ID A0A0A2LMF3_PENIT Unreviewed; 1199 AA.
AC A0A0A2LMF3;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
GN ORFNames=PITC_059750 {ECO:0000313|EMBL:KGO77535.1};
OS Penicillium italicum (Blue mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=40296 {ECO:0000313|EMBL:KGO77535.1, ECO:0000313|Proteomes:UP000030104};
RN [1] {ECO:0000313|EMBL:KGO77535.1, ECO:0000313|Proteomes:UP000030104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHI-1 {ECO:0000313|EMBL:KGO77535.1,
RC ECO:0000313|Proteomes:UP000030104};
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(2015).
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:KGO77535.1}.
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DR EMBL; JQGA01000146; KGO77535.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2LMF3; -.
DR STRING; 40296.A0A0A2LMF3; -.
DR HOGENOM; CLU_001042_5_0_1; -.
DR OMA; DQHQSMR; -.
DR OrthoDB; 231904at2759; -.
DR PhylomeDB; A0A0A2LMF3; -.
DR Proteomes; UP000030104; 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:UP000030104}.
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; 137664 MW; BDCA22D8CFE432A5 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 VEGEKAMAQI DAEIAECRQQ IEFLKVDKAQ LEDERREASK
TLAQNELQAK SLADNQAAAQ ALKSRYDSDL SSVQTAISER EAEHREILPR FNALKDQEDT
IKSQLTDAET SRQRLYAKQG RNSRFKNKSE RDKWLNMEVR ESHNSINTVQ GVISQTQEDI
QDLEREIAAL EPETERLRQQ IDGRGDTMHN VDQLVQDAKD ERDRLMDQRK ELWREEAKLD
SVLSNASQEV DRAERNLSQM MDNNTSRGTA AVRRIKRQHN LEGVYGTLAE LFDVNDRYRT
AVEVTAGQSL FHYVVDTDET ATTVLEILQK EKAGRVTFMP LNRLRSRPMN MPRASDTIPM
IDKLQYDPAY ERAFQHVFGK TIICPNLQVA SQYARSHGVN AITPEGDRSD KRGALTGGYH
DSRQSRLDAV KGLAKWRDEY ETKRNRGTEI RKELEKLDQM ITKAVGELQK LEQQRHQVQN
SSGPLRHELR VKRDLLQNKN DALDAKRRAL RNVESNLAAL NDQVNAFQTE LSSPFQKALT
SEEETRLETL SSTVQDLRRQ YQELSGQRSE LEARKSVLEV ELRENLNPRL DQLLNRDIDI
ADEEVQGNLK ETQREVKRIG QALEKLNARL KEVDDSIEEG NTRVVDLQQR NAETRREIEE
LARSIEKHQR RMEKSMQKKA ALTKQGAECA ANIRSLGVLP DEAFTKYQNT DSNTVVKKLH
KTNEALKKYS HVNKKAFEQY NSFTKQRETL TTRRSELDAS QKSIDDLISV LDQRKDEAIE
RTFKQVSREF HNVFEKLVPA GRGRLIIQRK TDRATRVDDD ADSDDEEARQ SVENYVGVGI
SVSFNSKHDD QQRIQQLSGG QKSLCALALV FAIQACDPAP FYLFDEIDAN LDAQYRTAVA
QMLKSISDST NGQFICTTFR PEMLHVAEKC YGVSFRQKAS TIDVVSREEA LKFVEEQKT
//
