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Database: UniProt
Entry: A0A162TXL1_MUCCL
LinkDB: A0A162TXL1_MUCCL
Original site: A0A162TXL1_MUCCL 
ID   A0A162TXL1_MUCCL        Unreviewed;       926 AA.
AC   A0A162TXL1;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=ABC transporter domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=MUCCIDRAFT_151412 {ECO:0000313|EMBL:OAD07952.1};
OS   Mucor lusitanicus CBS 277.49.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX   NCBI_TaxID=747725 {ECO:0000313|EMBL:OAD07952.1, ECO:0000313|Proteomes:UP000077051};
RN   [1] {ECO:0000313|EMBL:OAD07952.1, ECO:0000313|Proteomes:UP000077051}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 277.49 {ECO:0000313|EMBL:OAD07952.1,
RC   ECO:0000313|Proteomes:UP000077051};
RG   DOE Joint Genome Institute;
RA   Corrochano L.M., Kuo A., Marcet-Houben M., Polaino S., Salamov A.,
RA   Villalobos J.M., Alvarez M.I., Avalos J., Benito E.P., Benoit I.,
RA   Burger G., Camino L.P., Canovas D., Cerda-Olmedo E., Cheng J.-F.,
RA   Dominguez A., Elias M., Eslava A.P., Glaser F., Grimwood J., Gutierrez G.,
RA   Heitman J., Henrissat B., Iturriaga E.A., Lang B.F., Lavin J.L., Lee S.,
RA   Li W., Lindquist E., Lopez-Garcia S., Luque E.M., Marcos A.T., Martin J.,
RA   Mccluskey K., Medina H.R., Miralles-Duran A., Miyazaki A., Munoz-Torres E.,
RA   Oguiza J.A., Ohm R., Olmedo M., Orejas M., Ortiz-Castellanos L.,
RA   Pisabarro A.G., Rodriguez-Romero J., Ruiz-Herrera J., Ruiz-Vazquez R.,
RA   Sanz C., Schackwitz W., Schmutz J., Shahriari M., Shelest E.,
RA   Silva-Franco F., Soanes D., Syed K., Tagua V.G., Talbot N.J., Thon M.,
RA   De Vries R.P., Wiebenga A., Yadav J.S., Braun E.L., Baker S., Garre V.,
RA   Horwitz B., Torres-Martinez S., Idnurm A., Herrera-Estrella A.,
RA   Gabaldon T., Grigoriev I.V.;
RT   "Expansion of signal transduction pathways in fungi by whole-genome
RT   duplication.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG family.
CC       Eye pigment precursor importer (TC 3.A.1.204) subfamily.
CC       {ECO:0000256|ARBA:ARBA00005814}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OAD07952.1}.
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DR   EMBL; AMYB01000001; OAD07952.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A162TXL1; -.
DR   STRING; 747725.A0A162TXL1; -.
DR   VEuPathDB; FungiDB:QYA_151412; -.
DR   OrthoDB; 359054at2759; -.
DR   Proteomes; UP000077051; 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; cd03213; ABCG_EPDR; 1.
DR   CDD; cd00054; EGF_CA; 1.
DR   Gene3D; 2.10.25.10; Laminin; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR013525; ABC2_TM.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR48041; ABC TRANSPORTER G FAMILY MEMBER 28; 1.
DR   PANTHER; PTHR48041:SF139; PROTEIN SCARLET; 1.
DR   Pfam; PF01061; ABC2_membrane; 1.
DR   Pfam; PF00005; ABC_tran; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR   PROSITE; PS00022; EGF_1; 2.
DR   PROSITE; PS50026; EGF_3; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00076};
KW   EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077051};
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        255..280
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        671..694
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        706..727
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        748..775
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        787..809
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        816..834
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        900..922
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          27..66
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          308..550
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   DISULFID        56..65
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   926 AA;  102883 MW;  192984E5679273E2 CRC64;
     MLPGFECLQF ANCTDYDGKC KCPPGFGGDD CKQPLCGGLD EGRNRYPREN GTVCDCPDGW
     EGINCNVCTS DSVCDALVPT GQNGTCYRGG LTVYENHQMC NVTNRKILDQ LKDQIPQVTF
     SCNRHDATCD FQFWVDQIES FYCHLDTCAF KQTYEYDRNT TKYTCDKIDC RCIKDEMLCG
     KDGSIDLTDF LNDEIQGPAS FQCNGKACVF SEPAMNDLIS AVFGDDGIFL NCNSGECLHY
     TMVPGFERGE RPINWTMIGS GLGGVAVFLI LVGSGVTFLA KKSTRHDEIR LADDETGKLM
     SEHTPVDLVF DRIGYTLPNV SKPILVNATG SVRSGEILAI LGPSGAGKTT LLDILASRTK
     TGQVTGNLYV NGRQVPREEY AQLIGYVDQE DTMIPTLTVY ETILYSALLR LPRSMSTAAK
     KFRVMEVMQE LNIDSIKDSK IGQPGSRSIS GGERRRVSIA CELVTSPSIL FLDEPTSGLD
     AYNAFNVVES LVSLAQNYKR TIVFTIHQPR SNIVTLFDHL VLLAKGHTIY AGPQTETQRY
     FSQIGYTCPP GFNIGDYAID LTMGAIQHDT QVDIVVQEGE EEEETHESNA TDGLTPHLRQ
     LAQAYDDSTM AAELREEIAQ SIQESNSSGS SSAILSGDTA AIISTHKKPT FITQFRILSD
     RTFKNLYRNP MLMFAHYGIA VVLALVCGGL FYQVSNTIAG FQNRMGLFFF YEALLGFMCL
     TSLQVFSTER ILFIRERANG YYSPGTYFFA KILFDIIPLR VVPPLMMGLI SYYMVGLVEG
     VNEFFKFLLV LVLFNLTAAA LCLAIGVVFK NLSMANLLSV LVMLFSMLFA GLLLNKDSIS
     PAFAWLKYLS FFNYGLEALL VNEMLYLQLV EERFGLNIDV PGATILSTFG FNAKNYWPDV
     IRLASMFTAF ITFAFIWLVF VVKEKR
//
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