ID A0A367LHS2_9HYPO Unreviewed; 1842 AA.
AC A0A367LHS2;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 22-FEB-2023, entry version 12.
DE RecName: Full=Sister chromatid cohesion protein {ECO:0000256|RuleBase:RU364107};
GN ORFNames=L249_8048 {ECO:0000313|EMBL:RCI13986.1};
OS Ophiocordyceps polyrhachis-furcata BCC 54312.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX NCBI_TaxID=1330021 {ECO:0000313|EMBL:RCI13986.1, ECO:0000313|Proteomes:UP000253664};
RN [1] {ECO:0000313|EMBL:RCI13986.1, ECO:0000313|Proteomes:UP000253664}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCC 54312 {ECO:0000313|EMBL:RCI13986.1,
RC ECO:0000313|Proteomes:UP000253664};
RX PubMed=26511477; DOI=10.1186/s12864-015-2101-4;
RA Wichadakul D., Kobmoo N., Ingsriswang S., Tangphatsornruang S.,
RA Chantasingh D., Luangsa-ard J.J., Eurwilaichitr L.;
RT "Insights from the genome of Ophiocordyceps polyrhachis-furcata to
RT pathogenicity and host specificity in insect fungi.";
RL BMC Genomics 16:881-881(2015).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU364107}.
CC -!- SIMILARITY: Belongs to the SCC2/Nipped-B family.
CC {ECO:0000256|ARBA:ARBA00009252, ECO:0000256|RuleBase:RU364107}.
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:RCI13986.1}.
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DR EMBL; LKCN02000005; RCI13986.1; -; Genomic_DNA.
DR STRING; 1330021.A0A367LHS2; -.
DR Proteomes; UP000253664; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003682; F:chromatin binding; IEA:InterPro.
DR GO; GO:0061780; P:mitotic cohesin loading; IEA:InterPro.
DR GO; GO:0010468; P:regulation of gene expression; IEA:InterPro.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR026003; Cohesin_HEAT.
DR InterPro; IPR024986; Nipped-B_C.
DR InterPro; IPR033031; Scc2/Nipped-B.
DR PANTHER; PTHR21704:SF18; NIPPED-B-LIKE PROTEIN; 1.
DR PANTHER; PTHR21704; NIPPED-B-LIKE PROTEIN DELANGIN SCC2-RELATED; 1.
DR Pfam; PF12765; Cohesin_HEAT; 1.
DR Pfam; PF12830; Nipped-B_C; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|RuleBase:RU364107};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU364107};
KW Reference proteome {ECO:0000313|Proteomes:UP000253664};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|RuleBase:RU364107}.
FT DOMAIN 1419..1600
FT /note="Sister chromatid cohesion C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12830"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 154..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1621..1656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1768..1842
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1634..1656
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1842 AA; 202987 MW; 96BA98C139C1501E CRC64;
MLPDGPENGV DTLQQPSQPH PAITRPFTLQ ESLPYSPQTL TAPLLPDVIP DPTLGSGSPA
LRIAGLFPRD EFDRVNNEAL NHPQGSRILK QATDYVLHDL KPSQRTQYKF SAIPPAPPGP
PPGNSLSQGL SPMTRSVYDR VGSFFKSTKP NVASLKMNGE MPKPAKESPW LDSNRRSENP
EPYRSPSFRI EVAIPSKRTF DPSSFIDVAG SGHPPEPSSM QPELPSAKVK LPPPSNSSTA
TPKEQSPSAA RSLAFSIELP KANIKKEEYF EVCEVPDAPQ NLSSRRRETQ EVSDGQGVVV
TNLDQRQRSE VALDALDALL RSIFAAVGSA LAIEPGSEHI VTLTADQEPV MTSATQQKLH
GAIQKVIGLR CFDSVALEDL LQIVKLSEAS LRQVDGLEFR VDESWDEAAV DAWVQQLSEV
ETLLKAARTC LRVLSGGRED RQLYSESTIQ RCVDLFKSVL EDLVIPLVEL RNSAGLFKAV
QKHKKAVSST FICCQKLFAL LAELVTKIEL SESVINTLEY TASKVIFVEN AYYEKDSAIG
PQRFDGIRSV AMDMLCQIFL IKPEQRQGII DDILTSLEKL PVGKQSSRQF KLSDGGSIQP
VSALIMRLVQ ASSGRVNVDD GGGRAAILRH IDVDDAGAGE EASKKGQAPC TVTTEEQGAQ
QHAVAVQELE ATAAPLTEAA SRNASYVINF IVKRAIGSTK TGDTPYRNLL DLFVDDFTTC
LDSPDWPSAE LLLRLLMFMM VQLFEAGKTA APAKNMALEL LGAMSAAISR LRSHVKKTAG
SFEGSDADEL SQYLSELAML VLEQKSQTEH ISTWSGPYRV SLEYILRRCS DDPHLAGAAS
YVVADWANKV NVAYDTVQEG DDERDQELGR LAYRLRTMIE DRNWLSSQYT FKAVSASQAK
FAYLIMLLRS PLFEAFGKIV NILLGSMASD QATVRSKSLK SIHQVLETDP SILDGDSTVI
QLILECASDS STQVRDSALG LLGNCIGMRR GLETSLTPKI IERFQDAGVG VRKRAMKLAR
DIYLRNRSKA LRSAIANGLL RRAQDPDEGV RDLSRQMIEE VWFAPFYSNE NTAAFETSLA
EHVALIIQTV KTGTVTEVLD KVFQTVLRPQ NRSLEGPFSV CSRLVGTMFG MIDNPDSEDM
TVPSGRDALQ VLTIFAKADP KLFNFEQIRL LKPQLASFAG RDELAAFRAV TVIYKRVLPQ
LPMVHAEFLA EVRLQLLKAI GKIYSRVALD DLIACTHAVC ELLKDFAPLA NLVASSLLGI
QKLGKDKLDS RGLGQLCAYA IIVGSVCKHS DLDQQLNIFR DRFPRWKGDS VPRLIVDMLS
PFTSPSQSLE ARKAAIEAIG LVCQSWPRNY VLAKVYTAFQ QVFQDRVPAL ETLVLRSFKE
FLMTEEKRSE AGADAEAGSG EKKKKELTVM GGTNFDDVAS ATTQRFLKDM TRIALGSQDE
HAFLAMEVLG SINRQGLTHP KETGVTLMTL ETSANRKMAE LAFVEHRALH EKHETVLERE
YIKAVQSAYS YQRDVVQDRR GATTDPLQSK LHLLMEVLKI SKMKNRQRFL EKLCGQVDFD
LSKLDEDHVG FSRFVIESVA FMEFQTLGEV QTTVNAMEKM VASTGATVAQ AIESEVLDLR
MNDGDDDDAK NNNNNETSAE AQPVTTTATA TTMTTPPVEP RRLRQLAAAS VLLLSVWEVR
THLRKLYGMG TNRHDGKAKA LAKDLNKTPT KVQGVHGDRL WDELTSLVGA LESSDRMAAK
CREFVELMSV DKEFKPVEED DDEVGAAIHD GAGEMGRVTP SDDDDDDNDD DENSRGRKRK
GAAATPGARG KKRARSGSQP RKRGRPRKVV EDNNISRDGA WA
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