ID F4WCW7_ACREC Unreviewed; 1621 AA.
AC F4WCW7;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=ATP-binding cassette sub-family A member 3 {ECO:0000313|EMBL:EGI67948.1};
GN ORFNames=G5I_03400 {ECO:0000313|EMBL:EGI67948.1};
OS Acromyrmex echinatior (Panamanian leafcutter ant) (Acromyrmex octospinosus
OS echinatior).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Acromyrmex.
OX NCBI_TaxID=103372 {ECO:0000313|Proteomes:UP000007755};
RN [1] {ECO:0000313|EMBL:EGI67948.1}
RP NUCLEOTIDE SEQUENCE.
RA Nygaard S., Zhang G.;
RT "The genome of the leaf-cutting ant Acromyrmex echinatior suggests key
RT adaptations to social evolution and fungus farming.";
RL Submitted (FEB-2011) 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; GL888074; EGI67948.1; -; Genomic_DNA.
DR STRING; 103372.F4WCW7; -.
DR eggNOG; KOG0059; Eukaryota.
DR InParanoid; F4WCW7; -.
DR Proteomes; UP000007755; 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; cd03263; ABC_subfamily_A; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
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; IPR026082; ABCA.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR19229:SF250; ATP-BINDING CASSETTE SUB-FAMILY A MEMBER 3; 1.
DR PANTHER; PTHR19229; ATP-BINDING CASSETTE TRANSPORTER SUBFAMILY A ABCA; 1.
DR Pfam; PF12698; ABC2_membrane_3; 1.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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, ECO:0000313|EMBL:EGI67948.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000007755};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 224..247
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 267..291
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 311..333
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 340..358
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 364..384
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 802..825
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 973..992
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1013..1038
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1053..1076
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1083..1102
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1122..1143
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1196..1213
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 446..684
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 1290..1520
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
SQ SEQUENCE 1621 AA; 183743 MW; BF76511477BBB0C5 CRC64;
MASGWKIFGL LMYKNMIVRK RHWRMMIFLQ TLVPIAVFAL LQAVRDFSVQ PPVVVNVSTY
YPLYTQDELM EKIDNALHKV YYVPKNAYTD KIMESVRYCL HLLPENMNGF ANETEVVNVY
TRSQAQNPIL SAVAVIFKQY DQPTIKYKLR HSWKIPNSLY QNLLEGERIS TSTSMYVDMM
PFIQVQICLD EAFIKQIAPD SNVKMSIQRM PYPPYVKIDV ADTVFRMIIV SLGVTIFLIT
LCVETNYASK EKFIGINVLM AMNGVKLVYN LLSWLITGIL MSTIYIIPII ILFKNTFSDN
VEALLEYGNA FIFWLLFTVH IAHLITFGMH IAAYFSKPRF VTIALAIIYM AAISFHQNMA
RQEVFGVIPY FGIIFPNIML HRLLQESNAH ESKLIGIQWH NLFVPGETEY DIVGSPALDD
EATEFDYDKT NKDFEPVFGN ALTPGIQIRD LKKSYTTSWL RKSKVHALKG VSVDFYKGQI
TALLGHNGAG KTTLMSILTG VTSETEGKVF INGKNIRKHL NSIRNDLGLC PQENMVFPDL
NVFEQIEFFG LLKAKNKTRN EIKKDVLNLL AKLKLSEKKN FLPSKLSGGQ QRRLCLGMAL
IGDASIIILD EPTSGMDPET RRDTWDIILK LRGEKTILIS THNMEEADIL GDRIAIMHAG
RLRSYGTAMF LKKQYGHGHI EVTLSTKSWC VPEKVISKFD SRAQQLSVDS EKIVLNVPYT
DSLSQSLDKV ESEKKQLGVT GISVSLITLE QVFLKIVRSE DSEKHLNELF TAPLQKVTGT
ELCMQTISAL FCKKFTYIRK NLTILLTILI LPIFSVLLMA LSYSLPTDST DIVPLKLDMY
RYPKALYSSN NEPIAQKYKN IVQNVGGEAE RVASDINVTS ALLNSSMKNL VEYRNNLIVS
AEFNDTENNI WANGFYSGIA IHSVPLTVNL LSNSFIKAFA GDEYSIIASR QQLPNTIMSS
QIQMPEVDSM SRVLLFCMFF FPTMSLFVMH PLQETATKVK QLQRMTGVTS LSYWSTMFAI
DFLIFTIGVL LITLAFYIMD IILDIRLYYK VEILYLILTL ELFGINVLFL VYLFSFMNKS
RSTIITILGV APIGLVIIQY VLHQVLGNFD WLSPLHILQK RIFRLIPYVS LFHGQLAFFN
IAVQNARCRR LPNILHDIVC LAKDPCCGLD CKDGVCKNQL SYFKNFEDDM SFEESIVYLA
ITPILYFALL IILEEKLLLK LLTKMIGTKL RKEQDTMDDQ VKKEKLAVAV EINKINNQNV
NTKEELKSSA TETINLEPLQ SPISDGNSLF LVYELSKYYG KLMAVKEISF RVKPRECFGL
LGVNGAGKST TFRMLTGEEM SNSGIMYLKQ AEIHSQRTNY LSEMGYCPQT DALIPSLNAF
DHLRLFARLR GIPKTNVELE VNKWINRLNL TACMKQPSGT YSGGNKRRLN IAIALIGNPT
LVLLDEPTTG VDPAARRSLW NTLQSCQAAG QAIILTSHSM EECEALCNRL VIMVKGELVC
IGASQELKQR FGAGYDIHIQ LNPSRTDEDV NNIKKIIEST LTCDIRDENL GFLAYHVTDC
NVTWEKMYDT MKNLKQTYSC IEDYAVLSAT LEQLFIQFAR GTEIIESNIS PTRATSHSET
V
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