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Database: UniProt
Entry: A0A1Y3NGH2_PIRSE
LinkDB: A0A1Y3NGH2_PIRSE
Original site: A0A1Y3NGH2_PIRSE 
ID   A0A1Y3NGH2_PIRSE        Unreviewed;       908 AA.
AC   A0A1Y3NGH2;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=ABC-2 type transporter transmembrane domain-containing protein {ECO:0000259|Pfam:PF12698};
GN   ORFNames=PIROE2DRAFT_60267 {ECO:0000313|EMBL:OUM65101.1};
OS   Piromyces sp. (strain E2).
OC   Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC   Chytridiomycota incertae sedis; Neocallimastigomycetes; Neocallimastigales;
OC   Neocallimastigaceae; Piromyces.
OX   NCBI_TaxID=73868 {ECO:0000313|EMBL:OUM65101.1, ECO:0000313|Proteomes:UP000195826};
RN   [1] {ECO:0000313|EMBL:OUM65101.1, ECO:0000313|Proteomes:UP000195826}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2 {ECO:0000313|EMBL:OUM65101.1,
RC   ECO:0000313|Proteomes:UP000195826};
RG   DOE Joint Genome Institute;
RA   Haitjema C.H., Gilmore S.P., Henske J.K., Solomon K.V., De Groot R.,
RA   Kuo A., Mondo S.J., Salamov A.A., Labutti K., Zhao Z., Chiniquy J.,
RA   Barry K., Brewer H.M., Purvine S.O., Wright A.T., Boxma B., Van Alen T.,
RA   Hackstein J.H., Baker S.E., Grigoriev I.V., O'Malley M.A.;
RT   "A Parts List for Fungal Cellulosomes Revealed by Comparative Genomics.";
RL   Submitted (AUG-2016) 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; KZ150843; OUM65101.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y3NGH2; -.
DR   STRING; 73868.A0A1Y3NGH2; -.
DR   Proteomes; UP000195826; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR   InterPro; IPR013525; ABC2_TM.
DR   InterPro; IPR026082; ABCA.
DR   PANTHER; PTHR19229:SF36; ATP-BINDING CASSETTE SUB-FAMILY A MEMBER 5 ISOFORM X1; 1.
DR   PANTHER; PTHR19229; ATP-BINDING CASSETTE TRANSPORTER SUBFAMILY A ABCA; 1.
DR   Pfam; PF12698; ABC2_membrane_3; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000195826};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        422..442
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        609..632
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        652..682
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        689..711
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        723..744
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        775..800
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        864..885
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          422..749
FT                   /note="ABC-2 type transporter transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF12698"
FT   REGION          73..92
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          341..361
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        346..360
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   908 AA;  106741 MW;  627AD769F3B098BD CRC64;
     MGIWETPEMT ISIIMKEEEI RNAEKDYFIE TFLRNEALQK FELIKYNNQS YNWHSKKDIE
     SWDDNDNRID IENIENEEQN ENENENENEN ENIQKNNINY EIYVNVFDSE KKFKEYYKNN
     WINAGYYNKT IYGIIFKSPT KYTLQFKYDK EIYENIVRES DYTKDTVYGD FSDGNLKYQA
     DISIMSTSAM QLLVDKTIMK TISNSNTNNY INDSTYSAKD DFKVYDSKII NHTNIHANPE
     SDWSIYSSSN EEEDDNFTTN SNNKSKYDYL LTYTFPMKYS KSFKDIFEGL NKLIADDYNT
     VKKFSLTAPA LEDLFLKLEE NNEDKNNQTE QIRDSVIINM ENDNNNDNEN KTETSHDHDQ
     RNNQYLSQCD LKSNNNDSVM LKKLKVIFNE AKYIRISSLQ QIYNIFLLRL KVFFRNKIFD
     TFYFLLPIIV ITVTLQIGNY VLNMHSSEQK YSEIEIHPII YGSKNFWFKN TTEVSYDVLN
     VLNNIKTSSK IKTENDKKNI RVHSLNIPSY LGGFGGDLND NYSTSSYSSI FTIYHNLIYI
     YSLPLAINFL DNAILKEIYH KNCNIEVSYQ PFTSYYLDED SNEKPLIKME EDVNIEDLIK
     ISFEFKKEVN ILLIVEIGTI IATSVSVYGS VIVKDKEDGI THQLFLNGIK RINYWIGVFL
     SDTFCLIFLL VPMISTGIII GMDIFNTKVL FLTILLTLLW IFVSLLHQYF LSHFFSKYKS
     ASQFFIIVNP IISLIMGVLI IILVSNDESN LSRNETSPVI NDNQNEYNVY SVMNYLFCFL
     MYPPVTLIFF YGKIFSYIMF VKSNPLPEEI THFKNLPSTN ELLLQYKEKG LTKNIISSEI
     TRTFTNTLFP SISDILDKNK NPKFTTIIIG IIILILVYIY IIYLFDNINI TTIRRSREYQ
     KKRKRKIR
//
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