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Database: UniProt
Entry: A0A0D2BCW6_9EURO
LinkDB: A0A0D2BCW6_9EURO
Original site: A0A0D2BCW6_9EURO 
ID   A0A0D2BCW6_9EURO        Unreviewed;       617 AA.
AC   A0A0D2BCW6;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Nuclear fusion protein KAR5 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PV08_06509 {ECO:0000313|EMBL:KIW16455.1};
OS   Exophiala spinifera.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=91928 {ECO:0000313|EMBL:KIW16455.1, ECO:0000313|Proteomes:UP000053328};
RN   [1] {ECO:0000313|EMBL:KIW16455.1, ECO:0000313|Proteomes:UP000053328}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 89968 {ECO:0000313|EMBL:KIW16455.1,
RC   ECO:0000313|Proteomes:UP000053328};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Exophiala spinifera CBS89968.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Required for nuclear membrane fusion during karyogamy.
CC       {ECO:0000256|ARBA:ARBA00003389, ECO:0000256|RuleBase:RU368082}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|RuleBase:RU368082}. Nucleus membrane
CC       {ECO:0000256|RuleBase:RU368082}.
CC   -!- SIMILARITY: Belongs to the KAR5 family. {ECO:0000256|ARBA:ARBA00010473,
CC       ECO:0000256|RuleBase:RU368082}.
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DR   EMBL; KN847495; KIW16455.1; -; Genomic_DNA.
DR   RefSeq; XP_016236671.1; XM_016380844.1.
DR   AlphaFoldDB; A0A0D2BCW6; -.
DR   STRING; 91928.A0A0D2BCW6; -.
DR   GeneID; 27333592; -.
DR   VEuPathDB; FungiDB:PV08_06509; -.
DR   HOGENOM; CLU_444833_0_0_1; -.
DR   OrthoDB; 1940841at2759; -.
DR   Proteomes; UP000053328; Unassembled WGS sequence.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000742; P:karyogamy involved in conjugation with cellular fusion; IEA:UniProtKB-UniRule.
DR   GO; GO:0048288; P:nuclear membrane fusion involved in karyogamy; IEA:UniProtKB-UniRule.
DR   InterPro; IPR007292; Nuclear_fusion_Kar5.
DR   PANTHER; PTHR28012; NUCLEAR FUSION PROTEIN KAR5; 1.
DR   PANTHER; PTHR28012:SF1; NUCLEAR FUSION PROTEIN KAR5; 1.
DR   Pfam; PF04163; Tht1; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Endoplasmic reticulum {ECO:0000256|RuleBase:RU368082};
KW   Karyogamy {ECO:0000256|ARBA:ARBA00022459, ECO:0000256|RuleBase:RU368082};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU368082};
KW   Nucleus {ECO:0000256|RuleBase:RU368082};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053328};
KW   Signal {ECO:0000256|RuleBase:RU368082, ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU368082};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU368082}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..617
FT                   /note="Nuclear fusion protein KAR5"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002249714"
FT   TRANSMEM        469..487
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU368082"
FT   TRANSMEM        494..513
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU368082"
FT   TRANSMEM        543..566
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU368082"
FT   COILED          260..287
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   617 AA;  68953 MW;  9295084C1F3E88AB CRC64;
     MSVARGLCRL RPTHFIFLMC LFFSQLCQGK SFLGADLTWT AVRKERNDLQ PDLTDLLASR
     DMDQDPVFER AMHVIDNLAT QTTCQQTAAA QLLITCKASG KSSNAKAVNH ELLERSKTAY
     AVRVAVCETG EGRATIPPAC RPVLDIPRRL QGEIDVVNAK TLASCLEGLM LEHYYWTSYS
     NSRQDANILC QASTLEATRL DALLSYQKLA ELLPEFREVL ESTRSRWLGF LKQQEQEAQK
     LADTQQKNHA DLKTQHEEHA KSFRQVMNNA KEDLNAVSQQ LRQYVVETGS GLGHTHETLS
     HVLSDFTMLR DLVAEVTSAA GKTSAEIAAI HAEEMHNVRD IALATTESLN KLLSTEATQG
     INALLQQFSI GLDAISSSQI KQLARLDEQL RLSDDLAEAQ RMNIALGQEM YDTSSVLSSQ
     LHTASAAATD VSSRIDKVNE ALTRVEEASS VLSALFSFLA LPTHMMQQLH LRLLILFSMP
     AIILFFWKPR KYPYSVMASY VFLESLISIY AQYENVISGS VRRLSIRSQD ATTWAFSHAG
     QHYTLLFSAF GILLVMSCYA ILVACCKKAR HSRKQLLVES SHGNEDFQQL YVGYRLRGNK
     QLSSRSADRF RRAATVA
//
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