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Database: UniProt
Entry: A0A3Q4H8Z9_NEOBR
LinkDB: A0A3Q4H8Z9_NEOBR
Original site: A0A3Q4H8Z9_NEOBR 
ID   A0A3Q4H8Z9_NEOBR        Unreviewed;       632 AA.
AC   A0A3Q4H8Z9;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Alkylated DNA repair protein alkB homolog 8 {ECO:0000256|ARBA:ARBA00018748};
DE            EC=2.1.1.229 {ECO:0000256|ARBA:ARBA00012808};
DE   AltName: Full=Probable alpha-ketoglutarate-dependent dioxygenase ABH8 {ECO:0000256|ARBA:ARBA00031417};
DE   AltName: Full=S-adenosyl-L-methionine-dependent tRNA methyltransferase ABH8 {ECO:0000256|ARBA:ARBA00032026};
DE   AltName: Full=tRNA (carboxymethyluridine(34)-5-O)-methyltransferase ABH8 {ECO:0000256|ARBA:ARBA00030990};
GN   Name=ALKBH8 {ECO:0000313|Ensembl:ENSNBRP00000018311.1};
OS   Neolamprologus brichardi (Fairy cichlid) (Lamprologus brichardi).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Lamprologini; Neolamprologus.
OX   NCBI_TaxID=32507 {ECO:0000313|Ensembl:ENSNBRP00000018311.1, ECO:0000313|Proteomes:UP000261580};
RN   [1] {ECO:0000313|Ensembl:ENSNBRP00000018311.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-(carboxymethyl)uridine(34) in tRNA + S-adenosyl-L-methionine
CC         = 5-(2-methoxy-2-oxoethyl)uridine(34) in tRNA + S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:43208, Rhea:RHEA-COMP:10407, Rhea:RHEA-
CC         COMP:10408, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74851,
CC         ChEBI:CHEBI:74882; EC=2.1.1.229;
CC         Evidence={ECO:0000256|ARBA:ARBA00034996};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000256|ARBA:ARBA00001954};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the alkB family.
CC       {ECO:0000256|ARBA:ARBA00007879}.
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DR   AlphaFoldDB; A0A3Q4H8Z9; -.
DR   STRING; 32507.ENSNBRP00000018311; -.
DR   Ensembl; ENSNBRT00000018801.1; ENSNBRP00000018311.1; ENSNBRG00000014084.1.
DR   GeneTree; ENSGT00940000158563; -.
DR   Proteomes; UP000261580; Unplaced.
DR   Bgee; ENSNBRG00000014084; Expressed in mesonephros and 5 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR   GO; GO:0106335; F:tRNA (5-carboxymethyluridine(34)-5-O)-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0043412; P:macromolecule modification; IEA:UniProt.
DR   GO; GO:0008033; P:tRNA processing; IEA:UniProt.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   CDD; cd12431; RRM_ALKBH8; 1.
DR   Gene3D; 3.30.70.330; -; 1.
DR   Gene3D; 2.60.120.590; Alpha-ketoglutarate-dependent dioxygenase AlkB-like; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR027450; AlkB-like.
DR   InterPro; IPR037151; AlkB-like_sf.
DR   InterPro; IPR034256; ALKBH8_RRM.
DR   InterPro; IPR013216; Methyltransf_11.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR13069:SF21; ALKYLATED DNA REPAIR PROTEIN ALKB HOMOLOG 8; 1.
DR   PANTHER; PTHR13069; UNCHARACTERIZED; 1.
DR   Pfam; PF13532; 2OG-FeII_Oxy_2; 1.
DR   Pfam; PF08241; Methyltransf_11; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR   SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51471; FE2OG_OXY; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Reference proteome {ECO:0000313|Proteomes:UP000261580};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022603};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          202..322
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
FT   REGION          503..542
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        503..529
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   632 AA;  70515 MW;  6116717B00522BC2 CRC64;
     SESSIWNRRI KEKKLLRKQI KASHTLLKHE GIHTAPHLVV ANGGLGNNVS REELSAALKE
     MGEVESLLMP PHKPYAFVTY SALKAYTHLN GQKLQCGESS VMLCLSYVNS ASVPLPEGLV
     LLEDFVSPEE EALLLAAVDW SSTNEDVTAQ KALKHRRVKH YGFEFRYDNN NVDKDKPLPA
     GIPAECLPVL ERCLRNGHIN VMPDQLTVNQ YESGQGIPPH VDTHSAFEDT ILSLSLGAKT
     VMEFRHPDGR VVAVVLPGRS LLVMKGESRY LWTHGITPRK FDMVPACEQQ SPDHVTPEPG
     TRSNLTLSKR GTRTSFTFRK IRPEPCRCAP STLSPSTPSP PALPCCHADA ARLEEEYVHR
     VYDAIASHFS STRHSPWPRV CHFLSSLPPG SVLADVGCGN GKYLGVNPEM IAVGCDRSSA
     LVQICAERGF HAFVSDALNV PLRTASCDAC ISIAVIHHFS TEERRLAAMR ELVRLLKPGG
     HALIYVWAFE QEYNKQRSKY LKEHNKEHHG KENLTKNTSE DRREPHGKSA IQNSGHLEEG
     YEPVGKVTDG KLSVHTNRTA FNTQDLLVPW HLKEGKKPGE EDNLTAVFHR YYHVFHQGEL
     EQLCSQVDGV KVQSSYHDQG NWCLYSKINA NK
//
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