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Database: UniProt
Entry: A0A3B4FHB1_9CICH
LinkDB: A0A3B4FHB1_9CICH
Original site: A0A3B4FHB1_9CICH 
ID   A0A3B4FHB1_9CICH        Unreviewed;       979 AA.
AC   A0A3B4FHB1;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
OS   Pundamilia nyererei.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Pundamilia.
OX   NCBI_TaxID=303518 {ECO:0000313|Ensembl:ENSPNYP00000009955.1, ECO:0000313|Proteomes:UP000261460};
RN   [1] {ECO:0000313|Ensembl:ENSPNYP00000009955.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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};
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DR   AlphaFoldDB; A0A3B4FHB1; -.
DR   STRING; 303518.ENSPNYP00000009955; -.
DR   Ensembl; ENSPNYT00000010200.1; ENSPNYP00000009955.1; ENSPNYG00000007566.1.
DR   GeneTree; ENSGT00940000156361; -.
DR   Proteomes; UP000261460; Unplaced.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:UniProt.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0043170; P:macromolecule metabolic process; IEA:UniProt.
DR   CDD; cd15541; PHD_TIF1_like; 1.
DR   CDD; cd16585; RING-HC_TIF1_C-VI; 1.
DR   Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR   InterPro; IPR003649; Bbox_C.
DR   InterPro; IPR001487; Bromodomain.
DR   InterPro; IPR036427; Bromodomain-like_sf.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR027370; Znf-RING_euk.
DR   InterPro; IPR000315; Znf_B-box.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR45915; TRANSCRIPTION INTERMEDIARY FACTOR; 1.
DR   PANTHER; PTHR45915:SF4; TRANSCRIPTION INTERMEDIARY FACTOR 1-ALPHA; 1.
DR   Pfam; PF00439; Bromodomain; 1.
DR   Pfam; PF00628; PHD; 1.
DR   Pfam; PF00643; zf-B_box; 1.
DR   Pfam; PF13445; zf-RING_UBOX; 1.
DR   SMART; SM00502; BBC; 1.
DR   SMART; SM00336; BBOX; 2.
DR   SMART; SM00297; BROMO; 1.
DR   SMART; SM00249; PHD; 2.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57845; B-box zinc-binding domain; 1.
DR   SUPFAM; SSF47370; Bromodomain; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50014; BROMODOMAIN_2; 1.
DR   PROSITE; PS50119; ZF_BBOX; 2.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW   ProRule:PRU00035}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00024}.
FT   DOMAIN          40..100
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          127..174
FT                   /note="B box-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50119"
FT   DOMAIN          187..228
FT                   /note="B box-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50119"
FT   DOMAIN          734..780
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          822..884
FT                   /note="Bromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50014"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          402..424
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          468..527
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          543..602
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          622..679
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          695..727
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        407..424
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        493..527
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        639..656
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        664..679
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        700..727
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   979 AA;  109595 MW;  777E52A734AE3999 CRC64;
     MDAMEKQESG HTAVLSVENE AESTREERSG ALDQHDLDTC PVCHLSFHSK EPKLLPCLHT
     FCERCLPLPS RNLDVTEPSV SQSDDGATKP LNVIRCPVCR QECMAADVVD NMFVKESFEA
     PSSTVERAVQ LCMTCNDNTE AAGFCVECVE YLCTTCVEAH QRVKFTKDHM IRQKSEVSQD
     VCVVSNQRPM FCHIHKQEPL KLFCETCDLL TCRDCQLTKH KDHSYQFLKD AYKNHKEHME
     HMTHQLQEKK KLIEEVSDSI NSGLLLVEQN RTSVCDEIKK SVSSLILAIN KKGKILLDQL
     EAVTKDHESL LRKQQEDIGY LSQHLDHVID FIKWATAKNG GTALLYCKRL ILFQIENLLQ
     AKCSASFVPQ STIRFQCRAS YWASNVDLGT LMVESVPGHQ LGGFHHEHTH SGQSSSGSPH
     SIALGAPHST LAQLQMQVDK LNPQAHWQPQ PPPPPCTWHQ SIQLQQTVPG PLQRGSPSHS
     LPPQPDHRFT RPLPNHVSST RSILSPGLSP QYQQRRTGSG STYQTKPMDG FFSTPFYAQI
     TPPPLSGSVS LTHSQQRTEP TYMTRRNDST GPMYTVKPNY PQGAETSLSS RNAPGHQSSV
     VYTPVSQKKT SIFWKAPEIH QASGAVGSAA KKRQRSSPRP IIVIKDEPDD ESSYVHPKQR
     ASLPDSTDDQ PQINSQGEDV QTCIHSTDNK PCCPSHVPSE PLGQSKTGPP THISSVGEQQ
     QVEQNKTQLE DSNEASCAVC QTTGQLLCCQ KCHKAFHLTC HIPALLKSPR EWFCTFCCDL
     LMPEMEYVCK PEAKTIKKET DFEGAFSPVD KRKCERLLLY LFCSELNSVF QKSASLLVHA
     DDSLTIKGPV SFSTVKNRLE AEQSMCYQNP AEFVLDIRLI FGNCVACCEC QSNTELAVTC
     RRFKELFEDY LKLIYPDQTF PEIKPEMFQA ASPDCQDSQL QSLDNIFPLA KRQRTYSDSQ
     DAPSCHSGEE GIGLKLQFS
//
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