ID A0A0C9N0C3_9FUNG Unreviewed; 1523 AA.
AC A0A0C9N0C3;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=ABC metal ion transporter {ECO:0000313|EMBL:GAN09342.1};
GN ORFNames=MAM1_0261c08868 {ECO:0000313|EMBL:GAN09342.1};
OS Mucor ambiguus.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX NCBI_TaxID=91626 {ECO:0000313|EMBL:GAN09342.1};
RN [1] {ECO:0000313|EMBL:GAN09342.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NBRC 6742 {ECO:0000313|EMBL:GAN09342.1};
RA Takeda I., Yamane N., Morita T., Tamano K., Machida M., Baker S., Koike H.;
RT "Draft genome sequence of an oleaginous Mucoromycotina fungus Mucor
RT ambiguus NBRC6742.";
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Early endosome membrane
CC {ECO:0000256|ARBA:ARBA00004146}. Endosome membrane
CC {ECO:0000256|ARBA:ARBA00004608}. Endosome, multivesicular body membrane
CC {ECO:0000256|ARBA:ARBA00004333}. Golgi apparatus membrane
CC {ECO:0000256|ARBA:ARBA00004653}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004653}. Late endosome membrane
CC {ECO:0000256|ARBA:ARBA00004414}. Lysosome membrane
CC {ECO:0000256|ARBA:ARBA00004656}. Melanosome membrane
CC {ECO:0000256|ARBA:ARBA00024320}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion outer membrane
CC {ECO:0000256|ARBA:ARBA00004374}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004374}. Secreted, extracellular exosome
CC {ECO:0000256|ARBA:ARBA00004550}.
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DR EMBL; DF836550; GAN09342.1; -; Genomic_DNA.
DR STRING; 91626.A0A0C9N0C3; -.
DR OrthoDB; 3295317at2759; -.
DR Proteomes; UP000053815; Unassembled WGS sequence.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IEA:UniProt.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032585; C:multivesicular body 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; cd18595; ABC_6TM_MRP1_2_3_6_D1_like; 1.
DR CDD; cd18603; ABC_6TM_MRP1_2_3_6_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; IPR005292; MRP.
DR InterPro; IPR032410; MTABC_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR00957; MRP_assoc_pro; 1.
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 Pfam; PF16185; MTABC_N; 1.
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:UP000053815};
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 47..66
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 87..106
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 118..137
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 144..162
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 177..196
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 280..301
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 331..356
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 408..430
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 436..455
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 522..540
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 552..574
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 959..983
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1003..1030
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1085..1117
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1193..1212
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 293..579
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 619..844
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 963..1248
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 1283..1517
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 849..874
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1523 AA; 170785 MW; 90265CBB1A53108C CRC64;
MDSNQWVIQG HHSKEDPWSG LCRNNEGWGP FSDERVPDFT PCFEDTVITL LPYAFVIIGG
MIRFWILSKR ESLSSDMTRN WHYFAKMTTL LLILITTISS FLFSVLNDGM DWIDNAQVLV
QGVSILAVIF VIGLHHIEYN RNRVSSAILL FYWLFVIIAD GIKLRTKVMN DAPYTDGTQF
ALFATNYVLA IIIFSLENMQ RPKTQYIMLE EDELDSPEEK TNIFGRLTFS WMTPLMRLGY
QKPLTMDDLW NLKSDDQSAV VGVKFQENWQ KELNKSKPSL LRALVKTLGG PFALAAFFKA
LQDILQFTQP MLLKKLMVWV TSYNSEHPEP AYRGVLIAVA MFVTAICQTM FLHQYFQRCF
STGMRLRAAL VTSIYQKTLV LSNASRQKST VGEIVNHMSV DAQRLMDLCT YFHIVWSGPF
QIVIALFFLY NTMGPSIGAG VGILILAIPL NTYIARKMRA YQKTQMGNKD ARVKLMNEIL
NGIRVIKLYA WEMPFLEKIS FIRNDLELAT LKKIGVMSAV QNFTWTSIPF LVSLSTFAVY
VSISDHPLTS DIAFVAIALF GLLQFPLTVF PNVITSTIEA SVSLYRIENY LSSEELDPYA
VTREDYRNDP NYTENTPLVE ITNGEFKWAA EDPKSVLDNI NIKVKKGQVT AVVGRVGAGK
SSLISALLGD TVKIGGDVIL RGSAAYVPQQ PWVMNASLRD NIVFGHRWDA DFYDRVLEAC
SLKSDIAILN GGDQTEIGER GINLSGGQKA RVSLARAIYA RADIYLLDDP LSAVDAHVGR
HIFDHVIGPN GILKNKARIL VTHGISYLPQ VDEVVMLREG QIALSGSYEN LMSQKSELYA
LVTDFGNQPT KASGSEDGES NEGTIEAGEE DVLQPDTASI ELMPREEDAS LGRQRQRMNS
DVSMMSAKTL RRASLVSLHK NGKNAKNGDD SNRLITVEES AKGSVTWDVY KQYAKSCSLY
GVIAVLGLLV LAQIASVGTN LWLKYWSSKN QDHGSNNSVW FYLGIYALIG WSSTLFAMVQ
TLVLWVYCAI RSARVLHSEM LETIVRSPMS FFDTTPLGRI LNRFSKDQHT VDEVLPRTFN
GYFRVLFSVI STIVIIAFST PLFMVLVVPL GIIYIYVQRY YLATSRELKR LDSVGKSPIY
SHFQETISGV STIRAYEQQK RFMFENEGKL DDNQRAYFPS ISCNRWLAVR LEFLGSIIIL
AAALFAVIGV VYGSSKIDAG LVGLSVSYAL SVTQALNWVI RSYCEIETNV VSVERIKEYI
DLPTEKYNAV RGVNPMWPEK GLIEFRDYAT RYRPGLDLAL RDLSFTVAPK EKIGIIGRTG
AGKSSLSLSL FRIVEAARGS IFIDGVDISS LRLFDLRSRL TIIPQDPVLF AGSVRENLDP
FGTHDDAELW QALQHSHLQE HIAGMDGKLN AVVLEGGENF SVGQRQLICL ARALLRRTTI
LVLDEATAAI DVETDSIIQE TIRRQFANCT ILTIAHRINT VLDSDRILVL DKGSIAEFDS
PKKLLQDQDS IFYSMAKQAG LTE
//
