ID A0A2K3QQC9_9HYPO Unreviewed; 1252 AA.
AC A0A2K3QQC9;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
GN ORFNames=TCAP_00345 {ECO:0000313|EMBL:PNY29735.1};
OS Tolypocladium capitatum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Tolypocladium.
OX NCBI_TaxID=45235 {ECO:0000313|EMBL:PNY29735.1, ECO:0000313|Proteomes:UP000236621};
RN [1] {ECO:0000313|EMBL:PNY29735.1, ECO:0000313|Proteomes:UP000236621}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 113982 {ECO:0000313|EMBL:PNY29735.1,
RC ECO:0000313|Proteomes:UP000236621};
RA Quandt C.A., Patterson W., Spatafora J.W.;
RT "Harnessing the power of phylogenomics to disentangle the directionality
RT and signatures of interkingdom host jumping in the parasitic fungal genus
RT Tolypocladium.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PIRNR:PIRNR005719}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC1 subfamily.
CC {ECO:0000256|ARBA:ARBA00005597}.
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:PNY29735.1}.
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DR EMBL; NRSZ01000064; PNY29735.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K3QQC9; -.
DR STRING; 45235.A0A2K3QQC9; -.
DR OrthoDB; 231904at2759; -.
DR Proteomes; UP000236621; 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:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007062; P:sister chromatid cohesion; IEA:InterPro.
DR CDD; cd03275; ABC_SMC1_euk; 2.
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; IPR028468; Smc1_ABC.
DR InterPro; IPR010935; SMC_hinge.
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; 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; 1.
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:UP000236621}.
FT DOMAIN 539..654
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 78..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 190..305
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 334..389
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 420..517
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 690..751
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 825..926
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1048..1082
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1252 AA; 142891 MW; 842F0CC53A007591 CRC64;
MGKLIRLELF NFKSYKGHHT LLFGDSYFTS IIGPNGSGKS NSMDAISFVL GIKSSHLRSA
HLKDLVYRGR VLKTSKINDD GSAEANGGAN GFPDDEKASR GDPKTAWVMA VYEDDAGEEQ
RWKRSITSQG ASEYRINERV VTAQQYNESL ETENILIKAR NFLVFQGDVE AIASQSPQDL
TRLIEQISGS LEYKAEYEKL QVDAEQAAEN QNFQLHRRRG INSEIKQYRE QKKEADSFQK
KTDERDAAII THCLWKLYHF QKAMDESSAA IQDHHEDLKE LRRNVEAFEA RLEAARKDQN
AAGRQVGRTE KQIKLKERAI EDRENALVPF DEKIHESSQQ VDKLQAQSQK VARERDEQAG
IVRKVQKDIE SVEKAQEVFE RDIKEQMKEQ GRHISDADRK EYDTLRAQVM SRSGANQGKL
ENLERQRKAD EVTVNNLKGK VDSMTAAIEK VETELASTAE RRTSAETAAK EISSDIASKK
KEFNHLQSER VRTNQKRTEL EEKLDDVARK LREADDGRRQ NDREARMKEM VTALKRILPG
VRGRIGDLCS PKQKKYDEAV IVALGRDFDS VVVDTEKTGV DCVQYLKEQR FPPMTFIPLD
NIKVNAVNTS IKGFSGARLT IDTVNFDSSV ERAVSYACGS SVVCDTLDVA KHICYEKKIP
VKAVTLEGYI IHKAGLMTGG RGPEPKGGKR KFEEADVQNL QRMATRLRDE IDRLPKAARR
GTLEESLQID LAGLERRLAA TKDELAAFNK NWTSKNRELD HHRMQLREMQ PKHREQASQL
ESTRETVHKF MEAIARVEDQ VFADFCKRLG YGDIRAYDAS QGKFEQEVSE KRSQFEVQKQ
RLESRLKWEV ARHGDTETRI RRMQDQVRRL KQDIKSYTKE KSDIEEAMRQ ERDELEGLRE
TVEELKADLL DKNQKVSEAR ADVQRRSKDI DARQRDINAL ETTVQKNSAG KSGLLRRCRL
EQIQIPLAEG TLDNLPNEDD LLRQDPDAMD VDWDDEEMMG IALDDHGIEI DFDGLDSELK
ESDEASVEDS LTDKIAALSV ELEKLNPNMR AMERLESVET RLKQTDQEYE DSKAAAHAAK
EAFGNVKQKR YDLFNKAFTH IQEQISHVYK DLTRSEAYPL GGQAYLDIEE DTDMPYLSGI
KYHAMPPLKR FRDMEHLSGG EKTMAALALL FAIHSYQPSP FFVLDEVDAA LDNANVDKIK
KYIREHAGPG MQFIVISLKT GLFQDSESLV GVYRDQEVNS SRTLTLDLRK YA
//
