ID H2ANX8_KAZAF Unreviewed; 733 AA.
AC H2ANX8;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=RanBD1 domain-containing protein {ECO:0000259|PROSITE:PS50196};
GN Name=KAFR0A06430 {ECO:0000313|EMBL:CCF56078.1};
GN ORFNames=KAFR_0A06430 {ECO:0000313|EMBL:CCF56078.1};
OS Kazachstania africana (strain ATCC 22294 / BCRC 22015 / CBS 2517 / CECT
OS 1963 / NBRC 1671 / NRRL Y-8276) (Yeast) (Kluyveromyces africanus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kazachstania.
OX NCBI_TaxID=1071382 {ECO:0000313|EMBL:CCF56078.1, ECO:0000313|Proteomes:UP000005220};
RN [1] {ECO:0000313|EMBL:CCF56078.1, ECO:0000313|Proteomes:UP000005220}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22294 / BCRC 22015 / CBS 2517 / CECT 1963 / NBRC 1671 /
RC NRRL Y-8276 {ECO:0000313|Proteomes:UP000005220};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC {ECO:0000256|ARBA:ARBA00004567}.
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DR EMBL; HE650821; CCF56078.1; -; Genomic_DNA.
DR RefSeq; XP_003955213.1; XM_003955164.1.
DR AlphaFoldDB; H2ANX8; -.
DR STRING; 1071382.H2ANX8; -.
DR GeneID; 13886238; -.
DR KEGG; kaf:KAFR_0A06430; -.
DR eggNOG; KOG0864; Eukaryota.
DR eggNOG; KOG4719; Eukaryota.
DR HOGENOM; CLU_018357_0_0_1; -.
DR InParanoid; H2ANX8; -.
DR OrthoDB; 2730050at2759; -.
DR Proteomes; UP000005220; Chromosome 1.
DR GO; GO:0005643; C:nuclear pore; IEA:UniProtKB-SubCell.
DR GO; GO:0046907; P:intracellular transport; IEA:InterPro.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR015007; NUP2/50/61.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR000156; Ran_bind_dom.
DR InterPro; IPR045255; RanBP1-like.
DR PANTHER; PTHR23138:SF101; NUCLEOPORIN NUP2; 1.
DR PANTHER; PTHR23138; RAN BINDING PROTEIN; 1.
DR Pfam; PF08911; NUP50; 1.
DR Pfam; PF00638; Ran_BP1; 1.
DR SMART; SM00160; RanBD; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50196; RANBD1; 1.
PE 4: Predicted;
KW mRNA transport {ECO:0000256|ARBA:ARBA00022816};
KW Nuclear pore complex {ECO:0000256|ARBA:ARBA00023132};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Protein transport {ECO:0000256|ARBA:ARBA00023132};
KW Reference proteome {ECO:0000313|Proteomes:UP000005220};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Translocation {ECO:0000256|ARBA:ARBA00023010};
KW Transport {ECO:0000256|ARBA:ARBA00022816}.
FT DOMAIN 608..733
FT /note="RanBD1"
FT /evidence="ECO:0000259|PROSITE:PS50196"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 135..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 284..613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..216
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..416
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..455
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..505
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..561
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..594
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 733 AA; 79239 MW; 152CACFC70F2F59D CRC64;
MAKRIADSQM TRENRENSED DEPTVTVAST DIMSKRKIAM PKRKMAFKSI NSESVAKSES
SFGKAFTFNK KPSPEKDDKG AKLKALNLQF KEKITDFINR DPCVNLSSVF SKYETYLKTI
NGSDSPAVIA APVTAPSGAA SSPPIEIKKS ITPTLAPVNK DAEEESSSSS SEEEEVKVEG
PVFTLQAKPT TSDSPFTFDK KKLEQKNADS DSDNEIEIKG PSFTFTGKAK SDVFELNSSG
ATEANKTFFN FNKAAKENDA EEKKKPSFTF NVPVTTAKDN TNEIKKPSLT FGSQVNTAEK
EETNDVAAIS SSAVTANDTE SSKEESKQPA TFSFAKPSNS ETQPSTAFTF NVSANTTNEE
SNPFTVKALG SAESNSTGNP FTNSTSTHPE VKKPSFTFGS MTQANPTESK EKASFTFGKP
TTEIAEGEAK NSEPTVETKK VQEKPSFSFS VASKDKNAAE DSKTDGKPQF SFSFKKPNDE
SNISSSPFGK KPAENTENAT ITDAPKPSFT FGAPSLSDNE KKEGKPAFSF GNVPAAPSFT
FGQASNTSST SATSEPKSTP TAGFKFSLPF GESTQATGTA QPPTSSTANT EAETAAAEET
KEADANDPRG INMQNGEENE IVIFSQRAKL MVFNPESKNY DSRGVGEMKL LQQKDDKSKL
RLLCRSDGMG NILMNTSIVK SFNYEPLTAD NDNLVRTPTV DTDGKLITFI VKFKQKADGR
SFIKSIEDSK KDM
//
