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Database: UniProt
Entry: A0A2I0MGF4_COLLI
LinkDB: A0A2I0MGF4_COLLI
Original site: A0A2I0MGF4_COLLI 
ID   A0A2I0MGF4_COLLI        Unreviewed;       770 AA.
AC   A0A2I0MGF4;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   Name=MARCH7 {ECO:0000313|EMBL:PKK28746.1};
GN   ORFNames=A306_00006749 {ECO:0000313|EMBL:PKK28746.1};
OS   Columba livia (Rock dove).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Columba.
OX   NCBI_TaxID=8932 {ECO:0000313|EMBL:PKK28746.1, ECO:0000313|Proteomes:UP000053872};
RN   [1] {ECO:0000313|EMBL:PKK28746.1, ECO:0000313|Proteomes:UP000053872}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Blood {ECO:0000313|EMBL:PKK28746.1};
RX   PubMed=23371554; DOI=10.1126/science.1230422;
RA   Shapiro M.D., Kronenberg Z., Li C., Domyan E.T., Pan H., Campbell M.,
RA   Tan H., Huff C.D., Hu H., Vickrey A.I., Nielsen S.C., Stringham S.A.,
RA   Hu H., Willerslev E., Gilbert M.T., Yandell M., Zhang G., Wang J.;
RT   "Genomic diversity and evolution of the head crest in the rock pigeon.";
RL   Science 339:1063-1067(2013).
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   -!- 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:PKK28746.1}.
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DR   EMBL; AKCR02000014; PKK28746.1; -; Genomic_DNA.
DR   RefSeq; XP_005499185.1; XM_005499128.2.
DR   AlphaFoldDB; A0A2I0MGF4; -.
DR   Proteomes; UP000053872; Unassembled WGS sequence.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd16812; RING_CH-C4HC3_MARCH7; 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; PTHR14471:SF1; E3 UBIQUITIN-PROTEIN LIGASE MARCHF7; 1.
DR   PANTHER; PTHR14471; MARCH7/10 E3 UBIQUITIN PROTEIN LIGASE FAMILY MEMBER; 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   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053872};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          567..637
FT                   /note="RING-CH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51292"
FT   REGION          1..109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          126..153
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          212..238
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          251..332
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          347..394
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          412..498
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          533..553
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        15..39
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        49..65
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        74..88
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        251..276
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        285..314
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        430..448
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        450..466
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   770 AA;  85508 MW;  E2DA3FC71B8F7EF4 CRC64;
     MQRMESKPSR IPRRISVPAS SSPLGSRALT GNSLAGAYSA RESSRRLESG YQESGVLNSS
     SRDWGIGEGD THETPWKLTT SSPTRYSGTL DHPHAGRFLG SRSRLSTSSS SHFTSLCYGE
     SERTQGAYSR LHSQQRDSDS KRPKLSCTST SSVRNNGLTA FSDSSWRYSR IPRSSSVMLG
     SLGTELVRER RELERRTDLS VNNLVDHSYR NSDFSSSTYL QDRPASSYAE GARPKESSLS
     TLRLNASMNR QLPSDHQPSF FNRDSNMSSS RSSYSSRQRR NEFESPQRTM QPAFSLTAIR
     DETPSSSGSE RVLSSRRPLN EPAADSEGRR TTRQLLSRLA STMSSTFFSR RSSQDSLHTR
     SLSSEESTVV PRVQASTLSS SSGAVTPDVP GLQTSEASQG FSFLRRRWGL SGVSQNHNSD
     SDGESYRPDS ESRSTGSWLS SSLRNRCTPL FSRRRREGRD ESARISTSDT AARSQHVFRR
     REPATASPPD SAHSRRSSGI LPGSLFRFAV PPALGSSLSD NLMITVDIIP SGWNQSDGQE
     SGKSRVPPSR DPERLQKIKE SLLLEDSEDE EGDLCRICQM SSASSDNLLI EPCKCTGSLQ
     YVHQECMKKW LQSKINSGSS LEAVTTCELC KEKLHLNLED FDIHELYRAH ANEQADYELI
     SSGLYLVVLL HLCEQRFSDM LGTASEASTR VRFLRMILKT DAGRTLILQE TSGIAAEMLN
     WQEQHQNTFV FFPLLSKKCI DITVVSEALL NSKSTAAQRN SADLRTTQLV
//
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