ID A0A183C6U5_GLOPA Unreviewed; 1278 AA.
AC A0A183C6U5;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
OS Globodera pallida (Potato cyst nematode).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Tylenchomorpha; Tylenchoidea; Heteroderidae; Heteroderinae;
OC Globodera.
OX NCBI_TaxID=36090 {ECO:0000313|Proteomes:UP000050741, ECO:0000313|WBParaSite:GPLIN_000859100};
RN [1] {ECO:0000313|Proteomes:UP000050741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lindley {ECO:0000313|Proteomes:UP000050741};
RA Aslett M.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000050741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lindley {ECO:0000313|Proteomes:UP000050741};
RA Cotton J.A., Lilley C.J., Jones L.M., Kikuchi T., Reid A.J., Thorpe P.,
RA Tsai I.J., Beasley H., Blok V., Cock P.J.A., Van den Akker S.E.,
RA Holroyd N., Hunt M., Mantelin S., Naghra H., Pain A., Palomares-Rius J.E.,
RA Zarowiecki M., Berriman M., Jones J.T., Urwin P.E.;
RT "The genome and life-stage specific transcriptomes of Globodera pallida
RT elucidate key aspects of plant parasitism by a cyst nematode.";
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|WBParaSite:GPLIN_000859100}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PIRNR:PIRNR005719}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC4 subfamily.
CC {ECO:0000256|ARBA:ARBA00006005}.
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DR AlphaFoldDB; A0A183C6U5; -.
DR WBParaSite; GPLIN_000859100; GPLIN_000859100; GPLIN_000859100.
DR Proteomes; UP000050741; Unassembled WGS sequence.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; 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; 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; IPR010935; SMC_hinge.
DR InterPro; IPR036277; SMC_hinge_sf.
DR PANTHER; PTHR18937:SF172; 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; 2.
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 Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Nucleus {ECO:0000256|PIRNR:PIRNR005719}.
FT DOMAIN 591..697
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 897..958
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 972..1024
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 326..395
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 442..518
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 543..570
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 714..864
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 16..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 908..939
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 974..1000
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1278 AA; 146124 MW; CE331F2EA5B19FCA CRC64;
MRRNAKKKGE VIGSTDNQEN EEPTPANQEN INEDYDEEDL LNMKIPAPPE SFMHRDGNRM
VISHIEVENF KSYHGRQIIG PFHKSFTSII GPNGSGKSNV IDSLLFVFGY RASKIRSKKI
SVLIHSSAGR ENIQNCTVTI HFCKIVDVNE TEYKKVDGSN IAVARTAFKD NSSRYSLNGK
TVKFKEIGDL LRSNGVDLVH NRFLILQGEV EQISMMKPKA EKEDDEGMLE YLEDIIGSSR
LKQPINKLSR RIGRIDERRD IQLQRLQHAE KDKQKLTGPA REILLQMRLE NAVNCLTNRI
LLAKKYTIEE QLSQLEGVKG QRTTELAENQ QKHKELTNQA KQHSAQRQRL QCQLDKVQDE
VQSIERKIGE SKQAKVKATN DKKRLATRKN QLEENTGLER EKLTEWMSAP EKAKTKIEEY
RKQLLEANAV IDECSPLLIQ KLDEAQQLVR NERHEKTELE AKLSKVSVVE DDLNSKLLLA
QEKKLNLRRE EEAQRSKYDE LHNKLLDTEN KYAQVNRDFH STVEALPELE QTFEGKKVRM
GDLREREAKL ANLARDLRSQ YEERRQAEEQ WKGDNKMLER LMQAKQSGEI GGIFGRLGDL
GAIDQKYDVA ISTTCFALDH IVVEDVPTAQ QCIDLLKRHK LGVASFIALN KQSHFWNSIR
QQPNTPENAP RLFDLIRVAD EKIVDVSGSM TGGGNQQIRG KIGQNVRVDT REKTTDEQQS
IGELQQQMNN AEAELATIRR ECEQLETELQ QRQGQLNKMQ KNLREFELDK DHLGNTVKKL
REQIETQKKK VIEATADPVE ETERQLEVVS ARFSEAVEQL EKLDEINGKM NERNEEEMAL
QKKVDELKRS LKGIENEVAT LGAKLKAGDA KLSSLKCFRT KWLVNALSKE TSAIVGRPSK
KRPVAVDDEE ADEDDEDEGE GSDEERDGDG LDDEMEVEDG TMGNGQRQLG NGDDDETTDD
LELFLHDCAA IDDSDVNFEE TDGEVDDQME IDDSEGGEEE DDLRNDNHSN RGTTNPPKSR
AIANPDSLNK LFMPLPKLSE QVVRDEVDVN LLESHLAELE KRRRKHSVAN LTVVLDFMAK
LKKYQAEFKE LAAITEQRDL HRSLHDRLKK QRLHEFMEGF QQIATELRVT YQMITIQGDV
SLELVDSLDP FAEGIAFNVR PPKKSWKQIT NLSGGEKTLA SLSLVFGLHK YKPTPLYVMD
EIDAALDFRN VSIIANYLLE RTRNAQFIVI SLRNQMYEKA NRLIGIYKVN DCTRNVVVDP
QDMVKTFERD VKSRKIRS
//
