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Database: UniProt
Entry: A0A1V6TTL0_9EURO
LinkDB: A0A1V6TTL0_9EURO
Original site: A0A1V6TTL0_9EURO 
ID   A0A1V6TTL0_9EURO        Unreviewed;      2282 AA.
AC   A0A1V6TTL0;
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=SMC hinge domain-containing protein {ECO:0000259|SMART:SM00968};
GN   ORFNames=PENSTE_c002G07565 {ECO:0000313|EMBL:OQE29728.1};
OS   Penicillium steckii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=303698 {ECO:0000313|EMBL:OQE29728.1, ECO:0000313|Proteomes:UP000191285};
RN   [1] {ECO:0000313|Proteomes:UP000191285}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 24891 {ECO:0000313|Proteomes:UP000191285};
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|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the SMC family. SMC4 subfamily.
CC       {ECO:0000256|ARBA:ARBA00006005}.
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:OQE29728.1}.
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DR   EMBL; MLKD01000002; OQE29728.1; -; Genomic_DNA.
DR   STRING; 303698.A0A1V6TTL0; -.
DR   OrthoDB; 231904at2759; -.
DR   Proteomes; UP000191285; Unassembled WGS sequence.
DR   GO; GO:0005694; C:chromosome; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0051276; P:chromosome organization; IEA:InterPro.
DR   Gene3D; 1.10.287.1490; -; 1.
DR   Gene3D; 1.20.1060.20; -; 1.
DR   Gene3D; 2.70.98.10; -; 1.
DR   Gene3D; 3.30.70.1620; -; 1.
DR   Gene3D; 1.20.1050.60; alpha-1,2-mannosidase; 1.
DR   Gene3D; 1.20.1610.10; alpha-1,2-mannosidases domains; 1.
DR   Gene3D; 3.30.2080.10; GH92 mannosidase domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR014718; GH-type_carb-bd.
DR   InterPro; IPR005887; GH92_a_mannosidase_put.
DR   InterPro; IPR041371; GH92_N.
DR   InterPro; IPR012939; Glyco_hydro_92.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR003395; RecF/RecN/SMC_N.
DR   InterPro; IPR010935; SMC_hinge.
DR   InterPro; IPR036277; SMC_hinge_sf.
DR   NCBIfam; TIGR01180; aman2_put; 1.
DR   PANTHER; PTHR18937:SF172; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN; 1.
DR   PANTHER; PTHR18937; STRUCTURAL MAINTENANCE OF CHROMOSOMES SMC FAMILY MEMBER; 1.
DR   Pfam; PF07971; Glyco_hydro_92; 1.
DR   Pfam; PF17678; Glyco_hydro_92N; 1.
DR   Pfam; PF06470; SMC_hinge; 1.
DR   Pfam; PF02463; SMC_N; 1.
DR   SMART; SM00968; SMC_hinge; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR   SUPFAM; SSF75553; Smc hinge domain; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000191285}.
FT   DOMAIN          809..922
FT                   /note="SMC hinge"
FT                   /evidence="ECO:0000259|SMART:SM00968"
FT   REGION          1..246
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2263..2282
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          628..662
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          688..792
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          962..1203
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        25..40
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        80..100
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        101..127
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        167..181
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        219..246
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2282 AA;  254674 MW;  12DA314D99EA6FBF CRC64;
     MASLAKGRPS RRSAPRRSYV VEETSESEDP GNVTPTPSNH DNDEESAEEE EDYTPVPNQA
     KRASRSKRMT LDPVTPSTVK PARKSRQSVA SVAPESEASQ AEETDGNEND ENDENDENAE
     STDNDENDEG PSMVSVVADP DSPSHQAAKK RKSIEPAELD PGSPSNMAAL KRQSMASRKS
     RGSITPKAAK GSLPTPEPSA SPESEVRAQR ESVPPLADIT ESAVNQSSPS KPAEEPRSQV
     SYINPNSTVL EKPMDIVMKS RNMTAPAPAE PAEVKPRMII QNLILNNFKS YAGKQVVGPF
     HASFSSVVGP NGSGKSNVID SLLFVFGFRA SKMRQGKISA LIHNSAQYPN LPFCEVEVHF
     EQVLDLPDGG HEVIPDSHLI VSRRAFRNNS SKYYMNKKET NFTTVTTFLR DRGIDLDHKR
     FLILQGEVES IAQMKAKAAN EHDEGLLEYL EDIIGTSKYK TPIDEAAAEL ETFNDVCVEK
     NNRVQHVEKE KTALEDKKNQ AVAYMVEENE LSQKQSALYQ IYIAECADNV RVTEEAILQM
     QEQLNMELEK HEGNESGIKE LEKAYKRASR EWETMEKESQ GLMKEMAKYD KETVKFEEKK
     KFLVNKQKKL EKTMQTSRLA ASECQSTVEK HSDDIERKSA EVTQLEQEMQ AEEKELDSIR
     ESLKGKTQGL SDQIAAKQKS LEPWNEKINQ KQSAAAVAQS ELDILRERSN AGAVLLEEAR
     GKIGTIEETL QSKQTDLEER QAQKETLEGE VEKLKHDLKK YVAREPEVRA HVSSARQKAD
     EARVSLQNTQ NRGSVLTGLM RLKESGRIDG FHGRLGNLGT IDEKYDVAIS TACPALDNMV
     VETVEVGQQC IDYLRKNNLG RANFILLDRL PRRDMSSIYT PESVPRLYDL VKPKDPKFAP
     AFYSVMQNTL VAKDLEQANR IAYGARRWRV VTLDGQLIDV SGTMSGGGTR VARGAMSSKQ
     VADTTKDQVS RLESDLEELE KKFQHFQEKQ RNIESQMRDK TDEIPRVETK IQKIMIEIDS
     TKRSLVDAQR RVKELSAEHK PSKSDESQSA ALEEQIEAVN NEIEELNNAK SGIEEEIQTL
     QGKIMEVGGV RLRGQKAKVD GLKEQINLLT EEISNAEVQK SKNEKLITKH SKARDGSQKE
     LEQISADLEK LEEDVANQAT DASGWREKAE EAEEALETKK GELKTLKQEL DDKKAELNES
     RATEIEMRNK LDENQKALGE NQKRSRYWEE KLSKLSLQNV SDLGEEQEAM ELQTYTNDEL
     DAMNKESLKA VIAALEEKVQ NASVDLSVIE EYRRRTTEHE ARSADLANAL TSRDSAKSRL
     DGLRSARLNG FMEGFGIISL RLKEMYQMIT MGGNAELELV DSLDPFSEGI LFSVMPPKKS
     WKNIGNLSGG EKTLSSLALV FALHHYKPTP LYVMDEIDAA LDFRNVSIVA SYIKERTKNA
     QFVVISLRNN MFELASRLVG VYKVNHMTKS VTIENRDYIE ATTTTSPILD TGLSKFVNPF
     IGAEGPDGTG FGGGDIFVGG ARPFGVVKLG IDSTAANWST AVLNGGWTPD GNVTGFSMMH
     ESGTGGAPKY GVISQMPLTG LDGVNVLDNL TYSQERIGDD VASVGYFKTK LKSGVEVELS
     ASRHAGILEY SFPEGEKNIL IDLSHFTHDE KYLPASPGDA DGQLFAGGEI QIEDDGKAYS
     GYGTYAGGWN NGAPFTVYFY GEFNSRPNQA RTFSGPNTDP MPRYQNLANG GTSQPEFGNQ
     TDKINSGPMN NRIGVLLTWN DGPALHVTSR VGISFISTDR AKSYIKKEIP SWKLDDTVVD
     AVKEWNHDVF DKIQVPIDDS ANLTHVRLLY SSLYFMHLMP SDRTGENPLW DSGEPYWDDF
     YTMWDIFRCT VSFYHIFQPK YYESMIRSLI DIWKYAGFMP DGRSGNWNGL VQGGSDADNV
     LADAYVKGLR GGINWTEGYA AMVKDAEVTP YNTFDPTDFT ASTKEGRGAL DDWKELGFVS
     QDRNTRCISR TVEYSLNDFA VAQVAKGEMP EDVEKYMNRS AGWQNIWDEN VESLGFKGFL
     APRLADGRFN DSSYDPRLCG GCEWMDVSYE GIPWEYSFVV PHDVKTLIHL MGGAKTFESR
     LDMMFKPNTS VQNLGANGAG ITTLINIGNE PDFATPYLYN YINKQAKSVM QSRSLANQYF
     KDAAYGIPGN SDAGAMNSWL LWQMLGIYPV VTQPVYLISS PWFSDLNMTI NGDKTLRIKA
     TGLDEAYFVQ GVQINGKRWT KNWFEHEDLM VEGGTIEFQL GEEETEWETG DVPPSPGHVQ
     LK
//
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