ID D4ZDP4_SHEVD Unreviewed; 1949 AA.
AC D4ZDP4;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=Carrier domain-containing protein {ECO:0000259|PROSITE:PS50075};
GN OrderedLocusNames=SVI_3984 {ECO:0000313|EMBL:BAJ03955.1};
OS Shewanella violacea (strain JCM 10179 / CIP 106290 / LMG 19151 / DSS12).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=637905 {ECO:0000313|EMBL:BAJ03955.1, ECO:0000313|Proteomes:UP000002350};
RN [1] {ECO:0000313|Proteomes:UP000002350}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10179 / CIP 106290 / LMG 19151 / DSS12
RC {ECO:0000313|Proteomes:UP000002350};
RX PubMed=20458400; DOI=10.1039/c000396d;
RA Aono E., Baba T., Ara T., Nishi T., Nakamichi T., Inamoto E., Toyonaga H.,
RA Hasegawa M., Takai Y., Okumura Y., Baba M., Tomita M., Kato C., Oshima T.,
RA Nakasone K., Mori H.;
RT "Complete genome sequence and comparative analysis of Shewanella violacea,
RT a psychrophilic and piezophilic bacterium from deep sea floor sediments.";
RL Mol. Biosyst. 6:1216-1226(2010).
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DR EMBL; AP011177; BAJ03955.1; -; Genomic_DNA.
DR RefSeq; WP_013053246.1; NC_014012.1.
DR STRING; 637905.SVI_3984; -.
DR KEGG; svo:SVI_3984; -.
DR eggNOG; COG0318; Bacteria.
DR eggNOG; COG1020; Bacteria.
DR HOGENOM; CLU_000022_0_9_6; -.
DR OrthoDB; 9757559at2; -.
DR Proteomes; UP000002350; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:0008610; P:lipid biosynthetic process; IEA:InterPro.
DR GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR CDD; cd05930; A_NRPS; 1.
DR CDD; cd05931; FAAL; 1.
DR Gene3D; 3.30.300.30; -; 2.
DR Gene3D; 3.40.50.980; -; 2.
DR Gene3D; 1.10.1200.10; ACP-like; 2.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR010071; AA_adenyl_domain.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR040097; FAAL/FAAC.
DR InterPro; IPR013120; Far_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR001031; Thioesterase.
DR NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR PANTHER; PTHR44845:SF6; BETA-ALANINE-ACTIVATING ENZYME; 1.
DR PANTHER; PTHR44845; CARRIER DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00501; AMP-binding; 2.
DR Pfam; PF13193; AMP-binding_C; 1.
DR Pfam; PF07993; NAD_binding_4; 1.
DR Pfam; PF00550; PP-binding; 2.
DR Pfam; PF00975; Thioesterase; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 2.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00455; AMP_BINDING; 2.
DR PROSITE; PS50075; CARRIER; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Reference proteome {ECO:0000313|Proteomes:UP000002350};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 79..100
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1582..1657
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1949 AA; 217623 MW; B55A65FF5228CDEF CRC64;
MEPKSFNLAE QTSLVAVLQH RAQITPNKVA YIYLENGEDI EVPITYAELD CRARELAAQL
QGKNPLIQQE RVLLIYPQGI DFIVAFFATL YAGAIAVLVY PPSSKKMAQR LNGIVEDCNV
KLILSTAKVI SRMDRMNMVT DAGEQDEDAI NIPAQYWINS DNLDPEAARD FKQPIILGEH
LAFLQYTSGS TGTPKGVMIS HSNLMANQAA IKDIYQHDDK TIFVGWLPLI HDMGLIGNVL
QPMYLGISLV FMSPLHFVQK PVRWLRAISK YQATTSGGPN FAYDLCVRKI ADADLADLDL
SSWTLAYNGA EPVRKETVSR FNQRFSVCGL KPESHMAVYG LAEATLIVTG TNKQAVLATS
DNVDYMSSGT CVEVDRVRIV NPETCVEADE QQEGEIWVHG PSVAKGYWNR PEETQTTFKA
QILGSELHYM RTGDTGYCKN GEIHVTGRIK DIVIVQGKNF HPEDIEWSLI DVQGLRVGGS
VAFSLDVVDE QGQTSESLVV VAGVLESDSD KHPSIISNIR SFIYQDHQLQ VDRVVLIKPK
QIPMTTSGKV QRRLTRQMLV ANEFTILGDD LLAAVDDKST QARSSIVAAT TKAELELTSM
WGAILGLSAS DIGITDNFFD LGGSSLTMLE LSIQLNTTME LLFRYPTISS YLYRTSEYEF
PEVEKDIYLP AANIDRSLEG ETGISLITGG TGFFGLHFLQ SMMQRTQDKF VLLIRGENDD
VMNKKFTDAV AYFHMEKDID IGRVILIRGD LSEHHVGIPD DKYPWVCQNV DKIFHIGSHV
NNWLPYEGIR EINVDGTRSL LALARTGRKK EFHYTSTSTF SPDKADPSVF LEGDTIDKND
INRFFGYDIS KYASEQMCRI AREEGLICNI YRLVWIGGHI ETGLTKLNDG FNIMLRILIT
IKAFPKGNYL HDITPVDLLA DGMASVQGKA KNTDFNLTSQ SKESIDMKRL AVMLRGMGYQ
IDEVSRTEFV ERLKNYPLEQ WDEHCKSYRQ LVIRLFEDPT PKIESFYDGS NFRKHVDPNL
LVKMEQKFID TWFEKTVNFL VSNNALPTPE GNVYDDEIKT LLTWGQHKGE FTHQQCIHHV
FAQQVQRTPE AIAVRFNQDS LTYQELNERS EQVAQYLRNH AIAPGAVVGL CIERSTHLIV
SILAIFKAGC AYLPLDPNYP AASLDHMIED CAVKHILVAN KSPQALVLHR EKLISLTDVD
FAMYAASELA PGISNTGQQS RPSDLAYVIY TSGTTGKPKG VQVEHRSVVN HSLSMADVFG
LTGQDNVLQF STINFDSFIE EVFPSLFTGA TVVMIEQEKL TQVSELTELI LQQSVNVVKF
STAYWHTVSK VNLQQLGVRL LAIGGEEADI QKYNEWRVIN TDIPLINTYG PTETTVSASY
SVLNGPLDNI TIGRPIANTQ AYILDSNLVP VAIGFVGELY IAGEGVSRGY LNNAELTAQV
FIDNPFSGHS KMYKTGDLVR WDNAGNIEFM GRTDNQVKVR GYRIELGAIE SVLNDYQGIS
QAVVVLKQIE TKKKVVAYVV ANNEAIDIAE LGEHLSQALP SYMLPNLILP LDDIPLNPNG
KVDRGLLEKM EINSEKSINF TSPVTDNEIK MTAIWQDVLA VSSVGLHDDF MELGGHSLLV
MSLISEVNQE FNANVSINDI YESATVAKLL AVVENNDYEQ GSNLVEFPNV HLSKTELTQV
KPLFLVHGLG GHLASFYPLV KNLKQQLHDV YDIDIAVYGL EANGFKAQQQ HFASVDEMVS
EYIKLIKAKQ ASGPYLIGGW SYGVSIAYHI VQALINQGDE VEVFISIDAE APYVPKDFAE
FLRDNDVSGL NDLYQDEKLA ALLKNFGKRF GFISNDKECI KQQFYRFLGY SQDDSQDQVE
RFNKVAIANL LNAKDFNPST INPVNSLLVK ASQSVFDDYV ADWYDLLDSK MISLLTLTGD
HWSIMQEQEL ASNLARVLAV SSQVVINES
//
