGAAS GLVAGLGGLT
TAVSSASLLT GSGGLGGSGG GSGSGTTSVL GGGSAFGSGS SSGSSISQPR SSLPSLTSQA
KKDVMQRAAM LAAMQQNGGA KILGAHRVGR RQDRPNRKIR FGDYHKICEI EYGFNQGKPL
VANGRTLVHS TVVLRICGDE EREEQLYLFS DVLVTGTKIK KGRSKSEKNA NEVPANVATA
DEAEKAKDFS ADDRQQGLVA TVEESKVEMV AIGPEVKAET TTVEVFDKET LLDNPYAGHL
ENQQISRLTQ VQADVIEGDE RPMLKVSMPQ STSLLIFESV AARDNFMSLL TETIYAHKHY
LLSQSKYLAD LKKFKRHSAF SFDTSFLKTW GIPGGLNLGS FKPAGGSGGH GVIGPNTFIS
SPVTSPGGGA FDPYQHQQHL NRPQSMAGSL FGFALNGGPF QPFSDHSKES SYATLRGANA
AHALQYHHQQ QQMLQQQLQN RLSMSSVASG RVGGMDRTSS GSAFDALWFM KGSETVKNSR
RSVVHATAED ERDGLTEEYL PTNMVSGEPT TTANQPSSSS PIASPSLTVN TDLAAATAGS
SSVPSRPPLS TSSSFNSIAT LRNGAGWVRD EDATYCMVCT TTKFGVLIRK HHCRLCGRVI
CWKCCQMKDA VLLNNEQALS PTEAAALSQD FRKPIRVCLD CIEQNAAASQ EGNNNQPSQP
SSPQQQSSSF PLQGVLGKLM SSTMTSSPQI VASATNATGS STFAMPQTAS AQAPFQQRGQ
GSTPSSFYPR IMSYGRNGNP YPHHHRASLY RIDVERVGEE DEEEEEEEEQ EVAELLQKAD
EALESLALSQ PETISQEDPA TADSEGLDES NTIIKSRHGS VRLKDLDPAD INEEEVQNQI
MNLESEVESL LIQSAAAPLM FARAVGGSAH SRHQREGGTG AGKTRVIRGI PKEMMLQYGG
DGDDDDDDDA EDEEDEEVSM EELLAQQDER LKRILS
//
