ID A0A444X3H8_ARAHY Unreviewed; 1123 AA.
AC A0A444X3H8;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=Ahy_B10g103250 {ECO:0000313|EMBL:RYQ84207.1};
OS Arachis hypogaea (Peanut).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC dalbergioids sensu lato; Dalbergieae; Pterocarpus clade; Arachis.
OX NCBI_TaxID=3818 {ECO:0000313|EMBL:RYQ84207.1, ECO:0000313|Proteomes:UP000289738};
RN [1] {ECO:0000313|EMBL:RYQ84207.1, ECO:0000313|Proteomes:UP000289738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Fuhuasheng {ECO:0000313|Proteomes:UP000289738};
RC TISSUE=Leaves {ECO:0000313|EMBL:RYQ84207.1};
RA Chen X.;
RT "Sequencing of cultivated peanut Arachis hypogaea provides insights into
RT genome evolution and oil improvement.";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
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}.
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:RYQ84207.1}.
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DR EMBL; SDMP01000020; RYQ84207.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A444X3H8; -.
DR STRING; 3818.A0A444X3H8; -.
DR Proteomes; UP000289738; Chromosome b10.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Reference proteome {ECO:0000313|Proteomes:UP000289738};
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 166..189
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 209..232
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 355..375
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 482..502
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 545..564
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 592..616
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 650..669
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 814..841
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 861..882
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 909..932
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 944..961
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1001..1024
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1036..1055
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 75..136
FT /note="RING-CH-type"
FT /evidence="ECO:0000259|PROSITE:PS51292"
FT DOMAIN 83..130
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 253..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1123 AA; 124360 MW; D40CBAE9E61CD6B9 CRC64;
MEIAHEPPPS LDGSPIAAET VANSPPSSSS SSSPSSSASS LASSPRAAKG KEIESTASSA
APAPAASPTA RYEDDDEEEE DVCRICRNPG DAENPLRYPC ACSGSIKFVH QDCLLQWLNH
SNARQCEVCK HAFSFSPVYA ENAPARLPFQ EFVVGMAMKA CHVLQFFLRL SFVLSVWLLI
IPFITFWIWR LAFVRSFSEA QRLFLSHLST AVILTDCLHG FLLSASIVFI FLGATSLRDY
FRHLREIGGQ DADREDEVDR NGARIARRAP GQANRNINGD GNGEDAGGAQ GIAGAGQVIR
RNAENVAARW EMQAARLEAH VEQMFDGLDD ADGAEDVPFD ELVGMQGPVF HLVENAFTVL
ASNMIFLGVV IFVPFSLGRI ILHYLSWFFS TASGPVIAAM APLTDASLSL ANITLKNALT
AVKNLSSETQ ESGSIGQVAD MLKVNASGLS EMANNISESA SSDLLKGVSI GTSRLSDVTT
LAIGYIFILS LIFCYFGIVA LIRYTKGEPL MMGRFYGIAS IAETIPSLFR QFLAAMKHLM
TMVKVAFLLV IELGVFPLMC GWWLDVCTIQ MFGKTMVHRV QFFSASPLAS SLVHWVVGIV
YMLQISIFVS LLRGVLRNGV LYFLRDPADP NYNPFRDLID DPVHKHARRV LLSVAVYGSL
IVMLVFLPVK LAMRMAPSIF PLDISVSDPF TEIPADMLLF QICIPFAIEH FKLRTTIKSL
LRYWFTAVGW ALGLTDFLLP RPDDNGGQEN GNGEPVRQDR LQVVQAGVHD QGMVAFAGDD
LNRVINAAGD PNAAEDYDND EQSDSDSYAF ALRIVLLLVI AWMTLLVFNS ALIVVPISLG
RALFNSIPRL PITHGIKCND LYAFVIGSYV IWTAVAGVRY SIEQIKKRRA SVLFGQIWKW
CAIVMKSSAL LSIWIFVIPV LIGLLFELLV IVPMRVPVDE SPVFLLYQDW ALGLIFLKIW
TRLVMLDHMM PLVDDSWRVK FERVREDGFS RLQGLWVLRE IVLPIIMKLL TALCVPYVLA
RGVFPVLGYP LVVNSAVYRF AWLGCLCFSF LCFCAKRFHV WFTNLHNSIR DDRYLIGRRL
HNFGEHVEKA NEAGASTGVP DTILSDHEAD VGLRLRRINQ QAG
//