ID F8MYD0_NEUT8 Unreviewed; 1110 AA.
AC F8MYD0;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 24-JAN-2024, entry version 58.
DE RecName: Full=ABC transporter domain-containing protein {ECO:0000259|PROSITE:PS50893};
GN ORFNames=NEUTE1DRAFT_149152 {ECO:0000313|EMBL:EGO51327.1};
OS Neurospora tetrasperma (strain FGSC 2508 / ATCC MYA-4615 / P0657).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=510951 {ECO:0000313|EMBL:EGO51327.1};
RN [1] {ECO:0000313|EMBL:EGO51327.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FGSC 2508 {ECO:0000313|EMBL:EGO51327.1};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Ellison C.E., Stajich J.E., Jacobson D.J., Lindquist E., Lapidus A.,
RA Foster B., Aerts A., Riley R., Grigoriev I.V., Taylor J.W.;
RT "Massive changes in genome architecture accompany the transition to self-
RT fertility in the filamentous fungus Neurospora tetrasperma.";
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
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; GL891382; EGO51327.1; -; Genomic_DNA.
DR RefSeq; XP_009854970.1; XM_009856668.1.
DR AlphaFoldDB; F8MYD0; -.
DR GeneID; 20827065; -.
DR KEGG; nte:NEUTE1DRAFT149152; -.
DR VEuPathDB; FungiDB:NEUTE1DRAFT_149152; -.
DR HOGENOM; CLU_002848_0_1_1; -.
DR OrthoDB; 49929at2759; -.
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: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; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR19211:SF14; ATP-BINDING CASSETTE SUB-FAMILY F MEMBER 1; 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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 468..685
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 713..1030
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 1022..1110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1028..1061
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1076..1092
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1110 AA; 121547 MW; A7349106AF3B6D42 CRC64;
MTVPIMVADG AAPPVSQADV TSILDTVFNA KTSQASIDAA YGLCEVLLQS YGYRGLELYG
VLSELKKAAA DKKSGLKREG AQNLLGALFE RFPPRQPASE SLLTSPEAGL VACALDALAD
KGAVVREAAQ YGLDALYNNL SPEALVVGLL PALIAYLEKS TGKWQGTIGA YQLIEKISNK
AQITIGTTKE EAAEQDVLRE AMGTKLARLI PIVEGGMLDM KNEVAKQAVK TMTALTTLLS
NDDVAPRIPL LIETMQHPSP ATVQKAIHAL SMTTFVAIVT APVLALLTPF LERSLSNPGT
PQEVLRQTVV ITENLTKLVH DPIEARTFLP KLQPGIKSVV DRASLPEVRE IATRALAVMD
KAMGSDQDKV IERTHAEDVG TVLDAEVKKA GGLIGDPVVY QTVRKYVGEM VAEDVNHRHC
NRIAARTGPY LSFLVADPVA VGEAVQKHYV DEDAIKYGVP EKEDDGEIEI VNADFSLAYG
GMLLLQHTNL RLLKGHRYGL CGRNGAGKST LMKAIASGKL EGFPSQDVLR TCYVEHNQGE
DADISILDFM VKDPTIASEG RERISAVLEE FGFTSGPEGR QSQKVGSLSG GWKMKLALAR
AMLQKADVLL LDEPTNHLDV ANIKWLEEYL KSHTDITSLI VSHDSGFLDN VTTDIYHYEP
NKKLGHYKGN LAAFVNVRPE AKAYYTLSAS NVQFKFPPPG ILSGVKSQTR AIIRMTDVSF
TYPNAPKPSL SGVTCQLSLS SRVAIIGPNG AGKSTLIKLL TGEVIPTAGK VEKHPNLRIG
YIKQHALEHV EMHLEKTPNQ YLQWRYQHGD DREVHMKQTR QLTEADKEQM DKFVDVGDGK
GKRQVEALVG RQKYKKTFQY EVKWRGFLPK HNTMISRETL LELGFQKLIQ EFDDHESSRE
GLGYRELQPA VISKHFEDLG LDPEIANHNE IGSLSGGQKV KVVIAGAMWN NPHMLVLDEP
TNFLDRDSLG GLAVAIRDFK GGVVMISHNE EFVGALASET WNVVDGRVTH KGQNSAALDR
FEDSKPASAV TSGLNTPMGM SEPSTAVNSG VEDNSLGVTG ESMTFKAKKK KKMTKKDLKE
REARRRLRHI EWLNSPKGTP HPKDTDDEDE
//