ID F8NVJ1_SERL9 Unreviewed; 1018 AA.
AC F8NVJ1;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Chromo domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=SERLADRAFT_361098 {ECO:0000313|EMBL:EGO25400.1};
OS Serpula lacrymans var. lacrymans (strain S7.9) (Dry rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Coniophorineae; Serpulaceae; Serpula.
OX NCBI_TaxID=578457;
RN [1] {ECO:0000313|EMBL:EGO25400.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=S7.9 {ECO:0000313|EMBL:EGO25400.1};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Eastwood D.C., Floudas D., Binder M., Majcherczyk A., Schneider P.,
RA Aerts A., Asiegbu F.O., Baker S.E., Barry K., Bendiksby M., Blumentritt M.,
RA Coutinho P.M., Cullen D., Cullen D., Gathman A., Goodell B., Henrissat B.,
RA Ihrmark K., Kauserud H., Kohler A., LaButti K., Lapidus A., Lavin J.L.,
RA Lee Y.-H., Lindquist E., Lilly W., Lucas S., Morin E., Murat C.,
RA Oguiza J.A., Park J., Pisabarro A.G., Riley R., Rosling A., Salamov A.,
RA Schmidt O., Schmutz J., Skrede I., Stenlid J., Wiebenga A., Xie X.,
RA Kues U., Hibbett D.S., Hoffmeister D., Hogberg N., Martin F.,
RA Grigoriev I.V., Watkinson S.C.;
RT "Evolution of plant cell wall degrading machinery underlies the functional
RT diversity of forest fungi.";
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; GL945433; EGO25400.1; -; Genomic_DNA.
DR RefSeq; XP_007317522.1; XM_007317460.1.
DR AlphaFoldDB; F8NVJ1; -.
DR GeneID; 18809820; -.
DR KEGG; sla:SERLADRAFT_361098; -.
DR HOGENOM; CLU_002848_0_1_1; -.
DR OrthoDB; 49929at2759; -.
DR Proteomes; UP000008064; 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 CDD; cd03221; ABCF_EF-3; 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; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR023779; Chromodomain_CS.
DR InterPro; IPR047038; eEF3_chromodomain-like_sf.
DR InterPro; IPR021133; HEAT_type_2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR034085; TOG.
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 SMART; SM01349; TOG; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
DR PROSITE; PS00598; CHROMO_1; 1.
DR PROSITE; PS50013; CHROMO_2; 1.
DR PROSITE; PS50077; HEAT_REPEAT; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT REPEAT 55..92
FT /note="HEAT"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00103"
FT DOMAIN 408..625
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 651..967
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 780..841
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
SQ SEQUENCE 1018 AA; 111591 MW; D47919A5B01AFBAA CRC64;
MCANLVDRSD NDVLSSLQAF ALNKKSGYER ESAAIAYQSL PVVLGAPCAP LLLPSLPILF
DLFADKGEVV RLAAAASTKA ILQLLPPEAT RTAFRNLEEI LDKGKWQTKV GALDALKVFV
ATARDAVADE LGHILPKVEI AMHDTKKEVS TAAIKCATSL CTTLANADLA PHIPALVKCM
SNPDAVPACI KALSSTTFVA EVTAPALAVL VPLLIRGLND RSMEVQRRTV VVVDNLVKLV
RDPTVAARYL SPLVDGVEKI AKGAAFPEVR AFAGTALNTL LKSGASSSGS PPARDLDGET
SEVYTALLTL LPLDLALASA TPNGPKSPRH PLVARSLEFQ ASLIVDLVYF RRFQNKEAWQ
RCIGVYLTPW LGADDSATFA EAVRSHFHAI DQAKNATTQN GADGEGELLC DTLFSLAYGA
LLLLSHTTLK LYRGRRYGIL GTNGSGKSTL MRQLRDGKVE NFPPQDQLRC VMVEHSLQGE
DASLSILDFI ASDIDKALAD VPRTKIRQQL LEVGFDDTRQ SETVGGLSGG WKMKLELARA
MLYNADLLLL DEPTNHLDRG SVKWLEQYLI ANKNVTCLII SHDSGFLDNV TTDIIHYETK
KLVYYPGNLS TFVEKHPEAK SYYTLAATSV KFSFPPPGSL MGVRSNTRAI MKLSNCTFTY
PGRPAPSLHN VSCALSLSSR VGVIGPNGAG KSTLIKLLTG ETIPQEGAVY KHPALRVGYV
SQHATHHIER HLEKTPIGYI QWRFQDGHDR ELLEKATRVL TDEEKAVLDQ EWVGRNGTKR
KLELVMGRQK LKKTFQYEIK WRGLDHKFNT WVPRDELLAK GFTKLVQQFD DLESSREGAG
SRDTSALLVR KHLEDIGLDG DIAQYNEISG LSGGQKIKLV IAACLWNNPQ ICVLDEPSNF
LDREALGGLA VAIKEWAGAV VIISHNEEFV TALCPEIWHI EAGRMTHKGK IAVVEDAFAD
VKSPKGSDGG ITRAPIRKKK KLTRNQMKVQ EERRRLRKLA WLTHGGPKPE DTDSEVEL
//