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Database: UniProt
Entry: A0A0V0SNS5_9BILA
LinkDB: A0A0V0SNS5_9BILA
Original site: A0A0V0SNS5_9BILA 
ID   A0A0V0SNS5_9BILA        Unreviewed;      1191 AA.
AC   A0A0V0SNS5;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   SubName: Full=Cytochrome b-c1 complex subunit Rieske, mitochondrial {ECO:0000313|EMBL:KRX28198.1};
GN   Name=SYP {ECO:0000313|EMBL:KRX28198.1};
GN   ORFNames=T07_2837 {ECO:0000313|EMBL:KRX28198.1};
OS   Trichinella nelsoni.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=6336 {ECO:0000313|EMBL:KRX28198.1, ECO:0000313|Proteomes:UP000054630};
RN   [1] {ECO:0000313|EMBL:KRX28198.1, ECO:0000313|Proteomes:UP000054630}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS37 {ECO:0000313|EMBL:KRX28198.1};
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   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000256|ARBA:ARBA00034078};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
CC   -!- SIMILARITY: Belongs to the ELL/occludin family. {ECO:0000256|PROSITE-
CC       ProRule:PRU01324}.
CC   -!- SIMILARITY: Belongs to the Rieske iron-sulfur protein family.
CC       {ECO:0000256|ARBA:ARBA00010651}.
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:KRX28198.1}.
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DR   EMBL; JYDL01000001; KRX28198.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0SNS5; -.
DR   Proteomes; UP000054630; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProt.
DR   GO; GO:0005666; C:RNA polymerase III complex; IEA:InterPro.
DR   GO; GO:0008023; C:transcription elongation factor complex; IEA:InterPro.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008121; F:ubiquinol-cytochrome-c reductase activity; IEA:InterPro.
DR   GO; GO:0006383; P:transcription by RNA polymerase III; IEA:InterPro.
DR   GO; GO:0006368; P:transcription elongation by RNA polymerase II; IEA:InterPro.
DR   CDD; cd03470; Rieske_cytochrome_bc1; 1.
DR   Gene3D; 6.10.140.340; -; 1.
DR   Gene3D; 1.10.10.2670; E3 ubiquitin-protein ligase; 1.
DR   Gene3D; 2.102.10.10; Rieske [2Fe-2S] iron-sulphur domain; 1.
DR   Gene3D; 1.20.5.270; Ubiquinol cytochrome reductase, transmembrane domain; 1.
DR   InterPro; IPR037008; bc1_Rieske_TM_sf.
DR   InterPro; IPR042065; E3_ELL-like.
DR   InterPro; IPR019464; ELL_N.
DR   InterPro; IPR010844; Occludin_ELL.
DR   InterPro; IPR017941; Rieske_2Fe-2S.
DR   InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR   InterPro; IPR014349; Rieske_Fe-S_prot.
DR   InterPro; IPR005805; Rieske_Fe-S_prot_C.
DR   InterPro; IPR004192; Rieske_TM.
DR   InterPro; IPR007811; RPC4.
DR   InterPro; IPR006317; Ubiquinol_cyt_c_Rdtase_Fe-S-su.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   NCBIfam; TIGR01416; Rieske_proteo; 1.
DR   PANTHER; PTHR10134; CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR10134:SF20; CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF10390; ELL; 1.
DR   Pfam; PF07303; Occludin_ELL; 1.
DR   Pfam; PF00355; Rieske; 1.
DR   Pfam; PF05132; RNA_pol_Rpc4; 1.
DR   Pfam; PF02921; UCR_TM; 1.
DR   PRINTS; PR00162; RIESKE.
DR   SUPFAM; SSF50022; ISP domain; 1.
DR   SUPFAM; SSF81502; ISP transmembrane anchor; 1.
DR   SUPFAM; SSF144292; occludin/ELL-like; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS51980; OCEL; 1.
DR   PROSITE; PS51296; RIESKE; 1.
PE   3: Inferred from homology;
KW   2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054630};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          497..606
FT                   /note="OCEL"
FT                   /evidence="ECO:0000259|PROSITE:PS51980"
FT   DOMAIN          1116..1184
FT                   /note="Rieske"
FT                   /evidence="ECO:0000259|PROSITE:PS51296"
FT   REGION          168..217
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          364..493
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          608..640
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        370..392
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        393..448
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        472..493
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1191 AA;  133328 MW;  FCB30A4DE684DDE8 CRC64;
     MTAASSEIFP LAQRDVNLPQ LTAFIIKLTD SSLQSLQDSV RTCNGYAGSS SKFGSIEFQP
     DDCRISFGPD AQAFKFTLSK VQDASSKGPQ DAIEQCRDGS EWIKLGAVRH RIKVLATDDS
     YHNIKKKALR AEEEAKKSAL KVLKQPKEGV SKASEKIWNK VQDAMNASSK KGSVTSASSS
     FQSSGSSQLV SPPRSNGHQR HQLSSSTSSS LPTKSRFDIT KKSVRERIIH HLIIRPSTAN
     GMLNRLLKEG LSDVDRQQFE ATFNSVAQVR GGKSQSSTAG SGCVYDLQPQ CFSEVSCDWP
     FYTNYERQLV RRELNNGAQS SRGRNAYVID DIIPKKESSR VRPVTGSSSS SKLAKAKAAA
     VSASSAGVEH SLQEHHHQSC RDLDKEKSTP NKQRSVISDV SSSARIPPKE QSFSAGKKTT
     NGYPELTTHH RQANPHSAST TLQSRKRPAD VDSQMPKSKK PPPIEQHVAV TSNGYGHCSS
     EMGVSNHDSN GSPPSNCSFW KDFPSIDSDE QRRRYKQAFD NDYPEYISCY EQLNQFYEEI
     AIMVNQLKQY DKNSDEYSQL ERDICSKYHR WEEDKTIDEV RNRHYQLRLK LAVLKARVQD
     YDDRKAIPMA SRPPRLPLPG SSRGVAPRLP NSMPTRARPL PNLAKAGQRQ TPNVAQSLAA
     LPDNPRGSAR GGSRFRGNMK SRLMTSEGIF SEGFTNELEM KSASDVDHYG EVVVEESFKK
     EIPDETDEEA LEKLFYKENS EKLPTNFVTL LSENSISEEQ QKKQAVRNVF FADQNCSPVF
     VQLPCAIANV AQRMLDCVPL KEDNANSVEN DLEKGRETHV LEKFPEGHLG KLQLHKSGKV
     TLKLNSAHSL PLLMPVQINS DNFVEKLVCL HLNDNEPNGG TMDWLGTVKS RWIFRIQPEF
     FLHTESVKPL LLSFMQVAMK VVDFSRMNIS KKLLYGITGN ARNVELRKSG CVYGLNFSPA
     RFNNRNVMSK FTAYQSVFVK GLFTGSSQRY AHTDVTFPDF DEYRRDSTKD IKLRNEDTDV
     PRKMFSYLSL GVGTAATLYC TKTVALQVIS YKGPPFSEEA GAVTEINLNL VPEGKNSTFL
     WRGKPVFVRH RTAKEINVES QVDISKLRDP EHDHQRVQKP EWLIVLAPCT HLGCVPIPYA
     GDYKGYFCPC HGSHYDASGR IRRGPAPRNL EVPHYVFKDE NTVLIGKTHI A
//
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