ID J7SC00_9APHY Unreviewed; 1317 AA.
AC J7SC00;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=Dilute domain-containing protein {ECO:0000259|PROSITE:PS51126};
GN ORFNames=FIBRA_00275 {ECO:0000313|EMBL:CCL98281.1};
OS Fibroporia radiculosa.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Fibroporiaceae; Fibroporia.
OX NCBI_TaxID=599839 {ECO:0000313|EMBL:CCL98281.1, ECO:0000313|Proteomes:UP000006352};
RN [1] {ECO:0000313|EMBL:CCL98281.1, ECO:0000313|Proteomes:UP000006352}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TFFH 294 {ECO:0000313|EMBL:CCL98281.1,
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; HE796875; CCL98281.1; -; Genomic_DNA.
DR RefSeq; XP_012177564.1; XM_012322174.1.
DR STRING; 599839.J7SC00; -.
DR GeneID; 24093192; -.
DR HOGENOM; CLU_006124_0_0_1; -.
DR InParanoid; J7SC00; -.
DR OrthoDB; 1359946at2759; -.
DR Proteomes; UP000006352; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR CDD; cd15473; Myo5p-like_CBD_DIL_ANK; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 1.20.1540.10; Rhomboid-like; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR002710; Dilute_dom.
DR InterPro; IPR037986; Myo5p-like_CBD_DIL.
DR InterPro; IPR022764; Peptidase_S54_rhomboid_dom.
DR InterPro; IPR035952; Rhomboid-like_sf.
DR PANTHER; PTHR16027; DILUTE DOMAIN-CONTAINING PROTEIN YPR089W; 1.
DR PANTHER; PTHR16027:SF6; DILUTE DOMAIN-CONTAINING PROTEIN YPR089W; 1.
DR Pfam; PF01843; DIL; 1.
DR Pfam; PF01694; Rhomboid; 1.
DR SMART; SM01132; DIL; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF144091; Rhomboid-like; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
DR PROSITE; PS51126; DILUTE; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000006352};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1003..1022
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1105..1123
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1143..1164
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1170..1189
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1201..1220
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1226..1243
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1255..1276
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REPEAT 143..175
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 335..668
FT /note="Dilute"
FT /evidence="ECO:0000259|PROSITE:PS51126"
FT REGION 444..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 686..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 774..799
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 874..902
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..475
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 686..700
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1317 AA; 146586 MW; F6F35DDAC9C049AD CRC64;
MVVSSVAPVD LTVEPDLQPL YPTPSQIAHL LSPYVGLSPQ QKAELVSHSL TRACQFGDML
LLSHLLTDPN AHPYVDLGKQ DEDGLGLISA TILGFGSESE RDIEREECVR LLISEGCDAN
VADKGLLLVL IPLEPRINIE MAAGWSPLHY AALVSPPTLV SHLLTHGASP FSLTRRKLTA
LDIVTAHSTV PGREDVSLLL EEAMREEGWK GGRKEEQRRL LEKRTRRLGK RKNVQHDIEK
TLDIPSSWWG GPPESSLDSD SEDEEEMLDE TCYTPPPDYT SMLVFSPMAL PDIFQSLIVS
FEPSLRNSEP ANALYMLARF ACLTCDHNWL EDLIIGATDT IEETFFNRAD DAPTLVFWLY
NTTVWLHLMR CDNAINETCE MLGQFAHIEE ILNSVFVFII RLAERKIDQL LDAALLDYSP
LSTEFESIQF ESEWSFLRSF GNKKKTAGQP PRGGAPASPN NGSRPPSPPP PTSTSPTNSR
SFASLRQTFT RARGTSSSAP LQSLFADNFA PSTSPQPSPK DITAFITALH TLLHLSGINP
AMIIQLWSQV MYWTACETFN RVLTRKKYLC RSKAVQISMN LSVLEEWIGE MQLPRGVVSH
FAPVKDLLTW LQGLSSITEF PNLIATVQTL KNLNPLQMRR AVRDYRYEVN EPRMTEECSQ
YLAQLQKDWE RHRIKLGVEA LRKEIGERER EREREESASV SPSLDEGSES PAPAPPPESW
VAQRSIDALF DRTWEKSSWE PAKAPESLGE LMDSRFMLPL LLPSDPRMLG AVPVSRSDLK
EKRHTSRTSQ DSTTSRASFG GRGAMEWKLK SKKLRDVGTS TLRYVDGHRA IRRWTRPDEG
EEDDWDQPPP YSMDDIQPAH GDLSVDTSMH FTPLTRKPSV RSRGRASAIS DPMDKNTDPY
DEPYNPVYGP AYAKDYSYNP DGYNSTDSVT LGGKPNDAAN AGPGELYGKP EAYHAQEYSG
PFTVPPRQSP LEEPNMFQRY FGLYPLEQRI SDKRRGVGVQ KRAYVVWMLT LAMLGVLIYE
LVVNDKAQGT PISFKPAVNP MLGPSGSALI NLGARFPACM KIVSGIPLST ELPCLNDTAN
PVTSACPLED VCGFGGFHDE TPNQWFRFIT PIFLHAGIIH YLLNMLAQTT VSAQVEREMG
SVFFLVLYIA SGTFGNVLGG NFALVGQPSV GASGAIFGTT AIAWIDLFAH WRYQYRPGTK
LAWMVVELVI GVGLGFIPYV DNFAHLGGLL MGLLVGMAFY PIISPSARHR TIVITLRLIA
IPVAIVLFVV LIRNFYTSNP YAACSWCRYL SCIPTSSNGY CKGTGMFPAH LLTDYRS
//
