ID A0A0C3ASY6_9AGAM Unreviewed; 2000 AA.
AC A0A0C3ASY6;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KIM68062.1};
GN ORFNames=SCLCIDRAFT_7224 {ECO:0000313|EMBL:KIM68062.1};
OS Scleroderma citrinum Foug A.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Sclerodermatineae; Sclerodermataceae;
OC Scleroderma.
OX NCBI_TaxID=1036808 {ECO:0000313|EMBL:KIM68062.1, ECO:0000313|Proteomes:UP000053989};
RN [1] {ECO:0000313|EMBL:KIM68062.1, ECO:0000313|Proteomes:UP000053989}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Foug A {ECO:0000313|EMBL:KIM68062.1,
RC ECO:0000313|Proteomes:UP000053989};
RG DOE Joint Genome Institute;
RA Kuo A., Kohler A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA Hua S.X.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000053989}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Foug A {ECO:0000313|Proteomes:UP000053989};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (JAN-2015) 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; KN822010; KIM68062.1; -; Genomic_DNA.
DR STRING; 1036808.A0A0C3ASY6; -.
DR HOGENOM; CLU_000604_27_12_1; -.
DR InParanoid; A0A0C3ASY6; -.
DR OrthoDB; 1651462at2759; -.
DR Proteomes; UP000053989; 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; cd18579; ABC_6TM_ABCC_D1; 1.
DR CDD; cd03250; ABCC_MRP_domain1; 1.
DR Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 2.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 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; IPR044746; ABCC_6TM_D1.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR24223; ATP-BINDING CASSETTE SUB-FAMILY C; 1.
DR PANTHER; PTHR24223:SF415; ATP-BINDING CASSETTE SUB-FAMILY C MEMBER SUR; 1.
DR Pfam; PF00664; ABC_membrane; 2.
DR Pfam; PF00005; ABC_tran; 2.
DR Pfam; PF00501; AMP-binding; 1.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF90123; ABC transporter transmembrane region; 2.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
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.
DR PROSITE; PS00455; AMP_BINDING; 1.
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:UP000053989};
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 715..736
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 782..815
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 959..981
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1036..1058
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1078..1102
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1462..1485
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1505..1525
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1574..1591
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1597..1616
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1680..1700
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 795..1099
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 1168..1397
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 1461..1738
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 1778..1994
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 1402..1430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1406..1420
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2000 AA; 220097 MW; 1C6D4F5E1B3C0C94 CRC64;
MSGTMLTPTE ALLQVAKEHP FRVAVRSAGI LWSYSALWSR VRQIADQIPD LDNTRNPIGL
YMGLEIDYVA AAHAIWLAGR AVVFLSTKWT PEVLEVILAR AQVCLVLHGA TVPPEVSGVA
TISTLALLES QQPPSIVPPP LASEAVTEIP VICCITPTSG STGVPKSIVY PMRRSLAVLC
EESSTLLKPL DGQWLRGGTT FLRPLFEIRR FMFNQTTLYL DPSVSVADQC DALCQELEST
RNSQLLRVHF TPSVFRAFAD FAQMRAGDSP LPRGFRRVYW MVIGGESLSI RDLELARIVF
PCATIACNYA CSEVGFAGIS QMFIRPNDPV PSAISFGATQ GCSDLVLLDE SLGVISQAEE
GATGIIGFVT SQSATHYLGN EDATRHMFRP WNGEEMLLYT DDIGCMQADG AIAIKGRSSR
NVKVNGLFVD LDYVERSLAP AFANAGHRVT GFKLVKSNAT EKIVLFASTE STDAMFILKH
ARDALRTANG DDLAMVISSV RCIAEMPFNA SYKVDLAKLQ KMADEPCLLP PGLFAEAPGK
ISADAKVDAL AEEIAAEIAK LSKSKELIPV TTPLLYSGLN SITVVRLYFW LQSEHEYEEE
MTHLFEEEVT PLVLAMEILG DEADEDEDED EDIDEIVIEP SSPASQATIV EEEPPKIALA
DDADDLIKSD TCEPEFEEVD ISASRPRPVS TLVVMQPPVE PVPDSINDVP NHPTLHVTAF
SFLFMTWMTP LLSLGAKRPL LESDLLPLRR NDEAIIVERW IDPFWTQLRG WFFDRKRKLP
GLFNSVFGAA FGLWIISGLL WFISIGSMIL APLFLQQVIV AVNAPPAPTN NATALAEYND
VIMQNTGGFP LFLDNTYKLG GILLGLKLAA TLCGRSSDQL VKRMALNVKT VLISAVYKKA
LRLSAESSQK YNKGYIMSLV NVDCESVSKA WEVTHQVWSI PVQLTVVTVL LCRLLGASAW
AGIGVLFLAL FILIMVVPVF MRKASPWFMR LGDRRLKTIR EVLDGIRVVK VNGWENHFLN
KLEGIRSEQL RWLRQFNTGV ACFVIVGQIT NTLMPLAAFS LFGRENMGKI SAARVFPALS
LFGMLVDPLI ALPQLLSAFV IAMTSWGRIY VFLLAGEKTS TSDSLASGIM NINRYAITIT
GGAFSWPSAE TAAAPAPVKQ EKVIDDDADS IDLEKGADNE ESEEASGPLP FLRDVNISIK
RGSLTAVVGN VGSGKSSLLS AIIGEMMRVS GEVNCNGNVA YCAQQAWIQT STIQENILFG
RPLNIQQLQK AIQTTSFDTD LEGFPHGLAT QMSEKGNNLS GGQKARLALS RAVYSDADIY
LFDDVLAALD PRVGRNVFNN CIRKALRGKT RVLVTHQLQY LNQVDHIIVV SEGRIIEQGT
FDELVARNGE LNRLLSDVQS FSNDSETQKD NKRKSISGAQ KATDEKPNTP DQLIVQEERN
VGAVGVATWW AYLKATGGIS MAVILFLEIV MLQGSVVILS QWLTWWTEGK FSEEASTRIG
IYDGIGFASV LCLIVLNISV LMSTVRASRT FHSKALQGVL RAPMWWFEGQ PIGRIMNRFS
KDIEAIDQRL MPQLFQLVAG IGSLVSTVVI VGYSTPIMLA FMFPIAVIYW FVLRFYRKSL
RELKRLESTQ RGPLQSRISE TLDGIPTIMA YRRETDFANA VGSLLDTSNK PTFLRMHAEI
WVTLRMEALS SLIVFALVML AHTKLVGNST QFALALTYAS TLTYLMNLLL KSAANVEAEM
NSVERLMNYT ESLPQEPAAR LGSDPTQAMW PTRGQIVLRD IDAAYPSRPD KLVLRSVNLT
FRAGETVVIV GRTGSGKSTL LSLLLRMIDP SAGSVEIDGR DPFIFSGTIR SALDFEGKFD
DKALWQVLEL VGMKQFVTSQ ESKLDTVVED NGSNYSVGQR QLLCLAAAIL RNPKILLLDE
ATASIDAGAD VFIQQAMRRS CPNATILSVM HRLSDRILEE CDRVLVMEQG VPIEFASPRE
LLARPNSMFS KLMAAARNSS
//
