ID A0A1B8AMM9_FUSPO Unreviewed; 1290 AA.
AC A0A1B8AMM9;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 02-APR-2025, entry version 36.
DE RecName: Full=RING-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=FPOA_08139 {ECO:0000313|EMBL:OBS21803.1};
OS Fusarium poae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=36050 {ECO:0000313|EMBL:OBS21803.1, ECO:0000313|Proteomes:UP000091967};
RN [1] {ECO:0000313|EMBL:OBS21803.1, ECO:0000313|Proteomes:UP000091967}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2516 {ECO:0000313|EMBL:OBS21803.1,
RC ECO:0000313|Proteomes:UP000091967};
RA Vanheule A., Audenaert K., Warris S., Van De Geest H., Schijlen E.,
RA Hofte M., De Saeger S., Haesaert G., Waalwijk C., Van Der Lee T.;
RT "Living apart together: crosstalk between the core and supernumerary
RT genomes in a fungal plant pathogen.";
RL Submitted (JUN-2016) 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:OBS21803.1}.
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DR EMBL; LYXU01000003; OBS21803.1; -; Genomic_DNA.
DR STRING; 36050.A0A1B8AMM9; -.
DR OMA; YETIAMR; -.
DR Proteomes; UP000091967; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR CDD; cd10170; ASKHA_NBD_HSP70; 1.
DR CDD; cd20335; BRcat_RBR; 1.
DR CDD; cd20336; Rcat_RBR; 1.
DR CDD; cd22249; UDM1_RNF168_RNF169-like; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR Gene3D; 3.90.640.10; Actin, Chain A, domain 4; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR013126; Hsp_70_fam.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR14187; ALPHA KINASE/ELONGATION FACTOR 2 KINASE; 1.
DR PANTHER; PTHR14187:SF82; FAMILY CHAPERONE, PUTATIVE (AFU_ORTHOLOGUE AFUA_7G08575)-RELATED; 1.
DR Pfam; PF00012; HSP70; 1.
DR Pfam; PF01485; IBR; 1.
DR Pfam; PF22191; IBR_1; 1.
DR PRINTS; PR00301; HEATSHOCK70.
DR SMART; SM00647; IBR; 2.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR SUPFAM; SSF57850; RING/U-box; 3.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000091967};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 980..1290
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 984..1038
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 632..724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 787..821
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 888..917
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1158..1220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 632..646
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 787..807
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 904..917
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1162..1215
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1290 AA; 144288 MW; 87BE544FD64A9642 CRC64;
MDFDKLKITD RKIIVGIDFG TTYSGVAWAE SRNPTRRTCI TQWPVSTSNR EGESSDKVPS
KLRYNGDKIE WGFSIPITAP QDEVIEWFKL DLDPDLQAMS QSLSSDGARG GRNVDKLVTD
FISQLGDHLL YTLREKLGDS IVNSTPLEFV VTVPAIWSDL AKDKTKKACQ KASGLSASQQ
QVHLVSEPEA AAIYALHGLD PHGLKVGDTI VVVDAGGGTV DLISYTITGL KPILEVQEAA
PGSGALCGST FLNMRFAKYL RGKLGKEEGF DEEVMAEAME VFEKKVKRQF TLNTAPDETY
NIPVAGLANN KTLGISRGRF ALKASDLKTI FEPVVLEVIR LVKDQITASN VPVRAILLVG
GFGASSYLKE RLRISVDDSI QIMQPPNAWQ AIVQGAVLKG LANAAPELAV VRVKNRKARK
HYGTEWRARW DDKIHSHLKS NRTWCGLDGC YKVLAMEWFI TRGSEVSENE PYFTSFVWTG
PVSSGRIRKI KMTIYNDQLP RDAPVARDDN VKILSHVEAD VSHIPENQLS RRQGSDGQWY
YELNCKIEAV YLSASTTYTL LYNGQRYNTL PISKLLYAML RSLKNKASNV WQKRKASRTT
SISTPPPELQ ISSSALAESE VDAEAVIVHN DINNNHTTGN PPSYQDNPYP LPPNSIPSTI
WTHLEHEQQP RRQPSYPLPP TSVPSTVSTL SNYQPNQDHP TAQGHIEDPL EPDPDPYTSR
YVPYTDANPL KNNMFARQAG IYGRVNPDIM GGFGDDDESV WLVDDEETDQ EQHRNSQNLL
TPFESTSQLA LWSSGSPSSH NSQTHLQQPG APPAPAPAPA HFAQPTFHYQ RPSFLDNDDD
LVFGLSPDMV TTSGTTSNQN EELTPQSGYA PISASILDLT SLGVNDDYTE PLDARDHTGW
PSKSPRTTTA TAGPSSSTNT YVDLFEQQDN DMTIAYLLQL EQLETDVANE FSFGQRYQQS
ADSTDVIVTH QRTARSTVTG DLECVVCAST KHVDAFPRFS IAATCTHPPS TCLDCIQLSI
ESDLSSKLWT EIRCPECREL LEYADIQRYA NKQTFTKYET IAMRAAMSEA DNFVWCTSGC
GSGQIHESGS AQPIVTCLHC SHRSCFHHDV AWHETLSCDE YDQLLADPEN FRSHLELENE
RWSDAQQAQL ESDRAMAQGL LTEDRAEMKR REDRAEMKRR EDRARQERED RARQEREDRA
RQEREDRARQ EREQAQKAAK LARQIAARRK KEEAQSNATV SRTTRPCAGC GWAIEKNKGC
SHMTCIKCRY EFCWACDQPY TRGHNNYCRG
//
