ID A0A0V0TN68_9BILA Unreviewed; 1977 AA.
AC A0A0V0TN68;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Structural maintenance of chromosomes protein 1A {ECO:0000313|EMBL:KRX40477.1};
GN Name=FucTC {ECO:0000313|EMBL:KRX40477.1};
GN ORFNames=T05_11501 {ECO:0000313|EMBL:KRX40477.1};
OS Trichinella murrelli.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=144512 {ECO:0000313|EMBL:KRX40477.1, ECO:0000313|Proteomes:UP000055048};
RN [1] {ECO:0000313|EMBL:KRX40477.1, ECO:0000313|Proteomes:UP000055048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS417 {ECO:0000313|EMBL:KRX40477.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000256|ARBA:ARBA00004323}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004323}. Membrane
CC {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004606}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC1 subfamily.
CC {ECO:0000256|ARBA:ARBA00005597}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. GalNAc-T
CC subfamily. {ECO:0000256|ARBA:ARBA00005680}.
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:KRX40477.1}.
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DR EMBL; JYDJ01000199; KRX40477.1; -; Genomic_DNA.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000055048; Unassembled WGS sequence.
DR GO; GO:0008278; C:cohesin complex; IEA:InterPro.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
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:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR GO; GO:0007062; P:sister chromatid cohesion; IEA:InterPro.
DR CDD; cd03275; ABC_SMC1_euk; 1.
DR CDD; cd06257; DnaJ; 1.
DR CDD; cd02510; pp-GalNAc-T; 1.
DR CDD; cd00161; RICIN; 1.
DR Gene3D; 1.20.1060.20; -; 1.
DR Gene3D; 2.80.10.50; -; 1.
DR Gene3D; 3.30.70.1620; -; 1.
DR Gene3D; 1.10.287.110; DnaJ domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR045885; GalNAc-T.
DR InterPro; IPR001173; Glyco_trans_2-like.
DR InterPro; IPR036869; J_dom_sf.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR003395; RecF/RecN/SMC_N.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
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; PF00226; DnaJ; 1.
DR Pfam; PF00535; Glycos_transf_2; 1.
DR Pfam; PF00652; Ricin_B_lectin; 1.
DR Pfam; PF06470; SMC_hinge; 1.
DR Pfam; PF02463; SMC_N; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SMART; SM00458; RICIN; 1.
DR SMART; SM00968; SMC_hinge; 1.
DR SUPFAM; SSF46565; Chaperone J-domain; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR SUPFAM; SSF75553; Smc hinge domain; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000055048};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022968}.
FT DOMAIN 1835..1900
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
FT COILED 161..219
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 263..290
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 319..360
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 412..488
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 801..910
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1977 AA; 227894 MW; DBA1C669EDF09732 CRC64;
MGFLREIELE NFKSYKGYQR IGPFKKFTAI IGPNGSGKSN LMDAICFVLG EKTSSLRVRK
ISDLIYGAPV GKPVSTRCYV AMTYEDDDGR ILKFMRLVAG ASAEYRIDGA TVSHLQYTEA
LESINIFIRA KNFLVFQGAV ENIAMKNPKE CTLLFEEISR SGELKAEYET LKAEMMRAEQ
DTQLNYHRKR DIAAKRRAAK MEKEEAEKYQ KLKDSVAEKQ SRYYLMKLFS NDRESKRIFG
EMNGKHGEQS RIATKCSEVE EVLKERRKVY SKVTREVNKL EQQIYEMESE ITREKPSFIK
VKENVRHSER KLEAFHKAFE AARKNAERQQ EVIRQFEVQL KEANEQRDAF EAQLMQESES
QGLQLDSEQL AQYNSLKGEV VRQCASIQQE LDVLAREQQM DQELLDNDKR CNGEFCQKIK
QKESELEALK KRLEKLVDTI RNTENEIEEQ RSSLRSTEDE VRTAKTRLEQ VIVEVEDVNR
QLNDANVDSS ENSRIVKKQE LVENLKRIST GTVYGRVVDL CQPAHKRYQL AVTKILGKYM
NAIVVDTEKT AKECIQYMKE QRIESETFLP VDYIDVKPLN EKLRELREPR NVKLIFDVIQ
FEPPQIRRVV QFACGNSLVC ESVEDARNLA FSGAERHRAV ALDGTVFEKS GIISGGAGDL
KAKAKRWDEK AVAHLRSRKS ALIEEQKELH RIRRKEPDIS LMQNSVKQLE TRMKYMLTDK
ENTETRLLKN LESDLMQLKA ETEKYGPRIQ EIENRMASRR SNILQNQSRM NQVADHVFAD
FCKSIGVLNI RQYEEREIRF RQDKKQKMME FDNQIEKLKN ELEYQKSDDK SAQLEKIEAS
CNKEERELIK AKKEEQEHIR LLADLESQLK DLKAMRQTKK VELENKEAEL NEVKKELATI
QKELLSVQKQ TSAMETLLEQ KRSERHSLLQ TCKLENITLP IIRGSLDILS TTVSSQSSDT
TSSVVSEDGA TTLSSTSFMG NRQLYQLEAE ITFDFSSLNP DDWELSDDTE LRLAAEKLLK
EIGETQAFLQ TITAPNLKAS AKLEGVRERF AETSGEFEQA RKKAKNAKMA FEIIQKERCS
RFNRCFDQVS GKIDEIYKAL SRNFSSQAYL TADNPEEPYL DGVSFSVVAP GKRFRPMDSL
SGGEKTLAAL TLLFAIHSYN RAPFFVLDEI DAALDNTNIG KVAAFIREQA ANNMQLIVIS
LKEEFYNQAD ALIGIYSVTG SSIASSGLLT LDLTDYSETI LNEEMIFWHI LFLEFNGIPI
LRNAPVSYSK DWHNYTQMML DRARRGVGEH GNPVELPSSV AEKAEFDRLY KANGYSGWTS
DKISLYRAIK DLRHADCKRK SYLLLLPSTS VIVPFHNEHL SVLLRTVYTI VYRTPPELLL
EVILVNDAST KPELNDILER HVQRKFPNLV HVIRAGSDGR REGAAKASGQ VLMFMDAHSE
VGYNWLPPLL EPIKLHYRTV TCPFIDVIDC DTFAFRAQDE GARGSFDWKF HYKRLPLLNK
TGAEPFESPV MAGGYFAISK RWFDELGRYD DQLMIWGAEQ YELSFKLWQC HGRMIDIPCS
RIAHIYRCKY APFEDPGIGN FLERNYKRVA ETWMDEYKEY LYLRMPRLRN VDPGDLTKQR
EVRQRLKCNG FDWFMKNVMF DQPKHYPLVE PPDVMSGRIK NKHTGRCMDV KNAGLQTELT
TSQCKDYLKR QEFVLSWRSE IFQRLGENCL DSMNHGPGET VHLFACHGGG GNQNWTYSRN
TTMHLQMTAS NLCLDTDNTG RLFLNTCQLF CFCGGSGKTR CVQWRGFIHL FNLLTASFCS
ADYFKVNNNK NIVQSWMNST VDNKMDLSQY AANDDYYNIL GCDASSTMEQ IVAEFRVRAK
KLHPDKNSKS TSANEDFARL SRAKEILTDP HLRKSYDLWR NAGLNIPFDD WLRKANALRS
SVHWFHESPT LSIESSSQYA NKFSSGDIFY LVLQMQEIGV VNSRRYCHHC HTSQIWH
//
