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Database: UniProt
Entry: A0A0L0TDK9_ALLM3
LinkDB: A0A0L0TDK9_ALLM3
Original site: A0A0L0TDK9_ALLM3 
ID   A0A0L0TDK9_ALLM3        Unreviewed;      1416 AA.
AC   A0A0L0TDK9;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=P-loop containing nucleoside triphosphate hydrolase protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=AMAG_16423 {ECO:0000313|EMBL:KNE72664.1};
OS   Allomyces macrogynus (strain ATCC 38327) (Allomyces javanicus var.
OS   macrogynus).
OC   Eukaryota; Fungi; Fungi incertae sedis; Blastocladiomycota;
OC   Blastocladiomycetes; Blastocladiales; Blastocladiaceae; Allomyces.
OX   NCBI_TaxID=578462 {ECO:0000313|EMBL:KNE72664.1, ECO:0000313|Proteomes:UP000054350};
RN   [1] {ECO:0000313|EMBL:KNE72664.1, ECO:0000313|Proteomes:UP000054350}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 38327 {ECO:0000313|EMBL:KNE72664.1,
RC   ECO:0000313|Proteomes:UP000054350};
RG   The Broad Institute Genome Sequencing Platform;
RA   Russ C., Cuomo C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA   Lang F.B.F., Roger A.J., Ruiz-Trillo I., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA   Berlin A., Chapman S.B., Gearin G., Goldberg J., Griggs A., Gujja S.,
RA   Hansen M., Heiman D., Howarth C., Larimer J., Lui A., MacDonald P.J.P.,
RA   McCowen C., Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "Annotation of Allomyces macrogynus ATCC 38327.";
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000054350}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 38327 {ECO:0000313|Proteomes:UP000054350};
RG   The Broad Institute Genome Sequencing Platform;
RA   Russ C., Cuomo C., Shea T., Young S.K., Zeng Q., Koehrsen M., Haas B.,
RA   Borodovsky M., Guigo R., Alvarado L., Berlin A., Borenstein D., Chen Z.,
RA   Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA   Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Lewis B., Mehta T.,
RA   Park D., Pearson M., Roberts A., Saif S., Shenoy N., Sisk P., Stolte C.,
RA   Sykes S., Walk T., White J., Yandava C., Burger G., Gray M.W.,
RA   Holland P.W.H., King N., Lang F.B.F., Roger A.J., Ruiz-Trillo I.,
RA   Lander E., Nusbaum C.;
RT   "The Genome Sequence of Allomyces macrogynus strain ATCC 38327.";
RL   Submitted (NOV-2009) 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; GG745382; KNE72664.1; -; Genomic_DNA.
DR   STRING; 578462.A0A0L0TDK9; -.
DR   EnsemblFungi; KNE72664; KNE72664; AMAG_16423.
DR   VEuPathDB; FungiDB:AMAG_16423; -.
DR   eggNOG; KOG0054; Eukaryota.
DR   OMA; APYLMDN; -.
DR   OrthoDB; 3295317at2759; -.
DR   Proteomes; UP000054350; Unassembled WGS sequence.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; IEA:UniProt.
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; cd18579; ABC_6TM_ABCC_D1; 1.
DR   CDD; cd18580; ABC_6TM_ABCC_D2; 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; IPR044746; ABCC_6TM_D1.
DR   InterPro; IPR044726; ABCC_6TM_D2.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR24223; ATP-BINDING CASSETTE SUB-FAMILY C; 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; 1.
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:UP000054350};
KW   Signal {ECO:0000256|SAM:SignalP};
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   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..1416
FT                   /note="P-loop containing nucleoside triphosphate hydrolase
FT                   protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5005548749"
FT   TRANSMEM        34..54
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        61..82
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        94..111
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        123..144
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        244..265
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        285..303
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        358..380
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        386..404
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        859..885
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        897..916
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        983..1015
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1085..1107
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          245..484
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50929"
FT   DOMAIN          555..781
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   DOMAIN          863..1142
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50929"
FT   DOMAIN          1179..1411
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   REGION          787..839
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        787..816
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        825..839
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1416 AA;  155354 MW;  CAC5E61D0C631BE0 CRC64;
     MSLLAFAILA NRLWFLNARP DLPAEMTGGG RWLLVFKMIM AVANLAVVIV TLVVEATQPR
     PAAASTLFGW ISLCLPLAVA IFSHHLEHHR SRRASSSLSS LYLLTVVVLA VRLRTLALHR
     DDYTSTLTTL AGTQLGISAV LFIAENFSSK RMRTDARDGR KQADESPELT ASFLSKITFW
     WVLPLLSRAS KTVLTATDLW DLPHLWSSRP NQQRLQHAWE TELKKSGDKA SFARALAAAF
     GPRIAVMLLF ALLNTLIVLL TPKFVEYFVG FVVARGTLAE RPLSEGLAMV LVFIAYGITQ
     SVLNGQQRHI MQTEMARMLA AIRGVVYHKI MAIPSHDQSQ SGTSGNIVNH CQVDASRIVA
     AIQFVAAIAT VPFGLVLGMA LMYQQVGWAM MMVLVVTALL MALMSRIGGP MAKVQTESLK
     HNDTRIKLCS DALTGIKTYK LYGWTKPIAD RILAVRDAQL RALRKMTILL SIQAGSTDIM
     PTLSAYGSAD LTVQKVFVVT TLYRLISGPM ETLAFGWAPL LAAWVSVQRI TKFLNTPELA
     TYVDRSTDTT DPVAISVKDA QFAFVDDKPV LAIDQLEFAR GSVTAVVGRV GAGKTALLNA
     ILGEVYQTSP NGSVTVRGTV AYASQKAWIL NASLCENILF GLPYDEKKYR KIIEACALKR
     DLAMLVNGDQ TLIGDKGINL SGGQRARLNC ARALYADADL FLLDDPLSAV DAHVDRHLFD
     AWFNLDSGLL RGKTVVLVTH AVHHLPDVDR IVAVQDGKIA EVGTYAELMA REDGVVADLV
     REYMAKRRDD DEEETSGSAT DDVRNEEKKK KRALEKTLSS TTVASAKDDD KEVESSEESK
     ESGSVGWNVY MTYMRACGWV NVFAALLFAC IANAMIIFET IWLGMWGQAA TEGHADFGFY
     IGIYGVISVV FAIGILGSLY TTLAVAAFHA SIGMFTKVLH SVMRAPGWFF DVTPAGRILN
     RMASDQDKVD LQVPLNLMQF TFLLIYVIAV FINVIIASPW FALIVLPIGV LFVWIERLYL
     NVSREVQRLF QISLSPVFQH VTETLDGLPV IRGGYHHANR FEHMALDKID HSGQAWYASI
     CTTRWLYVQV ELVGNLIMGL VALLAVLVKD ANAALMGSAL SQAFVLVSIF SEIMTTYGNV
     ENTLVSVERI NEYMHLPAEA PEETTAVALD AKWPADGAIE IDDYSTTYRE GLDPVLKHVS
     VHVRAGERIG IVGRTGAGKS SLTLALFRII EATSGRITID GLDIAQLGLQ DLRTRLTILP
     QDPIIFHASV RDNLDPTGAN DDAAVWRALD SAGLADFIRE LEGQLDAPLT AASMSVGQSQ
     LLCLARALLR KTKILVLDEA TASVDPQTDE IVQKTIRREF AGCTILTIAH RVATVMDYDK
     ILTLDHGKVV EFDSPEALLA DQESVFYSLA KESKLI
//
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