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Conserved domains on  [gi|74760704|sp|Q96AG4|]
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RecName: Full=Leucine-rich repeat-containing protein 59; AltName: Full=Ribosome-binding protein p34; Short=p34; Contains: RecName: Full=Leucine-rich repeat-containing protein 59, N-terminally processed

Protein Classification

leucine-rich repeat domain-containing protein( domain architecture ID 11469232)

leucine-rich repeat (LRR) domain-containing protein may participate in protein-protein interactions

Gene Ontology:  GO:0005515
PubMed:  11751054|7583641|14747988
SCOP:  4003523

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
19-120 6.10e-26

Leucine-rich repeat (LRR) protein [Transcription];


:

Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 106.17  E-value: 6.10e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74760704  19 ELDLSLSDLNEVPvKELAALPKATILDLSCNKLTTLPSDFCGLTHLVKLDLSKNKLQQLPADFGRLVNLQHLDLLNNKLV 98
Cdd:COG4886 117 SLDLSGNQLTDLP-EELANLTNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQIT 195

                        90       100
                ....*....|....*....|..
gi 74760704  99 TLPVSFAQLKNLKWLDLKDNPL 120
Cdd:COG4886 196 DLPEPLGNLTNLEELDLSGNQL 217
DUF4670 super family cl37896
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 156-220 3.78e-06

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


The actual alignment was detected with superfamily member pfam15709:

Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 48.02  E-value: 3.78e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74760704   156 ERERQRRLEVEREAEKKREAKQRAKEAQERELRKREKAEEKERRRKEYDALKAAKREQEKKPKKE 220
Cdd:pfam15709 341 ERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEE 405
 
Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
19-120 6.10e-26

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 106.17  E-value: 6.10e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74760704  19 ELDLSLSDLNEVPvKELAALPKATILDLSCNKLTTLPSDFCGLTHLVKLDLSKNKLQQLPADFGRLVNLQHLDLLNNKLV 98
Cdd:COG4886 117 SLDLSGNQLTDLP-EELANLTNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQIT 195

                        90       100
                ....*....|....*....|..
gi 74760704  99 TLPVSFAQLKNLKWLDLKDNPL 120
Cdd:COG4886 196 DLPEPLGNLTNLEELDLSGNQL 217
LRR_8 pfam13855
Leucine rich repeat;
62-120 1.74e-12

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 61.39  E-value: 1.74e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74760704    62 THLVKLDLSKNKLQQLPAD-FGRLVNLQHLDLLNNKLVTL-PVSFAQLKNLKWLDLKDNPL 120
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGaFKGLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNRL 61
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 10-120 5.75e-08

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 54.08  E-value: 5.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74760704   10 NLRDKLDGNELDL-SLSDLNEVPVKELAALP------KATILDLSCNKLT-TLPSDFCGLTHLVKLDLSKNKLQ-QLPAD 80
Cdd:PLN00113 439 NLQGRINSRKWDMpSLQMLSLARNKFFGGLPdsfgskRLENLDLSRNQFSgAVPRKLGSLSELMQLKLSENKLSgEIPDE 518

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 74760704   81 FGRLVNLQHLDLLNNKLV-TLPVSFAQLKNLKWLDLKDNPL 120
Cdd:PLN00113 519 LSSCKKLVSLDLSHNQLSgQIPASFSEMPVLSQLDLSQNQL 559
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 156-220 3.78e-06

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 48.02  E-value: 3.78e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74760704   156 ERERQRRLEVEREAEKKREAKQRAKEAQERELRKREKAEEKERRRKEYDALKAAKREQEKKPKKE 220
Cdd:pfam15709 341 ERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEE 405
PTZ00121 PTZ00121
MAEBL; Provisional
 133-240 1.18e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.06  E-value: 1.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74760704   133 DEKQCKQCANKVLQHMKAVQADQERERQRRLEverEAEKKREAKQRAKEAQERELRKREKAEEKERRRKEYDALKAAKRE 212
Cdd:PTZ00121 1442 EAKKADEAKKKAEEAKKAEEAKKKAEEAKKAD---EAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKA 1518

                          90       100
                  ....*....|....*....|....*...
gi 74760704   213 QEKKPKKEANQAPKSKSGSRPRKPPPRK 240
Cdd:PTZ00121 1519 EEAKKADEAKKAEEAKKADEAKKAEEKK 1546
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 42-95 2.00e-05

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 44.78  E-value: 2.00e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 74760704  42 TILDLSCNKLTTLpSDFCGLTHLVKLDLSKNKLQ---QLPADFGRLVNLQHLDLLNN 95
Cdd:cd21340 123 RVLNISGNNIDSL-EPLAPLRNLEQLDASNNQISdleELLDLLSSWPSLRELDLTGN 178
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 132-228 6.88e-05

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 44.07  E-value: 6.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74760704   132 LDEKQCKQCANKVLQHMKAvQADQERERQRRLEVE-------REAEKKREAKQRAKEAQERELRKREKAEEKERRRKEYD 204
Cdd:TIGR02794  43 VDPGAVAQQANRIQQQKKP-AAKKEQERQKKLEQQaeeaekqRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQA 121

                          90       100
                  ....*....|....*....|....
gi 74760704   205 ALKAAKREQEKKPKKEANQAPKSK 228
Cdd:TIGR02794 122 EEAKAKQAAEAKAKAEAEAERKAK 145
NOP7 COG5163
Protein required for biogenesis of the 60S ribosomal subunit [Translation, ribosomal structure ...
 153-228 2.67e-04

Protein required for biogenesis of the 60S ribosomal subunit [Translation, ribosomal structure and biogenesis];


Pssm-ID: 227492 [Multi-domain]  Cd Length: 591  Bit Score: 42.37  E-value: 2.67e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74760704 153 ADQERERQRRLEVEREAEKKREAKQRAKEAQERELRKREKAEEKE-----------RRRKEYDALK---AAKREQEKKPK 218
Cdd:COG5163 496 DDEELQAQKELELEAQGIKYSETSEADKDVNKSKNKKRKVDEEEEekklkmimmsnKQKKLYKKMKysnAKKEEQAENLK 575

                        90
                ....*....|
gi 74760704 219 KEANQAPKSK 228
Cdd:COG5163 576 KKKKQIAKQK 585
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 146-223 1.61e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 39.48  E-value: 1.61e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74760704 146 QHMKAVQADQERERQRrlEVEREAEKKREAKQRAKEAQERELRKREKaEEKERRRKEYDALKAAK-REQEKKPKKEANQ 223
Cdd:cd16269 203 ERAKAEAAEQERKLLE--EQQRELEQKLEDQERSYEEHLRQLKEKME-EERENLLKEQERALESKlKEQEALLEEGFKE 278
 
Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
19-120 6.10e-26

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 106.17  E-value: 6.10e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74760704  19 ELDLSLSDLNEVPvKELAALPKATILDLSCNKLTTLPSDFCGLTHLVKLDLSKNKLQQLPADFGRLVNLQHLDLLNNKLV 98
Cdd:COG4886 117 SLDLSGNQLTDLP-EELANLTNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQIT 195

                        90       100
                ....*....|....*....|..
gi 74760704  99 TLPVSFAQLKNLKWLDLKDNPL 120
Cdd:COG4886 196 DLPEPLGNLTNLEELDLSGNQL 217
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
19-126 6.17e-26

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 106.17  E-value: 6.17e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74760704  19 ELDLSLSDLNEVPvKELAALPKATILDLSCNKLTTLPSDFCGLTHLVKLDLSKNKLQQLPADFGRLVNLQHLDLLNNKLV 98
Cdd:COG4886 140 ELDLSNNQLTDLP-EPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLGNLTNLEELDLSGNQLT 218

                        90       100       110
                ....*....|....*....|....*....|
gi 74760704  99 TLPVSFAQLKNLKWLDLKDNPLD--PVLAK 126
Cdd:COG4886 219 DLPEPLANLTNLETLDLSNNQLTdlPELGN 248
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
23-120 1.65e-24

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 102.32  E-value: 1.65e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74760704  23 SLSDLNEVPVKELAALPKATILDLSCNKLTTLPSDFCGLTHLVKLDLSKNKLQQLPADFGRLVNLQHLDLLNNKLVTLPV 102
Cdd:COG4886  97 NLTELDLSGNEELSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTDLPE 176

                        90
                ....*....|....*...
gi 74760704 103 SFAQLKNLKWLDLKDNPL 120
Cdd:COG4886 177 ELGNLTNLKELDLSNNQI 194
LRR_8 pfam13855
Leucine rich repeat;
62-120 1.74e-12

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 61.39  E-value: 1.74e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74760704    62 THLVKLDLSKNKLQQLPAD-FGRLVNLQHLDLLNNKLVTL-PVSFAQLKNLKWLDLKDNPL 120
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGaFKGLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNRL 61
LRR_8 pfam13855
Leucine rich repeat;
39-97 3.08e-11

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 57.92  E-value: 3.08e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74760704    39 PKATILDLSCNKLTTLPSD-FCGLTHLVKLDLSKNKLQQL-PADFGRLVNLQHLDLLNNKL 97
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGaFKGLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNRL 61
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
10-120 1.79e-10

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 61.10  E-value: 1.79e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74760704  10 NLRDKLDGNELDLSLSDLNEVPVKELAALPKATILDLSCNKLTTLPSDFCGLTHLVKLDLSKNKlqqlpaDFGRLVNLQH 89
Cdd:COG4886  44 SLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNE------ELSNLTNLES 117

                        90       100       110
                ....*....|....*....|....*....|.
gi 74760704  90 LDLLNNKLVTLPVSFAQLKNLKWLDLKDNPL 120
Cdd:COG4886 118 LDLSGNQLTDLPEELANLTNLKELDLSNNQL 148
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 10-120 5.75e-08

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 54.08  E-value: 5.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74760704   10 NLRDKLDGNELDL-SLSDLNEVPVKELAALP------KATILDLSCNKLT-TLPSDFCGLTHLVKLDLSKNKLQ-QLPAD 80
Cdd:PLN00113 439 NLQGRINSRKWDMpSLQMLSLARNKFFGGLPdsfgskRLENLDLSRNQFSgAVPRKLGSLSELMQLKLSENKLSgEIPDE 518

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 74760704   81 FGRLVNLQHLDLLNNKLV-TLPVSFAQLKNLKWLDLKDNPL 120
Cdd:PLN00113 519 LSSCKKLVSLDLSHNQLSgQIPASFSEMPVLSQLDLSQNQL 559
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
19-120 9.40e-08

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 53.16  E-value: 9.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74760704   19 ELDLSLSDLNEVPVKelaaLPKA-TILDLSCNKLTTLPSDFCglTHLVKLDLSKNKLQQLPADFGRlvNLQHLDLLNNKL 97
Cdd:PRK15370 245 EMELSINRITELPER----LPSAlQSLDLFHNKISCLPENLP--EELRYLSVYDNSIRTLPAHLPS--GITHLNVQSNSL 316

                         90       100
                 ....*....|....*....|...
gi 74760704   98 VTLPVSFAQlkNLKWLDLKDNPL 120
Cdd:PRK15370 317 TALPETLPP--GLKTLEAGENAL 337
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
19-133 5.76e-07

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 50.70  E-value: 5.76e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74760704  19 ELDLSLSDLNEVPvkELAALPKATILDLSCNKLTTLPsDFCGLTHLVKLDLSKNK-----LQQLPADFGRLVNLQHLDLL 93
Cdd:COG4886 232 TLDLSNNQLTDLP--ELGNLTNLEELDLSNNQLTDLP-PLANLTNLKTLDLSNNQltdlkLKELELLLGLNSLLLLLLLL 308

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 74760704  94 NNKLVTLPVSFAQLKNLKWLDLKDNPLDPVLAKVAGDCLD 133
Cdd:COG4886 309 NLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLA 348
LRR_8 pfam13855
Leucine rich repeat;
19-74 7.46e-07

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 45.59  E-value: 7.46e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 74760704    19 ELDLSLSDLNEVPVKELAALPKATILDLSCNKLTTL-PSDFCGLTHLVKLDLSKNKL 74
Cdd:pfam13855   5 SLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNRL 61
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 20-131 3.07e-06

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 48.69  E-value: 3.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74760704   20 LDLSLSDLN-EVPvKELAALPKATILDLSCNKLT-TLPSDFCGLTHLVKLDLSKNKLQ-QLPADFGRLVNLQHLDLLNNK 96
Cdd:PLN00113 289 LDLSDNSLSgEIP-ELVIQLQNLEILHLFSNNFTgKIPVALTSLPRLQVLQLWSNKFSgEIPKNLGKHNNLTVLDLSTNN 367

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 74760704   97 LV-TLPVSFAQLKNLKWLDLKDNPLDPVLAKVAGDC 131
Cdd:PLN00113 368 LTgEIPEGLCSSGNLFKLILFSNSLEGEIPKSLGAC 403
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 18-120 3.12e-06

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 48.69  E-value: 3.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74760704   18 NELDLSLSDLN-EVPVkELAALPKATILDLSCNKLT-TLPSDFCGLTHLVKLDLSKNKLQ-QLPADFGRLVNLQHLDLLN 94
Cdd:PLN00113 239 NHLDLVYNNLTgPIPS-SLGNLKNLQYLFLYQNKLSgPIPPSIFSLQKLISLDLSDNSLSgEIPELVIQLQNLEILHLFS 317

                         90       100
                 ....*....|....*....|....*..
gi 74760704   95 NKLV-TLPVSFAQLKNLKWLDLKDNPL 120
Cdd:PLN00113 318 NNFTgKIPVALTSLPRLQVLQLWSNKF 344
PLN03150 PLN03150
hypothetical protein; Provisional
 54-120 3.49e-06

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 48.27  E-value: 3.49e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74760704   54 LPSDFCGLTHLVKLDLSKNKLQ-QLPADFGRLVNLQHLDLLNNKLV-TLPVSFAQLKNLKWLDLKDNPL 120
Cdd:PLN03150 434 IPNDISKLRHLQSINLSGNSIRgNIPPSLGSITSLEVLDLSYNSFNgSIPESLGQLTSLRILNLNGNSL 502
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 156-220 3.78e-06

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 48.02  E-value: 3.78e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74760704   156 ERERQRRLEVEREAEKKREAKQRAKEAQERELRKREKAEEKERRRKEYDALKAAKREQEKKPKKE 220
Cdd:pfam15709 341 ERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEE 405
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 35-120 4.87e-06

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 47.92  E-value: 4.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74760704   35 LAALPKATILDLSCNKLT-TLPSDFCGLTHLVKLDLSKNKLQ-QLPADFGRLVNLQHLDLLNNKLV-TLPVSFAQLKNLK 111
Cdd:PLN00113 184 LTNLTSLEFLTLASNQLVgQIPRELGQMKSLKWIYLGYNNLSgEIPYEIGGLTSLNHLDLVYNNLTgPIPSSLGNLKNLQ 263


                 ....*....
gi 74760704  112 WLDLKDNPL 120
Cdd:PLN00113 264 YLFLYQNKL 272
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 140-239 6.68e-06

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 47.45  E-value: 6.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74760704   140 CANKVLQHMKAVQADQERERQRRLEvereaEKKREAKQRAKEAQERElRKREKaeekerrrkeydalkaaKREQEKKPKK 219
Cdd:pfam03154 570 CARTDLYFMPLAGSKLAKKREEALE-----KAKREAEQKAREEKERE-KEKEK-----------------ERERERERER 626

                          90       100
                  ....*....|....*....|.
gi 74760704   220 EANQAPKSKSGS-RPRKPPPR 239
Cdd:pfam03154 627 EAERAAKASSSShEGRMGDPQ 647
CCDC47 pfam07946
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ...
 159-219 6.75e-06

PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of the PAT complex, an endoplasmic reticulum (ER)-resident membrane multiprotein complex that facilitates multi-pass membrane proteins insertion into membranes. The PAT complex, formed by CCDC47 and Asterix proteins, acts as an intramembrane chaperone by directly interacting with nascent transmembrane domains (TMDs), releasing its substrates upon correct folding, and is needed for optimal biogenesis of multi-pass membrane proteins. CCDC47 is required to maintain the stability of Asterix. CCDC47 is associated with various membrane-associated processes and is component of a ribosome-associated ER translocon complex involved in multi-pass membrane protein transport into the ER membrane and biogenesis. It is also involved in the regulation of calcium ion homeostasis in the ER, being also required for proper protein degradation via the ERAD (ER-associated degradation) pathway.


Pssm-ID: 462322  Cd Length: 323  Bit Score: 46.79  E-value: 6.75e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74760704   159 RQRRLEVEREAeKKREAKQRAKEAQERelRKREKAEEKERRRKEYDA---LKAAKREQEKKPKK 219
Cdd:pfam07946 263 KKTREEEIEKI-KKAAEEERAEEAQEK--KEEAKKKEREEKLAKLSPeeqRKYEEKERKKEQRK 323
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 19-97 8.36e-06

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 47.15  E-value: 8.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74760704   19 ELDLSLSDLNEVPVKELAALPKATILDLSCNKLT-TLPSDFCGLTHLVKLDLSKNKLQ-QLPADFGRLVNLQHLDLLNNK 96
Cdd:PLN00113 503 QLKLSENKLSGEIPDELSSCKKLVSLDLSHNQLSgQIPASFSEMPVLSQLDLSQNQLSgEIPKNLGNVESLVQVNISHNH 582


                 .
gi 74760704   97 L 97
Cdd:PLN00113 583 L 583
PTZ00121 PTZ00121
MAEBL; Provisional
 133-240 1.18e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.06  E-value: 1.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74760704   133 DEKQCKQCANKVLQHMKAVQADQERERQRRLEverEAEKKREAKQRAKEAQERELRKREKAEEKERRRKEYDALKAAKRE 212
Cdd:PTZ00121 1442 EAKKADEAKKKAEEAKKAEEAKKKAEEAKKAD---EAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKA 1518

                          90       100
                  ....*....|....*....|....*...
gi 74760704   213 QEKKPKKEANQAPKSKSGSRPRKPPPRK 240
Cdd:PTZ00121 1519 EEAKKADEAKKAEEAKKADEAKKAEEKK 1546
PTZ00121 PTZ00121
MAEBL; Provisional
 138-240 1.32e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.67  E-value: 1.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74760704   138 KQCANKVLQHMKAVQADQERERQRRLEVErEAEKKREAKQRAKEAQERELRKREKAEEKERRRKEYDALKAAKREQEKKP 217
Cdd:PTZ00121 1277 ARKADELKKAEEKKKADEAKKAEEKKKAD-EAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAA 1355

                          90       100
                  ....*....|....*....|...
gi 74760704   218 KKEANQAPKSKSGSRPRKPPPRK 240
Cdd:PTZ00121 1356 ADEAEAAEEKAEAAEKKKEEAKK 1378
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 42-95 2.00e-05

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 44.78  E-value: 2.00e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 74760704  42 TILDLSCNKLTTLpSDFCGLTHLVKLDLSKNKLQ---QLPADFGRLVNLQHLDLLNN 95
Cdd:cd21340 123 RVLNISGNNIDSL-EPLAPLRNLEQLDASNNQISdleELLDLLSSWPSLRELDLTGN 178
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 35-121 2.13e-05

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 44.78  E-value: 2.13e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74760704  35 LAALPKATILDLSCNKLTTLPsDFCGLTHLVKLDLSKNKL-------------------QQLPADFG-----RLVN---- 86
Cdd:cd21340  42 LEFLTNLTHLYLQNNQIEKIE-NLENLVNLKKLYLGGNRIsvveglenltnleelhienQRLPPGEKltfdpRSLAalsn 120

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 74760704  87 -LQHLDLLNNKLVTLpVSFAQLKNLKWLDLKDNPLD 121
Cdd:cd21340 121 sLRVLNISGNNIDSL-EPLAPLRNLEQLDASNNQIS 155
Radial_spoke_3 pfam06098
Radial spoke protein 3; This family consists of several radial spoke protein 3 (RSP3) ...
 157-224 3.27e-05

Radial spoke protein 3; This family consists of several radial spoke protein 3 (RSP3) sequences. Eukaryotic cilia and flagella present in diverse types of cells perform motile, sensory, and developmental functions in organizms from protists to humans. They are centred by precisely organized, microtubule-based structures, the axonemes. The axoneme consists of two central singlet microtubules, called the central pair, and nine outer doublet microtubules. These structures are well-conserved during evolution. The outer doublet microtubules, each composed of A and B sub-fibres, are connected to each other by nexin links, while the central pair is held at the centre of the axoneme by radial spokes. The radial spokes are T-shaped structures extending from the A-tubule of each outer doublet microtubule to the centre of the axoneme. Radial spoke protein 3 (RSP3), is present at the proximal end of the spoke stalk and helps in anchoring the radial spoke to the outer doublet. It is thought that radial spokes regulate the activity of inner arm dynein through protein phosphorylation and dephosphorylation.


Pssm-ID: 461827  Cd Length: 286  Bit Score: 44.55  E-value: 3.27e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74760704   157 RERQRRLEVEREAEKkreAKQRAKEAQERELRkrekaEEKERRRKEYdalKAAKREQEKKPKKEANQA 224
Cdd:pfam06098 159 REQQRAFEELRNAEL---AEVQRLEEQERRLR-----EEKERRIAQQ---REALKKEKETAEKIAARA 215
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 44-120 3.57e-05

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 45.22  E-value: 3.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74760704   44 LDLSCNKLT-TLPSDFcgLTHLVKLDLSKNKLQ-QLPADFGRLVNLQHLDLLNNKLV-TLPVSFAQLKNLKWLDLKDNPL 120
Cdd:PLN00113 123 LNLSNNNFTgSIPRGS--IPNLETLDLSNNMLSgEIPNDIGSFSSLKVLDLGGNVLVgKIPNSLTNLTSLEFLTLASNQL 200
PTZ00121 PTZ00121
MAEBL; Provisional
 146-228 3.98e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.13  E-value: 3.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74760704   146 QHMKAVQADQERERQRRLEVEREAEKKREAKQRAKEAQERELRKREKAEEKERRRKEYDALKAAKREQEKKPKKEANQAP 225
Cdd:PTZ00121 1605 KKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAE 1684


                  ...
gi 74760704   226 KSK 228
Cdd:PTZ00121 1685 EDE 1687
DDRGK pfam09756
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and ...
 152-214 5.03e-05

DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and vertebrates. They contain a highly conserved DDRGK motif.


Pssm-ID: 370664 [Multi-domain]  Cd Length: 188  Bit Score: 43.11  E-value: 5.03e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74760704   152 QADQERERQRRLEVEREAEKKREAKQRAKEAQERELRKREKAEEKERRRKEYDALKAAKREQE 214
Cdd:pfam09756  12 ELKEAKRQQREAEEEEREEREKLEEKREEEYKEREEREEEAEKEKEEEERKQEEEQERKEQEE 74
PTZ00121 PTZ00121
MAEBL; Provisional
 148-235 5.05e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.13  E-value: 5.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74760704   148 MKAVQADQERERQRRLEV--EREAEKKREAKQRAKEAQERELRKREKAEEKERRRKEYDALKAAKREQEKKPKKEANQAP 225
Cdd:PTZ00121 1620 IKAEELKKAEEEKKKVEQlkKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAE 1699

                          90
                  ....*....|
gi 74760704   226 KSKSGSRPRK 235
Cdd:PTZ00121 1700 EAKKAEELKK 1709
PRK00247 PRK00247
putative inner membrane protein translocase component YidC; Validated
 142-240 5.66e-05

putative inner membrane protein translocase component YidC; Validated


Pssm-ID: 178945 [Multi-domain]  Cd Length: 429  Bit Score: 44.46  E-value: 5.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74760704  142 NKVLQHMKAVQADQERERQRRLEVEREAEkkREAKQRAKEAQERELRKREKAEEKERRRKEydalkAAKREQEKKPKKEA 221
Cdd:PRK00247 334 KTRTAEKNEAKARKKEIAQKRRAAEREIN--REARQERAAAMARARARRAAVKAKKKGLID-----ASPNEDTPSENEES 406

                         90
                 ....*....|....*....
gi 74760704  222 NQAPKSKSGSRPRKPPPRK 240
Cdd:PRK00247 407 KGSPPQVEATTTAEPNREP 425
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 146-234 6.08e-05

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 44.34  E-value: 6.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74760704   146 QHMKAVQADQERERQRRLEVEREAEKKREAKQRAKEAQERELRKREKA--EEKERRR---KEYDALKAAKREQEKKPKKE 220
Cdd:pfam17380 460 QQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAmiEEERKRKlleKEMEERQKAIYEEERRREAE 539

                          90
                  ....*....|....
gi 74760704   221 ANQAPKSKSGSRPR 234
Cdd:pfam17380 540 EERRKQQEMEERRR 553
PRK00247 PRK00247
putative inner membrane protein translocase component YidC; Validated
 156-243 6.24e-05

putative inner membrane protein translocase component YidC; Validated


Pssm-ID: 178945 [Multi-domain]  Cd Length: 429  Bit Score: 44.07  E-value: 6.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74760704  156 ERERQRRLEVEREAEKKREAKQRAKEAqEREL---RKREKAEEKERRRKEYDALKAAKRE-QEKKPKKEANQAPKSKSGS 231
Cdd:PRK00247 331 EIKKTRTAEKNEAKARKKEIAQKRRAA-EREInreARQERAAAMARARARRAAVKAKKKGlIDASPNEDTPSENEESKGS 409

                         90
                 ....*....|....
gi 74760704  232 RPRKPP--PRKHTR 243
Cdd:PRK00247 410 PPQVEAttTAEPNR 423
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 132-228 6.88e-05

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 44.07  E-value: 6.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74760704   132 LDEKQCKQCANKVLQHMKAvQADQERERQRRLEVE-------REAEKKREAKQRAKEAQERELRKREKAEEKERRRKEYD 204
Cdd:TIGR02794  43 VDPGAVAQQANRIQQQKKP-AAKKEQERQKKLEQQaeeaekqRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQA 121

                          90       100
                  ....*....|....*....|....
gi 74760704   205 ALKAAKREQEKKPKKEANQAPKSK 228
Cdd:TIGR02794 122 EEAKAKQAAEAKAKAEAEAERKAK 145
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 142-223 1.03e-04

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 43.30  E-value: 1.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74760704   142 NKVLQHMKAVQADQERERQRRLEVEREAEKKREAKQRAKEAQERELRKREKAEEKERRRKEydALKAAKREQEKKPKKEA 221
Cdd:TIGR02794  71 KKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAE--AKAKAEAEAERKAKEEA 148


                  ..
gi 74760704   222 NQ 223
Cdd:TIGR02794 149 AK 150
Caldesmon pfam02029
Caldesmon;
156-220 1.15e-04

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 43.32  E-value: 1.15e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74760704   156 ERERQRRLEVE-REAEKKREAKQRAKEAQERELRKREK----AEEKERRRKEYDALKAAKREQEKKPKKE 220
Cdd:pfam02029 251 EELRRRRQEKEsEEFEKLRQKQQEAELELEELKKKREErrklLEEEEQRRKQEEAERKLREEEEKRRMKE 320
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 132-218 1.41e-04

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 43.19  E-value: 1.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74760704   132 LDEKQCKQCANKVLQHMKAVQADQERERQ---RRLEVEREAEKKR-------------------EAKQRAKEAQERELRK 189
Cdd:pfam17380 406 ILEEERQRKIQQQKVEMEQIRAEQEEARQrevRRLEEERAREMERvrleeqerqqqverlrqqeEERKRKKLELEKEKRD 485

                          90       100       110
                  ....*....|....*....|....*....|.
gi 74760704   190 REKAEEKERR--RKEYDALKAAKREQEKKPK 218
Cdd:pfam17380 486 RKRAEEQRRKilEKELEERKQAMIEEERKRK 516
PLN02381 PLN02381
valyl-tRNA synthetase
 167-235 1.50e-04

valyl-tRNA synthetase


Pssm-ID: 215214 [Multi-domain]  Cd Length: 1066  Bit Score: 43.35  E-value: 1.50e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74760704   167 REAEKKREAKQRAKEAQERELRKREKAEEKERRRkeydaLKAAKREQEKKPKKEANQAPKSKSGSRPRK 235
Cdd:PLN02381    2 SRTESEAEKKILTEEELERKKKKEEKAKEKELKK-----LKAAQKEAKAKLQAQQASDGTNVPKKSEKK 65
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
 133-221 2.28e-04

Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 42.68  E-value: 2.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74760704   133 DEKQCKQCANKVLQHMKAVQADQERER---QRRLEVER---EAEKKREAKQRAKEAQERELRKREKAEEKERRRKEYDA- 205
Cdd:pfam05262 248 DEVRQKQQEAKNLPKPADTSSPKEDKQvaeNQKREIEKaqiEIKKNDEEALKAKDHKAFDLKQESKASEKEAEDKELEAq 327

                          90
                  ....*....|....*....
gi 74760704   206 ---LKAAKREQEKKPKKEA 221
Cdd:pfam05262 328 kkrEPVAEDLQKTKPQVEA 346
PRK05035 PRK05035
electron transport complex protein RnfC; Provisional
 164-226 2.29e-04

electron transport complex protein RnfC; Provisional


Pssm-ID: 235334 [Multi-domain]  Cd Length: 695  Bit Score: 42.63  E-value: 2.29e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74760704  164 EVEREAEKKREAKQR--------AKEAQERELRKREKAEekERRRKEYDALKAAK-REQEKKPKKEANQAPK 226
Cdd:PRK05035 440 AIEQEKKKAEEAKARfearqarlEREKAAREARHKKAAE--ARAAKDKDAVAAALaRVKAKKAAATQPIVIK 509
NOP7 COG5163
Protein required for biogenesis of the 60S ribosomal subunit [Translation, ribosomal structure ...
 153-228 2.67e-04

Protein required for biogenesis of the 60S ribosomal subunit [Translation, ribosomal structure and biogenesis];


Pssm-ID: 227492 [Multi-domain]  Cd Length: 591  Bit Score: 42.37  E-value: 2.67e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74760704 153 ADQERERQRRLEVEREAEKKREAKQRAKEAQERELRKREKAEEKE-----------RRRKEYDALK---AAKREQEKKPK 218
Cdd:COG5163 496 DDEELQAQKELELEAQGIKYSETSEADKDVNKSKNKKRKVDEEEEekklkmimmsnKQKKLYKKMKysnAKKEEQAENLK 575

                        90
                ....*....|
gi 74760704 219 KEANQAPKSK 228
Cdd:COG5163 576 KKKKQIAKQK 585
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 138-229 2.68e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 42.10  E-value: 2.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74760704  138 KQCANKVLQHMKAVQADQERERQRRLEVEREAEKKREAKQRAKEAQERELRKREKAEEKERRRKEYDALKA--------- 208
Cdd:PRK09510  79 EQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAeaeakraaa 158

                         90       100
                 ....*....|....*....|...
gi 74760704  209 --AKREQEKKPKKEANQAPKSKS 229
Cdd:PRK09510 159 aaKKAAAEAKKKAEAEAAKKAAA 181
PTZ00121 PTZ00121
MAEBL; Provisional
 133-240 3.40e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 3.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74760704   133 DEKQCKQCANKVLQHMKAVQADQERERQRRL-EVEREAEKKREAKQRAKEAQERelRKREKAEEKERRRKEYDALKAAKR 211
Cdd:PTZ00121 1403 DKKKADELKKAAAAKKKADEAKKKAEEKKKAdEAKKKAEEAKKADEAKKKAEEA--KKAEEAKKKAEEAKKADEAKKKAE 1480

                          90       100       110
                  ....*....|....*....|....*....|.
gi 74760704   212 EQEK--KPKKEANQAPKSKSGSRPRKPPPRK 240
Cdd:PTZ00121 1481 EAKKadEAKKKAEEAKKKADEAKKAAEAKKK 1511
PTZ00121 PTZ00121
MAEBL; Provisional
 133-240 3.43e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 3.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74760704   133 DEKQCKQCANKVLQHMKAVQADQERERQRRL-EVEREAEKKREAKQRAKEAQERelRKREKAEEK-ERRRKEYDALKAA- 209
Cdd:PTZ00121 1416 AKKKADEAKKKAEEKKKADEAKKKAEEAKKAdEAKKKAEEAKKAEEAKKKAEEA--KKADEAKKKaEEAKKADEAKKKAe 1493

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 74760704   210 ----------KREQEKKPKKEANQAPKSKSGSRPRKPPPRK 240
Cdd:PTZ00121 1494 eakkkadeakKAAEAKKKADEAKKAEEAKKADEAKKAEEAK 1534
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 62-99 3.44e-04

Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains.


Pssm-ID: 463713 [Multi-domain]  Cd Length: 44  Bit Score: 37.61  E-value: 3.44e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 74760704    62 THLVKLDLSKNKLQQLPAdFGRLVNLQHLDLLNNKLVT 99
Cdd:pfam12799   1 PNLEVLDLSNNQITDIPP-LAKLPNLETLDLSGNNKIT 37
PTZ00436 PTZ00436
60S ribosomal protein L19-like protein; Provisional
 144-235 3.71e-04

60S ribosomal protein L19-like protein; Provisional


Pssm-ID: 185616 [Multi-domain]  Cd Length: 357  Bit Score: 41.86  E-value: 3.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74760704  144 VLQHMKAVQADQERERQRrleVEREAEKKREAKQRAKEAQERELRKREKaeEKERRRKEYDALKAAKREQEKKPKKEANQ 223
Cdd:PTZ00436 138 LMEHIHKVKNEKKKERQL---AEQLAAKRLKDEQHRHKARKQELRKREK--DRERARREDAAAAAAAKQKAAAKKAAAPS 212

                         90
                 ....*....|..
gi 74760704  224 APKSKSGSRPRK 235
Cdd:PTZ00436 213 GKKSAKAAAPAK 224
PTZ00121 PTZ00121
MAEBL; Provisional
 125-240 3.84e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 3.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74760704   125 AKVAGDCLDEKQCKQCANKVLQHMKAVQADQERERQRRLEVEREAEKKREA--------KQRAKEAQER--ELRKREKAE 194
Cdd:PTZ00121 1242 AKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAdeakkaeeKKKADEAKKKaeEAKKADEAK 1321

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 74760704   195 EK-ERRRKEYDALKaaKREQEKKPKKEANQAPKSKSGSRPRKPPPRK 240
Cdd:PTZ00121 1322 KKaEEAKKKADAAK--KKAEEAKKAAEAAKAEAEAAADEAEAAEEKA 1366
PTZ00121 PTZ00121
MAEBL; Provisional
 134-219 4.23e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 4.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74760704   134 EKQCKQCANKVLQHMKAVQADQERERQRRLEVEREAEKKREAKQRAKEAQERELRKREKAEEKERRRKEYDALKAAKREQ 213
Cdd:PTZ00121 1632 KKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKE 1711


                  ....*.
gi 74760704   214 EKKPKK 219
Cdd:PTZ00121 1712 AEEKKK 1717
PTZ00121 PTZ00121
MAEBL; Provisional
 133-227 4.91e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 4.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74760704   133 DEKQCKQCANKVLQHMKAVQADQERERQRRLEVEREAEKKREAKQRAKEAQERElRKREKAEEKERRRKEYDALKAAKRE 212
Cdd:PTZ00121 1351 EAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDK-KKADELKKAAAAKKKADEAKKKAEE 1429

                          90
                  ....*....|....*..
gi 74760704   213 QEK--KPKKEANQAPKS 227
Cdd:PTZ00121 1430 KKKadEAKKKAEEAKKA 1446
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 155-226 5.04e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 41.74  E-value: 5.04e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74760704  155 QERERQRRLEVEREAEKKREAKQRAKEAQERELRKREKAEEKERRRKEY-DALKA-----AKREQEKKPKKEANQAPK 226
Cdd:PRK00409 561 QEEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQLQKGGYASVKAHELiEARKRlnkanEKKEKKKKKQKEKQEELK 638
PRK05035 PRK05035
electron transport complex protein RnfC; Provisional
 149-235 5.15e-04

electron transport complex protein RnfC; Provisional


Pssm-ID: 235334 [Multi-domain]  Cd Length: 695  Bit Score: 41.47  E-value: 5.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74760704  149 KAVQADQERER----QRRLE---VEREAEKKREAKQRAKEAQER-----ELRKREKAEEKERRRKEYDALK-----AAKR 211
Cdd:PRK05035 444 EKKKAEEAKARfearQARLErekAAREARHKKAAEARAAKDKDAvaaalARVKAKKAAATQPIVIKAGARPdnsavIAAR 523

                         90       100
                 ....*....|....*....|....
gi 74760704  212 EQEKKPKKEANQAPKSKSGSRPRK 235
Cdd:PRK05035 524 EARKAQARARQAEKQAAAAADPKK 547
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 149-224 5.18e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.46  E-value: 5.18e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74760704 149 KAVQADQERERQRRLEVEREAEKKREAKQRAKEAQERELRKREKAEEKERRRKEYDALKAAKREQEKKPKKEANQA 224
Cdd:COG1196 281 LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356
PTZ00121 PTZ00121
MAEBL; Provisional
 134-235 5.27e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 5.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74760704   134 EKQCKQCANKVLQHMKAVQADQERERQRRLEVEREAEKKREAKQ--RAKEAQEREL-RKREKAEEKERRRKEYDALK--A 208
Cdd:PTZ00121 1101 EEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEarKAEDAKRVEIaRKAEDARKAEEARKAEDAKKaeA 1180

                          90       100
                  ....*....|....*....|....*..
gi 74760704   209 AKREQEKKPKKEANQAPKSKSGSRPRK 235
Cdd:PTZ00121 1181 ARKAEEVRKAEELRKAEDARKAEAARK 1207
PTZ00121 PTZ00121
MAEBL; Provisional
 133-235 6.38e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 6.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74760704   133 DEKQCKQCANKVLQHMKAVQADQERERQRRLEVER----EAEKKREAKQRAKEAQER--ELRKREKAEEKERRRKEYDAL 206
Cdd:PTZ00121 1455 EAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKkkaeEAKKKADEAKKAAEAKKKadEAKKAEEAKKADEAKKAEEAK 1534

                          90       100       110
                  ....*....|....*....|....*....|.
gi 74760704   207 KA--AKREQEKKPKKEANQAPKSKSGSRPRK 235
Cdd:PTZ00121 1535 KAdeAKKAEEKKKADELKKAEELKKAEEKKK 1565
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
152-214 7.37e-04

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 41.01  E-value: 7.37e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74760704 152 QADQERERQRRLEVEREAEK-KREAKQRAKEAQERELRKREKAEEKERRRKEYD-ALKAAKREQE 214
Cdd:COG2268 227 ELEQEREIETARIAEAEAELaKKKAEERREAETARAEAEAAYEIAEANAEREVQrQLEIAERERE 291
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
156-224 8.42e-04

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 40.63  E-value: 8.42e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74760704 156 ERERQRRLEVEREAEKKREAKQR----AKEAQERELRKREKAE-EKERRRKeydalKAAKREQEKKPKKEANQA 224
Cdd:COG2268 199 RDARIAEAEAERETEIAIAQANReaeeAELEQEREIETARIAEaEAELAKK-----KAEERREAETARAEAEAA 267
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 143-229 9.53e-04

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 40.88  E-value: 9.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74760704   143 KVLQHMKAVQADQERERQRRLEVEREAEKKREA---KQRAKEAQERELRKREKA--EEKERRRKEYDALKAAKREQEKKP 217
Cdd:pfam17380 475 KKLELEKEKRDRKRAEEQRRKILEKELEERKQAmieEERKRKLLEKEMEERQKAiyEEERRREAEEERRKQQEMEERRRI 554

                          90
                  ....*....|..
gi 74760704   218 KKEANQAPKSKS 229
Cdd:pfam17380 555 QEQMRKATEERS 566
PTZ00121 PTZ00121
MAEBL; Provisional
 134-226 1.26e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 1.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74760704   134 EKQCKQCANKVLQHMKAVQADQERERQRRLEVEREAEKKREAKQRAKEAQERELRKREKAEEKE-----RRRKEYDALKA 208
Cdd:PTZ00121 1328 KKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKkadeaKKKAEEDKKKA 1407

                          90
                  ....*....|....*...
gi 74760704   209 AKREQEKKPKKEANQAPK 226
Cdd:PTZ00121 1408 DELKKAAAAKKKADEAKK 1425
PLN02381 PLN02381
valyl-tRNA synthetase
 156-221 1.29e-03

valyl-tRNA synthetase


Pssm-ID: 215214 [Multi-domain]  Cd Length: 1066  Bit Score: 40.27  E-value: 1.29e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74760704   156 ERERQRRLEVEREAEKKREAKQRAKEAQERELRKREKAEEKERRRKEYDALKAAKREQEKKPKKEA 221
Cdd:PLN02381    5 ESEAEKKILTEEELERKKKKEEKAKEKELKKLKAAQKEAKAKLQAQQASDGTNVPKKSEKKSRKRD 70
PRK00247 PRK00247
putative inner membrane protein translocase component YidC; Validated
 146-224 1.29e-03

putative inner membrane protein translocase component YidC; Validated


Pssm-ID: 178945 [Multi-domain]  Cd Length: 429  Bit Score: 40.22  E-value: 1.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74760704  146 QHMKAVQADQERERQRRLEVEREAEKKREAKQ-------------RAKEAQERELRKREKAEEKERRRKEYDALKAAKRE 212
Cdd:PRK00247 281 DEFKEHHAEQRAQYREKQKEKKAFLWTLRRNRlrmiitpwrapelHAENAEIKKTRTAEKNEAKARKKEIAQKRRAAERE 360

                         90
                 ....*....|..
gi 74760704  213 QEKKPKKEANQA 224
Cdd:PRK00247 361 INREARQERAAA 372
rne PRK10811
ribonuclease E; Reviewed
 154-243 1.44e-03

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 40.41  E-value: 1.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74760704   154 DQERERQRRLEVEREAEKKREAKQRAKEAQERELRKREKAEEKERRRKEydalKAAKREQEKKPKKEANQAPKSKSGSRP 233
Cdd:PRK10811  638 ENRRNRRQAQQQTAETRESQQAEVTEKARTQDEQQQAPRRERQRRRNDE----KRQAQQEAKALNVEEQSVQETEQEERV 713

                          90
                  ....*....|
gi 74760704   234 RKPPPRKHTR 243
Cdd:PRK10811  714 QQVQPRRKQR 723
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 134-224 1.55e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 39.79  E-value: 1.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74760704  134 EKQCKQCANKVLQHMKAvQADQERERQRRLEVEREAEKKREAKQRAKEAQERELRKR------EKAEEKERRRKEYDALK 207
Cdd:PRK09510 131 QKQAEEAAAKAAAAAKA-KAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKaeaeaaAKAAAEAKKKAEAEAKK 209

                         90
                 ....*....|....*..
gi 74760704  208 AAKREQEKKPKKEANQA 224
Cdd:PRK09510 210 KAAAEAKKKAAAEAKAA 226
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 146-223 1.61e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 39.48  E-value: 1.61e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74760704 146 QHMKAVQADQERERQRrlEVEREAEKKREAKQRAKEAQERELRKREKaEEKERRRKEYDALKAAK-REQEKKPKKEANQ 223
Cdd:cd16269 203 ERAKAEAAEQERKLLE--EQQRELEQKLEDQERSYEEHLRQLKEKME-EERENLLKEQERALESKlKEQEALLEEGFKE 278
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 146-223 1.62e-03

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 39.93  E-value: 1.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74760704   146 QHMKAVQADQERERQRRLEVEREAEKKREAkQRAKEAQERELRKREKAEEK------ERRRKEYDALKAAKREQEKKPKK 219
Cdd:pfam15709 440 QQEEAERAEAEKQRQKELEMQLAEEQKRLM-EMAEEERLEYQRQKQEAEEKarleaeERRQKEEEAARLALEEAMKQAQE 518


                  ....
gi 74760704   220 EANQ 223
Cdd:pfam15709 519 QARQ 522
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 145-223 1.67e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 40.11  E-value: 1.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74760704   145 LQHMKAVQADQER---ERQRRLEVEREAEKKREAKQRAKE------AQERELRK--REKAEEKERRRKEYDALKAAKREQ 213
Cdd:pfam17380 329 MDRQAAIYAEQERmamERERELERIRQEERKRELERIRQEeiameiSRMRELERlqMERQQKNERVRQELEAARKVKILE 408

                          90
                  ....*....|
gi 74760704   214 EKKPKKEANQ 223
Cdd:pfam17380 409 EERQRKIQQQ 418
PTZ00121 PTZ00121
MAEBL; Provisional
 149-228 1.70e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.12  E-value: 1.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74760704   149 KAVQADQERERQRRLE--VEREAEKKREAKQ-RAKEAQERELRKREKAEEKERRRKEYDALKAAKREQEKKPKKEANQAP 225
Cdd:PTZ00121 1676 KAEEAKKAEEDEKKAAeaLKKEAEEAKKAEElKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEE 1755


                  ...
gi 74760704   226 KSK 228
Cdd:PTZ00121 1756 KKK 1758
MPSS6 cd23673
mitochondrial 3' processome (MPsome) subunit 6; MPSS6 is a subunit of the mitochondrial 3' ...
 160-247 1.80e-03

mitochondrial 3' processome (MPsome) subunit 6; MPSS6 is a subunit of the mitochondrial 3' processome (MPsome) which is involved in 3'-5' trimming of messenger RNA (mRNA) precursors, in U-tailing of ribosomal RNA (rRNA) and some mRNAs, and in 3'-5' trimming and U-tailing of guide RNAs (gRNAs), during kinetoplast RNA processing. The mitochondrial DNA of Trypanosomatids, known as the kinetoplast DNA (kDNA or mtDNA), consists of a network of dozens of maxicircles and thousands of minicircles concatenated together. Maxicircles are equivalent to other eukaryotic mitochondrial DNAs, while minicircles encode gRNAs involved in U-insertion/deletion editing processes exclusive of Trypanosomatids that produce the maturation of the maxicircle-encoded transcripts. Although most gRNAs are encoded by minicircles, varying numbers of maxicircle-encoded gRNAs have been identified in kinetoplastids species. MPsome subunits include KDSS1 3'-5' exonuclease, RET1 terminal uridyltransferase (TUTase), and several subunits of as yet undefined functions (MPSS1-MPSS6). The maxicircle and minicircle RNAs are transcribed as 3' extended precursors and processed by MPsome-dependent 3'-5' degradation, and in the case of rRNAs and gRNAs also 3' uridylated. Trypanosoma brucei maxicircles encode 9S and 12S rRNAs, two gRNAs, two ribosomal proteins and 16 subunits of respiratory complexes. 12 of the 18 maxicircle genes are present as cryptogenes whose transcripts require U-insertion/deletion editing, mediated by gRNAs, to restore a protein-coding capacity. The MPsome catalyzes the primary uridylation of about 800 nt gRNA precursor transcripts, their processive degradation to a mature size of 40-60 nt, and secondary U-tail addition. MPSS6 is predicted (AlphaFold) to contain a C-terminal oligonucleotide/oligosaccharide binding (OB) fold-like domain.


Pssm-ID: 467890  Cd Length: 243  Bit Score: 39.30  E-value: 1.80e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74760704 160 QRRLEVEREaeKKREAKQRAKEAQER-ELRKREKAEEKERRRKE-YDALKAAK-----RE--QEKKPKkeaNQAPKSKSG 230
Cdd:cd23673  45 DAKIRLEES--KQKRLQRQLKDVEEElAALKNESERKTAAVRSArYVPAPPAKlflssAEliQEKSPQ---HFVAAEDSK 119

                        90
                ....*....|....*..
gi 74760704 231 SRPRKPPPRKHTRSWAV 247
Cdd:cd23673 120 AELSALPLLRSSGCVAV 136
PLN02316 PLN02316
synthase/transferase
 170-233 2.02e-03

synthase/transferase


Pssm-ID: 215180 [Multi-domain]  Cd Length: 1036  Bit Score: 39.85  E-value: 2.02e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74760704   170 EKKREAKQRAKEAQERElrkrEKAEEKERRRKEYDALKA----AKREQEKKpKKEANQAPKSKSGSRP 233
Cdd:PLN02316  253 EKRRELEKLAKEEAERE----RQAEEQRRREEEKAAMEAdraqAKAEVEKR-REKLQNLLKKASRSAD 315
PTZ00121 PTZ00121
MAEBL; Provisional
 149-235 2.31e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.74  E-value: 2.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74760704   149 KAVQADQERERQRRLEVEREAE--KKREAKQRAKEAQE-RELRKREKAE--------EKERRRKEYDALKAAKR------ 211
Cdd:PTZ00121 1152 KRVEIARKAEDARKAEEARKAEdaKKAEAARKAEEVRKaEELRKAEDARkaeaarkaEEERKAEEARKAEDAKKaeavkk 1231

                          90       100
                  ....*....|....*....|....*
gi 74760704   212 -EQEKKPKKEANQAPKSKSGSRPRK 235
Cdd:PTZ00121 1232 aEEAKKDAEEAKKAEEERNNEEIRK 1256
PTZ00121 PTZ00121
MAEBL; Provisional
 149-240 2.37e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.74  E-value: 2.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74760704   149 KAVQADQERERQRRLEVEREAEKKREAKQRAKEAQERELRKREKAEEKeRRRKEYDALKAAKREQEKKPKKEANQAPKSK 228
Cdd:PTZ00121 1498 KADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEK-KKADELKKAEELKKAEEKKKAEEAKKAEEDK 1576

                          90
                  ....*....|..
gi 74760704   229 SGSRPRKPPPRK 240
Cdd:PTZ00121 1577 NMALRKAEEAKK 1588
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 156-220 2.45e-03

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 37.71  E-value: 2.45e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74760704   156 ERERQRRLEVEREAEKKRE--AKQRAKEAQERELRKREKAEEKERRRKEYDALKAAKREQEKKPKKE 220
Cdd:pfam05672  28 EREEQERLEKEEEERLRKEelRRRAEEERARREEEARRLEEERRREEEERQRKAEEEAEEREQREQE 94
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 152-223 2.57e-03

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 37.71  E-value: 2.57e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74760704   152 QADQERERQRRLEVE----REAEKKREAKQRAKEAQERELRKREKAEEKERRRKEYDA-LKAAKREQEKKPKKEANQ 223
Cdd:pfam05672  40 EERLRKEELRRRAEEerarREEEARRLEEERRREEEERQRKAEEEAEEREQREQEEQErLQKQKEEAEAKAREEAER 116
PTZ00121 PTZ00121
MAEBL; Provisional
 133-235 2.70e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.35  E-value: 2.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74760704   133 DEKQCKQCANKVLQHMKAVQADQERERQRRLEVEREAEKKR--EAKQRAKEAQERELRKReKAEEKERRRKEYDALKAAK 210
Cdd:PTZ00121 1339 EEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKadAAKKKAEEKKKADEAKK-KAEEDKKKADELKKAAAAK 1417

                          90       100
                  ....*....|....*....|....*..
gi 74760704   211 R--EQEKKPKKEANQAPKSKSGSRPRK 235
Cdd:PTZ00121 1418 KkaDEAKKKAEEKKKADEAKKKAEEAK 1444
DDRGK pfam09756
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and ...
 166-221 3.15e-03

DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and vertebrates. They contain a highly conserved DDRGK motif.


Pssm-ID: 370664 [Multi-domain]  Cd Length: 188  Bit Score: 38.10  E-value: 3.15e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74760704   166 EREAEKKREAKQRAKEAQERELRK-----REKAEEKERRRKEYDALKAAKREQEKKPKKEA 221
Cdd:pfam09756   9 AKLELKEAKRQQREAEEEEREEREkleekREEEYKEREEREEEAEKEKEEEERKQEEEQER 69
SF-CC1 TIGR01622
splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors ...
 154-244 3.84e-03

splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors including the Pad-1 protein (N. crassa), CAPER (M. musculus) and CC1.3 (H.sapiens). These proteins are characterized by an N-terminal arginine-rich, low complexity domain followed by three (or in the case of 4 H. sapiens paralogs, two) RNA recognition domains (rrm: pfam00706). These splicing factors are closely related to the U2AF splicing factor family (TIGR01642). A homologous gene from Plasmodium falciparum was identified in the course of the analysis of that genome at TIGR and was included in the seed.


Pssm-ID: 273721 [Multi-domain]  Cd Length: 494  Bit Score: 38.75  E-value: 3.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74760704   154 DQERERQRRLEVEREAEKKREAKQRAKEA--QERELRKREKAEEKERRRKEYDALKAAKREQEKKPKKEANQAPKSKSGS 231
Cdd:TIGR01622  24 DKGRERSRDRSRDRERSRSRRRDRHRDRDyyRGRERRSRSRRPNRRYRPREKRRRRGDSYRRRRDDRRSRREKPRARDGT 103

                          90
                  ....*....|...
gi 74760704   232 RPRKPPPRKHTRS 244
Cdd:TIGR01622 104 PEPLTEDERDRRT 116
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 156-223 3.92e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 38.36  E-value: 3.92e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74760704   156 ERERQRRLEVEREAEKKREAKQRAKEA--QERELRKREKAEEKERRRKEYDALKAAKREQEKKPKKEANQ 223
Cdd:pfam13868 214 EQERKERQKEREEAEKKARQRQELQQAreEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEK 283
NtpE COG1390
Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal ...
 149-212 3.96e-03

Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 is part of the Pathway/BioSystem: A/V-type ATP synthase


Pssm-ID: 441000 [Multi-domain]  Cd Length: 196  Bit Score: 37.62  E-value: 3.96e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74760704 149 KAVQADQERERQR-RLEVEREAEK-KREAKQRAKEAQERELRKREKAEEKERRRKEYDALKAAKRE 212
Cdd:COG1390   9 EEILEEAEAEAEEiLEEAEEEAEKiLEEAEEEAEEIKEEILEKAEREAEREKRRIISSAELEARKE 74
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 133-228 4.00e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 38.63  E-value: 4.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74760704  133 DEKQCKQCANKvlQHMKAVQADQERERQRRLEVEREAEKKREAKQRAKEAQERELRKREKAEEKERRRKEYDALKA---- 208
Cdd:PRK09510  90 EELQQKQAAEQ--ERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAaaea 167

                         90       100
                 ....*....|....*....|....*..
gi 74760704  209 -------AKREQEKKPKKEANQAPKSK 228
Cdd:PRK09510 168 kkkaeaeAAKKAAAEAKKKAEAEAAAK 194
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 154-219 4.02e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 38.65  E-value: 4.02e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74760704  154 DQERE-RQRRLEVE---REAEKKREA-KQRAKEAQERELRKREKAEEKERrrkeyDALKAAKREQEKKPKK 219
Cdd:PRK00409 527 ELERElEQKAEEAEallKEAEKLKEElEEKKEKLQEEEDKLLEEAEKEAQ-----QAIKEAKKEADEIIKE 592
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 29-149 4.05e-03

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 38.68  E-value: 4.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74760704   29 EVPvKELAALPKATILDLSCNKLT-TLPSDFCGLTHLVKLDLSKNKLQ-------------------------QLPaDFG 82
Cdd:PLN00113 395 EIP-KSLGACRSLRRVRLQDNSFSgELPSEFTKLPLVYFLDISNNNLQgrinsrkwdmpslqmlslarnkffgGLP-DSF 472

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74760704   83 RLVNLQHLDLLNNKLV-TLPVSFAQLKNLKWLDLKDNpldpvlaKVAGDCLDE-KQCKQCANKVLQHMK 149
Cdd:PLN00113 473 GSKRLENLDLSRNQFSgAVPRKLGSLSELMQLKLSEN-------KLSGEIPDElSSCKKLVSLDLSHNQ 534
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 86-120 4.08e-03

Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains.


Pssm-ID: 463713 [Multi-domain]  Cd Length: 44  Bit Score: 34.53  E-value: 4.08e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 74760704    86 NLQHLDLLNNKLVTLPvSFAQLKNLKWLDLKDNPL 120
Cdd:pfam12799   2 NLEVLDLSNNQITDIP-PLAKLPNLETLDLSGNNK 35
PTZ00121 PTZ00121
MAEBL; Provisional
 134-226 4.26e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.97  E-value: 4.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74760704   134 EKQCKQCANKVLQHMKAVQADQERERQRRLEVEREAEKKREAKQRAKEAQERELRKREKAEEKERRRKEYDALKAAKREQ 213
Cdd:PTZ00121 1489 KKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEE 1568

                          90
                  ....*....|...
gi 74760704   214 EKKPKKEANQAPK 226
Cdd:PTZ00121 1569 AKKAEEDKNMALR 1581
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
151-221 4.57e-03

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 38.32  E-value: 4.57e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74760704 151 VQADQERERQR-RLEVEREAEKKREAKQRAKEaQERELRKREKA-----EEKERRRKEYDA-----LKAAKREQEKKPKK 219
Cdd:COG2268 249 KKAEERREAETaRAEAEAAYEIAEANAEREVQ-RQLEIAEREREielqeKEAEREEAELEAdvrkpAEAEKQAAEAEAEA 327


                ..
gi 74760704 220 EA 221
Cdd:COG2268 328 EA 329
CCDC47 pfam07946
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ...
 149-202 4.88e-03

PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of the PAT complex, an endoplasmic reticulum (ER)-resident membrane multiprotein complex that facilitates multi-pass membrane proteins insertion into membranes. The PAT complex, formed by CCDC47 and Asterix proteins, acts as an intramembrane chaperone by directly interacting with nascent transmembrane domains (TMDs), releasing its substrates upon correct folding, and is needed for optimal biogenesis of multi-pass membrane proteins. CCDC47 is required to maintain the stability of Asterix. CCDC47 is associated with various membrane-associated processes and is component of a ribosome-associated ER translocon complex involved in multi-pass membrane protein transport into the ER membrane and biogenesis. It is also involved in the regulation of calcium ion homeostasis in the ER, being also required for proper protein degradation via the ERAD (ER-associated degradation) pathway.


Pssm-ID: 462322  Cd Length: 323  Bit Score: 37.93  E-value: 4.88e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 74760704   149 KAVQADQERERQRRLEVEREAEKKREAKQRAKEAQERELRKREkaeEKERRRKE 202
Cdd:pfam07946 271 EKIKKAAEEERAEEAQEKKEEAKKKEREEKLAKLSPEEQRKYE---EKERKKEQ 321
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 40-118 5.16e-03

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 37.46  E-value: 5.16e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74760704  40 KATILDLSCNKLTTLPsDFCGLTHLVKLDLSKNKLQQLPaDFGRLVNLQHLDLLNNKLVTLPvSFAQLKNLKWLDLKDN 118
Cdd:cd21340   3 RITHLYLNDKNITKID-NLSLCKNLKVLYLYDNKITKIE-NLEFLTNLTHLYLQNNQIEKIE-NLENLVNLKKLYLGGN 78
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 152-224 5.17e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 38.38  E-value: 5.17e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74760704 152 QADQERERQRRLEVEREAEKKREAKQRAKEAQERELRKREKAEEKERRRKEYDALKAAKREQEKKPKKEANQA 224
Cdd:COG1196 408 AEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALA 480
PLN02316 PLN02316
synthase/transferase
 158-211 5.33e-03

synthase/transferase


Pssm-ID: 215180 [Multi-domain]  Cd Length: 1036  Bit Score: 38.31  E-value: 5.33e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 74760704   158 ERQRRLE--VEREAEKKREAKQRAKEAQERELRKREKAEEK----ERRRKEYDALKAAKR 211
Cdd:PLN02316  253 EKRRELEklAKEEAERERQAEEQRRREEEKAAMEADRAQAKaeveKRREKLQNLLKKASR 312
PTZ00121 PTZ00121
MAEBL; Provisional
 149-235 5.93e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.58  E-value: 5.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74760704   149 KAVQADQERERQRRLEVER--EAEKKREAKQRAKEAQERELRKRE--KAEEKERRRKEydalkAAKREQEKKPKKEANQA 224
Cdd:PTZ00121 1690 AAEALKKEAEEAKKAEELKkkEAEEKKKAEELKKAEEENKIKAEEakKEAEEDKKKAE-----EAKKDEEEKKKIAHLKK 1764

                          90
                  ....*....|.
gi 74760704   225 PKSKSGSRPRK 235
Cdd:PTZ00121 1765 EEEKKAEEIRK 1775
PTZ00121 PTZ00121
MAEBL; Provisional
 133-229 5.98e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.58  E-value: 5.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74760704   133 DEKQCKQCANKVLQHMKAVQADQERERQRRLEVEREAEKKR----------EAKQRAKEAQERELRKREKAE-EKERRRK 201
Cdd:PTZ00121 1275 EEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKkadeakkkaeEAKKKADAAKKKAEEAKKAAEaAKAEAEA 1354

                          90       100
                  ....*....|....*....|....*...
gi 74760704   202 EYDALKAAKREQEKKPKKEANQAPKSKS 229
Cdd:PTZ00121 1355 AADEAEAAEEKAEAAEKKKEEAKKKADA 1382
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 149-215 6.78e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 37.99  E-value: 6.78e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74760704 149 KAVQADQERERQRRLEVEREAEKKREAKQRAKEAQERELRKREKAEEKERRRKEYDALKAAKREQEK 215
Cdd:COG1196 302 QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368
PTZ00121 PTZ00121
MAEBL; Provisional
 133-235 6.94e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.20  E-value: 6.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74760704   133 DEKQCKQCANKVLQHMKAVQADQ--ERERQRRLEVEREAEKKREAKQRAKEAQERelRKREKAEEKERRRKEYDALK--- 207
Cdd:PTZ00121 1376 AKKKADAAKKKAEEKKKADEAKKkaEEDKKKADELKKAAAAKKKADEAKKKAEEK--KKADEAKKKAEEAKKADEAKkka 1453

                          90       100       110
                  ....*....|....*....|....*....|
gi 74760704   208 --AAKREQEKKPKKEANQAPKSKSGSRPRK 235
Cdd:PTZ00121 1454 eeAKKAEEAKKKAEEAKKADEAKKKAEEAK 1483
Caldesmon pfam02029
Caldesmon;
149-236 8.20e-03

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 37.54  E-value: 8.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74760704   149 KAVQADQERERQRRLEVEREAEKKREAKQRAKEAQERELRKREKAEEKERRRKEYDALKAAKREQEKKPKKEANQAPKSK 228
Cdd:pfam02029 122 DSRLGRYKEEETEIREKEYQENKWSTEVRQAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQK 201


                  ....*...
gi 74760704   229 SGSRPRKP 236
Cdd:pfam02029 202 RGHPEVKS 209
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 150-224 8.90e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 37.61  E-value: 8.90e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74760704 150 AVQADQERERQRRLEVEREAEKKREAKQRAKEAQERELRKREKAEEKERRRKEYDALKAAKREQEKKPKKEANQA 224
Cdd:COG1196 326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400
DUF612 pfam04747
Protein of unknown function, DUF612; This family includes several uncharacterized proteins ...
 146-223 9.40e-03

Protein of unknown function, DUF612; This family includes several uncharacterized proteins from Caenorhabditis elegans.


Pssm-ID: 282585 [Multi-domain]  Cd Length: 511  Bit Score: 37.35  E-value: 9.40e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74760704   146 QHMKAVQADQERERQRRLEVEREAEKKREAKQRAKEAQERELRKREKAEEKERRRKEYDALKAAKREQEKKPKKEANQ 223
Cdd:pfam04747  50 QRKEAFASLELTEQPQQVEKVKKSEKKKAQKQIAKDHEAEQKVNAKKAAEKEARRAEAEAKKRAAQEEEHKQWKAEQE 127
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
156-219 9.88e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 37.74  E-value: 9.88e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74760704  156 ERERQRRLEVEREAEKKREaKQRAKEAQERELRKREKAEEKERRRKEYDALKAAKREQEKKPKK 219
Cdd:PRK03918 347 LKELEKRLEELEERHELYE-EAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISK 409
 
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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