ID F0ZQ60_DICPU Unreviewed; 1013 AA.
AC F0ZQ60;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=DICPUDRAFT_153950 {ECO:0000313|EMBL:EGC33929.1};
OS Dictyostelium purpureum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=5786 {ECO:0000313|EMBL:EGC33929.1, ECO:0000313|Proteomes:UP000001064};
RN [1] {ECO:0000313|Proteomes:UP000001064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QSDP1 {ECO:0000313|Proteomes:UP000001064};
RX PubMed=21356102; DOI=10.1186/gb-2011-12-2-r20;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Sucgang R., Kuo A., Tian X., Salerno W., Parikh A., Feasley C.L., Dalin E.,
RA Tu H., Huang E., Barry K., Lindquist E., Shapiro H., Bruce D., Schmutz J.,
RA Salamov A., Fey P., Gaudet P., Anjard C., Babu M.M., Basu S.,
RA Bushmanova Y., van der Wel H., Katoh-Kurasawa M., Dinh C., Coutinho P.M.,
RA Saito T., Elias M., Schaap P., Kay R.R., Henrissat B., Eichinger L.,
RA Rivero F., Putnam N.H., West C.M., Loomis W.F., Chisholm R.L., Shaulsky G.,
RA Strassmann J.E., Queller D.C., Kuspa A., Grigoriev I.V.;
RT "Comparative genomics of the social amoebae Dictyostelium discoideum and
RT Dictyostelium purpureum.";
RL Genome Biol. 12:R20.1-R20.23(2011).
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; GL871120; EGC33929.1; -; Genomic_DNA.
DR RefSeq; XP_003289564.1; XM_003289516.1.
DR AlphaFoldDB; F0ZQ60; -.
DR STRING; 5786.F0ZQ60; -.
DR EnsemblProtists; EGC33929; EGC33929; DICPUDRAFT_153950.
DR GeneID; 10502678; -.
DR KEGG; dpp:DICPUDRAFT_153950; -.
DR eggNOG; KOG1609; Eukaryota.
DR InParanoid; F0ZQ60; -.
DR OMA; WLHYSLV; -.
DR OrthoDB; 1342875at2759; -.
DR Proteomes; UP000001064; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
DR CDD; cd16702; RING_CH-C4HC3_MARCH6; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
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; PS51292; ZF_RING_CH; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000001064};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 94..117
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 137..162
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 383..401
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 428..452
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 464..487
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 518..539
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 570..592
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 612..629
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 709..729
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 749..770
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 790..817
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 823..845
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 896..919
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 931..951
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..60
FT /note="RING-CH-type"
FT /evidence="ECO:0000259|PROSITE:PS51292"
FT REGION 221..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 293..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 667..687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..312
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1013 AA; 118105 MW; B60924A2C8F756BA CRC64;
MQEEDFCRVC RNGSTPDNPL SYPCKCSGSI KYIHQNCLLE WIQHSKSSSC ELCGHPFRFT
PIYSDNTPDV IPFYELISEA LIRFKWYIKK ISRIIYIIFC WLFIVPTLTC WVFNLFFGQK
WLLPPQFRNE NNKLIDIFYH FFIGTTLFFW IILASIASYM ILDFIHHKHA EIEIQDEFEI
DRDDTYLERL NNNNNNINRN VTQPQQQHPI INNIEQPIGN IVQNDNSTEN TNNTDSSNDS
FVINDELRFQ INDEIPNRLR QRLREHQQQQ QQHLEQLRLS EERAVAASLN HHNNINNNSA
ENDQQQDNQH QPQPQPQPQP QPQPQQQQQQ NQQNQQNQQD QQERVFFRIP GVFEMLRLQD
GPEEHENDIE NDDPNQIDDL ETFIVYNSIF LSTFLYIPYL IGQMLTEKIS IDVKQALQIA
DGTISQGAIS IIIGYSILSV VALCLLSFLI SQKISVKAMT LTHSFVKIAV ITVCELGILP
IIVGAFIDFC SLRVFGGCIQ TRIEFALKQK LTFLFSRWIF GIFFMVNFTN LCSILHQVFR
KGVIWFLKDP NDPDFDPFKD MIKLSFKRHV VKVCVSLCAY TIIGFLFVYL PALFLTLIPN
FLPINILMSD PITKGSADVL FIVAISYFPK FDARVTIKNI VSFWINNASR FLKLDSYLLP
DPQEKLRQQN RNNNNNQQQQ QVPAQQINKK TTEKIKKEIY KPKNFKTRLS IFIFLGWLTI
FSTICVYISL PVFIGRLTLH QFVNYENDIY SILVGLLISW VVSKGIYFLF SPLNNVNILQ
WSLVGAKILL LGVIMGILIP LLTGYLFDFI FMIPIMAPYD ETFFIHFSDI FQNWCLGSLL
LKFWYKWITA TNQPNNNRNN LLEDLDRPRD KWIDRFKQFK NNGFTNIDLK FTFSKIIFPI
SHFLLTMLTV PFCISKGLIP FFGGSLLLES ISFRYGFACY CFVLLFEKLV YKSKEWLVKF
HNAIRDDKYL VGKQLHNLDE PNKSILNNIN GTKASTSNSA TEKNIVSNYK SNE
//
