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Conserved domains on  [gi|17137692|ref|NP_477441|]
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STIP1 homology and U-box containing protein 1 [Drosophila melanogaster]

Protein Classification

tetratricopeptide repeat protein( domain architecture ID 1003384)

tetratricopeptide repeat (TPR) protein may adopt a right-handed helical structure with an amphipathic channel and may function as an interaction scaffold in the formation of multi-protein complexes

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RING-Ubox_CHIP cd16654
U-box domain, a modified RING finger, found in carboxyl terminus of HSP70-interacting protein ...
 213-283 2.86e-47

U-box domain, a modified RING finger, found in carboxyl terminus of HSP70-interacting protein (CHIP) and similar proteins; CHIP, also known as STIP1 homology and U box-containing protein 1 (STUB1), CLL-associated antigen KW-8, or Antigen NY-CO-7, is a multifunctional protein that functions both as a co-chaperone and an E3 ubiquitin-protein ligase. It couples protein folding and proteasome mediated degradation by interacting with heat shock proteins (e.g. HSC70) and ubiquitinating their misfolded client proteins, thereby targeting them for proteasomal degradation. It is also important for cellular differentiation and survival (or apoptosis), as well as susceptibility to stress. It targets a wide range of proteins, such as expanded ataxin-1, ataxin-3, huntingtin, and androgen receptor, which play roles in glucocorticoid response, tau degradation, and both p53 and cAMP signaling. CHIP contains an N-terminal tetratricopeptide repeat (TPR) domain responsible for protein-protein interaction, a highly charged middle coiled-coil (CC), and a C-terminal RING-like U-box domain acting as an ubiquitin ligase.


:

Pssm-ID: 438316 [Multi-domain]  Cd Length: 71  Bit Score: 152.34  E-value: 2.86e-47
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17137692 213 VPDFLCGKISFEILTDPVITPSGITYERKDIEEHLQRVGHFDPVTRVKLTQDQLIPNFSMKEVVDSFIAEN 283
Cdd:cd16654   1 VPDYLCCKISFELMRDPVITPSGITYERKDIEEHLQRVGHFDPITREPLTQDQLIPNLALKEAIEAFLEEN 71
CHIP_TPR_N pfam18391
CHIP N-terminal tetratricopeptide repeat domain; This is N-terminal tetratricopeptide repeat ...
 130-211 4.66e-36

CHIP N-terminal tetratricopeptide repeat domain; This is N-terminal tetratricopeptide repeat (TPR) domain found in C terminus of Hsp70 interacting proteins (CHIP). The TPR domain of CHIP binds directly to EEVD motifs located at the C termini of Hsc/Hsp70 and Hsp90.


:

Pssm-ID: 436460  Cd Length: 83  Bit Score: 123.85  E-value: 4.66e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137692   130 ARKKRWNVMEEKRIQQEIELQSYLNGLIKGDMESRLANLKLNGNVH-DEQLKDKQQEIEQECDDHIKELNNIFSKVDERR 208
Cdd:pfam18391   1 ARKKRWNVQEEKRIKQEIELQSYLNRLIDEDKERQLAELELSEEGSdDEEKEEEIDEIEQECDEYLAELNNLFAQVDERR 80


                  ...
gi 17137692   209 KKR 211
Cdd:pfam18391  81 RKR 83
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
21-111 4.79e-14

Tetratricopeptide (TPR) repeat [General function prediction only];


:

Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 70.04  E-value: 4.79e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137692  21 GNCLFAARKYDDAINCYSKAIIKNPTNATYFTNRALCNLKLKRWELCCQDSRRALDIDGNLLKGHFFLGQGLMEIDNFDE 100
Cdd:COG0457  49 GLAYLRLGRYEEALADYEQALELDPDDAEALNNLGLALQALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDE 128

                        90
                ....*....|.
gi 17137692 101 AIKHLQRAYDL 111
Cdd:COG0457 129 AIEAYERALEL 139
 
Name Accession Description Interval E-value
RING-Ubox_CHIP cd16654
U-box domain, a modified RING finger, found in carboxyl terminus of HSP70-interacting protein ...
 213-283 2.86e-47

U-box domain, a modified RING finger, found in carboxyl terminus of HSP70-interacting protein (CHIP) and similar proteins; CHIP, also known as STIP1 homology and U box-containing protein 1 (STUB1), CLL-associated antigen KW-8, or Antigen NY-CO-7, is a multifunctional protein that functions both as a co-chaperone and an E3 ubiquitin-protein ligase. It couples protein folding and proteasome mediated degradation by interacting with heat shock proteins (e.g. HSC70) and ubiquitinating their misfolded client proteins, thereby targeting them for proteasomal degradation. It is also important for cellular differentiation and survival (or apoptosis), as well as susceptibility to stress. It targets a wide range of proteins, such as expanded ataxin-1, ataxin-3, huntingtin, and androgen receptor, which play roles in glucocorticoid response, tau degradation, and both p53 and cAMP signaling. CHIP contains an N-terminal tetratricopeptide repeat (TPR) domain responsible for protein-protein interaction, a highly charged middle coiled-coil (CC), and a C-terminal RING-like U-box domain acting as an ubiquitin ligase.


Pssm-ID: 438316 [Multi-domain]  Cd Length: 71  Bit Score: 152.34  E-value: 2.86e-47
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17137692 213 VPDFLCGKISFEILTDPVITPSGITYERKDIEEHLQRVGHFDPVTRVKLTQDQLIPNFSMKEVVDSFIAEN 283
Cdd:cd16654   1 VPDYLCCKISFELMRDPVITPSGITYERKDIEEHLQRVGHFDPITREPLTQDQLIPNLALKEAIEAFLEEN 71
U-box pfam04564
U-box domain; The U-box is a domain of ~70 amino acids that is present in proteins from yeast ...
 213-285 7.95e-37

U-box domain; The U-box is a domain of ~70 amino acids that is present in proteins from yeast to human. It consists of the beta-beta-alpha-beta-alpha- fold typical of U-box and RING domains. The central alpha helix is flanked by two prominent surface-exposed loop regions. This domain is one class of E3 ligases, involved in the ubiquitination process. This domain is related to the Ring finger pfam00097 but lacks the zinc binding residues.


Pssm-ID: 398320 [Multi-domain]  Cd Length: 73  Bit Score: 125.89  E-value: 7.95e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17137692   213 VPDFLCGKISFEILTDPVITPSGITYERKDIEEHLQRVGHFDPVTRVKLTQDQLIPNFSMKEVVDSFIAENEW 285
Cdd:pfam04564   1 IPDEFLDPITFELMTDPVILPSGITYDRSTIERHLLSVDPTDPFTREPLTHDQLIPNLELKAKIDAWLEEKRW 73
CHIP_TPR_N pfam18391
CHIP N-terminal tetratricopeptide repeat domain; This is N-terminal tetratricopeptide repeat ...
 130-211 4.66e-36

CHIP N-terminal tetratricopeptide repeat domain; This is N-terminal tetratricopeptide repeat (TPR) domain found in C terminus of Hsp70 interacting proteins (CHIP). The TPR domain of CHIP binds directly to EEVD motifs located at the C termini of Hsc/Hsp70 and Hsp90.


Pssm-ID: 436460  Cd Length: 83  Bit Score: 123.85  E-value: 4.66e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137692   130 ARKKRWNVMEEKRIQQEIELQSYLNGLIKGDMESRLANLKLNGNVH-DEQLKDKQQEIEQECDDHIKELNNIFSKVDERR 208
Cdd:pfam18391   1 ARKKRWNVQEEKRIKQEIELQSYLNRLIDEDKERQLAELELSEEGSdDEEKEEEIDEIEQECDEYLAELNNLFAQVDERR 80


                  ...
gi 17137692   209 KKR 211
Cdd:pfam18391  81 RKR 83
Ubox smart00504
Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2 ...
 215-279 5.31e-23

Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2+-binding ligands. Probable involvement in E2-dependent ubiquitination.


Pssm-ID: 128780 [Multi-domain]  Cd Length: 63  Bit Score: 89.60  E-value: 5.31e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17137692    215 DFLCgKISFEILTDPVITPSGITYERKDIEEHLQRVGhFDPVTRVKLTQDQLIPNFSMKEVVDSF 279
Cdd:smart00504   1 EFLC-PISLEVMKDPVILPSGQTYERSAIEKWLLSHG-TDPVTGQPLTHEDLIPNLALKSAIQEW 63
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
21-111 4.79e-14

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 70.04  E-value: 4.79e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137692  21 GNCLFAARKYDDAINCYSKAIIKNPTNATYFTNRALCNLKLKRWELCCQDSRRALDIDGNLLKGHFFLGQGLMEIDNFDE 100
Cdd:COG0457  49 GLAYLRLGRYEEALADYEQALELDPDDAEALNNLGLALQALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDE 128

                        90
                ....*....|.
gi 17137692 101 AIKHLQRAYDL 111
Cdd:COG0457 129 AIEAYERALEL 139
3a0801s09 TIGR00990
mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) ...
 15-83 6.29e-10

mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) (mitochondrial import receptor for the ADP/ATP carrier) (translocase of outermembrane tom70); [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 273380 [Multi-domain]  Cd Length: 615  Bit Score: 59.61  E-value: 6.29e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17137692    15 LQLKEQGNCLFAARKYDDAINCYSKAIIKNPtNATYFTNRALCNLKLKRWELCCQDSRRALDIDGNLLK 83
Cdd:TIGR00990 128 AKLKEKGNKAYRNKDFNKAIKLYSKAIECKP-DPVYYSNRAACHNALGDWEKVVEDTTAALELDPDYSK 195
UFD2 COG5113
Ubiquitin fusion degradation protein 2 [Posttranslational modification, protein turnover, ...
 194-279 1.30e-07

Ubiquitin fusion degradation protein 2 [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227444 [Multi-domain]  Cd Length: 929  Bit Score: 52.68  E-value: 1.30e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137692 194 IKELNNIFSKVDERR--KKRE------VPDFLCGKISFEILTDPVITP-SGITYERKDIEEHLQRvGHFDPVTRVKLTQD 264
Cdd:COG5113 824 IEELRSFINRLEKVRviEAVEeedmgdVPDEFLDPLMFTIMKDPVKLPtSRITIDRSTIKAHLLS-DGTDPFNRMPLTLD 902

                        90
                ....*....|....*
gi 17137692 265 QLIPNFSMKEVVDSF 279
Cdd:COG5113 903 DVTPNAELREKINRF 917
PLN03088 PLN03088
SGT1, suppressor of G2 allele of SKP1; Provisional
 17-114 8.63e-07

SGT1, suppressor of G2 allele of SKP1; Provisional


Pssm-ID: 215568 [Multi-domain]  Cd Length: 356  Bit Score: 49.79  E-value: 8.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137692   17 LKEQGNCLFAARKYDDAINCYSKAIIKNPTNATYFTNRALCNLKLKRWELCCQDSRRALDIDGNLLKGHFFLGQGLMEID 96
Cdd:PLN03088   5 LEDKAKEAFVDDDFALAVDLYTQAIDLDPNNAELYADRAQANIKLGNFTEAVADANKAIELDPSLAKAYLRKGTACMKLE 84

                         90
                 ....*....|....*...
gi 17137692   97 NFDEAIKHLQRAYDLSKE 114
Cdd:PLN03088  85 EYQTAKAALEKGASLAPG 102
TPR smart00028
Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum ...
 17-47 9.71e-05

Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum of 34 amino acids each and self-associate via a "knobs and holes" mechanism.


Pssm-ID: 197478 [Multi-domain]  Cd Length: 34  Bit Score: 38.97  E-value: 9.71e-05
                           10        20        30
                   ....*....|....*....|....*....|.
gi 17137692     17 LKEQGNCLFAARKYDDAINCYSKAIIKNPTN 47
Cdd:smart00028   4 LYNLGNAYLKLGDYDEALEYYEKALELDPNN 34
TPR_1 pfam00515
Tetratricopeptide repeat;
17-47 1.99e-04

Tetratricopeptide repeat;


Pssm-ID: 459840 [Multi-domain]  Cd Length: 34  Bit Score: 37.79  E-value: 1.99e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 17137692    17 LKEQGNCLFAARKYDDAINCYSKAIIKNPTN 47
Cdd:pfam00515   4 LYNLGNAYFKLGKYDEALEYYEKALELNPNN 34
ACL4-like cd24142
Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 ...
 65-115 5.67e-04

Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 (ACL4) acts as a chaperone for the L4 ribosomal subunit, encoded by RPL4A and RPL4B, and is required for hierarchical ribosome assembly. It is required for the soluble expression of newly synthesized RPL4 and for the protection of RPL4 from the Tom1-dependent cellular degradation machinery. ACL4 shields ribosomal protein L4 until timely release and insertion into the pre-ribosome is possible, once ribosomal protein L18 is present.


Pssm-ID: 467942 [Multi-domain]  Cd Length: 306  Bit Score: 40.69  E-value: 5.67e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 17137692  65 ELCCQDSRRALDIDGNLLKGHFFLGQGLMEIDNFDEAIKHLQRAYDLSKEQ 115
Cdd:cd24142  17 ELALKFLQRALELEPNNVEALELLGEILLELGDVEEAREVLLRAIELDPDG 67
 
Name Accession Description Interval E-value
RING-Ubox_CHIP cd16654
U-box domain, a modified RING finger, found in carboxyl terminus of HSP70-interacting protein ...
 213-283 2.86e-47

U-box domain, a modified RING finger, found in carboxyl terminus of HSP70-interacting protein (CHIP) and similar proteins; CHIP, also known as STIP1 homology and U box-containing protein 1 (STUB1), CLL-associated antigen KW-8, or Antigen NY-CO-7, is a multifunctional protein that functions both as a co-chaperone and an E3 ubiquitin-protein ligase. It couples protein folding and proteasome mediated degradation by interacting with heat shock proteins (e.g. HSC70) and ubiquitinating their misfolded client proteins, thereby targeting them for proteasomal degradation. It is also important for cellular differentiation and survival (or apoptosis), as well as susceptibility to stress. It targets a wide range of proteins, such as expanded ataxin-1, ataxin-3, huntingtin, and androgen receptor, which play roles in glucocorticoid response, tau degradation, and both p53 and cAMP signaling. CHIP contains an N-terminal tetratricopeptide repeat (TPR) domain responsible for protein-protein interaction, a highly charged middle coiled-coil (CC), and a C-terminal RING-like U-box domain acting as an ubiquitin ligase.


Pssm-ID: 438316 [Multi-domain]  Cd Length: 71  Bit Score: 152.34  E-value: 2.86e-47
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17137692 213 VPDFLCGKISFEILTDPVITPSGITYERKDIEEHLQRVGHFDPVTRVKLTQDQLIPNFSMKEVVDSFIAEN 283
Cdd:cd16654   1 VPDYLCCKISFELMRDPVITPSGITYERKDIEEHLQRVGHFDPITREPLTQDQLIPNLALKEAIEAFLEEN 71
U-box pfam04564
U-box domain; The U-box is a domain of ~70 amino acids that is present in proteins from yeast ...
 213-285 7.95e-37

U-box domain; The U-box is a domain of ~70 amino acids that is present in proteins from yeast to human. It consists of the beta-beta-alpha-beta-alpha- fold typical of U-box and RING domains. The central alpha helix is flanked by two prominent surface-exposed loop regions. This domain is one class of E3 ligases, involved in the ubiquitination process. This domain is related to the Ring finger pfam00097 but lacks the zinc binding residues.


Pssm-ID: 398320 [Multi-domain]  Cd Length: 73  Bit Score: 125.89  E-value: 7.95e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17137692   213 VPDFLCGKISFEILTDPVITPSGITYERKDIEEHLQRVGHFDPVTRVKLTQDQLIPNFSMKEVVDSFIAENEW 285
Cdd:pfam04564   1 IPDEFLDPITFELMTDPVILPSGITYDRSTIERHLLSVDPTDPFTREPLTHDQLIPNLELKAKIDAWLEEKRW 73
CHIP_TPR_N pfam18391
CHIP N-terminal tetratricopeptide repeat domain; This is N-terminal tetratricopeptide repeat ...
 130-211 4.66e-36

CHIP N-terminal tetratricopeptide repeat domain; This is N-terminal tetratricopeptide repeat (TPR) domain found in C terminus of Hsp70 interacting proteins (CHIP). The TPR domain of CHIP binds directly to EEVD motifs located at the C termini of Hsc/Hsp70 and Hsp90.


Pssm-ID: 436460  Cd Length: 83  Bit Score: 123.85  E-value: 4.66e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137692   130 ARKKRWNVMEEKRIQQEIELQSYLNGLIKGDMESRLANLKLNGNVH-DEQLKDKQQEIEQECDDHIKELNNIFSKVDERR 208
Cdd:pfam18391   1 ARKKRWNVQEEKRIKQEIELQSYLNRLIDEDKERQLAELELSEEGSdDEEKEEEIDEIEQECDEYLAELNNLFAQVDERR 80


                  ...
gi 17137692   209 KKR 211
Cdd:pfam18391  81 RKR 83
Ubox smart00504
Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2 ...
 215-279 5.31e-23

Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2+-binding ligands. Probable involvement in E2-dependent ubiquitination.


Pssm-ID: 128780 [Multi-domain]  Cd Length: 63  Bit Score: 89.60  E-value: 5.31e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17137692    215 DFLCgKISFEILTDPVITPSGITYERKDIEEHLQRVGhFDPVTRVKLTQDQLIPNFSMKEVVDSF 279
Cdd:smart00504   1 EFLC-PISLEVMKDPVILPSGQTYERSAIEKWLLSHG-TDPVTGQPLTHEDLIPNLALKSAIQEW 63
RING-Ubox cd16453
U-box domain, a modified RING finger; The U-box protein family is a family of E3 enzymes that ...
 216-261 1.27e-15

U-box domain, a modified RING finger; The U-box protein family is a family of E3 enzymes that also includes the HECT family and the RING finger family. The E3 enzyme is ubiquitin-protein ligase that cooperates with a ubiquitin-activating enzyme (E1) and a ubiquitin-conjugating enzyme (E2), and plays a central role in determining the specificity of the ubiquitination system. It removes the ubiquitin molecule from the E2 enzyme and attaches it to the target substrate, forming a covalent bond between ubiquitin and the target. U-box proteins are characterized by the presence of a U-box domain of approximately 70 amino acids. The U-box is a modified form of the RING finger domain that lacks metal chelating cysteines and histidines. It resembles the cross-brace RING structure consisting of three beta-sheets and a single alpha-helix, which would be stabilized by salt bridges instead of chelated metal ions. U-box proteins are widely distributed among eukaryotic organisms and show a higher prevalence in plants than in other organisms.


Pssm-ID: 438117 [Multi-domain]  Cd Length: 44  Bit Score: 69.12  E-value: 1.27e-15
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 17137692 216 FLCgKISFEILTDPVITPSGITYERKDIEEHLQRvGHFDPVTRVKL 261
Cdd:cd16453   1 FLC-PISGELMKDPVITPSGITYDRSAIERWLLS-DNTDPFTREPL 44
RING-Ubox_WDSUB1-like cd16655
U-box domain, a modified RING finger, found in WD repeat, SAM and U-box domain-containing ...
 214-269 6.26e-15

U-box domain, a modified RING finger, found in WD repeat, SAM and U-box domain-containing protein 1 (WDSUB1) and similar proteins; WDSUB1 is an uncharacterized protein containing seven WD40 repeats and a SAM domain in addition to the U-box. Its biological role remains unclear. This subfamily also includes many uncharacterized kinase domain-containing U-box (AtPUB) proteins and several MIF4G motif-containing AtPUB proteins from Arabidopsis.


Pssm-ID: 438317 [Multi-domain]  Cd Length: 55  Bit Score: 67.53  E-value: 6.26e-15
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 17137692 214 PDFLCgKISFEILTDPVITPSGITYERKDIEEHLQRvGHFDPVTRVKLTQDQLIPN 269
Cdd:cd16655   2 DEFLC-PITQELMRDPVVAADGHTYERSAIEEWLET-HNTSPMTRLPLSSTDLVPN 55
RING-Ubox_PUB cd16664
U-box domain, a modified RING finger, found in Arabidopsis plant U-box proteins (AtPUB) and ...
 214-266 1.19e-14

U-box domain, a modified RING finger, found in Arabidopsis plant U-box proteins (AtPUB) and similar proteins; The plant PUB proteins, also known as U-box domain-containing proteins, are much more numerous in Arabidopsis which has 62 in comparison with the typical 6 in most animals. The majority of AtPUBs in this subfamily are known as ARM domain-containing PUB proteins, containing a C-terminally-located, tandem ARM (armadillo) repeat protein-interaction region in addition to the U-box domain. They have been implicated in the regulation of cell death and defense. They also play important roles in other plant-specific pathways, such as controlling both self-incompatibility and pseudo-self-incompatibility, as well as acting in abiotic stress. A subgroup of ARM domain-containing PUB proteins harbors a plant-specific U-box N-terminal domain.


Pssm-ID: 438326 [Multi-domain]  Cd Length: 53  Bit Score: 66.82  E-value: 1.19e-14
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 17137692 214 PDFLCGkISFEILTDPVITPSGITYERKDIEEHLQRVGHFDPVTRVKLTQDQL 266
Cdd:cd16664   2 EEFICP-ISLELMKDPVILATGQTYERAAIEKWLDSGNNTCPITGQPLTHTDL 53
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
21-111 4.79e-14

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 70.04  E-value: 4.79e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137692  21 GNCLFAARKYDDAINCYSKAIIKNPTNATYFTNRALCNLKLKRWELCCQDSRRALDIDGNLLKGHFFLGQGLMEIDNFDE 100
Cdd:COG0457  49 GLAYLRLGRYEEALADYEQALELDPDDAEALNNLGLALQALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDE 128

                        90
                ....*....|.
gi 17137692 101 AIKHLQRAYDL 111
Cdd:COG0457 129 AIEAYERALEL 139
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
21-111 7.45e-14

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 69.65  E-value: 7.45e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137692  21 GNCLFAARKYDDAINCYSKAIIKNPTNATYFTNRALCNLKLKRWELCCQDSRRALDIDGNLLKGHFFLGQGLMEIDNFDE 100
Cdd:COG0457  15 GLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNLGLALQALGRYEE 94

                        90
                ....*....|.
gi 17137692 101 AIKHLQRAYDL 111
Cdd:COG0457  95 ALEDYDKALEL 105
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 21-114 3.52e-13

Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 65.03  E-value: 3.52e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137692  21 GNCLFAARKYDDAINCYSKAIIKNPTNATYFTNRALCNLKLKRWELCCQDSRRALDIDGNLLKGHFFLGQGLMEIDNFDE 100
Cdd:COG4235  24 GRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALALDPDNPEALYLLGLAAFQQGDYAE 103

                        90
                ....*....|....
gi 17137692 101 AIKHLQRAYDLSKE 114
Cdd:COG4235 104 AIAAWQKLLALLPA 117
RING-Ubox_LubX-like_rpt1 cd23149
first U-box domain, a modified RING finger, found in Legionella pneumophila U-box protein LubX ...
 216-269 1.35e-12

first U-box domain, a modified RING finger, found in Legionella pneumophila U-box protein LubX and similar proteins; LubX, also called RING-type E3 ubiquitin transferase LubX, is part of the large arsenal of effectors in Legionella pneumophila that are translocated into the host cytosol during infection. LubX acts as an E3 ubiquitin-protein ligase (EC 2.3.2.27) that interferes with the host's ubiquitination pathway. LubX contains two RING-like U-box domains. U-box 1 is critical to the ubiquitin ligase activity, and U-box 2 mediates interaction with host target. This model corresponds to the first one.


Pssm-ID: 438511 [Multi-domain]  Cd Length: 55  Bit Score: 61.35  E-value: 1.35e-12
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 17137692 216 FLCgKISFEILTDPVITPSGITYERKDIEEHLqRVGHFDPVTRVKLTQDQLIPN 269
Cdd:cd23149   1 FTC-PITSGFMEDPVITPSGFSYERSAIERWL-ETKPEDPQTREPLTAKDLQPN 52
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 21-111 3.23e-12

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 66.56  E-value: 3.23e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137692  21 GNCLFAARKYDDAINCYSKAIIKNPTNATYFTNRALCNLKLKRWEL---CCqdsRRALDIDGNLLKGHFFLGQGLMEIDN 97
Cdd:COG3914 119 GNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLGRLEEaiaAL---RRALELDPDNAEALNNLGNALQDLGR 195

                        90
                ....*....|....
gi 17137692  98 FDEAIKHLQRAYDL 111
Cdd:COG3914 196 LEEAIAAYRRALEL 209
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 12-113 2.37e-11

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 60.74  E-value: 2.37e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137692  12 LSDLQLKEQGNCLFAARKYDDAINCYSKAIIKNPTNATYFTNRALCNLKLKRWELCCQDSRRALDIDGNLLKGHFFLGQG 91
Cdd:COG5010  52 KAFAIESPSDNLYNKLGDFEESLALLEQALQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAAL 131

                        90       100
                ....*....|....*....|..
gi 17137692  92 LMEIDNFDEAIKHLQRAYDLSK 113
Cdd:COG5010 132 LLSLGQDDEAKAALQRALGTSP 153
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
17-114 3.80e-11

Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 61.47  E-value: 3.80e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137692  17 LKEQGNCLFAARKYDDAINCYSKAIIKNPTNATYFTNRALCNLKLKRWELCCQDSRRALDIDGNLLKGHFFLGQGLMEID 96
Cdd:COG4785  76 YYERGVAYDSLGDYDLAIADFDQALELDPDLAEAYNNRGLAYLLLGDYDAALEDFDRALELDPDYAYAYLNRGIALYYLG 155

                        90
                ....*....|....*...
gi 17137692  97 NFDEAIKHLQRAYDLSKE 114
Cdd:COG4785 156 RYELAIADLEKALELDPN 173
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 16-131 2.33e-10

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 57.51  E-value: 2.33e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137692  16 QLKEQGNCLFAARKYDDAINCYSKAIIKNPTNATYFTNRALCNLKLKRWELCCQDSRRALDIDGNLLKGHFFLGQGLMEI 95
Cdd:COG4783   6 ALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLALLKA 85

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 17137692  96 DNFDEAIKHLQRAYDLSKEqkqnfgdDITLQLRLAR 131
Cdd:COG4783  86 GDYDEALALLEKALKLDPE-------HPEAYLRLAR 114
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 24-131 4.11e-10

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 60.01  E-value: 4.11e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137692  24 LFAARKYDDAINCYSKAIIKNPTNATYFTNRALCNLKLKRWELCCQDSRRALDIDGNLLKGHFFLGQGLMEIDNFDEAIK 103
Cdd:COG3914  88 LQALGRYEEALALYRRALALNPDNAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLGRLEEAIA 167

                        90       100
                ....*....|....*....|....*...
gi 17137692 104 HLQRAYDLSKeqkqnfgDDITLQLRLAR 131
Cdd:COG3914 168 ALRRALELDP-------DNAEALNNLGN 188
3a0801s09 TIGR00990
mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) ...
 15-83 6.29e-10

mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) (mitochondrial import receptor for the ADP/ATP carrier) (translocase of outermembrane tom70); [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 273380 [Multi-domain]  Cd Length: 615  Bit Score: 59.61  E-value: 6.29e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17137692    15 LQLKEQGNCLFAARKYDDAINCYSKAIIKNPtNATYFTNRALCNLKLKRWELCCQDSRRALDIDGNLLK 83
Cdd:TIGR00990 128 AKLKEKGNKAYRNKDFNKAIKLYSKAIECKP-DPVYYSNRAACHNALGDWEKVVEDTTAALELDPDYSK 195
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
23-117 1.42e-09

Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 54.02  E-value: 1.42e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137692  23 CLFAARKYDDAINCYSKAIIKNPTNATYFTNRALCNLKLKRWELcCQDSRRALDIDGNLLKGHFFLGQGLMEIDNFDEAI 102
Cdd:COG3063   1 LYLKLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDE-AIALEKALKLDPNNAEALLNLAELLLELGDYDEAL 79

                        90
                ....*....|....*
gi 17137692 103 KHLQRAYDLSKEQKQ 117
Cdd:COG3063  80 AYLERALELDPSALR 94
RING-Ubox_UBE4A cd16657
U-box domain, a modified RING finger, found in ubiquitin conjugation factor E4 A (UBE4A) and ...
 221-283 1.67e-09

U-box domain, a modified RING finger, found in ubiquitin conjugation factor E4 A (UBE4A) and similar proteins; This subfamily includes yeast ubiquitin fusion degradation protein 2 (UFD2p) and its mammalian homolog, UBE4A. Yeast UFD2p, also known as ubiquitin conjugation factor E4 or UB fusion protein 2, is a polyubiquitin chain conjugation factor (E4) in the ubiquitin fusion degradation (UFD) pathway which catalyzes elongation of the ubiquitin chain through Lys48 linkage. It binds to substrates conjugated with one to three ubiquitin molecules and catalyzes the addition of further ubiquitin moieties in the presence of ubiquitin-activating enzyme (E1), ubiquitin-conjugating enzyme (E2) and ubiquitin ligase (E3), yielding multiubiquitylated substrates that are targets for the 26S proteasome. UFD2p is implicated in cell survival under stress conditions and is essential for homoeostasis of unsaturated fatty acids. It interacts with UBL-UBA proteins Rad23 and Dsk2, which are involved in the endoplasmic reticulum-associated degradation, ubiquitin fusion degradation, and OLE-1 gene induction pathways. UBE4A is a U-box-type ubiquitin-protein ligase that is located in common neuroblastoma deletion regions and may be subject to mutations in tumors. It may have a specific role in different biochemical processes other than ubiquitination, including growth or differentiation. Members of this family contain an N-terminal ubiquitin elongating factor core and a RING-like U-box domain at the C-terminus.


Pssm-ID: 438319  Cd Length: 70  Bit Score: 53.05  E-value: 1.67e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17137692 221 ISFEILTDPVITP-SGITYERKDIEEHLQRVGHfDPVTRVKLTQDQLIPNFSMKEVVDSFIAEN 283
Cdd:cd16657   7 IMYTLMKDPVILPsSKVTVDRSTIKRHLLSDQT-DPFNRSPLTLDMVIPNEELKQKIEEFLAEK 69
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 21-132 1.07e-08

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 55.77  E-value: 1.07e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137692  21 GNCLFAARKYDDAINCYSKAIIKNPTNATYFTNRALCNLKLKRWELCCQDSRRALDIDGNLLKGHFFLGQGLM---EIDN 97
Cdd:COG3914 153 GEALRRLGRLEEAIAALRRALELDPDNAEALNNLGNALQDLGRLEEAIAAYRRALELDPDNADAHSNLLFALRqacDWEV 232

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 17137692  98 FDEAIKHLQrAYDLSKEQKQNF------GDDITLQLRLARK 132
Cdd:COG3914 233 YDRFEELLA-ALARGPSELSPFallylpDDDPAELLALARA 272
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 21-115 1.75e-08

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 52.12  E-value: 1.75e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137692  21 GNCLFAARKYDDAINCYSKAIIKNPTNATYFTNRALCNLKLKRWELCCQDSRRALDIDGNLLKGHFFLGQGLMEIDNFDE 100
Cdd:COG4783  45 GEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALGRPDE 124

                        90
                ....*....|....*
gi 17137692 101 AIKHLQRAYDLSKEQ 115
Cdd:COG4783 125 AIAALEKALELDPDD 139
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 19-114 8.99e-08

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 52.04  E-value: 8.99e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137692  19 EQGNCLFAARKYDDAINCYSKAIIKNPTNATYFTNRALCNLKLKRWELCCQDSRRALDIDGNLLKGHFFLGQGLMEIDNF 98
Cdd:COG2956  81 ELAQDYLKAGLLDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDY 160

                        90
                ....*....|....*.
gi 17137692  99 DEAIKHLQRAYDLSKE 114
Cdd:COG2956 161 DEAIEALEKALKLDPD 176
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 19-145 1.05e-07

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 52.04  E-value: 1.05e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137692  19 EQGNCLFAARKYDDAINCYSKAIIKNPTNATYFTNRALCNLKLKRWELCCQDSRRALDIDGNLLKGHFFLGQGLMEIDNF 98
Cdd:COG2956 149 ELAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAELYLEQGDYEEAIAALERALEQDPDYLPALPRLAELYEKLGDP 228

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 17137692  99 DEAIKHLQRAYdlskEQKQNFGDDITLQLRLARKKRWNVMEEKRIQQ 145
Cdd:COG2956 229 EEALELLRKAL----ELDPSDDLLLALADLLERKEGLEAALALLERQ 271
RING-Ubox_PRP19 cd16656
U-box domain, a modified RING finger, found in pre-mRNA-processing factor 19 (Prp19) and ...
 216-268 1.20e-07

U-box domain, a modified RING finger, found in pre-mRNA-processing factor 19 (Prp19) and similar proteins; Prp19, also known as nuclear matrix protein 200 (NMP200), senescence evasion factor (SNEV), or DNA repair protein Pso4 (psoralen-sensitive mutant 4), is a ubiquitously expressed multifunctional E3 ubiquitin ligase with pleiotropic activities in DNA damage signaling, repair, and replicative senescence. It functions as a critical component of DNA repair and DNA damage checkpoint complexes. It senses DNA damage, binds double-stranded DNA in a sequence-independent manner, facilitates processing of damaged DNA, promotes DNA end joining, regulates replication protein A (RPA2) phosphorylation and ubiquitination at damaged DNA, and regulates RNA splicing and mitotic spindle formation in its integral capacity as a scaffold for a multimeric core complex. Prp19 contains an N-terminal E3 ubiquitin ligase U-box domain with E2 recruitment function that facilitates dimerization and is essential for its auto-ubiquitination activity in vitro or when overexpressed, a coiled-coil Prp19 homology region that mediates its tetramerization and interaction with CDC5L and SPF27, and a C-terminal seven-bladed WD40 beta-propeller type of leucine-rich architectural repeats that form an asymmetrical barrel-shaped structure important for substrate recognition and recruitment.


Pssm-ID: 438318  Cd Length: 54  Bit Score: 47.56  E-value: 1.20e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 17137692 216 FLCGkISFEILTDPVITP-SGITYERKDIEEHLQRVGHfDPVTRVKLTQDQLIP 268
Cdd:cd16656   1 MVCA-ISGEVPEEPVVSPkSGHVFEKRLIEKYIAENGT-DPVTGEPLTEEDLIE 52
UFD2 COG5113
Ubiquitin fusion degradation protein 2 [Posttranslational modification, protein turnover, ...
 194-279 1.30e-07

Ubiquitin fusion degradation protein 2 [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227444 [Multi-domain]  Cd Length: 929  Bit Score: 52.68  E-value: 1.30e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137692 194 IKELNNIFSKVDERR--KKRE------VPDFLCGKISFEILTDPVITP-SGITYERKDIEEHLQRvGHFDPVTRVKLTQD 264
Cdd:COG5113 824 IEELRSFINRLEKVRviEAVEeedmgdVPDEFLDPLMFTIMKDPVKLPtSRITIDRSTIKAHLLS-DGTDPFNRMPLTLD 902

                        90
                ....*....|....*
gi 17137692 265 QLIPNFSMKEVVDSF 279
Cdd:COG5113 903 DVTPNAELREKINRF 917
RING-Ubox_UBE4B cd16658
U-box domain, a modified RING finger, found in ubiquitin conjugation factor E4 B (UBE4B) and ...
 225-284 1.33e-07

U-box domain, a modified RING finger, found in ubiquitin conjugation factor E4 B (UBE4B) and similar proteins; UBE4B, also known as UFD2a, is a U-box-type ubiquitin-protein ligase that functions as an E3 ubiquitin ligase and an E4 polyubiquitin chain elongation factor, which catalyzes formation of Lys27- and Lys33-linked polyubiquitin chains rather than the Lys48-linked chain. It is a mammalian homolog of yeast UFD2 ubiquitination factor and it participates in the proteasomal degradation of misfolded or damaged proteins through association with chaperones. It is located in common neuroblastoma deletion regions and may be subject to mutations in tumors. UBE4B has contradictory functions upon tumorigenesis as an oncogene or tumor suppressor in different types of cancers. It is essential for Hdm2 (also known as Mdm2)-mediated p53 degradation. It mediates p53 polyubiquitination and degradation, as well as inhibits p53-dependent transactivation and apoptosis, and thus plays an important role in regulating phosphorylated p53 following DNA damage. UBE4B is also associated with other pathways independent of the p53 family, such as polyglutamine aggregation and Wallerian degeneration, both of which are critical in neurodegenerative diseases. Moreover, UBE4B acts as a regulator of epidermal growth factor receptor (EGFR) degradation. It is recruited to endosomes in response to EGFR activation by binding to Hrs, a key component of endosomal sorting complex required for transport (ESCRT) 0, and then regulates endosomal sorting, affecting cellular levels of the EGFR and its downstream signaling. UBE4B contains a ubiquitin elongating factor core and a RING-like U-box domain at the C-terminus.


Pssm-ID: 438320  Cd Length: 74  Bit Score: 48.04  E-value: 1.33e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137692 225 ILTDPVITPSGITYERKDIEEHLQRVGHfDPVTRVKLTQDQLIPNFSMKEVVDSFIAENE 284
Cdd:cd16658  16 LMTDPVILPSGTIMDRSIILRHLLNSQT-DPFNRQPLTEDMLEPVPELKERIQAWIREKQ 74
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 17-114 1.83e-07

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 51.27  E-value: 1.83e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137692  17 LKEQGNCLFAARKYDDAINCYSKAIIKNPTNATYFTNRALCNLKLKRWELCCQDSRRALDIDGNLLKGHFFLGQGLMEID 96
Cdd:COG2956 113 LRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAELYLEQG 192

                        90
                ....*....|....*...
gi 17137692  97 NFDEAIKHLQRAYDLSKE 114
Cdd:COG2956 193 DYEEAIAALERALEQDPD 210
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
44-111 3.82e-07

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 50.01  E-value: 3.82e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17137692  44 NPTNATYFTNRALCNLKLKRWELCCQDSRRALDIDGNLLKGHFFLGQGLMEIDNFDEAIKHLQRAYDL 111
Cdd:COG0457   4 DPDDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALEL 71
PLN03088 PLN03088
SGT1, suppressor of G2 allele of SKP1; Provisional
 17-114 8.63e-07

SGT1, suppressor of G2 allele of SKP1; Provisional


Pssm-ID: 215568 [Multi-domain]  Cd Length: 356  Bit Score: 49.79  E-value: 8.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137692   17 LKEQGNCLFAARKYDDAINCYSKAIIKNPTNATYFTNRALCNLKLKRWELCCQDSRRALDIDGNLLKGHFFLGQGLMEID 96
Cdd:PLN03088   5 LEDKAKEAFVDDDFALAVDLYTQAIDLDPNNAELYADRAQANIKLGNFTEAVADANKAIELDPSLAKAYLRKGTACMKLE 84

                         90
                 ....*....|....*...
gi 17137692   97 NFDEAIKHLQRAYDLSKE 114
Cdd:PLN03088  85 EYQTAKAALEKGASLAPG 102
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 32-111 2.55e-06

Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 45.77  E-value: 2.55e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137692  32 DAINCYSKAIIKNPTNATYFTNRALCNLKLKRWELCCQDSRRALDIDGNLLKGHFFLGQGLMEIDNFDEAIKHLQRAYDL 111
Cdd:COG4235   1 EAIARLRQALAANPNDAEGWLLLGRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALAL 80
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
21-109 2.93e-06

Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 47.22  E-value: 2.93e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137692  21 GNCLFAARKYDDAINCYSKAIIKNPTNATYFTNRALCNLKLKRWELCCQDSRRALDIDGNLLKGHFFLGQGLMEIDnFDE 100
Cdd:COG4785 114 GLAYLLLGDYDAALEDFDRALELDPDYAYAYLNRGIALYYLGRYELAIADLEKALELDPNDPERALWLYLAERKLD-PEK 192


                ....*....
gi 17137692 101 AIKHLQRAY 109
Cdd:COG4785 193 ALALLLEDW 201
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
17-112 6.72e-06

Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 46.06  E-value: 6.72e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137692  17 LKEQGNCLFAARKYDDAINCYSKAIIKNPTNATYFTNRALCNLKLKRWELCCQDSRRALDIDGNLLKGHFFLGQGLMEID 96
Cdd:COG4785  42 ADLALALAAAALAAAALAAERIDRALALPDLAQLYYERGVAYDSLGDYDLAIADFDQALELDPDLAEAYNNRGLAYLLLG 121

                        90
                ....*....|....*.
gi 17137692  97 NFDEAIKHLQRAYDLS 112
Cdd:COG4785 122 DYDAALEDFDRALELD 137
RING-Ubox_LubX-like_rpt2 cd23150
second U-box domain, a modified RING finger, found in Legionella pneumophila U-box protein ...
 216-282 7.39e-06

second U-box domain, a modified RING finger, found in Legionella pneumophila U-box protein LubX and similar proteins; LubX, also called RING-type E3 ubiquitin transferase LubX, is part of the large arsenal of effectors in Legionella pneumophila that are translocated into the host cytosol during infection. LubX acts as an E3 ubiquitin-protein ligase (EC 2.3.2.27) that interferes with the host's ubiquitination pathway. LubX contains two RING-like U-box domains. U-box 1 is critical to the ubiquitin ligase activity, and U-box 2 mediates interaction with host target. This model corresponds to the second one.


Pssm-ID: 438512 [Multi-domain]  Cd Length: 69  Bit Score: 43.22  E-value: 7.39e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17137692 216 FLCgKISFEILTDPVITPSGITYERKDIEEHLQRVGHfDPVTRVKLTQDQLIPNFSMKEVVDSFIAE 282
Cdd:cd23150   4 FLC-PISKTLIKTPVITAQGKVYDQEALSNFLIATGN-KDETGKKLSIDDVVVFDELYQQIKVYNFY 68
TPR smart00028
Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum ...
 17-47 9.71e-05

Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum of 34 amino acids each and self-associate via a "knobs and holes" mechanism.


Pssm-ID: 197478 [Multi-domain]  Cd Length: 34  Bit Score: 38.97  E-value: 9.71e-05
                           10        20        30
                   ....*....|....*....|....*....|.
gi 17137692     17 LKEQGNCLFAARKYDDAINCYSKAIIKNPTN 47
Cdd:smart00028   4 LYNLGNAYLKLGDYDEALEYYEKALELDPNN 34
TPR_1 pfam00515
Tetratricopeptide repeat;
17-47 1.99e-04

Tetratricopeptide repeat;


Pssm-ID: 459840 [Multi-domain]  Cd Length: 34  Bit Score: 37.79  E-value: 1.99e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 17137692    17 LKEQGNCLFAARKYDDAINCYSKAIIKNPTN 47
Cdd:pfam00515   4 LYNLGNAYFKLGKYDEALEYYEKALELNPNN 34
TPR_11 pfam13414
TPR repeat;
21-61 2.14e-04

TPR repeat;


Pssm-ID: 315977 [Multi-domain]  Cd Length: 42  Bit Score: 38.22  E-value: 2.14e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 17137692    21 GNCLFAARKYDDAINCYSKAIIKNPTNATYFTNRALCNLKL 61
Cdd:pfam13414   1 GDAYYEQGKYEEAIEAYKKALKLDPDNPEAYYNLGLAYYKL 41
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
21-83 2.38e-04

Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 39.38  E-value: 2.38e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17137692  21 GNCLFAARKYDDAINcYSKAIIKNPTNATYFTNRALCNLKLKRWELCCQDSRRALDIDGNLLK 83
Cdd:COG3063  33 GLLLLEQGRYDEAIA-LEKALKLDPNNAEALLNLAELLLELGDYDEALAYLERALELDPSALR 94
LcrH_SycD TIGR02552
type III secretion low calcium response chaperone LcrH/SycD; Genes in this family are found in ...
 24-114 3.78e-04

type III secretion low calcium response chaperone LcrH/SycD; Genes in this family are found in type III secretion operons. LcrH, from Yersinia is believed to have a regulatory function in the low-calcium response of the secretion system. The same protein is also known as SycD (SYC = Specific Yop Chaperone) for its chaperone role. In Pseudomonas, where the homolog is known as PcrH, the chaperone role has been demonstrated and the regulatory role appears to be absent. ScyD/LcrH contains three central tetratricopeptide-like repeats that are predicted to fold into an all-alpha-helical array.


Pssm-ID: 274197 [Multi-domain]  Cd Length: 135  Bit Score: 39.58  E-value: 3.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137692    24 LFAARKYDDAINCYSKAIIKNPTNATYFTNRALCNLKLKRWELCCQDSRRALDIDGNLLKGHFFLGQGLMEIDNFDEAIK 103
Cdd:TIGR02552  27 LYQQGRYDEALKLFQLLAAYDPYNSRYWLGLAACCQMLKEYEEAIDAYALAAALDPDDPRPYFHAAECLLALGEPESALK 106

                          90
                  ....*....|.
gi 17137692   104 HLQRAYDLSKE 114
Cdd:TIGR02552 107 ALDLAIEICGE 117
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 72-131 4.05e-04

Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 39.60  E-value: 4.05e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137692  72 RRALDIDGNLLKGHFFLGQGLMEIDNFDEAIKHLQRAYDLSkeqkqnfGDDITLQLRLAR 131
Cdd:COG4235   7 RQALAANPNDAEGWLLLGRAYLRLGRYDEALAAYEKALRLD-------PDNADALLDLAE 59
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 20-108 5.25e-04

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 41.61  E-value: 5.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137692    20 QGNCLFAARKYDDAINCYSKAIIKNPTNATYFTNRALCNLKLKRWELCCQDSRRALDIDGNLLKGHFFLGQGLMEIDNFD 99
Cdd:TIGR02917 199 KGDLLLSLGNIELALAAYRKAIALRPNNIAVLLALATILIEAGEFEEAEKHADALLKKAPNSPLAHYLKALVDFQKKNYE 278


                  ....*....
gi 17137692   100 EAIKHLQRA 108
Cdd:TIGR02917 279 DARETLQDA 287
ACL4-like cd24142
Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 ...
 65-115 5.67e-04

Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 (ACL4) acts as a chaperone for the L4 ribosomal subunit, encoded by RPL4A and RPL4B, and is required for hierarchical ribosome assembly. It is required for the soluble expression of newly synthesized RPL4 and for the protection of RPL4 from the Tom1-dependent cellular degradation machinery. ACL4 shields ribosomal protein L4 until timely release and insertion into the pre-ribosome is possible, once ribosomal protein L18 is present.


Pssm-ID: 467942 [Multi-domain]  Cd Length: 306  Bit Score: 40.69  E-value: 5.67e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 17137692  65 ELCCQDSRRALDIDGNLLKGHFFLGQGLMEIDNFDEAIKHLQRAYDLSKEQ 115
Cdd:cd24142  17 ELALKFLQRALELEPNNVEALELLGEILLELGDVEEAREVLLRAIELDPDG 67
SPL-RING_NSE2 cd16651
SPL-RING finger found in E3 SUMO-protein ligase NSE2 and similar proteins; NSE2, also known as ...
 216-277 9.60e-04

SPL-RING finger found in E3 SUMO-protein ligase NSE2 and similar proteins; NSE2, also known as MMS21 homolog (MMS21) or non-structural maintenance of chromosomes element 2 homolog (Non-SMC element 2 homolog, NSMCE2), is an autosumoylating small ubiquitin-like modifier (SUMO) ligase required for the response to DNA damage. It regulates sumoylation and nuclear-to-cytoplasmic translocation of skeletal and heart muscle-specific variant of the alpha subunit of nascent polypeptide associated complex (skNAC)-Smyd1 in myogenesis. It is also required for resisting extrinsically induced genotoxic stress. Moreover, NSE2 together with its partner proteins SMC6 and SMC5 form a tight subcomplex of the structural maintenance of chromosomes SMC5-6 complex, which includes another two subcomplexes, NSE1-NSE3-NSE4 and NSE5-NSE6. SMC6 and NSE3 are sumoylated in an NSE2-dependent manner, but SMC5 and NSE1 are not. NSE2-dependent E3 SUMO ligase activity is required for efficient DNA repair, but not for SMC5-6 complex stability. NSE2 contains a RING variant known as a Siz/PIAS (protein inhibitor of activated signal transducer and activator of transcription)-like RING (SPL-RING) finger that is likely shared by the SP-RING type SUMO E3 ligases, such as PIAS family proteins. The SPL-RING finger is a variant of the RING finger, which lacks the second, fifth, and sixth zinc-binding residues of the consensus C3H2C3-/C3HC4-type RING fingers. It harbors only one Zn binding site and is required for the sumoylating activity.


Pssm-ID: 438313 [Multi-domain]  Cd Length: 67  Bit Score: 36.86  E-value: 9.60e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17137692 216 FLCgKISFEILTDPVI-TPSGITYERKDIEEHLQRVGHFD--PVT--RVKLTQDQLIPNFSMKEVVD 277
Cdd:cd16651   1 LKC-PITQQLMVDPVRnKKCGHTYEKAAILQYLQSRKKKAkcPVAgcRNTVSKSDLVPDPELKRRIE 66
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 24-110 1.11e-03

Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane constriction [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 441335 [Multi-domain]  Cd Length: 113  Bit Score: 38.05  E-value: 1.11e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137692  24 LFAARKYDDAINCYSKAIIKNPT-----NATYFtnRALCNLKLKRWELCCQDSRRALDIDGN---LLKGHFFLGQGLMEI 95
Cdd:COG1729   3 LLKAGDYDEAIAAFKAFLKRYPNsplapDALYW--LGEAYYALGDYDEAAEAFEKLLKRYPDspkAPDALLKLGLSYLEL 80

                        90
                ....*....|....*
gi 17137692  96 DNFDEAIKHLQRAYD 110
Cdd:COG1729  81 GDYDKARATLEELIK 95
COG4700 COG4700
Uncharacterized conserved protein ECs_4300, contains TPR-like domain [Function unknown];
21-108 2.09e-03

Uncharacterized conserved protein ECs_4300, contains TPR-like domain [Function unknown];


Pssm-ID: 443735 [Multi-domain]  Cd Length: 249  Bit Score: 38.71  E-value: 2.09e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137692  21 GNCLFAARKYDDAINCYSKAIIKN-PTNATYFTNRALCNLKLKRWELCCQ--DSRRALDIDGNLLKGHFFLGQGLMEIDN 97
Cdd:COG4700  96 ADALLELGRYDEAIELYEEALTGIfADDPHILLGLAQALFELGRYAEALEtlEKLIAKNPDFKSSDAHLLYARALEALGD 175

                        90
                ....*....|.
gi 17137692  98 FDEAIKHLQRA 108
Cdd:COG4700 176 LEAAEAELEAL 186
TPR_2 pfam07719
Tetratricopeptide repeat; This Pfam entry includes outlying Tetratricopeptide-like repeats ...
 17-46 2.51e-03

Tetratricopeptide repeat; This Pfam entry includes outlying Tetratricopeptide-like repeats (TPR) that are not matched by pfam00515.


Pssm-ID: 429619 [Multi-domain]  Cd Length: 33  Bit Score: 34.81  E-value: 2.51e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 17137692    17 LKEQGNCLFAARKYDDAINCYSKAIIKNPT 46
Cdd:pfam07719   4 LYNLGLAYYKLGDYEEALEAYEKALELDPN 33
TPR_12 pfam13424
Tetratricopeptide repeat;
48-114 2.60e-03

Tetratricopeptide repeat;


Pssm-ID: 315987 [Multi-domain]  Cd Length: 77  Bit Score: 35.83  E-value: 2.60e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17137692    48 ATYFTNRALCNLKLKRWELCCQDSRRALDIDGNLLKGH--------FFLGQGLMEIDNFDEAIKHLQRAYDLSKE 114
Cdd:pfam13424   3 ATALNNLAAVLRRLGRYDEALELLEKALEIARRLLGPDhpltattlLNLGRLYLELGRYEEALELLERALALAEK 77
RING-Ubox_PPIL2 cd16663
U-box domain, a modified RING finger, found in peptidyl-prolyl cis-trans isomerase-like 2 ...
 216-271 2.64e-03

U-box domain, a modified RING finger, found in peptidyl-prolyl cis-trans isomerase-like 2 (PPIL2) and similar proteins; PPIL2 (EC 5.2.1.8), also known as PPIase, CYC4, cyclophilin-60 (Cyp60), cyclophilin-like protein Cyp-60, or Rotamase PPIL2, is a nuclear-specific cyclophilin which interacts with the proteinase inhibitor eglin c and regulates gene expression. PPIL2 belongs to the cyclophilin family of peptidylprolyl isomerases and catalyzes cis-trans isomerization of proline-peptide bonds, which is often a rate-limiting step in protein folding. It positively regulates beta-site amyloid precursor protein cleaving enzyme (BACE1) expression and beta-secretase activity. Moreover, PPIL2 plays an important role in the translocation of CD147 to the cell surface, and thus may present a novel target for therapeutic interventions in diseases where CD147 functions as a pathogenic factor in cancer, human immunodeficiency virus infection, or rheumatoid arthritis. PPIL2 contains an N-terminal RING-like U-box domain and a C-terminal cyclophilin (Cyp)-like chaperone domain.


Pssm-ID: 438325  Cd Length: 73  Bit Score: 36.00  E-value: 2.64e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 17137692 216 FLCGKISFEILTDPVITPSGITYERKDIEEHLQRVGHfDPVTRVKLTQDQLIP-NFS 271
Cdd:cd16663   2 FDCCALSLQPFENPVCTPDGIVFDLLNIVPYLKKYGK-NPVTGEPLEAKDLIKlNFH 57
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 19-136 4.44e-03

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 37.79  E-value: 4.44e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137692  19 EQGNCLFAARKYDDAINCYSKAIIKNPTNATYFTNRALCNLKLKRWELCCQDSRRALDIDGNLLKGHFFLGQGLMEIDNF 98
Cdd:COG2956  13 FKGLNYLLNGQPDKAIDLLEEALELDPETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQDYLKAGLL 92

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 17137692  99 DEAIKHLQRAYDLSkeqkqnfGDDITLQLRLA----RKKRWN 136
Cdd:COG2956  93 DRAEELLEKLLELD-------PDDAEALRLLAeiyeQEGDWE 127
zf-NOSIP pfam15906
Zinc-finger of nitric oxide synthase-interacting protein;
210-247 5.17e-03

Zinc-finger of nitric oxide synthase-interacting protein;


Pssm-ID: 318178  Cd Length: 75  Bit Score: 35.00  E-value: 5.17e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 17137692   210 KREVPDFLCGKISFEILTDPVITPSGITYERKDIEEHL 247
Cdd:pfam15906  34 KDAIKDFDCCCLSLQACHDPVLTEDGYLYEKEAILEYI 71
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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