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Database: UniProt
Entry: J4IBU8_9APHY
LinkDB: J4IBU8_9APHY
Original site: J4IBU8_9APHY 
ID   J4IBU8_9APHY            Unreviewed;      1675 AA.
AC   J4IBU8;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   RecName: Full=ER membrane protein complex subunit 1 {ECO:0000256|ARBA:ARBA00020824};
GN   ORFNames=FIBRA_07498 {ECO:0000313|EMBL:CCM05286.1};
OS   Fibroporia radiculosa.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Fibroporiaceae; Fibroporia.
OX   NCBI_TaxID=599839 {ECO:0000313|EMBL:CCM05286.1, ECO:0000313|Proteomes:UP000006352};
RN   [1] {ECO:0000313|EMBL:CCM05286.1, ECO:0000313|Proteomes:UP000006352}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TFFH 294 {ECO:0000313|EMBL:CCM05286.1,
RC   ECO:0000313|Proteomes:UP000006352};
RX   PubMed=22247176; DOI=10.1128/AEM.06745-11;
RA   Tang J.D., Perkins A.D., Sonstegard T.S., Schroeder S.G., Burgess S.C.,
RA   Diehl S.V.;
RT   "Short-read sequencing for genomic analysis of the brown rot fungus
RT   Fibroporia radiculosa.";
RL   Appl. Environ. Microbiol. 78:2272-2281(2012).
CC   -!- SUBUNIT: Component of the ER membrane protein complex (EMC).
CC       {ECO:0000256|ARBA:ARBA00011276}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004115}; Single-pass type I membrane protein
CC       {ECO:0000256|ARBA:ARBA00004115}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein
CC       {ECO:0000256|ARBA:ARBA00004479}.
CC   -!- SIMILARITY: Belongs to the EMC1 family.
CC       {ECO:0000256|ARBA:ARBA00007904}.
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DR   EMBL; HE797184; CCM05286.1; -; Genomic_DNA.
DR   RefSeq; XP_012184569.1; XM_012329179.1.
DR   STRING; 599839.J4IBU8; -.
DR   GeneID; 24100197; -.
DR   HOGENOM; CLU_241670_0_0_1; -.
DR   InParanoid; J4IBU8; -.
DR   OrthoDB; 37872at2759; -.
DR   Proteomes; UP000006352; Unassembled WGS sequence.
DR   GO; GO:0072546; C:EMC complex; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IEA:InterPro.
DR   GO; GO:0008081; F:phosphoric diester hydrolase activity; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR   CDD; cd09122; PLDc_Tdp1_1; 1.
DR   CDD; cd09123; PLDc_Tdp1_2; 1.
DR   Gene3D; 6.10.140.100; -; 1.
DR   Gene3D; 3.30.870.10; Endonuclease Chain A; 2.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR   InterPro; IPR026895; EMC1.
DR   InterPro; IPR011678; EMC1_C.
DR   InterPro; IPR002372; PQQ_repeat.
DR   InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR   InterPro; IPR010347; Tdp1.
DR   InterPro; IPR003903; UIM_dom.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   PANTHER; PTHR21573:SF0; ER MEMBRANE PROTEIN COMPLEX SUBUNIT 1; 1.
DR   PANTHER; PTHR21573; UNCHARACTERIZED; 1.
DR   Pfam; PF07774; EMC1_C; 1.
DR   Pfam; PF13360; PQQ_2; 1.
DR   Pfam; PF06087; Tyr-DNA_phospho; 1.
DR   SMART; SM00726; UIM; 2.
DR   SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR   SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1.
DR   PROSITE; PS50330; UIM; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006352};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..1675
FT                   /note="ER membrane protein complex subunit 1"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003778869"
FT   DOMAIN          797..1001
FT                   /note="ER membrane protein complex subunit 1 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF07774"
FT   REGION          1095..1209
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1570..1592
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1126..1166
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1167..1209
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1313
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR610347-1"
FT   ACT_SITE        1557
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR610347-1"
FT   BINDING         1315
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR610347-2"
FT   BINDING         1559
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR610347-2"
SQ   SEQUENCE   1675 AA;  184885 MW;  B4AD797DA8B898D4 CRC64;
     MRAVRFLLAV SWATRIWALH SSEVGVVDWH KPFIGTPLLD AHSVAPKFHR IGDAGEPTHS
     VVLTATASNV LAALDPVDGH IVWRYMFEGD EHVIGYKQHG NVVAAVSGPG GATLRLLDAS
     AGHLLFERRL HSPESGRLFD PEMLGTSIAF GSEGQDSDIF VLSNAHIVRR IDGKTGDVEW
     GWTAPDEACK ESSLVAYSKI ISTSSTVYVI GLAKSFAAYT VHVSALSATT GELISSINVP
     SSIRDGLADF LTLRNVRDYN IAPHVVWLES ESVRSFALSP ELAAKPMMIK GADYKRILDV
     GLEDFGQIVA LKKDSTAHVF ALGKEGLKGI WEFAESVSSN RYTESIYSSA VDKDGRPYVA
     RVFWSHVFKK ASAHIFAAHL SDGKGLASGF TFPFETSVHG VISHVAVDAA NPGDLQIIAR
     LALTTSTGAV QLWHQDQLQW TREEGLSDIR AVELVDLSER KVATARIDDE SFGDRIKRQI
     AEAQDFPQYA TSFVKRFVTG SYASVSSSVA PDVNASEPLA RDAFGFRKVI VAATSQGKLY
     GIDSANGEVL WSRVFGLGWA ANVGGQVLPV KIFVTRTVSD GDSPQVVLVT QRKATNSLVD
     TVVFHVDALT GDDATGKSPS KDILQGVDVI SGPLVEAFML RTDAGRVVVL LDEFAQIYLY
     PNTPESQDAF RRLAPSLHIP LRTGRPGHRT ITGHRISPEP EFTGRHLSLP TWTLALPPSE
     DILAIVPRTQ QPVASLGKVL GNRTTLYKYL NPHLMAVVTS STSRCSIYLV DGSKGTIVYH
     AVLPSADSKC DVNVVLAENW LVYHYFDSEA TGVNEAKGHR IVSVELYEGG GVDDKTRRLD
     KLRIVFLLQQ NNFPYSLRAS ARERVTVRRS ADAEAFHTVA NENYQIQSFP RRFLDPRRPK
     RKPTSEEMEE WLTQYDALLP DDPKRVLSHD YQVVGTKHIL TSPALLESTS LVFAYGQDLF
     FTRITPSNTF DLLSENFNKA QLVLTIAGLA LAIVIAKPMP RAAVALSLAV SSSYFHLSPR
     TRCSATDPLV QEAMNGYIDD DIEVAKAIAL SLQESQPKPS YPRQIDYITI SDDEDEQDDD
     EKQFQADLQR AIQASKQEEG TSLSPARPAE RQASAPTAAT PFLSERAQLE KERLARQKRL
     RPDVDHDAQA GSEEDSDVRD AKRQRLSSSS SARSYRANPG SSSSAKSGPI ASGSHSWART
     QAISSQSGAA SSSKEQLFWE GELRQTGNAH VDPRKDTLPT FRLTDILAPR DDIAFAIVSA
     YVYNYSWLYS LFSPNTPVIA VAQDPEGQET IKTILPNWIK TTPFLRNGMG CMHMKFMLLF
     YKSGRLRIMI STANMIEYDW RDIENTAWVQ DVPLRSAPIS HDPKAEDFAA AMVRVLRAIS
     VAPALVSHLR NDHPDLPLQR LEEFRMKWDF SKVKVSLVPS IAGKHEGWPK VILAGHTALM
     KALRNLNAAA DKDKEVILEC QGSSIGNYST QWMNEFHCSA RGESAQSWLD VSKARRAKLS
     FPPVKILFPT SQYVRDSALG EAGGGTMFCR RNQWEGAKFP RELFHQSRSK RGKVLMHSKM
     ILGMFRSRPS VFSGSSNRSD SETEDEDDPE SDQEKLIGWL YVGSHNFTPS AWGTLSGSAF
     NPTLNITNYE LGIVLPLRSE EEANRMVCWE RPPKKYAHGK DEPWIQSESP AFAQG
//
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