ФБТ БИ 2курс / lahneko
.docMama
1e-06
XP_001465109.1
Query 17 GLAVSTVLMVMKAFVGLIGGSQAMLADAMYSLKDMLNALMVIIGTTISSKPL-DAEHPYG 75
G A + V K ++G GGS A++AD +SL D+L ++ + ++S K L P G
Sbjct 57 GGATNVFFCVTKLWIGSAGGSVALVADGFHSLTDILADIISYVAISLSRKKLPRCRFPLG 116
Query 76 HGKVEFILSMVVSVVFIVLTGYLLVHAVQ 104
G++E +++V+ + LLV +++
Sbjct 117 IGRLETSGAVIVAAILFFGGVALLVQSLE 145
Region 63..>153
/region_name="Cation_efflux"
/note="Cation efflux family; pfam01545"
/db_xref="CDD:201849"
Cation efflux family
Members of this family are integral membrane proteins, that are found to increase tolerance to divalent metal ions such as cadmium, zinc, and cobalt. These proteins are thought to be efflux pumps that remove these ions from cells.
Mamb
3e-10
XP_001465109.1
Query 122 ASVTVIVNELMYRYQICVGNENNSPAIIANAWDNRSDAISSAAVMVGVIASVIGFPIADT 181
A+ +V+ EL++R+ VG S ++ANA+ +R+DA S ++GV V+G P D
Sbjct 240 ATASVVCKELLFRWTRRVGLRAGSRVVVANAYHHRADAWSGGVSLLGVAGQVMGLPGVDG 299
Query 182 IAAIGVSALVGRIGLELIGKAVHGLMD 208
+A + VS + +IG + +V D
Sbjct 300 LAGLAVSLSICKIGYGIFKDSVLEFFD 326
Region <228..>344
/region_name="Cation_efflux"
/note="Cation efflux family; cl00316"
/db_xref="CDD:213092"
|
|
|
Mamo
|
|
0.19 |
XP_001463690.1
Query 477 AAAEAGDEMDELMALAEGTTR------PKTSGIALPEGPTRSAVLGLPMGLFSGILGISG 530
AAAE G + +L ALA+ +R S +LP P S +P G LGI G
Sbjct 169 AAAERGLSLTQLKALADRVSRNMRSIGASLSSCSLPGNPASSV---MPSGTVEVGLGIHG 225
Query 531 --GVIEVPLQ 538
G+ ++P Q
Sbjct 226 EKGLFQIPFQ 235
Region 7..329
/region_name="PRK14481"
/note="dihydroxyacetone kinase subunit DhaK; Provisional;
cl10557"
/db_xref="CDD:212308"
|
|
|
Mame
|
|
0.013 |
XP_001463667.1
Query 695 PGATPVAGGGKGA-QVAEVLAGSRAAVAGLQANDLIIEVNNRPVTSPARLDAAIKAATAA 753
PG P A G +GA +V V A AG+ D+++ V NRPV S ++ AA+ A
Sbjct 586 PGVLPGALGRQGAVRVESVTPLQLAERAGVCRGDVLLSVANRPVGSCEQMRAALAVVRAT 645
Query 754 GQQILLKVHRNG-QEFWIV 771
+ L+V+R+ QE +
Sbjct 646 QTPVTLEVYRHTIQEIVFI 664
Region 576..655
/region_name="PDZ_serine_protease"
/note="PDZ domain of tryspin-like serine proteases, such
as DegP/HtrA, which are oligomeric proteins involved in
heat-shock response, chaperone function, and apoptosis.
May be responsible for substrate recognition and/or
binding, as most PDZ domains bind...; cd00987"
/db_xref="CDD:29044"
PDZ domain of tryspin-like serine proteases, such as DegP/HtrA, which are oligomeric proteins involved in heat-shock response, chaperone function, and apoptosis. May be responsible for substrate recognition and/or binding, as most PDZ domains bind C-terminal polypeptides, though binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of protease-associated PDZ domains a C-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in Eumetazoan signaling proteins.
Mamn
0.031
|
XP_001467583.1 |
|
Query 277 CGGSDILFFGGLFVMVGALTSVGILDWAVAWLEGVTAGHDRVRAILLMWMAAGVTIFVGG 336
CG + + L VM+ SVG+ D + ++ + AG D VR
Sbjct 795 CGYFIVHKYDRLRVMLFETASVGVADLDLLSMDALWAGKDNVRE---------------- 838
Query 337 GTSAAVFAPVAATLRLDG 354
GT A F PV +RL+G
Sbjct 839 GTLADRFNPVECNVRLEG 856
Region 342..>456
/region_name="TerD_like"
/note="Uncharacterized proteins involved in stress
response, similar to tellurium resistance terD; cd06974"
/db_xref="CDD:132992"
Uncharacterized proteins involved in stress response, similar to tellurium resistance terD
Tellurium resistance terD like proteins. This family is composed of uncharacterized proteins involved in stress response, such as the tellurium resistance proteins, chemical-damaging agent resistance proteins, and general stress proteins from a variety of organisms. The tellurium resistance proteins are homologous terA,-D,-E,-F,-Z,-X gene products, which confer tellurium resistance mediated by plasmids. Currently, the biochemical mechanism of tellurium resistance remains unknown. The family also contains several ter gene homologues, YceC, YceD, YceE, for which there is no clear evidence for any involvement in the tellurium resistance. A putative cAMP-binding protin CABP1 shows a significant similarity to the terD protein and is also included in this family.
Mamm
1e-06
XP_001465109.1
Query 118 IVLWA----ALVSIGVNVGMYFYSRCVAIETNSPLIKTMAKHHHGDATASGAVALGIIGA 173
++LW A S+ ++ ++R V + S ++ A HH DA + G LG+ G
Sbjct 231 VILWTMVGVATASVVCKELLFRWTRRVGLRAGSRVVVANAYHHRADAWSGGVSLLGVAG- 289
Query 174 HYLNMPWIDPAVALWETIDLLLLGKVVFMDAYRGLMDHTAGEAV 217
+ +P +D L ++ + +G +F D+ D+ E V
Sbjct 290 QVMGLPGVDGLAGLAVSLSICKIGYGIFKDSVLEFFDYQNAEEV 333
Region <228..>344
/region_name="Cation_efflux"
/note="Cation efflux family; cl00316"
/db_xref="CDD:213092"
Cation efflux family
Members of this family are integral membrane proteins, that are found to increase tolerance to divalent metal ions such as cadmium, zinc, and cobalt. These proteins are thought to be efflux pumps that remove these ions from cells.