Domain of unknown function (DUF4430); Although this family has overlaps with SLBB, the majority of its sequences are unique. Several family members, eg UniProtKB:A0RGA8, that do not overlap have an LPXTG-cell wall anchor at their C-terminus, a SSF_Family 10_polysaccharide_lyase or Glycosyltransferase structure associated with them in the middle region, as shown by InterPro, as well as this domain at the N-terminus.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1313375687  93 GTSVLEALKQVAGVRVESLGERN-FVISVDGE-----DGYYI-YEVNGKLPDISMDKFRLKEDTVV 151
Cdd:pfam14478   1 GDTVLDVLKANLKVKEIKGSYDGgFITSINGLeqdtgKNSYWmYSVNGKMPNVGAGDYKLKNGDKI 66

DNA-binding transcriptional regulator, ArsR family [Transcription];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375687   2 ATIEDLFSVMKSSTRRDILKLLMKEDMHISGIARAMKISVPQASKHIKILEEKNLVEKKIFGRTHVLRAKTENIYKILDG 81
Cdd:COG0640     8 EELAELFKALADPTRLRILRLLAEGELCVGELAEALGLSQSTVSHHLKVLREAGLVTSRREGRWVYYRLADEALAELLEW 87

                  ...
gi 1313375687  82 FSE 84
Cdd:COG0640    88 LLE 90

helix_turn_helix, Arsenical Resistance Operon Repressor;

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1313375687   18 DILKLLMKEDMHISGIARAMKISVPQASKHIKILEEKNLVEKKIFGRTHVLRAKTENIYKILDGF 82
Cdd:smart00418   1 KILKLLAEGELCVCELAEILGLSQSTVSHHLKKLREAGLVESRREGKRVYYSLTDEKVADLLEEL 65

Domain of unknown function (DUF4430); Although this family has overlaps with SLBB, the majority of its sequences are unique. Several family members, eg UniProtKB:A0RGA8, that do not overlap have an LPXTG-cell wall anchor at their C-terminus, a SSF_Family 10_polysaccharide_lyase or Glycosyltransferase structure associated with them in the middle region, as shown by InterPro, as well as this domain at the N-terminus.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1313375687  93 GTSVLEALKQVAGVRVESLGERN-FVISVDGE-----DGYYI-YEVNGKLPDISMDKFRLKEDTVV 151
Cdd:pfam14478   1 GDTVLDVLKANLKVKEIKGSYDGgFITSINGLeqdtgKNSYWmYSVNGKMPNVGAGDYKLKNGDKI 66

DNA-binding transcriptional regulator, ArsR family [Transcription];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375687   2 ATIEDLFSVMKSSTRRDILKLLMKEDMHISGIARAMKISVPQASKHIKILEEKNLVEKKIFGRTHVLRAKTENIYKILDG 81
Cdd:COG0640     8 EELAELFKALADPTRLRILRLLAEGELCVGELAEALGLSQSTVSHHLKVLREAGLVTSRREGRWVYYRLADEALAELLEW 87

                  ...
gi 1313375687  82 FSE 84
Cdd:COG0640    88 LLE 90

metalloregulator ArsR/SmtB family transcription factor; Transcriptional repressors that sense toxic heavy metals such as arsenic or cadmium, and are released from DNA so that resistance factors will be expressed, include ArsR, SmtB, ZiaR, CadC, CadX, KmtR, etc. However, some members of this family, including the sporulation delaying system autorepressor SdpR and its family (see NF033789), may lack metal-binding cites and instead regulate other cellular processes.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1313375687   6 DLFSVMKSSTRRDILKLLMKEDMHISGIARAMKISVPQASKHIKILEEKNLVEKKIFGRTHVLRAKTENIYKIL 79
Cdd:NF033788    3 ELFKALADPTRLRILELLAEGELCVCELAEALGLSQSAVSQHLKVLRDAGLVTSRREGRWVYYRLADEHVAELL 76

Helix-turn-helix domain; This domain represents a DNA-binding Helix-turn-helix domain found in transcriptional regulatory proteins.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1313375687   5 EDLFSVMKSSTRRDILKLLMKED-MHISGIARAMKISVPQASKHIKILEEKNLVE 58
Cdd:pfam12840   1 DDVAEALADPTRLRILRALVGDEpLTASELARRLDISRNTLSYHLRKLEEAGLVE 55

Bacterial regulatory protein, arsR family; Members of this family contains a DNA binding 'helix-turn-helix' motif. This family includes other proteins which are not included in the Prosite definition.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1313375687  13 SSTRRDILKLLMKEDMHISGIARAMKISVPQASKHIKILEEKNLV 57
Cdd:pfam01022   1 DPTRLKILKLLAEGELCVCELAEELGLSQSTVSHHLKKLREAGLV 45

Predicted transcriptional regulator, contains HTH domain [Transcription];

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1313375687   4 IEDLFSVMKSSTRRDILKLLMKEDMHISGIARAMKISVPQASKHIKILEEKNLVEK 59
Cdd:COG4742     6 LDLLDFLFLSEKRKNILLLLAEGPKTRSELAESLDVSRSTILRQLKELEERGLIER 61

Predicted transcriptional regulator [Transcription];

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1313375687  18 DILKLLMKEDMHISGIARAMKISVPQASKHIKILEEKNLVEKKIFGRTHVLR 69
Cdd:COG3432    12 DILEALKNEGAKKTRIMYKANLSYDRLKKYLDLLEEKGLIEKEDDGGRRIYR 63

TBC1 domain family member 2A pleckstrin homology (PH) domain; TBC1D2A (also called PARIS-1/Prostate antigen recognized and identified by SEREX 1 and ARMUS) contains a PH domain and a TBC-type GTPase catalytic domain. TBC1D2A integrates signaling between Arf6, Rac1, and Rab7 during junction disassembly. Activated Rac1 recruits TBC1D2A to locally inactivate Rab7 via its C-terminal TBC/RabGAP domain and facilitate E-cadherin degradation in lysosomes. The TBC1D2A PH domain mediates localization at cell-cell contacts and coprecipitates with cadherin complexes. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.

                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1313375687  38 KISVPQASKHIKILEEKNLVEKKIFGRTHVLRAKTE 73
Cdd:cd01265    47 SIDLSGAAFSYDPEAEPGQFEIHTPGRVHILKASTR 82

MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a non-specific resistance system. The expression of the mar operon is controlled by a repressor, MarR. A large number of compounds induce transcription of the mar operon. This is thought to be due to the compound binding to MarR, and the resulting complex stops MarR binding to the DNA. With the MarR repression lost, transcription of the operon proceeds. The structure of MarR is known and shows MarR as a dimer with each subunit containing a winged-helix DNA binding motif.

                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1313375687  22 LLMKEDMHISGIARAMKISVPQASKHIKILEEKNLVEKK 60
Cdd:pfam12802  14 LARNPGLTVAELARRLGISKQTVSRLVKRLEAKGLVERE 52