ID F1KXA3_ASCSU Unreviewed; 705 AA.
AC F1KXA3;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Iron-sulfur cluster assembly 1 homolog, mitochondrial {ECO:0000256|ARBA:ARBA00039743};
OS Ascaris suum (Pig roundworm) (Ascaris lumbricoides).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Ascaris.
OX NCBI_TaxID=6253 {ECO:0000313|EMBL:ADY42507.1};
RN [1] {ECO:0000313|EMBL:ADY42507.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21685128; DOI=10.1101/gr.121426.111;
RA Wang J., Czech B., Crunk A., Wallace A., Mitreva M., Hannon G.J.,
RA Davis R.E.;
RT "Deep small RNA sequencing from the nematode Ascaris reveals conservation,
RT functional diversification, and novel developmental profiles.";
RL Genome Res. 21:1462-1477(2011).
CC -!- SIMILARITY: Belongs to the HesB/IscA family.
CC {ECO:0000256|ARBA:ARBA00006718}.
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DR EMBL; JI167436; ADY42507.1; -; mRNA.
DR AlphaFoldDB; F1KXA3; -.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:InterPro.
DR Gene3D; 2.30.30.140; -; 1.
DR Gene3D; 2.60.300.12; HesB-like domain; 1.
DR Gene3D; 2.40.50.770; RecQ-mediated genome instability protein Rmi1, C-terminal domain; 1.
DR InterPro; IPR000361; FeS_biogenesis.
DR InterPro; IPR016092; FeS_cluster_insertion.
DR InterPro; IPR017870; FeS_cluster_insertion_CS.
DR InterPro; IPR035903; HesB-like_dom_sf.
DR InterPro; IPR042470; RMI1_N_C_sf.
DR InterPro; IPR013894; RMI1_OB.
DR InterPro; IPR002999; Tudor.
DR NCBIfam; TIGR00049; iron-sulfur cluster assembly accessory protein; 1.
DR PANTHER; PTHR10072:SF41; IRON-SULFUR CLUSTER ASSEMBLY 1 HOMOLOG, MITOCHONDRIAL; 1.
DR PANTHER; PTHR10072; IRON-SULFUR CLUSTER ASSEMBLY PROTEIN; 1.
DR Pfam; PF01521; Fe-S_biosyn; 1.
DR Pfam; PF08585; RMI1_N_C; 1.
DR SMART; SM01161; DUF1767; 1.
DR SMART; SM00333; TUDOR; 1.
DR SUPFAM; SSF89360; HesB-like domain; 1.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 1.
DR PROSITE; PS01152; HESB; 1.
DR PROSITE; PS50304; TUDOR; 1.
PE 2: Evidence at transcript level;
FT DOMAIN 526..583
FT /note="Tudor"
FT /evidence="ECO:0000259|PROSITE:PS50304"
FT REGION 274..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 327..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..294
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..406
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 705 AA; 78758 MW; 70BE7AD7551A2B80 CRC64;
MSFPGADELA NEGWPITVER LKEVFGDKQF NDSSKLLQTL LDTDIREYSV PLLADRLNNR
LCELKGPVVV QISKLRNVQC SRLTDPSRLN DGLNKIQLTD GHLNINALQF DPIPTLTTNT
PAGTKICLLG VVPLESGLVL INAANCRVLG GRVERLVEKW RLEQNWMYKS MRNVDSSAPK
WVPFSKRRLN NDIQGYANNS EMKSFRANDV INNIKSKKEE GESEHFGAAR KAQIEQAISE
VSTTKKFAPS QLKIKAPPNE SSPNVVKNSK KEIASGIRQS GEQRKGRRFS RDDIDKEAMI
HQPPSRPPTL FDFVQSKVPN CDSISHTITP INNPSTGGTF RSQDGSFTSD DNRRFERNFF
QRGNGNSVDG RGDIRGGQVG RRGAKRGNSN RDRRRDNRAT VSRDRQDERF IINNRAFPPL
NTQTNALGAI TNGLSAMNMS ASTSSAGDRP MNRCDNEMYG TYRGTRRQDY GNDYGADTRT
QGAYIPMEDS SGNYEQDGTR RSLTDGAMQF FHRYGNARSN TTTRRPWKVG DKCLAPWNDG
QLYISTLLSL GPADMCSVQY DEYGNKRARR FGRLSMASRL GGAAARVVKG VARRTPARAA
LTLTPEAVQR VKLLMQKEPE MKALKIGVRQ RGCNGLTYTL NYAKEKGKFD EEVVQDGVKI
WIDTKAQLTL LGTEMDYIKS PLSSEFVFRN PNIKGTCGCG ESFSI
//
