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
//