ID   A0A182TF83_9DIPT        Unreviewed;      1187 AA.
AC   A0A182TF83;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   22-FEB-2023, entry version 30.
DE   RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
OS   Anopheles melas.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=34690 {ECO:0000313|EnsemblMetazoa:AMEC001234-PA, ECO:0000313|Proteomes:UP000075902};
RN   [1] {ECO:0000313|Proteomes:UP000075902}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CM1001059 {ECO:0000313|Proteomes:UP000075902};
RG   The Broad Institute Genomics Platform;
RA   Neafsey D.E., Besansky N., Howell P., Walton C., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Anopheles melas CM1001059_A (V2).";
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:AMEC001234-PA}
RP   IDENTIFICATION.
RC   STRAIN=CM1001059 {ECO:0000313|EnsemblMetazoa:AMEC001234-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|PIRNR:PIRNR005719}.
CC   -!- SIMILARITY: Belongs to the SMC family. SMC2 subfamily.
CC       {ECO:0000256|ARBA:ARBA00005231}.
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DR   AlphaFoldDB; A0A182TF83; -.
DR   STRING; 34690.A0A182TF83; -.
DR   EnsemblMetazoa; AMEC001234-RA; AMEC001234-PA; AMEC001234.
DR   VEuPathDB; VectorBase:AMEC001234; -.
DR   Proteomes; UP000075902; Unassembled WGS sequence.
DR   GO; GO:0005694; C:chromosome; 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:0030261; P:chromosome condensation; IEA:UniProtKB-KW.
DR   CDD; cd03273; ABC_SMC2_euk; 1.
DR   CDD; cd00890; Prefoldin; 1.
DR   Gene3D; 1.10.287.1490; -; 1.
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; IPR027120; Smc2_ABC.
DR   InterPro; IPR010935; SMC_hinge.
DR   InterPro; IPR036277; SMC_hinge_sf.
DR   PANTHER; PTHR43977:SF2; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN; 1.
DR   PANTHER; PTHR43977; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 3; 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   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   DNA condensation {ECO:0000256|ARBA:ARBA00023067};
KW   Nucleus {ECO:0000256|PIRNR:PIRNR005719}.
FT   DOMAIN          518..638
FT                   /note="SMC hinge"
FT                   /evidence="ECO:0000259|SMART:SM00968"
FT   REGION          779..813
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          246..287
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          317..351
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          416..502
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          982..1009
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1187 AA;  134254 MW;  1CC2DE3F5035F4DA CRC64;
     MYIKSIVIDG FKSYGRRTEV QGFDPEFNAI TGLNGTGKSN ILDSICFVLG ISNLVHVRAT
     SLQDLVYKSG QAGITKATVT LIFDNSNPNQ CPIGYETCRE ISITRQIVVG GKNKYLINGK
     SVQNKRVQDL FCSVQLNVNN PNFLIMQGRI TKVLNMKPAE ILSMIEEAAG TSMYEAKRDS
     ALKLIEKKDA KLNELYAVIR EEIEPKLEKL RKEREHYIEF QKVCRDIEYL TRLYVSYRYL
     QLCKGVEESE RTIANLQSVI GESEQKIESN CATAQTLEQE AKELQERIDT EGGGVLGELE
     QQLAVESKKE ATVAAERNTM KDSIGQEQRK LKNLQKSIRD DEQALAGKEV EMQRRGESFQ
     ALKDACEADE QAFAKAQKRF EAVSAGLSTN EDGEAATLQD QLIAAKQKSA EATTAIKQSE
     MELKHSQQLL RDKQKNMNSS DAAYLEDKRK LTKVEGQIGQ LERELQLTGY EEGSMETLAG
     RRQALQQEVR GLRSELDRRN AHRWELQYRD PEPGFDRRSV KGMVAKLVTV KDPKYAQALG
     TVAGGSLYSV ITDTDTTSKK LLQKGQLQTR TTMIPLNKIS GRKIDPSVAR FAEELVGKEN
     VTTALSCISY DPEVDQAMQF AFGHSFIVKN LEIANKITFH PRIKTRSVTL DGDVVDPGGT
     LSGGARAKGN AVLLDVAEIN RIQAMLQEKE AELRDISAEV SNIEKTAHRF GQLKEQHDML
     NYELNNLKQR LAQTSFQQTK EEIEELNKKI ETLQKTIVEA RETQTQCSAK VKDLQAKIAD
     GKGHRERELK TAEEDLKRSK KKSEESRKNW KKHEQDFETL KLEIEELQKG IVTAKEQAAK
     LEEQIAALQQ RLVEVSGTTD EMTAAVTALK QQIKQHKEKM NSQSKELKAK YHQRDKLLKQ
     NDELKLEIKK KENEITKVRN ENKDGYDRIS GMEQKYPWIP EDKEFFGVKN TRYDYNKEDP
     QEAGRKLKKL QDSKDKMSRN VNQKAMVLLE REEEQYKEVM RRKKVVEDDK KKIQAIITDL
     DEEKKKKLKV AWSEVDENFG SIFSTLLPGT QARLVPPDGV DFMKGLEVKV GFNGMWKESL
     TELSGGQRSL VALSLILAML KYKPAPLYIL DEVDAALDLS HTQNIGNMLK AHFTNSQFII
     VSLKDGMFNN ANVLFRTKFI DGMSGVTRTV NVANIKRAAA DAASRGR
//