ID A0A2K6NVW2_RHIRO Unreviewed; 442 AA.
AC A0A2K6NVW2;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Radical S-adenosyl methionine domain-containing protein {ECO:0000256|RuleBase:RU364116};
GN Name=RSAD1 {ECO:0000313|Ensembl:ENSRROP00000008413.1};
OS Rhinopithecus roxellana (Golden snub-nosed monkey) (Pygathrix roxellana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61622 {ECO:0000313|Ensembl:ENSRROP00000008413.1, ECO:0000313|Proteomes:UP000233200};
RN [1] {ECO:0000313|Ensembl:ENSRROP00000008413.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: May be a heme chaperone, appears to bind heme. Homologous
CC bacterial proteins do not have oxygen-independent coproporphyrinogen-
CC III oxidase activity. Binds 1 [4Fe-4S] cluster. The cluster is
CC coordinated with 3 cysteines and an exchangeable S-adenosyl-L-
CC methionine. {ECO:0000256|RuleBase:RU364116}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173,
CC ECO:0000256|RuleBase:RU364116}.
CC -!- SIMILARITY: Belongs to the anaerobic coproporphyrinogen-III oxidase
CC family. HemW subfamily. {ECO:0000256|ARBA:ARBA00006100}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_010384440.1; XM_010386138.1.
DR RefSeq; XP_010384441.1; XM_010386139.1.
DR RefSeq; XP_010384442.1; XM_010386140.1.
DR AlphaFoldDB; A0A2K6NVW2; -.
DR STRING; 61622.ENSRROP00000008413; -.
DR Ensembl; ENSRROT00000032489.1; ENSRROP00000008413.1; ENSRROG00000028670.1.
DR GeneID; 104680278; -.
DR KEGG; rro:104680278; -.
DR CTD; 55316; -.
DR GeneTree; ENSGT00390000011216; -.
DR OMA; HIPWCVR; -.
DR OrthoDB; 5629at2759; -.
DR Proteomes; UP000233200; Unplaced.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004109; F:coproporphyrinogen oxidase activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; IEA:InterPro.
DR CDD; cd01335; Radical_SAM; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR034505; Coproporphyrinogen-III_oxidase.
DR InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM.
DR InterPro; IPR010723; HemN_C.
DR InterPro; IPR004559; HemW-like.
DR InterPro; IPR007197; rSAM.
DR NCBIfam; TIGR00539; hemN_rel; 1.
DR PANTHER; PTHR13932; COPROPORPHYRINIGEN III OXIDASE; 1.
DR PANTHER; PTHR13932:SF10; RADICAL S-ADENOSYL METHIONINE DOMAIN-CONTAINING PROTEIN 1, MITOCHONDRIAL; 1.
DR Pfam; PF06969; HemN_C; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR SFLD; SFLDG01082; B12-binding_domain_containing; 1.
DR SFLD; SFLDF00562; HemN-like__clustered_with_heat; 1.
DR SFLD; SFLDF00288; HemN-like__clustered_with_nucl; 1.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR SMART; SM00729; Elp3; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|RuleBase:RU364116};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU364116};
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|RuleBase:RU364116};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU364116};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU364116};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU364116};
KW Mitochondrion {ECO:0000256|RuleBase:RU364116};
KW Reference proteome {ECO:0000313|Proteomes:UP000233200};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|RuleBase:RU364116};
KW Transit peptide {ECO:0000256|RuleBase:RU364116}.
FT DOMAIN 34..270
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 442 AA; 48633 MW; BA265BF5FA4A6D26 CRC64;
MVLPGARARG WAAAARAAQR RRRVEGAGGS PSPEPAGRRA ALYVHWPYCE KRCSYCNFNK
YIPRGVEEAA MQKCLVTEAQ TLLRLSGVQR VESVFFGGGT PSLASPHTVA AVLEAVAQTA
HLPADSEVTL EANPTSTPGS RLAEFGAAGV NRLSIGLQSL DNTELRLLGR THSARDALRT
LAEARRLFPG RVSVDFMLGL PAQQVGPWLG QLQELLHHCD DHLSLYQLSL ERGTALFAQV
QQGALPAPDP ELAAEMYQRG RAVLREAGFR QYEVSNFARN GALSTHNWTY WQCGQYLGIG
PGAHGRFMPQ GAGSHTREAR IQTLEPDNWM KEVMMFGHGT RKRVPLGRLE LLEEVLALGL
RTDVGITHQH WQQFEPQLTL CDVFGANKEV QELLEQGLLQ LDHRGLRCSW EGLAVLDSLL
LTLLPQLQEA WQQRTPSPVP GG
//
