ID A0A1J1I2J0_9DIPT Unreviewed; 1603 AA.
AC A0A1J1I2J0;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=CLUMA_CG008006, isoform A {ECO:0000313|EMBL:CRK94501.1};
GN ORFNames=CLUMA_CG008006 {ECO:0000313|EMBL:CRK94501.1};
OS Clunio marinus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Chironomoidea; Chironomidae;
OC Clunio.
OX NCBI_TaxID=568069 {ECO:0000313|EMBL:CRK94501.1, ECO:0000313|Proteomes:UP000183832};
RN [1] {ECO:0000313|EMBL:CRK94501.1, ECO:0000313|Proteomes:UP000183832}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Syromyatnikov M.Y., Popov V.N.;
RL Submitted (APR-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}.
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DR EMBL; CVRI01000039; CRK94501.1; -; Genomic_DNA.
DR STRING; 568069.A0A1J1I2J0; -.
DR OrthoDB; 3471553at2759; -.
DR Proteomes; UP000183832; 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; ATP-BINDING CASSETTE TRANSPORTER SUBFAMILY A ABCA; 1.
DR PANTHER; PTHR19229:SF250; ATP-BINDING CASSETTE, SUB-FAMILY A (ABC1), MEMBER 3B; 1.
DR Pfam; PF12698; ABC2_membrane_3; 2.
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; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 3: Inferred from homology;
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:UP000183832};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 245..271
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 283..308
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 314..333
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 345..365
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 385..409
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 822..841
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1018..1040
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1060..1087
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1099..1120
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1132..1151
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1163..1187
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1207..1227
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 466..696
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 1279..1509
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
SQ SEQUENCE 1603 AA; 184341 MW; 6C46133AA518C6F4 CRC64;
MSFEKYRILL WKNWIIQKRH YKSGIFEILF PVLLIILFTW VKYDFTKNSY YNESSVRISE
SSYNDLNRCM YGSFEYAFAY SPKSPWIEDF FQKTFNDSIK YDRLGSITAF ENAEALNEFL
INSENEELVG IEFEDSLKDS VDKPKVFKFA LRFYDYNSYY YYPHYCMQSL FYELEASFID
TFDHPELPQL YSDSSIYYII SNEEDFFGIL KLIKMTHVLQ NVAIERESRL KETMRIMGLS
NTLHWTGWFT SSFVILLLAF TLVVIILKFK IISGTALLEH SNIFLIWLLF MIYSIALITF
AFLISVIFKK ATTAGNLGTI IYLATFVFFF QFRNSFRSMN YFLKFIYCLP LNTGLAQVIS
IVYDYEKAKI GLQFSNLTSH INSSSFSVLE VMLALLIASI LQLLLMIYIE QVFVGTIGIA
RPWYFPLSPL LRLFKKQKNV RRQSNGEVKN DGEDFEQDPS NIKAGIEIMK LSKYFGPSKV
VDNFNLKIFE NQITVLLGHN GAGKTTTMNM LTGLITPSSG TAFLNGHDVI TNISEARSSL
GLCPQHNILI DEMTVAEHII LFCRLKGVKD MREITEEIDK FANLLEMQDK MNELSKSLSG
GQKRKLSIAV ALCGNSRIVM LDEPTSGLDA GARRSLWNLL IEEKKNRTIL LTTHNMDEAD
VLGDRIAIMN EGKLQTVGSS FFLKKRFGSG YKFICVKKEG CNPNNILDTL KVFAPDSYIE
LDDQTETVFI IKEEHLHNFH KMFKKIEDEI ENLKISTFGC SMTTLEEVFI KVGTSASKSE
EKSSNKTNFN DFTPSRKVTG LSLILYQMYA MIWIKFHYTR RNFYTIGWLI IISALVIYIL
MVTPITFSYN SYNGVSHIQD LTLEALNETM TVVKDDGSNP RLVETYVGLF SGKAQVEVFS
DGFEEALLEM YRLSQETVDE KYLIGAVFSE DMILAFSKYR FDLSYYTSII SSHTMNRAIL
KYVAGSEYDM SIADKFYKFS SDGTTTQTTT TTTTEESTTI NEDTPEDLLY EAEIILNFIY
MFLMFYFILC YWPSAFIAIK VKERVRRSKL LQFISGTNRF TYWLTSFFID FVTMLIVIYT
VVGIVALNQR AFFRTGEQLG TLMAVFSFYS FTAIPFIYIA SFLFAKPATA ETLVSVYGLI
CGILYVVYAS FKFFWKLELF SSFLYWIFIF LGPFSLIDCF VKLSFGYYKG HYDDTDYNAF
RFHEDSLGTN IVMFFVSGIF FISICLLKDH FLFGKLIFKL FKSYQYVPKN SNSYIDDDVK
NEEEKVQKME KHQLKQENLL LKDLSKLYGR NVAVNKLNLS VDNGECFGLL GINGAGKTST
FKMMTGDEII SSGDAWIQGY SMENSMIKAQ KAIGYCPQFD AFTFELSGRE NMKAFALVRG
IPRNEIDKIS MKLATELGFQ MHLEKKAKDY SGGNKRKLST ALALLGDPNL IFLDEPTTGI
DPYSKRQLWT IINKIRYSGK SIILTSHSME ECEALCTRIA IMASGEFKCL GSVQHLKNKF
SKGYILTIKM KQDNEQLLNE IRTRVHNTFA SSQFKEKYME LLTFHITSVD LKWSAIFGKM
FELKAEMEIS DFSITQMSLE QVFLHFTREG QSSNVGSANL IRV
//