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Database: UniProt
Entry: W6QCE9_PENRF
LinkDB: W6QCE9_PENRF
Original site: W6QCE9_PENRF 
ID   W6QCE9_PENRF            Unreviewed;      1199 AA.
AC   W6QCE9;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   24-JAN-2024, entry version 47.
DE   RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
GN   Name=sudA {ECO:0000313|EMBL:CDM34353.1};
GN   ORFNames=PROQFM164_S03g001077 {ECO:0000313|EMBL:CDM34353.1};
OS   Penicillium roqueforti (strain FM164).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=1365484 {ECO:0000313|EMBL:CDM34353.1};
RN   [1] {ECO:0000313|EMBL:CDM34353.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FM164 {ECO:0000313|EMBL:CDM34353.1};
RX   PubMed=24407037; DOI=10.1038/ncomms3876;
RA   Cheeseman K., Ropars J., Renault P., Dupont J., Gouzy J., Branca A.,
RA   Abraham A.L., Ceppi M., Conseiller E., Debuchy R., Malagnac F., Goarin A.,
RA   Silar P., Lacoste S., Sallet E., Bensimon A., Giraud T., Brygoo Y.;
RT   "Multiple recent horizontal transfers of a large genomic region in cheese
RT   making fungi.";
RL   Nat. Commun. 5:2876-2876(2014).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR005719}.
CC   -!- SIMILARITY: Belongs to the SMC family. SMC3 subfamily.
CC       {ECO:0000256|ARBA:ARBA00005917}.
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DR   EMBL; HG792017; CDM34353.1; -; Genomic_DNA.
DR   AlphaFoldDB; W6QCE9; -.
DR   STRING; 1365484.W6QCE9; -.
DR   OMA; DQHQSMR; -.
DR   OrthoDB; 231904at2759; -.
DR   GO; GO:0005694; C:chromosome; 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:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0051276; P:chromosome organization; IEA:InterPro.
DR   CDD; cd03272; ABC_SMC3_euk; 1.
DR   Gene3D; 1.20.1060.20; -; 1.
DR   Gene3D; 3.30.70.1620; -; 1.
DR   Gene3D; 6.10.250.3110; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR003395; RecF/RecN/SMC_N.
DR   InterPro; IPR024704; SMC.
DR   InterPro; IPR041741; SMC3_ABC_euk.
DR   InterPro; IPR010935; SMC_hinge.
DR   InterPro; IPR036277; SMC_hinge_sf.
DR   PANTHER; PTHR43977; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 3; 1.
DR   PANTHER; PTHR43977:SF1; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 3; 1.
DR   Pfam; PF06470; SMC_hinge; 1.
DR   Pfam; PF02463; SMC_N; 1.
DR   PIRSF; PIRSF005719; SMC; 1.
DR   SMART; SM00968; SMC_hinge; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   SUPFAM; SSF75553; Smc hinge domain; 1.
PE   3: Inferred from homology;
KW   Cell cycle {ECO:0000256|ARBA:ARBA00022776};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Mitosis {ECO:0000256|ARBA:ARBA00022776};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR005719}.
FT   DOMAIN          522..634
FT                   /note="SMC hinge"
FT                   /evidence="ECO:0000259|SMART:SM00968"
FT   REGION          640..660
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          186..220
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          267..308
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          406..503
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          694..821
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          849..925
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1199 AA;  137463 MW;  AD6B551DCDD168BA CRC64;
     MYVKQIIIQG FKSYKDQTVI EPFSPKHNVI VGRNGSGKSN FFAAIRFVLS DAYTHLGREE
     RQALLHEGSG SAVMSAYVEI IFDNSDDRFP TGKPEVVLRR TIGIKKDEYT LDRKNATKND
     VMNLLESAGF SRSNPYYIVP QGRVTALTNM KDSERLILLK EVAGTQVYEA RRSESLKIMS
     ETNSKRAKID ELLDYINERL AELEEEKDEL RSYQEKDKER RCLEYTIYSL EQQEIGKVLN
     EIEERRQNGV EDADNNRDQF VEGEKAIAEI DVEIAECRQQ IEFLKVDKAQ LEDERREASK
     TLAQNELQAK SLADNQAAAQ ALKSRYDSDL SSVQTAISER EAEHREILPR FNALKDQEET
     VRSQLTDAET SRQRLYAKQG RNSRFKNKSE RDKWLNMEVR ESHNSISTVQ GVISQTQEDI
     RDLESEIAAL EPETERLRQQ IDGRGDTMHT VDQQVQDAKD ERDRLMDQRK ELWREEAKLD
     SVLSNASQEV DRAERNLSHM MDNNTSRGIA AVRRITRQHN LEGVYGTLAE LFDVNDRYRT
     AVEVTAGQSL FHYVVDTDET ATTVLEILQK EKAGRVTFMP LNRLRTRPMN MPRASDTIPM
     IDKLQYDPAY DRAFQHVFGK TIICPNLQVA SQYARSHGVN AITPEGDRSD KRGALTGGYH
     DSRQSRLDAV KILAKWRDEY ETKRNRGTEI RKELEKLDQL ITKAVGELQK LEQQRHQVQN
     SSGPLRHELR AKRDLLQNKT DTLDAKRRAL RNVESNLAAL NDQVNAFQTE LSSPFQKALT
     SEEEAQLETL SSTVQDLRRQ YQELAGQRSE LEARKSVLEV ELRENLNPRL DQLLNRDIDI
     ADEEVQGNLK ETQREVKRIG QTLEKLNARL KEVDTSIEEG TSRVIDLQQR NAETRREIED
     LARSIEKHQR RMEKSMQKKA ALTKQGAECA ANIRSLGVLP DEAFTKYQNT DSNTVVKKLH
     KTNEALKKYS HVNKKAFEQY NSFTKQRETL TTRRSELDAS QKSIDDLISV LDQRKDEAIE
     RTFKQVSREF HNVFEKLVPA GRGRLIIQRK TDHAPRVGED VDSDDEAARQ SVENYVGVGI
     SVSFNSKHDD QQRIQQLSGG QKSLCALALV FAIQACDPAP FYLFDEIDAN LDAQYRTAVA
     QMLKSISDST NGQFICTTFR PEMLHVAEKC YGVSFRQKAS TIDVVSREEA LKFVEEQKT
//
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