ID F8NJH2_SERL9 Unreviewed; 616 AA.
AC F8NJH2;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=RecF/RecN/SMC N-terminal domain-containing protein {ECO:0000259|Pfam:PF02463};
GN ORFNames=SERLADRAFT_458485 {ECO:0000313|EMBL:EGO30022.1};
OS Serpula lacrymans var. lacrymans (strain S7.9) (Dry rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Coniophorineae; Serpulaceae; Serpula.
OX NCBI_TaxID=578457;
RN [1] {ECO:0000313|EMBL:EGO30022.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=S7.9 {ECO:0000313|EMBL:EGO30022.1};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Eastwood D.C., Floudas D., Binder M., Majcherczyk A., Schneider P.,
RA Aerts A., Asiegbu F.O., Baker S.E., Barry K., Bendiksby M., Blumentritt M.,
RA Coutinho P.M., Cullen D., Cullen D., Gathman A., Goodell B., Henrissat B.,
RA Ihrmark K., Kauserud H., Kohler A., LaButti K., Lapidus A., Lavin J.L.,
RA Lee Y.-H., Lindquist E., Lilly W., Lucas S., Morin E., Murat C.,
RA Oguiza J.A., Park J., Pisabarro A.G., Riley R., Rosling A., Salamov A.,
RA Schmidt O., Schmutz J., Skrede I., Stenlid J., Wiebenga A., Xie X.,
RA Kues U., Hibbett D.S., Hoffmeister D., Hogberg N., Martin F.,
RA Grigoriev I.V., Watkinson S.C.;
RT "Evolution of plant cell wall degrading machinery underlies the functional
RT diversity of forest fungi.";
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; GL945429; EGO30022.1; -; Genomic_DNA.
DR RefSeq; XP_007314264.1; XM_007314202.1.
DR AlphaFoldDB; F8NJH2; -.
DR GeneID; 18817734; -.
DR KEGG; sla:SERLADRAFT_458485; -.
DR HOGENOM; CLU_001042_0_4_1; -.
DR OrthoDB; 231904at2759; -.
DR Proteomes; UP000008064; Unassembled WGS sequence.
DR GO; GO:0008278; C:cohesin complex; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0007062; P:sister chromatid cohesion; IEA:InterPro.
DR CDD; cd03275; ABC_SMC1_euk; 1.
DR Gene3D; 1.10.287.1490; -; 1.
DR Gene3D; 3.30.70.1620; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR003395; RecF/RecN/SMC_N.
DR InterPro; IPR028468; Smc1_ABC.
DR InterPro; IPR036277; SMC_hinge_sf.
DR PANTHER; PTHR18937:SF12; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN; 1.
DR PANTHER; PTHR18937; STRUCTURAL MAINTENANCE OF CHROMOSOMES SMC FAMILY MEMBER; 1.
DR Pfam; PF02463; SMC_N; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF75553; Smc hinge domain; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils}.
FT DOMAIN 227..600
FT /note="RecF/RecN/SMC N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02463"
FT COILED 110..165
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 204..315
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 412..446
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 616 AA; 69889 MW; 8D575CDFED2227B3 CRC64;
MHHACGDALV CDSMEVARYV CYDKGQEVKA VTLEGTIIHK SGLITGGRST HGGGKKWDEK
DVKGLYRVRD ALTAQLQELS RSKPRGKADE NLIAEVTRLE SVIAVVKDDL SACKLRLNGA
KDELKHLERE LRKLAPELRR AQTTHNSLKE KVDSLAAVIN EAEDGVFASF CNNIGVSNIR
EYEEQQLKVA EEESLARVRY DQQIMRLTHQ SQFEEEQYKN IRERLSTLQN MVQAEQAKMT
ELENKKRDIE REIAEAQETL SELRDELNGL NETLEQKNKS VEHVKRAHAK ASKVLDQALK
EIGTKNDEIE KLALERSSTY RKCRLEDIKV PLRDGNLRNV PMEENLREEV AMDVDEDEDG
TQRPRQVQNY GIEVDFDILD DDERSNNSPE TIAEFDSSIA KLNADIERMA PNLKAMERLD
DVEAKLVQTE READKARKDS KTARDQFSEV KRRRCELFNK AYNHISDRID QVYKDLTKGK
ASPMGGVAYL SLEDSEEPYN AGIKYHAMPP MKRFRDMEQL SGGEKTVAAL ALLFAIHSYQ
PAPFFVLDEV DAALDNTNVA KVANYIRTQA STSFQFVVIS LKGSLYERGH ALVGIYRDQD
VNSSRTLTLD LTQYAG
//
