ID A0A0D7BK06_9AGAR Unreviewed; 468 AA.
AC A0A0D7BK06;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Nuclear fusion protein KAR5 {ECO:0008006|Google:ProtNLM};
GN ORFNames=CYLTODRAFT_441713 {ECO:0000313|EMBL:KIY70868.1};
OS Cylindrobasidium torrendii FP15055 ss-10.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Physalacriaceae;
OC Cylindrobasidium.
OX NCBI_TaxID=1314674 {ECO:0000313|EMBL:KIY70868.1, ECO:0000313|Proteomes:UP000054007};
RN [1] {ECO:0000313|EMBL:KIY70868.1, ECO:0000313|Proteomes:UP000054007}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FP15055 ss-10 {ECO:0000313|EMBL:KIY70868.1,
RC ECO:0000313|Proteomes:UP000054007};
RX PubMed=25683379; DOI=10.1016/j.fgb.2015.02.002;
RA Floudas D., Held B.W., Riley R., Nagy L.G., Koehler G., Ransdell A.S.,
RA Younus H., Chow J., Chiniquy J., Lipzen A., Tritt A., Sun H., Haridas S.,
RA LaButti K., Ohm R.A., Kues U., Blanchette R.A., Grigoriev I.V., Minto R.E.,
RA Hibbett D.S.;
RT "Evolution of novel wood decay mechanisms in Agaricales revealed by the
RT genome sequences of Fistulina hepatica and Cylindrobasidium torrendii.";
RL Fungal Genet. Biol. 76:78-92(2015).
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; KN880462; KIY70868.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D7BK06; -.
DR OrthoDB; 1406522at2759; -.
DR Proteomes; UP000054007; 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 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:UP000054007};
KW Signal {ECO:0000256|RuleBase:RU368082};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU368082};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU368082}.
FT TRANSMEM 380..402
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368082"
SQ SEQUENCE 468 AA; 52242 MW; 4DCA84392216B324 CRC64;
MDYSRRSDCF RNAAIAIQVR CTDLEMDETE RVHAAISMTL CELRTAKHLS PPLECTVASL
SDDLGGCVEA LSRSAQFWSS YSGYLREVPQ LCASYLRLND IDAARTIYHN ISLEKTLLLQ
QMLQRERDAQ SVTDMLGNHL MNMATMSSSF EQSMAVLHNL MDGISVQHSA DRDMAMASTQ
DMIAETRAMN GIVLAQLSSG LDASLADIIN RHTSSMEHAL AEFSVLLSTN TESLFAGFSD
RYLRTLDSMQ QDAHDRWSLV GTGVNELRAT VNHLVETTGR TITTLEASNT QGLLLADTQA
AATDAANDLA ITLSQLTQDA RHNFDQINAS IALMQDSFVA RASWLRTGIT EFLGLVLRVD
PHSLHSMDHV FRMVSLCWDV WAYFVQSVGS LIMSTVLVLY SYRTASFCRR RKARPLRHAH
LENIDEESKL IFVHPTPSSV PAPQPQSISS RRRRVSRIPD RLVNASYF
//
