ID M5FP84_DACPD Unreviewed; 1692 AA.
AC M5FP84;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=MI domain-containing protein {ECO:0000259|PROSITE:PS51366};
GN ORFNames=DACRYDRAFT_25350 {ECO:0000313|EMBL:EJT96883.1};
OS Dacryopinax primogenitus (strain DJM 731) (Brown rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Dacryopinax.
OX NCBI_TaxID=1858805 {ECO:0000313|EMBL:EJT96883.1, ECO:0000313|Proteomes:UP000030653};
RN [1] {ECO:0000313|EMBL:EJT96883.1, ECO:0000313|Proteomes:UP000030653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DJM-731 SS1 {ECO:0000313|EMBL:EJT96883.1,
RC ECO:0000313|Proteomes:UP000030653};
RX PubMed=22745431; DOI=10.1126/science.1221748;
RA Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT 31 fungal genomes.";
RL Science 336:1715-1719(2012).
CC -!- SIMILARITY: Belongs to the eukaryotic initiation factor 4G family.
CC {ECO:0000256|ARBA:ARBA00005775}.
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DR EMBL; JH795879; EJT96883.1; -; Genomic_DNA.
DR STRING; 1858805.M5FP84; -.
DR HOGENOM; CLU_002459_2_1_1; -.
DR OMA; MARIHAN; -.
DR OrthoDB; 92033at2759; -.
DR Proteomes; UP000030653; Unassembled WGS sequence.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.180; -; 2.
DR Gene3D; 1.20.970.30; eIF4G, eIF4E-binding domain; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR022745; eIF4G1_eIF4E-bd.
DR InterPro; IPR036211; eIF4G_eIF4E-bd_sf.
DR InterPro; IPR045208; IF4G.
DR InterPro; IPR003891; Initiation_fac_eIF4g_MI.
DR InterPro; IPR003890; MIF4G-like_typ-3.
DR PANTHER; PTHR23253; EUKARYOTIC TRANSLATION INITIATION FACTOR 4 GAMMA; 1.
DR PANTHER; PTHR23253:SF9; EUKARYOTIC TRANSLATION INITIATION FACTOR 4G1, ISOFORM B-RELATED; 1.
DR Pfam; PF12152; eIF_4G1; 1.
DR Pfam; PF02847; MA3; 1.
DR Pfam; PF02854; MIF4G; 1.
DR SMART; SM00544; MA3; 1.
DR SMART; SM00543; MIF4G; 1.
DR SUPFAM; SSF48371; ARM repeat; 2.
DR SUPFAM; SSF101489; Eukaryotic initiation factor 4f subunit eIF4g, eIF4e-binding domain; 1.
DR PROSITE; PS51366; MI; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000030653}.
FT DOMAIN 1551..1672
FT /note="MI"
FT /evidence="ECO:0000259|PROSITE:PS51366"
FT REGION 1..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 419..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 588..749
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 761..816
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 932..968
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1020..1099
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1373..1450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1493..1514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..212
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..233
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..253
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..312
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..508
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..547
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..566
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 588..603
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..715
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 723..749
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 767..783
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 794..816
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1020..1036
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1085..1099
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1375..1404
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1692 AA; 179482 MW; 942C8BE78B76DC7F CRC64;
MSKASTASLP KTQPSTPASG SSTPATAASS TQATRPVSAW SRGPPLTART APTTAPLSAV
PTSAPASAPA PAPAPVPSSA PAQKSAWNTP AQASQPPSGT VTPTGTGTGT HARKASSVVK
DGIAAVAGNG ASKPGSAMSF GSVGENARST PTAAPASAPP TATVADAKTF GSLPATAKKD
ESASKKDAPA ASASSEKPAE KPKDHKPKKK VDLNALFQVV PQPSSSAPSP SPSTTAGPSL
PPTSPPPAGT PVTGRPPTGQ GQSNIYNSIP MRPPPQNMPM MQNMPMMPGN MRPFVPSGPG
RGGPPGQGPN GVPRPEPAGA GRGAGPGPGP GQGQQPGSPP PHGRGMMSPM MGMMSSGPGQ
QWAYYPGLPH PYYPEGQPMP NSPYTYWPQV QVPHPGMPMQ GQQYPHPMQQ QQGMVPVPVQ
MQFQGGPGPG QGPGQQLLVP QHTMSPGAHG RPLPGPGPGA QQQPLPGPGT PISISGLPSP
LPSHVHPPGQ PIPQGIQQLP PTPLPHPSTP STLRSALPGP NPPNNPNFRY PAPTPTPGAP
GPGSLTGPPT PGGASQLNSR ATEFVPSSAR KTIKITRDDG TPVSLSAFST HSHGRSASVI
GSGASARGSP APGTLELKDT KEVKRVVVRL ESEADKARRE REAKEKEEKE AKEREAKEKE
EREAREKEER EAKEKEEREA REKEELERKK REEEEREKER LLAEEKEKEK ARLAAEAEAA
AAAKAKAKAK AEAEEAEEKA RKEEEARVKA EALAAAALVA AAAAKAEEQQ KELERRQAQA
EELAEKADTL SALPSAGASA SQTPTSPSTP DLSAASISLK PLNGGFSDAK IRRPVPGALD
LKSALNAAAK SAPPLSSAQA SALLSARPIE DINAIQYPAG IRTPNPDLNA HGPPGKFRYD
RDFLMQFMNV CKDRPETLPP LDAIGIENSD AMTQQYPQGG GRAPGGPQDR RNRASVSGKL
GLGITGNPGA PFAGKGGFSM GNFQAPVRAG AEGDRYRSVS SFAGPAGVAL VGRPVAMTRT
ASGSGLSGQV PGSPGGGNRN RSLRGRQRPE SRQPSQMIPP PNTPGFEPIE PLQKSENRWK
PQLAVPRSQR DREPADTPEM VERKVKALLN KLTLEKFDSI SDQIVGFANR SEQETDGHTL
IHVIKLVFEK ATDEPAWSEM YARLCRKLME RISPKVFDVQ VKNAEGTLIV GGQLFRKYLL
NRCQEDFERG WAARRQLAEE NAGGHGKEGE EAIFSDEYYA VQKAKRRSLG LVKLIGELFK
LQMLTERIMH ECIRKMLANV ENPEEEEIES LCKLLTTVGQ QLDTEKAKAH MTIYFQRMKE
MVKILRERAE RKEVSSRMMY MLQDIIDLRE RYNWQPRQKG SAPGPMTIAE VHQAAEREQA
QKEAEKVRQA MSRGGSRRGD PREYGPDGWQ NVPSGPAARA PAPAKAGDLS KFGNISKQSG
PIGGFGPSNV FKKADPKVAR SEAAATPTRT NMFNILNAAD GTAETEAMAH KAPSRKPSVD
LSAGAAAQEA GGQRKRLKLL PRSIPLAKDE ESAPPSAVES IDEVAGMSEQ KAEALIKEDI
QEFWQVGDLG EAANYFKDLP SNYHDKLIDK FVSDALNKKD ADIVMVAGVF SRCAAAGTVS
PESFKKGLLP TIEFLDDVAV DVPQAYPFMA KLLKGTQLSQ ADLEELASKI SVEGSPLVAP
KDKLLKEVAK LA
//
