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Database: UniProt
Entry: U1G9F4_ENDPU
LinkDB: U1G9F4_ENDPU
Original site: U1G9F4_ENDPU 
ID   U1G9F4_ENDPU            Unreviewed;      1789 AA.
AC   U1G9F4;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   RecName: Full=RING-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=EPUS_02782 {ECO:0000313|EMBL:ERF68326.1};
OS   Endocarpon pusillum (strain Z07020 / HMAS-L-300199) (Lichen-forming
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Verrucariales; Verrucariaceae; Endocarpon.
OX   NCBI_TaxID=1263415 {ECO:0000313|EMBL:ERF68326.1, ECO:0000313|Proteomes:UP000019373};
RN   [1] {ECO:0000313|Proteomes:UP000019373}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Z07020 / HMAS-L-300199 {ECO:0000313|Proteomes:UP000019373};
RX   PubMed=24438332; DOI=10.1186/1471-2164-15-34;
RA   Wang Y.-Y., Liu B., Zhang X.-Y., Zhou Q.-M., Zhang T., Li H., Yu Y.-F.,
RA   Zhang X.-L., Hao X.-Y., Wang M., Wang L., Wei J.-C.;
RT   "Genome characteristics reveal the impact of lichenization on lichen-
RT   forming fungus Endocarpon pusillum Hedwig (Verrucariales, Ascomycota).";
RL   BMC Genomics 15:34-34(2014).
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DR   EMBL; KE721523; ERF68326.1; -; Genomic_DNA.
DR   RefSeq; XP_007806101.1; XM_007807910.1.
DR   GeneID; 19237832; -.
DR   eggNOG; KOG0927; Eukaryota.
DR   eggNOG; KOG2114; Eukaryota.
DR   HOGENOM; CLU_238384_0_0_1; -.
DR   OrthoDB; 5491867at2759; -.
DR   Proteomes; UP000019373; Unassembled WGS sequence.
DR   GO; GO:0005768; C:endosome; IEA:UniProt.
DR   GO; GO:0099023; C:vesicle tethering complex; IEA:UniProt.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:UniProtKB-UniRule.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR   CDD; cd16688; RING-H2_Vps11; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000547; Clathrin_H-chain/VPS_repeat.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR024763; VPS11_C.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR23323; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN; 1.
DR   PANTHER; PTHR23323:SF24; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 11 HOMOLOG; 1.
DR   Pfam; PF00005; ABC_tran; 2.
DR   Pfam; PF00637; Clathrin; 1.
DR   Pfam; PF12451; VPS11_C; 1.
DR   Pfam; PF17122; zf-C3H2C3; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
DR   PROSITE; PS50236; CHCR; 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:UP000019373};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          36..304
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   DOMAIN          449..771
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   DOMAIN          1679..1729
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          404..437
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1393..1427
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        408..433
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1395..1416
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1789 AA;  198046 MW;  01462B0AC02FCD20 CRC64;
     MKVPITLPIR YRAPPSIENL IQIQNGTFYR QHPGGLQESN TPLFPNLYFS LPAFPLRRDS
     ETGKQQQHWA VVGASGGSTF LEILRGTHIC LPPNARTFPY LSSEDIEAKD YRLRSPTWAI
     QYVGFTSGKG QGLVGGIRGS YLSARYESRR EETDWSVLQY LKGEMELNPS KELHYEDASF
     NALLSQVIKD LRLEQLTSLP VSNLSNGQTR RARIAKALLG RPEVLLLDEP FMGLDPPTLV
     SLSPILRGLA YKSSPRLIMS LRPQDPIPDW ITHLAVLGHQ DTLALAGPKK EVLFAVHRWA
     NAHKGPQNGT AAKMAALMTN RHGPPPLDFG YTLSATGVSR DVTNSQIVSS KTPTYISATD
     ELVPEHLSVA YRLVWQKAAG KPREKADLDD LLSLTCLLPA EFNRQDDVPA PSNESFSISE
     DPRRGQHNSG FPVSNFPMRP HPELGKSLIE LKNVIVSYGS KTVLGYGVQS GFQVPGLNLD
     IRQGTRLALL GPNGSGKTTL LSLLTSDHPQ SYSLPIKYFG RSRLPSPGQP GVSLWEIQSR
     IGHSSPEIHA FFPKGLTIRR SLESAWAETF AAKPEPTNSS KALVDAFLRW WEPELNPCHQ
     PLPPLEAPAI PIDDSVSSSY PSFKHSSQTA NELEWASLPL NTFGSLSFQS QRLLLLLRAI
     IKTPDIVILD EAFSGFSPEV RDKAMRFLGA GENSVPHQHQ AATYRTCMDD GDGESSRWPL
     RDDRTRVETI CHTTRVTPNE PIVGKEGMTH EKKKRVDRLR RKTKSELTAE GDLADDSVEY
     AFHGLSNEQA LIVVSHVREE IPDLVNEYIR LPGEEEVSEQ RRGIEMVVAT GVLACKSEVI
     ALPTIAGSDS IFLGDSNGDV RILSRALRVV RLFHAADPSS HGSITHLKQI DATSLLVTIC
     EDLSSDPVLK VWALDKEEKK TKGPKCLCTI GVQNGRRQFP VSAFVALEDL TQVAVGFANG
     AVTVIRGDLI HDRGTKQRIV FESEEPITGL AIRESPMTIL YIATTGRISN LVISGKGQGQ
     PPRTVDSQGC AVRCMSVDKE TGDIIIARDD AVYYYGPNGR GPSFAFDGPK KMITTFKDYV
     GLVCPPKVAQ VSKSNTYRRL GGSGMGDLFS TSSFSLLETD LRYIAHTESL STELYRYEEK
     TLQQKLEILY QRNLYILAIN LAQKAGVDTA TQNVIFRKYG DYLYQKGDYD TAMQQYLRAI
     DNTEPSQILR KFLDTQRIHN LIEYLEELHE HDKATADHTT LLLNCYAKLK DTEKLDAFIR
     APGELKFDLE TAISMCRQGG YFEQAAYLAT KHGENSLVVD ILIEDSKKYP EALAYIWQLE
     PLAAYPNLMK YSRVLLEHCP DEATQVFIDY YTGNYRPKEE VTATQEPQPQ NQASAFQNLS
     ALLPLPYMNR SAVASPAPEA QQQTTTADTK LASNADTPTP EYPIPRPRTA FSSFIPHPSH
     FIRFLEALTS QPNISSTDKT DLYTTLFEMY LEAANSESTT SSEREAWQHK AKALITSQPQ
     ISTQSSDQPL SFIPTSSVLL LSSLSNFPTG TTLVRERANL YTDILRSHTT AKDTSGAISA
     LRRYGPEDPS LYPIALSYFS SSTTILSQPG VKEELQSVLR KIDQDSLMAP LQVVKVLSQG
     GAVSMGMVKS YLSDNISRER KEIRNNRTLI ESYRKESAAK ISELEDLGSK PIVFQARRCS
     ACGGQLDLPT VHFACKHSFH QRCLNTGSVS QAAQADATAE GRAECPVCKP QNDTIKAHRR
     AQVESADQHE LFKAALERSQ ERFETVAEFF GRGVMNLNSV GNGPGAGGG
//
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