ID A0A0V0ZN17_9BILA Unreviewed; 1105 AA.
AC A0A0V0ZN17;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 22-FEB-2023, entry version 24.
DE SubName: Full=Cleavage stimulation factor subunit 3 {ECO:0000313|EMBL:KRY13566.1};
GN Name=Mphosph6 {ECO:0000313|EMBL:KRY13566.1};
GN ORFNames=T12_13138 {ECO:0000313|EMBL:KRY13566.1};
OS Trichinella patagoniensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=990121 {ECO:0000313|EMBL:KRY13566.1, ECO:0000313|Proteomes:UP000054783};
RN [1] {ECO:0000313|EMBL:KRY13566.1, ECO:0000313|Proteomes:UP000054783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS2496 {ECO:0000313|EMBL:KRY13566.1};
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the prohibitin family.
CC {ECO:0000256|ARBA:ARBA00009658}.
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:KRY13566.1}.
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DR EMBL; JYDQ01000136; KRY13566.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0ZN17; -.
DR Proteomes; UP000054783; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0031124; P:mRNA 3'-end processing; IEA:InterPro.
DR CDD; cd03401; SPFH_prohibitin; 1.
DR Gene3D; 1.25.40.1040; -; 1.
DR Gene3D; 3.30.479.30; Band 7 domain; 1.
DR InterPro; IPR001107; Band_7.
DR InterPro; IPR036013; Band_7/SPFH_dom_sf.
DR InterPro; IPR003107; HAT.
DR InterPro; IPR000163; Prohibitin.
DR InterPro; IPR045243; Rna14-like.
DR InterPro; IPR008847; Suf.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR19980:SF0; CLEAVAGE STIMULATION FACTOR SUBUNIT 3; 1.
DR PANTHER; PTHR19980; RNA CLEAVAGE STIMULATION FACTOR; 1.
DR Pfam; PF01145; Band_7; 1.
DR Pfam; PF05843; Suf; 1.
DR PRINTS; PR00679; PROHIBITIN.
DR SMART; SM00386; HAT; 9.
DR SMART; SM00244; PHB; 1.
DR SUPFAM; SSF117892; Band 7/SPFH domain; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000054783}.
FT DOMAIN 38..200
FT /note="Band 7"
FT /evidence="ECO:0000259|SMART:SM00244"
FT REGION 943..968
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 951..968
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1105 AA; 127912 MW; 6E145651AE1D44C4 CRC64;
MADKVMDLMS RMLRNPKGLS AGIGLLAGAT GLTYALSQSF YTVDGGHRAI VFSRISGVGK
EIFTEGLHFR IPWLHYPIIY DVRARPHKVT SPTGSKDLQM VNISLRVLSR PDAAYLPKIY
RTLGVDWDER VLPSIINEVL KSVVAKFNAS QLITQRQQVS LLIRKQLVER ARDFHIILDD
VSITELSFGR EYTQAVEAKQ VAAQEAQRAA FVVERSKQER QQKIVQAQGE AQAAKLIGEA
LGKDPGYLKL RKIRAAQNIA RTLAQSANRA YLNTGSLMLN LADDDFFTSV EQVALKPKKN
FLRLQICILL KETVNIPVSS DLKNSAYRNF IVFERLSMAG VIMQISPESR VKGDAYDIEA
WYMLLREHLK KPIADSRPFF ERLVENFPVC GRFWRYYVEQ EIRAQNYEEA EKLFQRCLPK
VLHIELWKCY VRYVRETKGS LLSFQEQMAH VYDFAMEKIG FDIQSYQVYT DYVNFLKSVQ
AVGGYAENQR ISAIRKVYHR GVSTPLTNVE LLWSEYCAWE KSVNPVLAEK LIADKHRDYQ
SARRVMKEME TVMRGLNRNK VSVPPRRTLS EFRQFALWKQ LIDWEKSNPL QTDDYALYAK
RVIYAYEQAL LCFSFHCNIW YEASVFIQQA SDLLIERGDA KLGMSLMNAN ISLFERAVHS
LKLNNMLLHF AYADFEEQRM KFDKTQVIYN RLVECNDVNP TLAYIQFMKY FRRTEGIKSA
RALFKKARED GRCEYHVYVA AAFMEYRCCK DETVASKIFE MALQIFGPKP DLVECYLDYL
KQLNIHLENT NFRSVVERLL NTENLPINQL LEFWNKYCNY VQCVGNSEEI KDVFQRRGKC
LQKHYGVKSS GLYIDLCRYG TLLPCSYKQL PATDYLVMNM LSRNLIKLES SKNEIFAELK
TKVQIIVSDK TKPKPDVSEM QRFVPKLPLW SCLREYPEDG NGQVEKELYR EEEDEEREEG
KEEEEEEEEV IRVKGEEEVI PLHAAHHITY CLPKPSASPI EVNAEEILNS LCRIYPHSAQ
KKMSKISNPG SEKDKILNQI GVAMKLYVDS IEAKEEMERK KRSGSFSDSE EEPLYTSEEL
AKVNVYHKRR QMQRTINLPS MATAL
//