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Database: UniProt
Entry: A0A1V6TRF4_9EURO
LinkDB: A0A1V6TRF4_9EURO
Original site: A0A1V6TRF4_9EURO 
ID   A0A1V6TRF4_9EURO        Unreviewed;      1199 AA.
AC   A0A1V6TRF4;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
GN   ORFNames=PENFLA_c004G02437 {ECO:0000313|EMBL:OQE28962.1};
OS   Penicillium flavigenum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=254877 {ECO:0000313|EMBL:OQE28962.1, ECO:0000313|Proteomes:UP000191342};
RN   [1] {ECO:0000313|Proteomes:UP000191342}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 14082 {ECO:0000313|Proteomes:UP000191342};
RX   PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA   Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA   Frisvad J.C., Workman M., Nielsen J.;
RT   "Global analysis of biosynthetic gene clusters reveals vast potential of
RT   secondary metabolite production in Penicillium species.";
RL   Nat. Microbiol. 2:17044-17044(2017).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR005719}.
CC   -!- SIMILARITY: Belongs to the SMC family. SMC3 subfamily.
CC       {ECO:0000256|ARBA:ARBA00005917}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OQE28962.1}.
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DR   EMBL; MLQL01000004; OQE28962.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V6TRF4; -.
DR   STRING; 254877.A0A1V6TRF4; -.
DR   OrthoDB; 231904at2759; -.
DR   Proteomes; UP000191342; Unassembled WGS sequence.
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; 1.10.287.1490; -; 1.
DR   Gene3D; 1.20.1060.20; -; 1.
DR   Gene3D; 3.30.70.1620; -; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000191342}.
FT   DOMAIN          522..634
FT                   /note="SMC hinge"
FT                   /evidence="ECO:0000259|SMART:SM00968"
FT   REGION          640..662
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;  137497 MW;  B69F8BDEADF0BC59 CRC64;
     MYVKQIIIQG FKSYKDQTVI EPFSPKHNVI VGRNGSGKSN FFAAIRFVLS DAYTHLGREE
     RQALLHEGSG SAVMSAYVEI IFDNSDDRFP TGKPEVVLRR TIGIKKDEYT LDRKNATKND
     VMNLLESAGF SRSNPYYIVP QGRVTALTNM KDSERLVLLK EVAGTQVYEA RRSESLKIMN
     ETNSKRAKID ELLDYINERL AELEEEKDEL RSYQEKDKER RCLEYTIYSL EQQEIGKVLN
     EIEERRQNGV EDADNNRDQF IEGEKAIAQI DAEIAECRQQ IEFLKVDKAQ LEDERRDASK
     TLAQNELRAK SLSDNQAAAQ AMKSRYDTDL RSVQSAISER EAEHREILPR FNVLKDQEDS
     VKSQLTDAET SRQRLYAKQG RNSRFKNKSE RDKWLNMEVR ESHNSINTVQ GVISQTQEDI
     QDLEGEIAAL EPETESLRQQ IDGRGDTMHN VDQQVQDAKD ERDRLMDQRK ELWREEAKLD
     SVLSNASQEV DRAERNLSQM MDNNTSRGIA AVRRIKRQHN LEGVYGTLAE LFDVNDRYRT
     AVEVTAGQSL FHYVVDTDET ATTVLEILQK EKAGRVTFMP LNRLRSRPMN IPRASDTIPM
     IDKLQYDPAY ERAFQHVFGK TIICPNLQVA SQYARSHGVN AITPEGDRSD KRGALTGGYH
     DSRQSRLDAV KGLAKWRDEY ETKRNRGTEI RKELEKLDQM ITKAVGELQK LEQQRHQVQN
     SSGPLRHELR AKRDLLQNKK DALDAKRRAL RNVESNLAAL NDQVNAFQTE LSSPFQKALT
     SEEEARLETL SSTVQDLRGQ YQELSGQRSE LEARKSVLEV ELRENLNPRL DQLLNRDIDI
     ADEEVQGNLK ETQREVKRIG QALEKLNARL KEVDTSIEEG NTRVMDLQQR NADTRREIEE
     LARSIEKHQR RMEKSMQKKA ALTKQGAECA ANIRSLGVLP DEAFTKYQNT DSNTVVKKLH
     KTNEALKKYS HVNKKAFEQY NSFTKQRETL TTRRSELDAS QKSIDDLISV LDQRKDEAIE
     RTFKQVSREF HNVFEKLVPA GRGRLIIQRK TDRATRLDDD VDSDDEEARQ SVENYVGVGI
     SVSFNSKHDD QQRIQQLSGG QKSLCALALV FAIQACDPAP FYLFDEIDAN LDAQYRTAVA
     QMLKSISDST NGQFICTTFR PEMLLVAEKC YGVSFRQKAS TIDVVSREEA LKFVEEQKT
//
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