ID   A0A1S3HFU2_LINUN        Unreviewed;      1405 AA.
AC   A0A1S3HFU2;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Structural maintenance of chromosomes protein 6 {ECO:0000313|RefSeq:XP_013384922.1};
GN   Name=LOC106154913 {ECO:0000313|RefSeq:XP_013384922.1};
OS   Lingula unguis.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC   Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX   NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013384922.1};
RN   [1] {ECO:0000313|RefSeq:XP_013384922.1}
RP   IDENTIFICATION.
RC   TISSUE=Gonads {ECO:0000313|RefSeq:XP_013384922.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the SMC family. SMC6 subfamily.
CC       {ECO:0000256|ARBA:ARBA00006793}.
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DR   RefSeq; XP_013384922.1; XM_013529468.1.
DR   STRING; 7574.A0A1S3HFU2; -.
DR   EnsemblMetazoa; XM_013529468.1; XP_013384922.1; LOC106154913.
DR   GeneID; 106154913; -.
DR   KEGG; lak:106154913; -.
DR   InParanoid; A0A1S3HFU2; -.
DR   OrthoDB; 78166at2759; -.
DR   Proteomes; UP000085678; Unplaced.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0006302; P:double-strand break repair; IEA:InterPro.
DR   Gene3D; 1.10.287.1490; -; 2.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038729; Rad50/SbcC_AAA.
DR   PANTHER; PTHR19306; STRUCTURAL MAINTENANCE OF CHROMOSOMES 5,6 SMC5, SMC6; 1.
DR   PANTHER; PTHR19306:SF6; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 6; 1.
DR   Pfam; PF13476; AAA_23; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   SUPFAM; SSF57997; Tropomyosin; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000085678}.
FT   DOMAIN          57..284
FT                   /note="Rad50/SbcC-type AAA"
FT                   /evidence="ECO:0000259|Pfam:PF13476"
FT   REGION          1..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          402..485
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          660..882
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          922..1144
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..23
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1405 AA;  162641 MW;  32D5F4BEF1F09015 CRC64;
     MSKRRTNTEQ HRPLKRMKDE GRSDNDDDDG DIMDQSQRPD FRTASMGEEA DMGIIERIQL
     KNFMCHTRLD FPFCPNINFI TGNNGSGKSA ILTGLVVGLG GGAKATSRGT SVRGFIKNGK
     QSGEVIIKLR NRGSEAFKHD QYGDSIIIKR TVKAVGGSAY RLENAEGKLV SNKKEELDHI
     VDHFNIQINN PVAVLNQDTS RNFLHSKNPN DKYKFFLKAT QLEQMKQDYC SITEQMEITK
     GIISTKETTV PTLHAEVLEW EKKFKAVQNC DDLRGKIQAL KNEIAWAIVI ECEESLKPLT
     KAHRVEDART PKFQQKVDEC QAKLDECMVG HKEIQDKLKT YSTEAQKLVP QHADAKKVLS
     EKKKVVRAVQ LEERKIQSEL RTVTKDRDQT LERINEIRNS AQEDHESERI AREQKIRGLE
     EELNGCQGRR KTTEHEVEQF RAAVTKYKEE GYRLSNNEKE VRHTLEEKKN QLRNLQDARS
     DRLKRFGAWV PTLLEKIEVA HRQNRFHQKP RGPLGKYALA XECCLKNLMH SYCCTDYHDE
     KILNQIMTQV CPKGRPKPTI IVSRFLEHVH DVSQFRSRCE FPTVLDMLEL DDPVVANALV
     DQRGIENVIL IKNAVQARQF MGKNKDRNTK EAFVGNGDQV FSFPTFRYYA SSTDKASFLK
     ADVEEEIRSL EVEIAGIQQE AENLRKKRAS VDSDIQSNQM EERRTQTKLM KISERIEKLM
     SEIDELKSIE DPEPVDVTTL EEEVGGFNQQ IEELQGKVNE VRDKLKETQA EVQKAEEEFK
     QIDEKMRSIA DGAEPLKEEL AHAETQIEVA KSNKKHYDGK MKEHEKKLSD IKKLVEAKKK
     EIEEKCAKAE AVCPRKNTRR TQRNLESEII QIEKQLKAQE KRHSCHFLFL FLQAFVGNGD
     QVFSFPTFRY YASSTDKASF LKADVEEEIR SLEVEIGGIQ QEAENLRKKR ASVDSDIQSN
     QMEERRTQTK LMKISERIEK LMSEIDELKS IEDPEPVDVT TLEEEVGGFN QQIEELQGKV
     NEVRDKLKET QAEVQKAEEE FKQIDEKMRS IADGAEPLKE ELAHAETQIE VAKSNKKHYD
     GKMKEHEKKL SDIKKLVEAK KKEIEEKCAK AEAVCPRKNT RRTQRNLESE IIQIEKQLKA
     QEKSHGNKEE ITRKYYETKD AYLKIKKEIK QFGNFLKKLE ITMEIRQEIY KKLRSSLAYR
     TKMNFINTLR SRFFVGRLVF RHNTQTLNME LLQDVMGTRQ HQFIEFRKMI ALRAKYYFIV
     MLSNRSYVGK MTFNHKKEIL ELSVQPSNQS AEGAKDMRAL SGGERSFSTV CFILALWDAM
     ESPFRCMDEF DVYMDMVNRR ISMDMLMEVA KNQKTRQFIF LTPQNMSNLQ PSPTLKIFKM
     PDPQRGSGVI ETTREREEEQ EAMAT
//