ID   A0A1U8CWP0_ALLSI        Unreviewed;      1138 AA.
AC   A0A1U8CWP0;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   Name=RC3H1 {ECO:0000313|RefSeq:XP_014372406.1};
OS   Alligator sinensis (Chinese alligator).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC   Alligator.
OX   NCBI_TaxID=38654 {ECO:0000313|Proteomes:UP000189705, ECO:0000313|RefSeq:XP_014372406.1};
RN   [1] {ECO:0000313|RefSeq:XP_014372406.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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   -!- SUBCELLULAR LOCATION: Cytoplasm, P-body
CC       {ECO:0000256|ARBA:ARBA00004201}.
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DR   RefSeq; XP_014372406.1; XM_014516920.2.
DR   RefSeq; XP_014372407.1; XM_014516921.1.
DR   AlphaFoldDB; A0A1U8CWP0; -.
DR   STRING; 38654.A0A1U8CWP0; -.
DR   GeneID; 102385575; -.
DR   CTD; 149041; -.
DR   InParanoid; A0A1U8CWP0; -.
DR   OrthoDB; 2909513at2759; -.
DR   Proteomes; UP000189705; Unplaced.
DR   GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   CDD; cd16781; mRING-HC-C3HC3D_Roquin1; 1.
DR   Gene3D; 1.20.120.1790; -; 1.
DR   Gene3D; 4.10.1000.10; Zinc finger, CCCH-type; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR041523; ROQ_II.
DR   InterPro; IPR048575; Roquin_1_2-like_ROQ.
DR   InterPro; IPR000571; Znf_CCCH.
DR   InterPro; IPR036855; Znf_CCCH_sf.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR13139; RING FINGER AND CCCH-TYPE ZINC FINGER DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR13139:SF6; ROQUIN-1; 1.
DR   Pfam; PF18386; ROQ_II; 1.
DR   Pfam; PF21206; Roquin_1_2-like_ROQ; 1.
DR   Pfam; PF14634; zf-RING_5; 1.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00356; ZnF_C3H1; 1.
DR   SUPFAM; SSF90229; CCCH zinc finger; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50103; ZF_C3H1; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU00723}; Reference proteome {ECO:0000313|Proteomes:UP000189705};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00723};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00723}.
FT   DOMAIN          14..54
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          413..441
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   ZN_FING         413..441
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT   REGION          513..570
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1043..1138
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        550..564
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1047..1074
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1088..1117
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1138 AA;  126017 MW;  FB2289942085A873 CRC64;
     MPVQAPQWTD FLSCPICTQT FDETIRKPIS LGCGHTVCKM CLNKLHRKAC PFDQTTINTD
     IELLPVNSAL LQLVGAQVPE QQPITLCSGA EDTKHYEEGK KCVEELALYL KPLSSARGVG
     LNSTTQSVLS RPMQRKLVTL VHCQLVEEEG RIRAMRAARS LGERTVTELI LQHQNPQQLS
     SNLWAAVRAR GCQFLGPAMQ EEALKLVLLA LEDGSALSRK VLVLFVVQRL EPRFPQASKT
     SIGHVVQLLY RASCFKVTKR DEDSSLMQLK EEFRTYEALR REHDSQIVQI AMEAGLRIAP
     DQWSSLLYGD QSHKSHMQSI IDKLQTPASF AQSVQELTIA LQRTGDPANL NRLRPHLELL
     ANIDPSPDAP SPTWEQLENG LVAVRTVVHG LVDYIQNHSK KGTDQQQPPQ HSKYKTYMCR
     DMKQRGGCPR GASCTFAHSQ EELEKFRKMN KRLVPRRPLS ASLGQLNEVG LPSAAILSDE
     GAVDLPSRKS SALPNGIVST GSTVAQLISR GTDSSYDSAL KPGKIDHLSS SAPGSPPDLL
     ESVPKSSLPA LPVNPHPVPT RGPADLPPMS VSKQMQMVPR GSQLYPAQQP DMFYQDPRGA
     APPFDPGPYQ QGVYYSTQSS QCMPRFVRPP SAPEPGPPYL EHYPAYLPDR VVNSQYTPPQ
     QYPPMGQPIY PPHYDSRRVY PPAQPYQRED IVRGSPVPIE IPQTAVPPYV QESRDRYQQM
     EGYCPVAPHL GQIRPSCHRE PCNRFPSSPQ PHPSLDELHR RRKEIMAQLE ERKVISPPPF
     APSPTLPHTF HPEEYLDEDL KVAGKYKGND YSQYSPWSCD TIGSYIGTKD AKPKDVVAAG
     SVDMANVDNK TIRDQRLDMQ RRAAETGDDD LIPFGDRPTV SRFGAISRTS KAMYQSSGPM
     QAMAVQGAST KSMNISDYSP YGTHGSWGSS PYLPHQNIPS QGRFSDRERL SMSDITGHGK
     PLPSAEREQQ LRLELQQLNH QISQQTQLRG LEAASNRLLL QREATTLAGQ PQPPPPPSKW
     PGMISSEQLS LELHQVEREI GKRTRELSME SQSSLDMKSK LGTSKQTENG QLEPQNKVPA
     EDLALTFSSD VPNGSALTQE NISLLSNKTT SLSLTEDPEG GGDSHDSQRT GVTPTSAP
//