ID A0A0V1ABJ1_9BILA Unreviewed; 1301 AA.
AC A0A0V1ABJ1;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=NFU1 iron-sulfur cluster scaffold homolog, mitochondrial {ECO:0000256|ARBA:ARBA00018782};
DE Flags: Fragment;
GN Name=mif4gdb {ECO:0000313|EMBL:KRY22187.1};
GN ORFNames=T12_973 {ECO:0000313|EMBL:KRY22187.1};
OS Trichinella patagoniensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=990121 {ECO:0000313|EMBL:KRY22187.1, ECO:0000313|Proteomes:UP000054783};
RN [1] {ECO:0000313|EMBL:KRY22187.1, ECO:0000313|Proteomes:UP000054783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS2496 {ECO:0000313|EMBL:KRY22187.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Molecular scaffold for [Fe-S] cluster assembly of
CC mitochondrial iron-sulfur proteins. {ECO:0000256|ARBA:ARBA00002175}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC -!- SIMILARITY: Belongs to the AATF family.
CC {ECO:0000256|ARBA:ARBA00008966}.
CC -!- SIMILARITY: Belongs to the NifU family.
CC {ECO:0000256|ARBA:ARBA00006420}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRY22187.1}.
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DR EMBL; JYDQ01000011; KRY22187.1; -; Genomic_DNA.
DR Proteomes; UP000054783; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:InterPro.
DR Gene3D; 1.25.40.180; -; 1.
DR Gene3D; 3.30.300.130; Fe-S cluster assembly (FSCA); 1.
DR Gene3D; 3.30.2410.10; Hect, E3 ligase catalytic domain; 1.
DR Gene3D; 3.30.1370.70; Scaffold protein Nfu/NifU, N-terminal domain; 1.
DR InterPro; IPR025160; AATF.
DR InterPro; IPR039223; AATF/Bfr2.
DR InterPro; IPR012617; AATF_C.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR034904; FSCA_dom_sf.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR003890; MIF4G-like_typ-3.
DR InterPro; IPR014824; Nfu/NifU_N.
DR InterPro; IPR036498; Nfu/NifU_N_sf.
DR InterPro; IPR001075; NIF_FeS_clus_asmbl_NifU_C.
DR PANTHER; PTHR15565; AATF PROTEIN APOPTOSIS ANTAGONIZING TRANSCRIPTION FACTOR; 1.
DR PANTHER; PTHR15565:SF0; PROTEIN AATF; 1.
DR Pfam; PF13339; AATF-Che1; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF08712; Nfu_N; 1.
DR Pfam; PF01106; NifU; 1.
DR Pfam; PF08164; TRAUB; 1.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00543; MIF4G; 1.
DR SMART; SM00932; Nfu_N; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF117916; Fe-S cluster assembly (FSCA) domain-like; 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR SUPFAM; SSF110836; Hypothetical protein SAV1430; 1.
DR PROSITE; PS50237; HECT; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000054783};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT TRANSMEM 362..383
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1152..1301
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 696..778
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 901..942
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 696..723
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 724..773
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 912..929
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1270
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRY22187.1"
SQ SEQUENCE 1301 AA; 149686 MW; 9A10DA11256FA730 CRC64;
LTMESVALQN SPRKSPSKGV RKPFQLYRPP NMRKNDILTK SMENIEDPPL STVRKAEKKA
ELNEAETVVQ FRRSKTVGKS SNRLSVPCFF PASAASAAEL KGNGTVVPPK EAPLQSVIAK
RCHASVKDLS KRKELNDADF KKIEEFFNSL HLAGDKNVAS FLNSKCSSTE HACAIGQVLI
KLAIENGKKK STIAKLCHLL LRSASSNEFR KGLVAGCNQY FERRHKLRTE FVTYWHEFIT
FLSELCSDSS FTSESDLVNV VFRVFNYLLV PPVLDAIKME ELECIISSLL NAGYSLERQY
PDRLIDLRNT FRNAFLDAKE PWVRKMILLL VELSAGSWRL SEDANRYYFQ TNTPVIIMYH
QLFHLIIYCG HISTTSCLVF IFSYTFFNQL GRYFSFFISF QLMFYNKFKP CFIQICSNIL
FNVLKRSMYI QVMETPNPHS LKFLPGIPVL PGRTAEFPNR SSAENSPLAR AIFRIRGVKS
VFFGEDFITV TKNSEVKDWV AMKPEIFSTI MDFFTSKQNI IIDDSTEKDA ADDDNDTVAM
IKDLLNTRIR PTIQDDGGDV VFMGFDDGIV KLKLQGACTG CPSSVYTLKN GIENMLKFYV
PEVKGVEQVV DEVEEIAEKE FQKIAVVMNV REEIEALQNP FPGNFDDSDS DDVTKAQLVP
FSSEEELVTE TVSKFSRIRA ANLKLLDEEN PRYKGQVVNR SQLEQFTNSD EETVSSSATD
VSEEMDISDN DEQEEDEDEE EEEEEEADDY DGDDDDEDDD DDDEDEDQDG RMLMDDGEND
YMEQGMKMRN ENYISDQESD NMIHTFSRVD LLDQKERGIA VQQQLKLWEQ MLSLKIRFQK
LLQSANRLPQ SADYREKLLQ SDDELLETFS SARRSVQKLL DELLEFQDHL FSGNKQTVHL
STKRKIDQRD DDDDELSDIV DDEDEDDDEK QQQMEKKSDE TISIPAKRRR LQLSGYSDLL
QHLHDAFKSY QNEALEKWYQ RTRLGGIGVS AKKDFSAFES NAVAQIAQIL TDRKRLIQRT
QLKRLEYDII GKEEKCADED RNVNIFDDSD FHEQLLREFI QKRMNDITDP VLLGRHWSKF
QKLRDKSKKS KVDRKASKGR RIRIQVMSKL VNFMAPVDKS KMTNETRYDS SFDVHLYFLQ
YFNVSVFDRC RFQNIRDGVR DVLPVSMLDT VNAENFRLLL TGQSDVSVKF LKTLIMITDE
SSSAAADKSF PREKFDQLKK WFWSVVSSIT ADEKQDLIYF WTGSPTLAPS MEHFKPTPND
DMYLSTANTC ISRLCIALYS GKNILQQKLF IAIKIKTFGF V
//
