ID A0A0V0SLT9_9BILA Unreviewed; 1372 AA.
AC A0A0V0SLT9;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=cytochrome-b5 reductase {ECO:0000256|ARBA:ARBA00012011};
DE EC=1.6.2.2 {ECO:0000256|ARBA:ARBA00012011};
GN Name=IPO7 {ECO:0000313|EMBL:KRX27347.1};
GN ORFNames=T07_1024 {ECO:0000313|EMBL:KRX27347.1};
OS Trichinella nelsoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6336 {ECO:0000313|EMBL:KRX27347.1, ECO:0000313|Proteomes:UP000054630};
RN [1] {ECO:0000313|EMBL:KRX27347.1, ECO:0000313|Proteomes:UP000054630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS37 {ECO:0000313|EMBL:KRX27347.1};
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 -!- SIMILARITY: Belongs to the flavoprotein pyridine nucleotide cytochrome
CC reductase family. {ECO:0000256|ARBA:ARBA00006105}.
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:KRX27347.1}.
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 EMBL; JYDL01000003; KRX27347.1; -; Genomic_DNA.
DR Proteomes; UP000054630; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004128; F:cytochrome-b5 reductase activity, acting on NAD(P)H; IEA:UniProtKB-EC.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR CDD; cd06183; cyt_b5_reduct_like; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001494; Importin-beta_N.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR10997:SF18; D-IMPORTIN 7_RANBP7; 1.
DR PANTHER; PTHR10997; IMPORTIN-7, 8, 11; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF03810; IBN_N; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00406; CYTB5RDTASE.
DR SMART; SM00913; IBN_N; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS51384; FAD_FR; 1.
DR PROSITE; PS50166; IMPORTIN_B_NT; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000054630};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1081..1102
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 22..105
FT /note="Importin N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50166"
FT DOMAIN 1116..1222
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 887..947
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1008..1030
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 893..907
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 912..931
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 932..947
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1372 AA; 157293 MW; EDE9CE9CEAA89B68 CRC64;
MELNKIIMAL KATLDPKGRH QAEEYLEGIK KIVGFTPLLL QILLTDDVEQ PVRQAASIYF
KNMVMTYWDE SPSEVVHGST TGLMFTIHEQ DRHIIRQNII EAIVKSVEVI RAQLAVSVRT
ILKTDFPGRW PDIIGKLMEL LNESDAEKWL GSLTVLYQLV KNYEYSRNIN RQPIADVMVK
VLPQLHLRMC HLIDNSSQES VHLQKMILKI YHALVLYHLH TDILSESHFL EWIIVVIRVL
EIPVPPESLA VDPEDRPQLV WWKCKKWSAR ILSRIYDRFH EDKNSDPGFL ALRRVFFKHC
LMQTIQSMLK VLNCYRQNEY ISPQVLYLAL EYLTTGVRET NGWKAVKAHV MDIIQTVIFP
LLCFSNEDDE LWHTDPQEYI RSKLDLFDEF LKPSSAGIRF LHSVMKRKNY LGELVKMVNH
VLSTPDVAPQ HVDGAFNFFG VLSTKLTKKA YLPFVCEMLK TQVIPRFSDP HGFLRARASY
VIYMYSDCNF DDKDLIEKMM IGVIMLILND PELPVKVDAA LAFQSILRFD EEEDLSYITP
YVRPLALALL NLLKETECDD ISNVLNRLVQ HFSTEIVPVA VEIAQNLVNI FTSLVHPTLD
DDESDSHDNR CMTAMGVINT LEALIDATED YPDVSIHLEP VLMLVIEMVI SQKMIDYYEE
VISLTYSLTA VNISPRMWMM FHLMYELFSG DGIDYFSDMI SVFYNYVTVG SSEFLNDGGQ
RLMALYNVCS TALTYETDVG DNLAVKLMEI IILQFRGKVE TFLCPAIELV AKRLEVGKRT
SDFLIVCLDL FFACLLHSPQ LTIEITQRLY VNEQKETLLH YFLANWFSDM NIFISLHDRK
MCLIGLCSLI QLNQRPPVVA ELGSRILPSC ITTLKALSRL YDNKLKKQNE ESSDEEEETE
DDSSSESLVS DQESGEAHED VNMFVEKEED KSDSGNEDEY SDDTDYDEDL EEFSTVVDRN
DTGFDEIVIF KETMCNVQVH DPQWYSSLVS NMSAEELAQL RDVFETAERR RVAKKQPRQK
RPEKRRQVDN RKTSEKAAIC ITVFVVLLAI ELSKKRFFGT IRNVLCHFLT SNCTTMLNDN
WITTAALLAG VGLASAAVYY YAFIKRKPKK LLEDPSVNYS IVLASKEKVN HDTRMFRFSL
HSADQVLGLG VGQHVHLSAK INGQLVVRPY TPVSDIDERG SIYFKDTHPL FPEGGKMTQY
LDNLKIGDSI NIRGPGGLLT YNGRGRFAIK SSKKADPVQK KYKKVAMLAG GSGITPMYQL
IKASLADSYD KLEMHLIYAN KSEQDILLFE ELLNLEMKHP TRFRVWFTID ARKGKVWTYS
IGFINSEIIK EIFPQPSADL LVLMCGPDAM IETACQPNLD KLGYARDNRF KY
//
