ID A0A367KX12_RHIST Unreviewed; 2678 AA.
AC A0A367KX12;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN Name=UFD4_2 {ECO:0000313|EMBL:RCI06412.1};
GN ORFNames=CU098_006648 {ECO:0000313|EMBL:RCI06412.1};
OS Rhizopus stolonifer (Rhizopus nigricans).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX NCBI_TaxID=4846 {ECO:0000313|EMBL:RCI06412.1, ECO:0000313|Proteomes:UP000253551};
RN [1] {ECO:0000313|EMBL:RCI06412.1, ECO:0000313|Proteomes:UP000253551}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LSU 92-RS-03 {ECO:0000313|EMBL:RCI06412.1,
RC ECO:0000313|Proteomes:UP000253551};
RX PubMed=29674435; DOI=10.1534/g3.118.200235;
RA Gryganskyi A.P., Golan J., Dolatabadi S., Mondo S., Robb S., Idnurm A.,
RA Muszewska A., Steczkiewicz K., Masonjones S., Liao H.L., Gajdeczka M.T.,
RA Anike F., Vuek A., Anishchenko I.M., Voigt K., de Hoog G.S., Smith M.E.,
RA Heitman J., Vilgalys R., Stajich J.E.;
RT "Phylogenetic and Phylogenomic Definition of Rhizopus Species.";
RL G3 (Bethesda) 8:2007-2018(2018).
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=2.3.2.26; Evidence={ECO:0000256|ARBA:ARBA00000885};
CC -!- SIMILARITY: Belongs to the UPL family. K-HECT subfamily.
CC {ECO:0000256|ARBA:ARBA00006331}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RCI06412.1}.
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DR EMBL; PJQM01000159; RCI06412.1; -; Genomic_DNA.
DR STRING; 4846.A0A367KX12; -.
DR EnsemblFungi; RCI06412; RCI06412; CU098_006648.
DR Proteomes; UP000253551; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR Gene3D; 3.30.2410.10; Hect, E3 ligase catalytic domain; 1.
DR Gene3D; 3.90.1750.10; Hect, E3 ligase catalytic domains; 1.
DR Gene3D; 2.120.10.80; Kelch-type beta propeller; 2.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR011043; Gal_Oxase/kelch_b-propeller.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR045322; HECTD1/TRIP12-like.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR PANTHER; PTHR45670; E3 UBIQUITIN-PROTEIN LIGASE TRIP12; 1.
DR PANTHER; PTHR45670:SF1; E3 UBIQUITIN-PROTEIN LIGASE TRIP12; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF13415; Kelch_3; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF50965; Galactose oxidase, central domain; 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000253551};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT TRANSMEM 1936..1960
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1197..1567
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT DOMAIN 2332..2676
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 622..654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2001..2062
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2276..2323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..74
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..102
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 632..654
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2026..2060
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1528
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 2678 AA; 299833 MW; 51A58E93ECFCF2D8 CRC64;
MEQNSRQLKR KTRKDSSKTH LETTDRYSLR NRKESPTKPT TRKLISKKTN NEDIIDDSLD
DYNHEKHQGY YEDEDEDDMH YDHEEEHDEA EEDDEDEDDD DEMDEIARVR RTLGLQMQGL
FGGSMSSDFG RFKSILSSLK SNDDPTMQLI ALQELAEILS VSSEDNLAGY FSSDSFVREL
VRIMKGTDDL IPQDGGDMDE DMMLALAMSE GLSGGNPEVM LLACRCISNL LEAMPTAITS
VVSHGAIRVL CQKLKSIQYI DLAEQALYAL EKISAQLPRA VVHEDGLSAV LMYFDFFSIH
AQRTALRTAS NCMRGIDLES FSQVMEVTPI LMNTITYSDR SIVELTCLCW VRISESYRNN
RECLERALTV DLLKILFSLI PITGNPNAVH PATFNDLLRI FRSISKASPL LSFELLKLGI
IEAFYQILTG SNSAPTSITT NQHIVFDSKW RDSVPTIMKI IVDLLPSLPK DDMFSSRRFK
SSSTDRTRSL DHAADPRVTW FRENSDVLTN LDTILIPLVL DMYASTVNLR VRQLVTHTLV
KLLFYSQEDT LSKVLKNVPL SSFLSGILTR QEHPVLIIDA LYQVELMIQR LPDVYHFLFE
REGVLHEIES LSKLPLVEEE APQKQKELSS QRSEDTTITV DETTGSSHSG ISSSSRRLFD
GHDLHAIMRS HHFLQQQQRL RHHHNLENEK GIGRGSTRKY IIQLAQHFVE HYFPKPNAED
GIANNSLKEI TKLTNMLLSS TNSTCEQALK ELSVYLYDSA MGISSFELIN SGLVKALLSF
LTSTKEFKSS LEARTQGFDR VFIQEPDIDQ DGNNSLKKLV VRLQDILSRF ETFEVVTPLE
SSSTDSLRNP TSMLAKQLRL RLTGTSDNIP TSYKQLMVST HAVATFRVLE DYLLARISAS
FALSHSDDEE NEVELDEHNH LLIEGENDSM DVDENDENLV DTEMDETVGK ATSSSSKKEK
KDGEWKIRFS LNGTVVSNDS TVYAAVHQYE MNSANRPSTY LGRNIWASSY PVTYERVWVP
ASSTTEDETK KSNVVRQLAD VIQPKELKDD STCNYALQLL KALSPAIAKN PQGISAQDFI
NRKLTAKANR QLEEPLIVAS SCLPSWIYWL MSEAPFLFPF ETRYLFIQST SFGYARLIAR
WQSLQMRNNS QNGTRTDTSE QPTLGRMERQ KVRIMRNQML ESAIKILDLF GSSPTVLEVE
YMGEKGTGMG PTLEFYASTS KEFSKHSLNM WRGSNRLEEG YVDASAGLFP KTLPRSSSRS
TKKIIQLFKA LGQFIAKGLL DFRIVDIPFS PAFFKVALGN AEPNIELLKE IDPQLAKSIK
MLESYIKQKR EIYDDLFKSP EEKAKAVRNI VVDNTRLEDL YLDFTLPGDD SYELKTGGSD
INVTINNVEE YIDLIQDAIL GSGISQQIAA FREGFNGLFA IDDLKLLTEN ELVSLFGKAE
EDWSHAILAD TIRADHGFTM DSDPVRHLLE ILSDFNDIER RQFLQFTTGS PRLPIGGWKA
LRPIFTVVRK IPEAPLTADD YLPSVMTCAN YFKMPAYTTK EILRQRLITS MNEVIVESQL
VGDLGIIQTN VPWRAGHASA FQYPYVILYG GSQDISISSP TTSVMGTNDV WVWDIRNGSW
YHPTIQTQSG NTMLPQIYFK ATTLPSQGQI IALVSNTTGG SATGVIQKLD INSWSWSFPT
TNFQASARTV GYSMLTINNT IYTYGGLSVD QNGYANANAV QNALSMMDAN SYQWSSGSNG
LGLADHSTCY LKACNCLVTF GGTPTGNPTD VTDAVNLYDL SKRVWNVQGI QTPAGASAPG
ARRLHTANCL DDLMIVYGGG TNQPADTDVW VLNATSYPTM TWQRITMANQ TQGPNSRMGH
SAVLDKPNKK IYIFGGWGLS ASNDSNMYVL DYVNWGWTRI ATTGYPHDAL PNINSTTSND
PTGNEQQATN KLSAGAIAGA AVGSALGLIL IAAIIAFLFI RKKRRQQQQD KDAMVVIGEE
FSDEYKATRA KKDNPFYYNP DGFYNTNDDD DDNDNEHRRP AHHGGYFINN NNNNSRSTHR
MSKAWTGTSS PRNSYTRPSE IGDSDRVVTG VLEAITPIDD GTVAATHGSR SPRESLRNSK
VLLVTPTEYT KQGQVPNEII SQKPNEFSIP AIRQQSTRQV PVHHHLGLPT PITPDENIVP
MSASMEVLRS IGTNASSMMN HTGASQFDNT TSTDDKRKNA SGVIFTHTTV PTPDFEEQEE
NWTFTDSLSV GQPYSAPPIQ YISPNSHQLS TATSTQTWDT KDAPNFQISL VHHHNNQPLQ
GQYPSSTLNM PMAQTVTPPS TSTNSSQNNS SSTNDMHKSN PQVNIYNTVS PLDALASLGQ
QPTNSLENTP GSSRHNSSVI VKSMTRENSN HSTDGFIQLA PFISALPHRY QIDKAKPPIT
GPTNNILFAI AGENELAPVA IKSFGRREAW ERECRTLIKL KSPCVVEILE VLTIQGNEQH
HVHDDERKDI QYVTVMERLD ETLNTWIRHK QHSKNNGRIA RDILKCLFWC HNNGIAFCDL
KPSNIMHRQG EPWKLIDFEA SRTIGEECVG VITPRYCPPE VARATTYGLE GANGVVATAS
VDLWSLGCVI YELETKKALF PSKIKDETIL HFVSHPSPST PILNNGLRWN ESKELEIPQF
DKLVPNPHTR QLIKILLSRD PNKRTSASQL LENPYFSS
//
