ID A0A0V1DDD2_TRIBR Unreviewed; 1354 AA.
AC A0A0V1DDD2;
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:KRY59673.1};
GN ORFNames=T03_12284 {ECO:0000313|EMBL:KRY59673.1};
OS Trichinella britovi (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY59673.1, ECO:0000313|Proteomes:UP000054653};
RN [1] {ECO:0000313|EMBL:KRY59673.1, ECO:0000313|Proteomes:UP000054653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS120 {ECO:0000313|EMBL:KRY59673.1};
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:KRY59673.1}.
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DR EMBL; JYDI01000010; KRY59673.1; -; Genomic_DNA.
DR Proteomes; UP000054653; 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:UP000054653};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1055..1076
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 1089..1202
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..1031
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 1354 AA; 155283 MW; 6061A5A7DB697A2C 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 NGWKAVKPHV MDIIQTVIFP
LLCFSNEDDE LWHTDPQEYI RSKLDLFDEF LKPSSAGIRF LHSVMKRKNY LGELVKMVNH
VLSTPDVAPQ HVDGAFNFFG VLSTKLTKKA YLPFVCEMLK TQVIPRFSDP HGFLRARASY
VIYMYSDCNF DDKDLIEKMM IGVIMLILND PELPVKVDAA LAFQSILRFD EEADLSYITP
YVRPLALALL NLLKETECDD ISNVLNRLVQ HFSTEIVPVA VEIAQNLVNI FTSLVHPALD
DDESDSHDNR CMTAMGVINT LEALIDATED YPDVSIHLEP VLTLVIEMVI SQKMIDYYEE
VISLTYSLTA VNISPRMWMM FHLMYELFSG DGIDYFSDMI SVFYNYVTVG SSEFLNDGGQ
RLMALYNVCS TALTYETDVG DNLAVKLMEI IILQFRGKVE TFLCPAIELV AKRLEVGKRT
SDFLIVCLDL FFACLLHNPQ LTIEITQRLY VNEQKETLLH YFLANWFSDM NIFISLHDRK
MCLIGLCSLI QLNQRPPVVA ELGSRILPSC ITTLKALSRL YDNKLKKQNE ESSDEEEETE
DDSSSESLVS DQESGEAHED VNMFIEKEED KSDSGNEDEY SDDTDYDEDL EEFSTVVDRN
DTGFDEIVIF KETMCNVQVH DPQWYSSLVS NMSAEELAQL RDVFETAERR RVAKKQPRQK
RPEKRRQVDN RKTPEKAAIC LFLTSNCTTM LNDNWITTAA LLAGVGLASA AVYYYAFVKR
KPKKLLEDPS VNYSIVLASK EVCENLNKVN HDTRMFRFSL HSADQVLGLG VGQHVHLSAK
INGQLVVRPY TPVSDINERG SIYFKDTHPL FPEGGKMTQY LDNLKIGDSI NIRGPGGRFA
IKSSKKADPV QKKYKKVAML AGGSGITPMY QLIKASLADS YDKLEIHLIY ANKSWSFEQL
FLQSEQDILL FEELLNLEMN HPTRFRVWFT IDARKGKVWT YSIGFINSEI IKEIFPQPSA
DLLVLMCGPD AMIETACQPN LDKLGYARDN RFKY
//
