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Database: UniProt
Entry: C5MI21_CANTT
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Original site: C5MI21_CANTT 
ID   C5MI21_CANTT            Unreviewed;      1229 AA.
AC   C5MI21;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 81.
DE   RecName: Full=Alpha-factor-transporting ATPase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CTRG_05714 {ECO:0000313|EMBL:EER30718.1};
OS   Candida tropicalis (strain ATCC MYA-3404 / T1) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=294747 {ECO:0000313|EMBL:EER30718.1, ECO:0000313|Proteomes:UP000002037};
RN   [1] {ECO:0000313|EMBL:EER30718.1, ECO:0000313|Proteomes:UP000002037}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-3404 / T1 {ECO:0000313|Proteomes:UP000002037};
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA   Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA   Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA   Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA   Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA   Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA   Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; GG692403; EER30718.1; -; Genomic_DNA.
DR   RefSeq; XP_002551416.1; XM_002551370.1.
DR   AlphaFoldDB; C5MI21; -.
DR   STRING; 294747.C5MI21; -.
DR   EnsemblFungi; CTRG_05714-t43_1; CTRG_05714-t43_1-p1; CTRG_05714.
DR   GeneID; 8300929; -.
DR   KEGG; ctp:CTRG_05714; -.
DR   VEuPathDB; FungiDB:CTRG_05714; -.
DR   eggNOG; KOG0055; Eukaryota.
DR   HOGENOM; CLU_000604_17_8_1; -.
DR   OrthoDB; 1693178at2759; -.
DR   Proteomes; UP000002037; Unassembled WGS sequence.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:EnsemblFungi.
DR   GO; GO:0043332; C:mating projection tip; IEA:EnsemblFungi.
DR   GO; GO:0005886; C:plasma membrane; IEA:EnsemblFungi.
DR   GO; GO:0015440; F:ABC-type peptide transporter activity; IEA:EnsemblFungi.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0000770; P:peptide pheromone export; IEA:EnsemblFungi.
DR   CDD; cd18577; ABC_6TM_Pgp_ABCB1_D1_like; 1.
DR   CDD; cd18578; ABC_6TM_Pgp_ABCB1_D2_like; 1.
DR   CDD; cd03228; ABCC_MRP_Like; 1.
DR   Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 1.
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   InterPro; IPR039421; Type_1_exporter.
DR   PANTHER; PTHR24221; ATP-BINDING CASSETTE SUB-FAMILY B; 1.
DR   PANTHER; PTHR24221:SF503; LP14331P; 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:UP000002037};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        39..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        81..111
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        189..208
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        275..295
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        661..684
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        704..724
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        783..803
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        809..830
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          41..332
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50929"
FT   DOMAIN          364..599
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   DOMAIN          664..951
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50929"
FT   DOMAIN          986..1224
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
SQ   SEQUENCE   1229 AA;  137785 MW;  13467FE6A26AB12D CRC64;
     MKAEIDEKEP FPETDADNLE VDVSKNVFMF VELSKDWPII ILGVLLMAAS AAATPINTYV
     YGKIMGQLSE FYINGSSYHL FINQIGRLCG VLIGVGGAKL ILVWMGMFIW LKFGEIQQHR
     AREEIFDKIL KEPTSWYDLN TNLMGEMTQV NRCIEELRSG NGEIMANIVQ TCGLVISLII
     MSFYQSWQIT LIVMASAPVM AVVGWYFGKL TYKAQEQENE YTSQASKILD WCLVNPISVR
     IFNGKYIELS KFNHIVNTSA KSYYKVANAI AANSGVLKFL TLMMFVQGFW FGVYLMQKGR
     VTIGQLFTTF SSTLMLGQTI SGVTSLLAVL NTSHAAAGKI AKYLQTEEEP QLATCYPSYS
     VDNIEFDNVT FKYPSRDEII LKGVTFKIQQ NRFNYIIGKS GAGKSTIPLI IMNLYPTIGG
     AVRIDGIPIQ YLDPKYIAQN ITLLQQNPVM FNNKTILENI ALGVIDDYDT LEDIPRHLVE
     KAAKFSLLSD LDLDMKVSGS SLSGGQQQRI SIARAYLKDS PVLIMDESFS ALDNQNKQVL
     FQRIKKWRNG KTTIFITHEY DNIEDDDFVI IMEHGNVKDQ GEFIKFKNDE VVTSYKAQAY
     EEVKEPEVTK EKAHTNYDYK TNPYILKDLE SASIDEDKEE EKLMGVIAIL KYCSSSITRK
     WLLALGVLIS LLEGAANPIF SYCFSKLLAI SMEASIGVNV TSKIVVWSCI SLSIAGFTGI
     STYLSEFILQ YCSENWIVSL RQMSFDKINN QDMSYFNSKL EPAEITTLLM NDTRDLRSLV
     SQYISLVTTL VTMVLIGVIW SIVTGWKLAL VGIAFVPLVL LVTCAYGIIL EIAENKYKTS
     VVDVETQIHQ TMTSIKTIRL FHMNRYFKES YDEALVGLKS VGTYRAFQTG IGFAISDLCS
     AISQGIILFY GMQLAGKFQY SYFQLLEVIT LLTFTISNAS SLINHLPDIA RGQRAGTFVV
     KLLESTPISK VETEGKIIPR PSDKAISFNN VTFAYPSDLL EPKLKNVTFD ININETVGLV
     GESGSGKSTI ISILLRLYGA KSVKLFNEDI SQIDIDWLRE TIGIVPQFPK FFDGSIYDNL
     LYGMNPIRIV SEQEVTNVLK LVNMYEFIVS LPEGIQTCIG EGSNSLVSGG QLQRLSIARA
     ILRNPKILIF DECTSNLDPI NSKQIIKLIE SLNGKFTILF ITHDKEMMRI ADNLIVLKNG
     KLVEQGSYLQ LISSKGELSE ITKSPDIFL
//
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