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Database: UniProt
Entry: A0A197K3Y6_9FUNG
LinkDB: A0A197K3Y6_9FUNG
Original site: A0A197K3Y6_9FUNG 
ID   A0A197K3Y6_9FUNG        Unreviewed;      1477 AA.
AC   A0A197K3Y6;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=P-loop containing nucleoside triphosphate hydrolase protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=K457DRAFT_16641 {ECO:0000313|EMBL:OAQ32195.1};
OS   Linnemannia elongata AG-77.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mortierellomycotina;
OC   Mortierellomycetes; Mortierellales; Mortierellaceae; Linnemannia.
OX   NCBI_TaxID=1314771 {ECO:0000313|EMBL:OAQ32195.1, ECO:0000313|Proteomes:UP000078512};
RN   [1] {ECO:0000313|EMBL:OAQ32195.1, ECO:0000313|Proteomes:UP000078512}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AG-77 {ECO:0000313|EMBL:OAQ32195.1,
RC   ECO:0000313|Proteomes:UP000078512};
RG   DOE Joint Genome Institute;
RA   Uehling J., Gryganskyi A., Hameed K., Tschaplinski T., Misztal P., Wu S.,
RA   Desiro A., Vande Pol N., Du Z.-Y., Zienkiewicz A., Zienkiewicz K.,
RA   Morin E., Tisserant E., Splivallo R., Hainaut M., Henrissat B., Ohm R.,
RA   Kuo A., Yan J., Lipzen A., Nolan M., Labutti K., Barry K., Goldstein A.,
RA   Labbe J., Schadt C., Tuskan G., Grigoriev I., Martin F., Vilgalys R.,
RA   Bonito G.;
RT   "Genome sequencing reveals origins of a unique bacterial endosymbiosis in
RT   the earliest lineages of terrestrial Fungi.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; KV442026; OAQ32195.1; -; Genomic_DNA.
DR   STRING; 1314771.A0A197K3Y6; -.
DR   OrthoDB; 3295317at2759; -.
DR   Proteomes; UP000078512; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   CDD; cd18597; ABC_6TM_YOR1_D1_like; 1.
DR   CDD; cd18606; ABC_6TM_YOR1_D2_like; 1.
DR   CDD; cd03250; ABCC_MRP_domain1; 1.
DR   CDD; cd03244; ABCC_MRP_domain2; 1.
DR   Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 2.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR011527; ABC1_TM_dom.
DR   InterPro; IPR036640; ABC1_TM_sf.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR24223; ATP-BINDING CASSETTE SUB-FAMILY C; 1.
DR   PANTHER; PTHR24223:SF443; MULTIDRUG-RESISTANCE LIKE PROTEIN 1, ISOFORM I; 1.
DR   Pfam; PF00664; ABC_membrane; 2.
DR   Pfam; PF00005; ABC_tran; 2.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF90123; ABC transporter transmembrane region; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS50929; ABC_TM1F; 2.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078512};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   TRANSMEM        177..198
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        254..276
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        282..307
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        367..388
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        400..422
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        885..902
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        922..949
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          137..423
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50929"
FT   DOMAIN          582..803
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   DOMAIN          889..1164
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50929"
FT   DOMAIN          1204..1436
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   REGION          94..113
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          476..593
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          830..861
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        476..511
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        839..860
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1477 AA;  164559 MW;  CB008283F7725204 CRC64;
     MSIKDKIFKK KVAPPVPEPG STPGICPEET ANFFYRLTFT WVQPLMSIGS TRPLEKEDIW
     EMIERRRADY VSAIFRQEWA KEVAKHEASL SKEKNKDVDL NNASSSELKK KNKKNKEYRP
     KLWKALNRTF LYQFWSAGVL KVIGDALQVF QPLVIKAILN FVTNSLRNRE LGQAPPLWHG
     ILMSIGLYLM GIFASIALHQ FWQRSTSTGV GIRTALITTI YRKGLLLSSK AKQDFSTGKV
     TNLMSTDTTR LDFVAGYFHV IWTAPLMIAL ILILLIDNMG PTALVGFVFL LIVGPLQAKI
     VAALSVIRRK STLITDARVK LTQEVLQGMR VIKFYGWEDA FLSKLEDLRN KELKYVRTLL
     ISRSGIAAIN LTVPVLAATL TFVAYSLAGN ELTPAVVFSS LSLFNIMRMP LMILPQIVSA
     LVDAQVSIRR IEDLLMAEEL EDLPPVNPDL EHAIDITNGN FHWETTLKTL TMEELQKQEK
     EERKRGANKK EHKKELKAKE KAEKKEIKKL AKANGISQQE AEKLYREGRE KTISEQSSET
     MSIQEKMLSK IQEKDPSPDT ESILNSSHES DDNEKAQQES GVESQGSIHS EEKGTFGLKN
     IDLKIPRGQL VAIVGAVGSG KSSLLNALVG EMKKVSGTMS YGGTIGYCPQ SAWIQNATVK
     DNILFGLPLD EARYQRVIKD CALERDIQIL PDGDQTEIGE RGINLSGGQK QRVNIARAVY
     YDADVVLLDD PLSAVDAHVG KYLFKNCILG ALQGKTRVLV THQLHVLPQV DYVICMKDGE
     IVERGTFHEL MVNDGEFASL MKAHGGIEES EEVADDNSVD SAVTTTGAEK VAGGVSEDGN
     GEKTDEKKKE GGKAKKGLMS QEERATGSVD GTIYKTYVNA AGGKFLVPLL LFLLIITQVA
     KVGNDLWLSW WTKDNFHKSQ KFYMVLYAVW GIAQGVFQFI NGFFFSIAGA NAAKVLHQRA
     LKNIFRAPSS FFDTTPLGRI INRFSKDVDA TDNLLSEAYR MFTGTAAIVL STFILISVIF
     PYFLIPLVPM LFFYYYAAVY YRSSSREIKR IDSILRSSLY AHFSETLSGL ATIRAYREQE
     RFIGRNAYFI DLENRPYFMS YSIQRWLGVR IETIANTLVF CTSLLGVCGR YDIDPATIGL
     VLSYSMSVTG TFNWCVRQFA EVENNMNAVE RLYHYSEELT VEADAVIPDN RPSDNWPSAG
     AITIRNLEMR YRPELPSVLH NLSLDIQGGE KIGVVGRTGA GKSSIMMALF RLVEPSKGTM
     EIDGVDICKI GLFDLRTRLA IIPQDPVLFS GTIRSNLDPF EKRTDQELWE VLERSDLKTY
     VTSCEGGLDS QVTEFGENLS VGQRQLLCLA RAMLTRARVI IMDEATASVD VATDVMLQKA
     IRVDFAQSTV LTIAHRLNTV IDYSRVLVLD HGEIKEFDTP ANLLSRPDSV FSSMVDETGP
     ANAALLRQLA NAAAAGNAIA VEEVFGATES DVKGYSV
//
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