ID A0A074XBD2_AURPU Unreviewed; 1532 AA.
AC A0A074XBD2;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=M438DRAFT_277002 {ECO:0000313|EMBL:KEQ82835.1};
OS Aureobasidium pullulans EXF-150.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043002 {ECO:0000313|EMBL:KEQ82835.1, ECO:0000313|Proteomes:UP000030706};
RN [1] {ECO:0000313|EMBL:KEQ82835.1, ECO:0000313|Proteomes:UP000030706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-150 {ECO:0000313|EMBL:KEQ82835.1,
RC ECO:0000313|Proteomes:UP000030706};
RX PubMed=24984952;
RA Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT "Genome sequencing of four Aureobasidium pullulans varieties:
RT biotechnological potential, stress tolerance, and description of new
RT species.";
RL BMC Genomics 15:549-549(2014).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; KL584986; KEQ82835.1; -; Genomic_DNA.
DR STRING; 1043002.A0A074XBD2; -.
DR HOGENOM; CLU_001266_1_0_1; -.
DR OrthoDB; 1342875at2759; -.
DR Proteomes; UP000030706; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd16702; RING_CH-C4HC3_MARCH6; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR011016; Znf_RING-CH.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR13145:SF0; E3 UBIQUITIN-PROTEIN LIGASE MARCHF6; 1.
DR PANTHER; PTHR13145; SSM4 PROTEIN; 1.
DR Pfam; PF12906; RINGv; 1.
DR SMART; SM00744; RINGv; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS51292; ZF_RING_CH; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Reference proteome {ECO:0000313|Proteomes:UP000030706};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT TRANSMEM 116..137
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 255..274
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 671..693
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 713..738
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 901..921
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 995..1016
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1057..1078
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1098..1117
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1243..1266
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1286..1304
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1340..1364
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1384..1402
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1432..1452
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1472..1491
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 27..88
FT /note="RING-CH-type"
FT /evidence="ECO:0000259|PROSITE:PS51292"
FT DOMAIN 35..82
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 427..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 280..310
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..487
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..532
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1532 AA; 170790 MW; A001DBB3084D55F5 CRC64;
MSTSRRSSST PDIMNDPQFD PTPASDKSPA EGDTCRICRS EGSDAEPLFY PCKCSGSIKF
VHQDCLMEWL SHSNKKHCEL CKTPFRFTKL YDSHMPHTLP LPIFVKRACL HTANYLLTWA
RAVTVALVWL VVLPWFIRWS WRGLFWVLDA GWARDPWLAR MSPAAQQANA STPTADSIDE
KEPFGLSLSR FLLGALFYPL KPLGPPGSYS STNTTLETSF ASPYSSLLSD VKAVNSLTSH
AWVNRFILDM LEGEIITILV VIAFILVFLI REWVVQQQPI INAAAHIRDA ELQLDAAERA
ARNLQDFQDE ERRPHVDRYT HLFEEPSDSE ASGDESTHFI GWHKMEEVMD TAGIPYRFGG
EDHDDFMERF QYVGELLLGQ LKLAEDSGIL PTEIAENMWA ILDNLSPTRR DLWRGILLRE
DKLALSDDEN VGGPAATDSE TQEDSDDETL QESQRRPNMP PRDASSHAQR VLQSIEEPSN
NPENTSRLLD VEADGDSSRG SWQFVSSASD AESPSTTRTP LSSSSQAGEP ADAQETATVD
ADALGHSTAS TLQATLNPEQ HKGPITRLFD WFWADIVLDD EDNEPLPGVA DEEIARNEAV
EPPFVHLHDE EHVHDHDHDH DHDHEGAQDP EVLQAAAEAG LDAEAIEDAE DLEGILELIG
MQGPLIGLGQ TAMFCAVLIT TTLWTAIGVP YLFGKIALLF LGDPITSMIM TPLRFVSGFA
DAVVDIAVYA GGAATYFGSE ILTRLLSMLF GSVCRKFSLS YVEPLAKRAH HAANGASGRL
VNLLGGDGPM EFGLLMKSIQ ARQSLLSMKA EVAQVIGFFA KCLSGASYHL QKSTAPELLQ
ILNEIAASCF HQAASSYAWV RTVLREGFSE AINDGTFTFT VKSDDSLLDP SLAVWTSADR
CLTVLAGYVL LAMIGAMYLL RKESLFSSPG LQNVEKSFAD LLKQAGGVLK VILIISIEML
AFPLYCGMLL DCALLPLFEN ASIASRLAFA ERSPWLFVFM HWFIGTCYMF HFALFVSMCR
RILRSGVLYF IRDPDDPTFH PVRDVLERSV TTQLRKIAFS GLVYGGLVIV CLGGAIWGTA
RFGVFPVRWA RPEANLEFPI DFLGYNLLAP VVASYLFPSK GMETFFGTWL KLCARSLRLS
QFLFGERRKI EEGYSNDESW ITRFNPWKDQ DAIINSGSFV YDGKYVRAPA TDQVRIPRGE
RVFLEVSDAD ERIDGTNPGN GIHGRQPDNF NKVYIPPWFR LRIFTFISCL WMFAIAMGFG
VTVVPMIFGR LILSMAVSDR IAPNDLYAFA VGITTLGIAL QAIFNGRQGL KSTQENISKQ
NLAAVSAIIK KQTWRLIRSA YVYGFAVIIV PTLFALVLEL YLILPLRTYM GPASMVAPHT
FNILQDWTLG FIYGRVVLRL LLLSRTSRPA AALRMITRDG FTNPNVKLAT RAFVLPTLLL
FSIVLFCPPL IASVLDLTDI VSESIRTKVY RYSYPICASQ VLGLWCTWEL AEGMRRWRGR
IKDEVYLIGE RLHNFGERRP PEGSKSVVRR QS
//
