LOCUS       VTR95461.1              1105 aa    PRT              BCT 03-FEB-2020
DEFINITION  Gemmata massiliana carbamoyl phosphate synthase large
            subunit : Carbamoyl-phosphate synthase (glutamine-hydrolyzing)
            OS=Pirellula staleyi (strain ATCC 27377 / DSM 6068 / ICPB
            4128) GN=Psta_1525 PE=3 SV=1: CPSase_L_chain: CPSase_L_D2:
            CPSase_L_D3: CPSase_L_chain: CPSase_L_D2: MGS protein.
ACCESSION   LR593886-4762
PROTEIN_ID  VTR95461.1
SOURCE      Gemmata massiliana
  ORGANISM  Gemmata massiliana
            Bacteria; Planctomycetes; Planctomycetia; Gemmatales; Gemmataceae;
            Gemmata.
REFERENCE   1
  AUTHORS   
  CONSRTM   Science for Life Laboratories
  JOURNAL   Submitted (14-MAY-2019) to the INSDC. DEPARTMENT OF CELL AND
            MOLECULAR BIOLOGY, Uppsala University, Molecular Evolution,
            Biomedicinskt centrum (BMC), Husargatan 3, 752 37 Uppsala, Sweden
FEATURES             Qualifiers
     source          /organism="Gemmata massiliana"
                     /chromosome="1"
                     /isolate="Soil9"
                     /mol_type="genomic DNA"
                     /isolation_source="soil"
                     /db_xref="taxon:1210884"
     protein         /locus_tag="SOIL9_22530"
                     /note="BLAST_uniprot:hit_4 ;
                     ACCESSION=tr|M5TT22|M5TT22_9PLAN ;
                     ALN/Q_length_ratio=0.976 ; DESCRIPTION=Carbamoyl-phosphate
                     synthase (glutamine-hydrolyzing) OS=Rhodopirellula
                     sallentina SM41 GN=RSSM_06198 PE=3 SV=1 ; EVALUE=0.0 ;
                     Q/S_length_ratio=1.020"
                     /note="BLAST_uniprot:hit_2 ;
                     ACCESSION=tr|L0D7N3|L0D7N3_SINAD ;
                     ALN/Q_length_ratio=0.970 ; DESCRIPTION=Carbamoyl-phosphate
                     synthase (glutamine-hydrolyzing) OS=Singulisphaera
                     acidiphila (strain ATCC BAA-1392 / DSM 18658 / VKM B-2454
                     / MOB10) GN=Sinac_0210 PE=3 SV=1 ; EVALUE=0.0 ;
                     Q/S_length_ratio=1.026"
                     /note="BLAST_uniprot:hit_12 ;
                     ACCESSION=tr|F2B0B4|F2B0B4_RHOBT ;
                     ALN/Q_length_ratio=0.979 ; DESCRIPTION=Carbamoyl-phosphate
                     synthase (glutamine-hydrolyzing) OS=Rhodopirellula baltica
                     WH47 GN=RBWH47_02665 PE=3 SV=1 ; EVALUE=0.0 ;
                     Q/S_length_ratio=1.020"
                     /note="BLAST_uniprot:hit_5 ;
                     ACCESSION=tr|M5T584|M5T584_9PLAN ;
                     ALN/Q_length_ratio=0.976 ; DESCRIPTION=Carbamoyl-phosphate
                     synthase (glutamine-hydrolyzing) OS=Rhodopirellula sp.
                     SWK7 GN=RRSWK_03223 PE=3 SV=1 ; EVALUE=0.0 ;
                     Q/S_length_ratio=1.020"
                     /note="BLAST_uniprot:hit_7 ;
                     ACCESSION=tr|M5RL13|M5RL13_9PLAN ;
                     ALN/Q_length_ratio=0.977 ; DESCRIPTION=Carbamoyl-phosphate
                     synthase (glutamine-hydrolyzing) OS=Rhodopirellula
                     maiorica SM1 GN=RMSM_03052 PE=3 SV=1 ; EVALUE=0.0 ;
                     Q/S_length_ratio=1.019"
                     /note="BLAST_uniprot:hit_15 ;
                     ACCESSION=tr|L7CQ44|L7CQ44_RHOBT ;
                     ALN/Q_length_ratio=0.979 ; DESCRIPTION=Carbamoyl-phosphate
                     synthase (glutamine-hydrolyzing) OS=Rhodopirellula baltica
                     SWK14 GN=RBSWK_00179 PE=3 SV=1 ; EVALUE=0.0 ;
                     Q/S_length_ratio=1.020"
                     /note="BLAST_uniprot:hit_8 ;
                     ACCESSION=tr|A3ZRT7|A3ZRT7_9PLAN ;
                     ALN/Q_length_ratio=0.979 ; DESCRIPTION=Carbamoyl-phosphate
                     synthase (glutamine-hydrolyzing) OS=Blastopirellula marina
                     DSM 3645 GN=DSM3645_12586 PE=3 SV=1 ; EVALUE=0.0 ;
                     Q/S_length_ratio=1.016"
                     /note="BLAST_uniprot:hit_14 ; ACCESSION=Q7UJ58 ;
                     ALN/Q_length_ratio=0.979 ; DESCRIPTION=Carbamoyl-phosphate
                     synthase large chain OS=Rhodopirellula baltica (strain
                     SH1) GN=carB PE=3 SV=1 ; EVALUE=0.0 ;
                     Q/S_length_ratio=1.020"
                     /note="BLAST_uniprot:hit_10 ;
                     ACCESSION=tr|M5SFC8|M5SFC8_9PLAN ;
                     ALN/Q_length_ratio=0.979 ; DESCRIPTION=Carbamoyl-phosphate
                     synthase (glutamine-hydrolyzing) OS=Rhodopirellula
                     europaea SH398 GN=RESH_04418 PE=3 SV=1 ; EVALUE=0.0 ;
                     Q/S_length_ratio=1.020"
                     /note="BLAST_uniprot:hit_9 ;
                     ACCESSION=tr|A6C484|A6C484_9PLAN ;
                     ALN/Q_length_ratio=0.976 ; DESCRIPTION=Carbamoyl-phosphate
                     synthase (glutamine-hydrolyzing) OS=Planctomyces maris DSM
                     8797 GN=PM8797T_11499 PE=3 SV=1 ; EVALUE=0.0 ;
                     Q/S_length_ratio=1.019"
                     /note="BLAST_uniprot:hit_3 ;
                     ACCESSION=tr|L0DQG7|L0DQG7_SINAD ;
                     ALN/Q_length_ratio=0.970 ; DESCRIPTION=Carbamoyl-phosphate
                     synthase (glutamine-hydrolyzing) OS=Singulisphaera
                     acidiphila (strain ATCC BAA-1392 / DSM 18658 / VKM B-2454
                     / MOB10) GN=Sinac_7091 PE=3 SV=1 ; EVALUE=0.0 ;
                     Q/S_length_ratio=1.026"
                     /note="BLAST_uniprot:hit_13 ;
                     ACCESSION=tr|K5D8A5|K5D8A5_RHOBT ;
                     ALN/Q_length_ratio=0.979 ; DESCRIPTION=Carbamoyl-phosphate
                     synthase (glutamine-hydrolyzing) OS=Rhodopirellula baltica
                     SH28 GN=RBSH_01670 PE=3 SV=1 ; EVALUE=0.0 ;
                     Q/S_length_ratio=1.020"
                     /note="BLAST_uniprot:hit_11 ;
                     ACCESSION=tr|M2AVZ1|M2AVZ1_9PLAN ;
                     ALN/Q_length_ratio=0.979 ; DESCRIPTION=Carbamoyl-phosphate
                     synthase (glutamine-hydrolyzing) OS=Rhodopirellula
                     europaea 6C GN=RE6C_02505 PE=3 SV=1 ; EVALUE=0.0 ;
                     Q/S_length_ratio=1.020"
                     /note="BLAST_uniprot:hit_6 ;
                     ACCESSION=tr|D5SP30|D5SP30_PLAL2 ;
                     ALN/Q_length_ratio=0.981 ; DESCRIPTION=Carbamoyl-phosphate
                     synthase (glutamine-hydrolyzing) OS=Planctomyces
                     limnophilus (strain ATCC 43296 / DSM 3776 / IFAM 1008 /
                     290) GN=Plim_0334 PE=3 SV=1 ; EVALUE=0.0 ;
                     Q/S_length_ratio=1.014"
                     /note="BLAST_uniprot:hit_1 ;
                     ACCESSION=tr|D2QXL5|D2QXL5_PIRSD ;
                     ALN/Q_length_ratio=0.978 ; DESCRIPTION=Carbamoyl-phosphate
                     synthase (glutamine-hydrolyzing) OS=Pirellula staleyi
                     (strain ATCC 27377 / DSM 6068 / ICPB 4128) GN=Psta_1525
                     PE=3 SV=1 ; EVALUE=0.0 ; Q/S_length_ratio=1.009"
                     /note="Pfam_scan:hit_1 (6..123);
                     Pfam:PF00289.17:CPSase_L_chain;
                     Pfam_type:Domain;HMM_aln_Length:109; HMM_Length:110;
                     EVALUE:1.4e-20; BITSCORE: 73.4"
                     /note="Pfam_scan:hit_2 (128..335);
                     Pfam:PF02786.12:CPSase_L_D2;
                     Pfam_type:Domain;HMM_aln_Length:209; HMM_Length:211;
                     EVALUE:4.9e-70; BITSCORE: 235.1"
                     /note="Pfam_scan:hit_3 (427..551);
                     Pfam:PF02787.14:CPSase_L_D3;
                     Pfam_type:Domain;HMM_aln_Length:119; HMM_Length:123;
                     EVALUE:5.7e-44; BITSCORE: 148.8"
                     /note="Pfam_scan:hit_4 (578..689);
                     Pfam:PF00289.17:CPSase_L_chain;
                     Pfam_type:Domain;HMM_aln_Length:107; HMM_Length:110;
                     EVALUE:1e-20; BITSCORE: 73.8"
                     /note="Pfam_scan:hit_5 (694..908);
                     Pfam:PF02786.12:CPSase_L_D2;
                     Pfam_type:Domain;HMM_aln_Length:208; HMM_Length:211;
                     EVALUE:1.4e-30; BITSCORE: 106.1"
                     /note="Pfam_scan:hit_6 (987..1073); Pfam:PF02142.17:MGS;
                     Pfam_type:Domain;HMM_aln_Length:93; HMM_Length:95;
                     EVALUE:1.2e-17; BITSCORE: 63.5"
                     /note="GO_domain:GO:0008150"
                     /note="GO_domain:GO:0043167"
BEGIN
        1 MPKRTDIKKI LLIGSGPIII GQACEFDYSG TQACKALREE GYSVVLVNSN PATIMTDPET
       61 ADRTYIEPIT WEVVEKIIVA ERPDALLPTL GGQTALNTAM DLFKKGVLAK HGVEMIGANA
      121 DVIDKAEDRQ RFKDAMLKIG VSVPKSVVVH SLEEAMRAVE EVGLPCVLRP SFTMGGTGGG
      181 IAYNRDEYRD LITHGLQLSP TTEVLVEESV IGWKEYELEV MRDRADNVVI ICSIENLDPM
      241 GVHTGDSITV APAQTLSDKE YQRMRDKAKD IIREIGVETG GSNIQFAINP ADGRMIAIEM
      301 NPRVSRSSAL ASKATGFPIA KIAAKLAVGY TLDELRNDIT RETPACFEPT IDYVVTKVPR
      361 FAFEKFPEAN PTLTTQMKSV GETMAIGRTF KESLQKALRG LEVNRFGLGC DKRDRWGTAN
      421 PPAREEITFK LSSPNAERVW YLRYAFLAGM SLDEIHQRTK IDPWFLRGVE DLVNIEHELR
      481 AVGSLDKVTP ELMLKAKQSG FIDRQLAHIW NVAEAEVRKL RKSFGIEAVF KSVDTCAAEF
      541 EAYTPYYYST YEPGARVQQP GQPVFFSPGE DEVRPFSGKS RIMILGGGPN RIGQGIEFDY
      601 CCVQAAFALR DNGYEVIMVN SNPETVSTDY DTSDHLFFEP LTPEDVLNIN DKMKPEGVIV
      661 QFGGQTPLNL ATPLQDAGVP IIGTSVDSID VAENRERFAK LVNEIGLLQP ANGTAVDESQ
      721 ALRVARRIGF PILVRPSFVL GGRDMKIVYN EDELTAYIRR VEPDLSRDRP VLIDQFLENA
      781 TEVDVDCLSD GTRTVIGGVM QHIEEAGIHS GDSACVIPPY SLPADVISEI KVQARKLATA
      841 LNVKGLMNIQ FAVAGIRAGG IVTDKPKVYI LEANPRASRT VPFVSKATGV PLARLAALVM
      901 VGKTLDELGV KDEVIPTHYS IKESVFPFNK FPGVDIILGP EMKSTGEVMG IDDSMPMAFA
      961 KAQLAASSRL PEGGTVFISV ANRDKDAVLP IARGFAEMGF KVIATRGTAQ FLRERGVPVE
     1021 DVPKIAEGRP NLLDHMKNGK VQLVINTPTG RGSSTDESKI RAEAVASRVT AITTLSAAQA
     1081 AVEACRALKQ QQLTVTALQD RFPQK
//