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Database: UniProt
Entry: A0A1L9UMP5_ASPBC
LinkDB: A0A1L9UMP5_ASPBC
Original site: A0A1L9UMP5_ASPBC 
ID   A0A1L9UMP5_ASPBC        Unreviewed;      1011 AA.
AC   A0A1L9UMP5;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=von Willebrand and RING finger domain protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ASPBRDRAFT_123415 {ECO:0000313|EMBL:OJJ72967.1};
OS   Aspergillus brasiliensis (strain CBS 101740 / IMI 381727 / IBT 21946).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=767769 {ECO:0000313|EMBL:OJJ72967.1, ECO:0000313|Proteomes:UP000184499};
RN   [1] {ECO:0000313|Proteomes:UP000184499}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 101740 / IMI 381727 / IBT 21946
RC   {ECO:0000313|Proteomes:UP000184499};
RX   PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA   de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA   Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA   Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA   Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA   Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA   Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA   Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA   Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA   Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA   Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA   Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA   Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA   Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA   Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA   Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA   Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA   van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA   Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA   Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA   Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA   Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT   "Comparative genomics reveals high biological diversity and specific
RT   adaptations in the industrially and medically important fungal genus
RT   Aspergillus.";
RL   Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
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DR   EMBL; KV878683; OJJ72967.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1L9UMP5; -.
DR   STRING; 767769.A0A1L9UMP5; -.
DR   VEuPathDB; FungiDB:ASPBRDRAFT_123415; -.
DR   OMA; SEAHWAQ; -.
DR   OrthoDB; 663280at2759; -.
DR   Proteomes; UP000184499; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   CDD; cd16448; RING-H2; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR002035; VWF_A.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR10579; CALCIUM-ACTIVATED CHLORIDE CHANNEL REGULATOR; 1.
DR   PANTHER; PTHR10579:SF43; LOW QUALITY PROTEIN: EPITHELIAL CHLORIDE CHANNEL PROTEIN-LIKE ISOFORM X1-RELATED; 1.
DR   Pfam; PF15411; PH_10; 1.
DR   Pfam; PF00092; VWA; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00327; VWA; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   SUPFAM; SSF53300; vWA-like; 1.
DR   PROSITE; PS50234; VWFA; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184499};
KW   Transferase {ECO:0000256|ARBA:ARBA00022676};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT   DOMAIN          23..69
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          496..669
FT                   /note="VWFA"
FT                   /evidence="ECO:0000259|PROSITE:PS50234"
FT   REGION          99..190
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          250..271
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          809..828
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          869..913
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        130..165
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        166..184
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        811..828
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        890..913
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1011 AA;  111601 MW;  C78B068813EDA884 CRC64;
     MAGLMDVDRT RTRRDRTFVG TECAICDEPL EHTLRGERVL QFSCTHVSHE ACFYEYIREF
     EGQYCPTCDA PLGLDTSRGG NMLDLEKLSN IVRSVTSDAA THRSGMSNLP PWEPVPVQAR
     RPSDAGSHAG SRPHNRDSRD TYVRRDSRDN SSHRERVERL TMGSRQHHSR NGSVAGSSDY
     NESHQHAANG RRHDYDVQAM ESDLSPRPAV TKNPIPAPTV TIRSEFPTLN RSRQQQSLTC
     LITVEVPEGS WQPDASDLTA NGKDQPQDEP YGAMRFPPNQ EPKPIPYENQ ENLDDLAEDL
     RNKVDNWHGL EFNRFGKLRL HGHMSVGKDR TSWQELECYL FGEMLICVKE KKTTQRRSYD
     DDQSKPKPTR CTLKGSILIK KHLNSMEAAT DEPILALNLS VSELPCFYLR FPNRSQLELW
     RRSLLDLHPM ESASPNNDYD YDNSGAEEED YRNNQIKRQA SINSSYGAAR SINTAITDYT
     NMGTESPAPS IHIPLDLVVV IPVSSSMQGL KITLLRDALR FLVQSLGPRD RMGLVTFGSS
     SGGVPIVGMT TKSWGGWPKI LESIRPVGQK SLRADVVEGA NVAMDLLMQR KSSNPISTIL
     LISDTSTSDP DSVDFVVSRA EAAKVNIHSF GLGLTHKPDT IIELSTRTKG SYVYVKDWMM
     LRECVAGCLG ALQTTSHQNV KLKLRLPEGS PAKFVKISGA LHTTKRATGR DAEAALGDLR
     FGDKRDVLVQ LVIPPDNSTQ DLTPQDAWES LVSGLEALGG MSDGDDQRVA SVEEVPLIQA
     DLTYGDFLRE GHLTHSPRPS LLAITMLPPN PKAKPGRPSS PPIPPHPSIV QRRMELLTSD
     MLTRALTLVS RGQHDRAQHL LTETRSILKG LGKGGLPPLP PGARPAGTSD SGSRADTPTS
     SSPKSSMFDG HSSAASDTAT ITSVSAVDGQ TMTALDADLQ SALEWINHPA VFSRDSRKAV
     LQGIGVISSQ RAYTFRSPSE AHWAQRVAGV RRLTERSKEW RETGDDALTE E
//
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