ID N4TPT4_FUSC1 Unreviewed; 1079 AA.
AC N4TPT4;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=[NU+] prion formation protein 1 {ECO:0000313|EMBL:ENH65543.1};
GN ORFNames=FOC1_g10006928 {ECO:0000313|EMBL:ENH65543.1};
OS Fusarium oxysporum f. sp. cubense (strain race 1) (Panama disease fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=1229664 {ECO:0000313|EMBL:ENH65543.1, ECO:0000313|Proteomes:UP000016928};
RN [1] {ECO:0000313|Proteomes:UP000016928}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 1 {ECO:0000313|Proteomes:UP000016928};
RA Fang X., Huang J.;
RT "Genome sequencing and comparative transcriptomics of race 1 and race 4 of
RT banana pathogen: Fusarium oxysporum f. sp. cubense.";
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000016928}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 1 {ECO:0000313|Proteomes:UP000016928};
RX PubMed=24743270;
RA Guo L., Han L., Yang L., Zeng H., Fan D., Zhu Y., Feng Y., Wang G.,
RA Peng C., Jiang X., Zhou D., Ni P., Liang C., Liu L., Wang J., Mao C.,
RA Fang X., Peng M., Huang J.;
RT "Genome and Transcriptome Analysis of the Fungal Pathogen Fusarium
RT oxysporum f. sp. cubense Causing Banana Vascular Wilt Disease.";
RL PLoS ONE 9:E95543-E95543(2014).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCF family.
CC EF3 subfamily. {ECO:0000256|ARBA:ARBA00011054}.
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DR EMBL; KB730492; ENH65543.1; -; Genomic_DNA.
DR AlphaFoldDB; N4TPT4; -.
DR STRING; 1229664.N4TPT4; -.
DR VEuPathDB; FungiDB:FOC1_g10006928; -.
DR HOGENOM; CLU_002848_0_1_1; -.
DR OMA; EDHRKFG; -.
DR Proteomes; UP000016928; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006338; P:chromatin remodeling; IEA:UniProt.
DR CDD; cd03221; ABCF_EF-3; 1.
DR CDD; cd18626; CD_eEF3; 1.
DR Gene3D; 2.40.50.990; -; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR015688; eEF3_ABC2_chromodomain-like.
DR InterPro; IPR047038; eEF3_chromodomain-like_sf.
DR InterPro; IPR021133; HEAT_type_2.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR19211:SF14; ATP-BINDING CASSETTE SUB-FAMILY F MEMBER 3; 1.
DR PANTHER; PTHR19211; ATP-BINDING TRANSPORT PROTEIN-RELATED; 1.
DR Pfam; PF00005; ABC_tran; 2.
DR Pfam; PF00385; Chromo; 1.
DR SMART; SM00382; AAA; 2.
DR SMART; SM00298; CHROMO; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF54160; Chromo domain-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
DR PROSITE; PS50077; HEAT_REPEAT; 1.
PE 3: Inferred from homology;
KW Amyloid {ECO:0000313|EMBL:ENH65543.1};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Prion {ECO:0000313|EMBL:ENH65543.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000016928};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT REPEAT 217..255
FT /note="HEAT"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00103"
FT DOMAIN 478..695
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 723..1040
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1032..1079
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1034..1062
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1079 AA; 118152 MW; F955918EA608CAAE CRC64;
MPHPVTPPSQ DPTMVSNEAP PPPSQETIND LLNTIFTAKT SAASIDACYG LCEIILSSVG
VAGLNEYGII AEIKKAAADK KSGLRRESSQ NLLGAVFERF LPRQPVSEVV LLLQDGGLVG
CALDALSDKG AVVREAAQYG LDAAFGILSP EALVAGLLPA LTEYLSKKTG KWQGTVGAYK
LLQKMADKAQ ISIGGTKEEA LEKDILREAM GAKLAGLIPI VENGMHDLKA EVEKQAVHTM
NSLTTLLSND DVAPRIPLLI DTMQHPSSQT LQKAIHALSQ TTFVAIVTSP VLALLTPFLE
RSLNNPTTAQ EVLRQTVVIV ENLTKLVHDP IEARTFLPKL IPGVKSVCDR ASLPEVREIA
ERALATMEKA MGDDKDVVAR TAGDDVAKIL DEQIKANGGL AGSLDLWKQA RPYISDMVAI
DVNYRFVNRI SGRIAPYVKS FVKDAEAPQK IADTIQQHYV DEDHRRYGVP EKEDDGEVEI
VNADFSLAYG GMLLLSHTNL RLLKGHRYGL CGRNGAGKST LMRSIANGKL EGFPPQDVLR
TCYVEHNQGE DADISILEFV AKDPEIATQG RERISEVLAE FGFTAGPEGR QAERVGSLSG
GWKMKLALAR AMLQRADVLL LDEPTNHLDV ANIAWLENYL KSHPDITSLI VSHDSGFLDN
VTTDIYHYEP NKKLACYKGN LANFVKIRPE AKSYYTLSAS TVQFKFPPPG ILTGVKSQTR
AIIRMSNVSY AYPGATKPSL QEVSCQLSLS SRVAIIGPNG AGKSTLIKLL TGETIPTTGK
VEKHPNLRIG YIKQHALEHV EMHLEKTPNQ YLQWRYQHGD DREVHMKQTR VLSDADRAQM
EKWVDLKDGK SPRQIESLVG RSKYKKTFQY EVKWRGLLPK NNTMISRETL TELGFDKLVQ
EFDDHEASRE GLGYRELQPK VISKHFEDLG LDPEIANHNE IGSLSGGQKV KVVIAGAMWN
NPHLLVLDEP TNFLDRDSLG GLAVAIRDFK GGVILISHNE EFVGALCSEQ WHVRDGRVAL
RGNAAVSLDR FEDSRPSSGV NSTAASSVVS SAVNSGIEDN SDMNPKGTPH PPDTDDEDN
//