|
Name |
Accession |
Description |
Interval |
E-value |
| Jnk-SapK_ap_N |
pfam09744 |
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins ... |
29-184 |
5.73e-73 |
|
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins conserved from yeasts to humans. Most of the proteins in this entry have an RhoGEF pfam00621 domain at their C-terminal end.
Pssm-ID: 462875 [Multi-domain] Cd Length: 150 Bit Score: 239.44 E-value: 5.73e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 29 VSGLAGSIYREFERLIHCYDEEVVKELMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRKQAEEKF 108
Cdd:pfam09744 1 VYDLASSIGKEFERLIDRYGEDVVKGLMPKVVNVLELLESLASRNQEHNVELEELREDNEQLETQYEREKALRKRAEEEL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564370964 109 IEFEDALEQEKKELQIQVEHYEFQTRQLElkaknyADQISRLEERESEMKKEYNALHQRHTEMIQTYVEHIERSKM 184
Cdd:pfam09744 81 EEIEDQWEQETKDLLSQVESLEEENRRLE------ADHVSRLEEKEAELKKEYSKLHERETEVLRKLKEVVDRQRD 150
|
|
| WD40_2 |
pfam19056 |
WD40 repeated domain; This entry contains an array of WD40 repeats found in RhoGEF proteins. |
925-1141 |
8.32e-47 |
|
WD40 repeated domain; This entry contains an array of WD40 repeats found in RhoGEF proteins.
Pssm-ID: 465964 Cd Length: 487 Bit Score: 175.98 E-value: 8.32e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 925 EPSGESSATTSSAAPTMWLGAQNGWLYVHSAVANWKKCL--HSIKLKDSVLSLVHVKGRVLVALADGTLAIFHRGEDGQW 1002
Cdd:pfam19056 88 EEAVRAERTAKKPGPTICLGLEDGSISVYGSVDTAKKCLlqHFTPERSPVLCLKHSPQFLFAGLVNGKVAVYARAEDGLW 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 1003 DLSNYHLMDLGHphHSIRCMAVVDDRVWCGYKNKVHVIQPKTMQIEKSFDAHPRRESQVRQLAWIGDGVWVSIRLDSTLR 1082
Cdd:pfam19056 168 DPEPPKLVKLGV--LPVRSLLALEDTVWASCGNQVTVISGETLQTEQSFEAHQDEGMSVSHMVVAGGGVWMAFSSGSSIR 245
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 564370964 1083 LYHAHTHQHLQDVDIEPYVSKMLGtgklGFSFVRITALLIAGNRLWVGTGNGVVISIPL 1141
Cdd:pfam19056 246 LFHTETLEHLQDINIATRVHFMLP----GQKRVSVTSLLICQGLLWVGTNLGVIVALPV 300
|
|
| JIP_LZII |
pfam16471 |
JNK-interacting protein leucine zipper II; This is the second leucine zipper domain (LZII) of ... |
386-454 |
5.86e-28 |
|
JNK-interacting protein leucine zipper II; This is the second leucine zipper domain (LZII) of several JNK-interacting proteins (JIP). It interacts with the small GTP-binding protein ARF6.
Pssm-ID: 465127 [Multi-domain] Cd Length: 69 Bit Score: 107.78 E-value: 5.86e-28
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564370964 386 MGKEVGNLLLENSQLLETKNALNVVKNDLIAKVDQLSGEQEVLKGELEAAKQAKVKLENRIKELEEELK 454
Cdd:pfam16471 1 MGKEVENLIAENTELLATKNALNIVKDDLIARVDELSSEQEQLREELKALQAAKEKLKKRIKELEEELK 69
|
|
| RILP-like |
cd14445 |
Rab interacting lysosomal protein-like 1 and 2 (Rilpl1 and Rilpl2); This domain is found in ... |
32-103 |
5.40e-12 |
|
Rab interacting lysosomal protein-like 1 and 2 (Rilpl1 and Rilpl2); This domain is found in Rab interacting lysosomal protein-like 1 and 2, and appears to be conserved in Bilateria. The Rilp-like proteins regulate the concentration of ciliary membrane proteins in the primary cilium. Rilpl2 interacts with myosin-Va and has been linked to the regulation of cellular morphology in neurons; it forms a complex with Rac1 and activates Rac1-Pak signaling, dependent on myosin-Va.
Pssm-ID: 271220 [Multi-domain] Cd Length: 89 Bit Score: 63.00 E-value: 5.40e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564370964 32 LAGSIYREFERLIHCYDEEVVKELMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLltqyEREKALRKQ 103
Cdd:cd14445 21 IASAIGKEFERLIDRYGPEAVAGLMPKVVRVLELLEALASRNERENLEIEELRLEVDRL----ELEKRERAQ 88
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
61-182 |
4.44e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 51.17 E-value: 4.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 61 NVLENLDSVLSENQEH-----------EVELELLREDNEQL---LTQYERE-KALRKQAEEKFIEFEDaLEQEKKELQIQ 125
Cdd:TIGR04523 321 KKLEEIQNQISQNNKIisqlneqisqlKKELTNSESENSEKqreLEEKQNEiEKLKKENQSYKQEIKN-LESQINDLESK 399
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564370964 126 VEHYEFQTRQLE-------------------LKAKNY--ADQISRLEERESEMKKEYNALHQRhTEMIQTYVEHIERS 182
Cdd:TIGR04523 400 IQNQEKLNQQKDeqikklqqekellekeierLKETIIknNSEIKDLTNQDSVKELIIKNLDNT-RESLETQLKVLSRS 476
|
|
| COG3292 |
COG3292 |
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms]; |
1015-1137 |
1.07e-05 |
|
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
Pssm-ID: 442521 [Multi-domain] Cd Length: 924 Bit Score: 49.99 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 1015 PHHSIRCMAVVDD-----RVWCG-YKNKVHVIQPKTMQIeKSFDAHPRRESQVRQLAWIGDG-VWVSIRlDSTLRLYHAH 1087
Cdd:COG3292 265 SGNSVRSIAEDSDgnlwiRLWIGtYGGGLFRLDPKTGKF-KRYNPNGLPSNSVYSILEDSDGnLWIGTS-GGGLYRYDPK 342
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 564370964 1088 THQhlqdvdIEPYvskmlgTGKLGFSFVRITALLI-AGNRLWVGTGNGVVI 1137
Cdd:COG3292 343 TGK------FTKF------SEDNGLSNNFIRSILEdSDGNLWVGTNGGLYR 381
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
79-181 |
8.14e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 8.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 79 ELELLREDNEQLLTQYEREKALRKQAEEKFIEFEDALEQ----EKKELQIQVEHYEFQTRQLELKAKNYADQISRLEERE 154
Cdd:COG4913 296 ELEELRAELARLEAELERLEARLDALREELDELEAQIRGnggdRLEQLEREIERLERELEERERRRARLEALLAALGLPL 375
|
90 100
....*....|....*....|....*..
gi 564370964 155 SEMKKEYNALHQRHTEMIQTYVEHIER 181
Cdd:COG4913 376 PASAEEFAALRAEAAALLEALEEELEA 402
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
33-164 |
8.64e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 8.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 33 AGSIYREFERLIHCYDEEVVKE--LMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRKQAEEKFIE 110
Cdd:PRK03918 167 LGEVIKEIKRRIERLEKFIKRTenIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKE 246
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 564370964 111 FEdALEQEKKELQIQVEHYEFQTRQLELKAKNYADQISRLEEREsEMKKEYNAL 164
Cdd:PRK03918 247 LE-SLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELK-EKAEEYIKL 298
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
41-540 |
9.40e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.98 E-value: 9.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 41 ERLIHCYDEEVvKELMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLLTQY----EREKALRKQAEE---KFIEFED 113
Cdd:TIGR02169 307 ERSIAEKEREL-EDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYaelkEELEDLRAELEEvdkEFAETRD 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 114 ALEQEKKEL-QIQVEHYEFQTRQLELKaknyaDQISRLEERESEMKKEYNALHQRHTEM------IQTYVEHIERSKMQQ 186
Cdd:TIGR02169 386 ELKDYREKLeKLKREINELKRELDRLQ-----EELQRLSEELADLNAAIAGIEAKINELeeekedKALEIKKQEWKLEQL 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 187 VGGGGQTESSLpgRSRKERPTSLNvfpladgmcpnDEMSESgQSSAAATPSTTGTKSNTPTSSvpSAAVTPLNESLQplG 266
Cdd:TIGR02169 461 AADLSKYEQEL--YDLKEEYDRVE-----------KELSKL-QRELAEAEAQARASEERVRGG--RAVEEVLKASIQ--G 522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 267 DYGSVTKNNKRarEKRNSRNMEVQVTQEMRNVSIgmgssDEWSDVQDIIDSTPELDVCPET-----RLDRTGSSPTQGIV 341
Cdd:TIGR02169 523 VHGTVAQLGSV--GERYATAIEVAAGNRLNNVVV-----EDDAVAKEAIELLKRRKAGRATflplnKMRDERRDLSILSE 595
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 342 NKAFGINTDSLYHE--LSTAGSEVIGD------VDEGADLLGEFSvrddFFGMGKEvgnlLLENSQLL----ETKNALNV 409
Cdd:TIGR02169 596 DGVIGFAVDLVEFDpkYEPAFKYVFGDtlvvedIEAARRLMGKYR----MVTLEGE----LFEKSGAMtggsRAPRGGIL 667
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 410 VKNDLIAKVDQLSGEQEVLKGELEAAKQAKVKLENRIKELEEELKRVKSEAVTARRE----------PREEVEDVSSYLc 479
Cdd:TIGR02169 668 FSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEieqleqeeekLKERLEELEEDL- 746
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564370964 480 TELDkipmaQRRRFTRVEMARVLMERNQYKERLMELQEAVrwtEMIRASREHPSVQEKKKS 540
Cdd:TIGR02169 747 SSLE-----QEIENVKSELKELEARIEELEEDLHKLEEAL---NDLEARLSHSRIPEIQAE 799
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
380-530 |
2.73e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 44.53 E-value: 2.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 380 RDDFFGMGKEVGNLLLENSQLLETKNALNVVKNDLIAKVDQLSGEQEVLKGELEAAKQAKVKLENRIKELEEE---LKRV 456
Cdd:pfam00038 60 RRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEElafLKKN 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 457 KSEAVtarREPREEVED------VSSYLCTELDKIpMAQRRRFTRVEMARVLME-RNQYKERLMELQEAV-RWTEMIRAS 528
Cdd:pfam00038 140 HEEEV---RELQAQVSDtqvnveMDAARKLDLTSA-LAEIRAQYEEIAAKNREEaEEWYQSKLEELQQAAaRNGDALRSA 215
|
..
gi 564370964 529 RE 530
Cdd:pfam00038 216 KE 217
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
63-521 |
2.96e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 2.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 63 LENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRKQAEEKFIEFEDALE-----QEKKELQIQVEHYEFQTRQLE 137
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllplyQELEALEAELAELPERLEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 138 LKAKNYADQISRLEERESE-------------------------MKKEYNALHQRHTEmIQTYVEHIERSKMQQVGGGGQ 192
Cdd:COG4717 153 ERLEELRELEEELEELEAElaelqeeleelleqlslateeelqdLAEELEELQQRLAE-LEEELEEAQEELEELEEELEQ 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 193 TESSLPGRSRKERPTSLNVFPLAdgmcpndemsesgqssAAATPSTTGTKSNTPTSSVPSAAVTPLNESLQPLGDYGSVt 272
Cdd:COG4717 232 LENELEAAALEERLKEARLLLLI----------------AAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLA- 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 273 knnkRAREKRNSRNMEVQVTQEMRNVsigmgSSDEWSDVQDIIDSTPELDVCPETRLDRTGSSpTQGIVNKAfgintDSL 352
Cdd:COG4717 295 ----REKASLGKEAEELQALPALEEL-----EEEELEELLAALGLPPDLSPEELLELLDRIEE-LQELLREA-----EEL 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 353 YHELSTAGSEvigdvDEGADLLGEFSVRDDffgmgKEVGNLLLENSQLLETKNALNVVKNDLIAKVDQLS-----GEQEV 427
Cdd:COG4717 360 EEELQLEELE-----QEIAALLAEAGVEDE-----EELRAALEQAEEYQELKEELEELEEQLEELLGELEelleaLDEEE 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 428 LKGELEAAKQAKVKLENRIKELEEELKRVKSEavTARREPREEVEDVSSYLCTELDKIpMAQRRRFTRVEMARVLME--R 505
Cdd:COG4717 430 LEEELEELEEELEELEEELEELREELAELEAE--LEQLEEDGELAELLQELEELKAEL-RELAEEWAALKLALELLEeaR 506
|
490
....*....|....*...
gi 564370964 506 NQYKERLME--LQEAVRW 521
Cdd:COG4717 507 EEYREERLPpvLERASEY 524
|
|
| PRK12495 |
PRK12495 |
hypothetical protein; Provisional |
834-938 |
2.33e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 183558 [Multi-domain] Cd Length: 226 Bit Score: 41.01 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 834 SRGDTPVLDKGQG-DVAATANGKVNPSQSTEEATEATEVPDPGPSESEA-------TTVRPGPLTEHVFTDPAPTqsSST 905
Cdd:PRK12495 69 TEDGAAGDDAGDGaEATAPSDAGSQASPDDDAQPAAEAEAADQSAPPEAsstsatdEAATDPPATAAARDGPTPD--PTA 146
|
90 100 110
....*....|....*....|....*....|...
gi 564370964 906 QPASENGSESDGSIVQPQVEPSGESSATTSSAA 938
Cdd:PRK12495 147 QPATPDERRSPRQRPPVSGEPPTPSTPDAHVAG 179
|
|
| DUF4045 |
pfam13254 |
Domain of unknown function (DUF4045); This presumed domain is functionally uncharacterized. ... |
834-918 |
3.73e-03 |
|
Domain of unknown function (DUF4045); This presumed domain is functionally uncharacterized. This domain family is found in bacteria and eukaryotes, and is typically between 384 and 430 amino acids in length.
Pssm-ID: 433066 [Multi-domain] Cd Length: 415 Bit Score: 41.31 E-value: 3.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 834 SRGDTPVldKGQGDVAATANGKVNPSQSTEEATEATEVPD--PGPSESEATTVRPGPLTEH------VFTDPA-PTQSSS 904
Cdd:pfam13254 37 SRQNSFA--SNRGSVAGPSGSLSPGLSPTKLSREGSPESTsrPSSSHSEATIVRHSKDDERpstpdeGFVKPAlPRHSRS 114
|
90
....*....|....
gi 564370964 905 TQPASENGSESDGS 918
Cdd:pfam13254 115 SSALSNTGSEEDSP 128
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
86-181 |
4.10e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 39.10 E-value: 4.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 86 DNEQLLTQYEREKALRKQAEEKFIEFEDALEQEKKELQIQVEhyEFQTRQLELKAKNYADQISRLEERESEMKKEYNA-- 163
Cdd:smart00935 5 DVQKILQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKE--KLQKDAATLSEAAREKKEKELQKKVQEFQRKQQKlq 82
|
90 100
....*....|....*....|
gi 564370964 164 --LHQRHTEMIQTYVEHIER 181
Cdd:smart00935 83 qdLQKRQQEELQKILDKINK 102
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
389-542 |
5.23e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 5.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 389 EVGNLLLENSQLLETK----NALNVVKNDLIAKVDQLSGEQEVL---KGELEAAK-------QAKVKLENRIKELEEELK 454
Cdd:PRK03918 190 NIEELIKEKEKELEEVlreiNEISSELPELREELEKLEKEVKELeelKEEIEELEkelesleGSKRKLEEKIRELEERIE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 455 RVKSEAvtarREPREEVEDVssylcTELDKipmaqrrrftRVEMARVLME-RNQYKERLMELQ-EAVRWTEMIRASREHP 532
Cdd:PRK03918 270 ELKKEI----EELEEKVKEL-----KELKE----------KAEEYIKLSEfYEEYLDELREIEkRLSRLEEEINGIEERI 330
|
170
....*....|
gi 564370964 533 SVQEKKKSTI 542
Cdd:PRK03918 331 KELEEKEERL 340
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Jnk-SapK_ap_N |
pfam09744 |
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins ... |
29-184 |
5.73e-73 |
|
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins conserved from yeasts to humans. Most of the proteins in this entry have an RhoGEF pfam00621 domain at their C-terminal end.
Pssm-ID: 462875 [Multi-domain] Cd Length: 150 Bit Score: 239.44 E-value: 5.73e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 29 VSGLAGSIYREFERLIHCYDEEVVKELMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRKQAEEKF 108
Cdd:pfam09744 1 VYDLASSIGKEFERLIDRYGEDVVKGLMPKVVNVLELLESLASRNQEHNVELEELREDNEQLETQYEREKALRKRAEEEL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564370964 109 IEFEDALEQEKKELQIQVEHYEFQTRQLElkaknyADQISRLEERESEMKKEYNALHQRHTEMIQTYVEHIERSKM 184
Cdd:pfam09744 81 EEIEDQWEQETKDLLSQVESLEEENRRLE------ADHVSRLEEKEAELKKEYSKLHERETEVLRKLKEVVDRQRD 150
|
|
| WD40_2 |
pfam19056 |
WD40 repeated domain; This entry contains an array of WD40 repeats found in RhoGEF proteins. |
925-1141 |
8.32e-47 |
|
WD40 repeated domain; This entry contains an array of WD40 repeats found in RhoGEF proteins.
Pssm-ID: 465964 Cd Length: 487 Bit Score: 175.98 E-value: 8.32e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 925 EPSGESSATTSSAAPTMWLGAQNGWLYVHSAVANWKKCL--HSIKLKDSVLSLVHVKGRVLVALADGTLAIFHRGEDGQW 1002
Cdd:pfam19056 88 EEAVRAERTAKKPGPTICLGLEDGSISVYGSVDTAKKCLlqHFTPERSPVLCLKHSPQFLFAGLVNGKVAVYARAEDGLW 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 1003 DLSNYHLMDLGHphHSIRCMAVVDDRVWCGYKNKVHVIQPKTMQIEKSFDAHPRRESQVRQLAWIGDGVWVSIRLDSTLR 1082
Cdd:pfam19056 168 DPEPPKLVKLGV--LPVRSLLALEDTVWASCGNQVTVISGETLQTEQSFEAHQDEGMSVSHMVVAGGGVWMAFSSGSSIR 245
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 564370964 1083 LYHAHTHQHLQDVDIEPYVSKMLGtgklGFSFVRITALLIAGNRLWVGTGNGVVISIPL 1141
Cdd:pfam19056 246 LFHTETLEHLQDINIATRVHFMLP----GQKRVSVTSLLICQGLLWVGTNLGVIVALPV 300
|
|
| JIP_LZII |
pfam16471 |
JNK-interacting protein leucine zipper II; This is the second leucine zipper domain (LZII) of ... |
386-454 |
5.86e-28 |
|
JNK-interacting protein leucine zipper II; This is the second leucine zipper domain (LZII) of several JNK-interacting proteins (JIP). It interacts with the small GTP-binding protein ARF6.
Pssm-ID: 465127 [Multi-domain] Cd Length: 69 Bit Score: 107.78 E-value: 5.86e-28
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564370964 386 MGKEVGNLLLENSQLLETKNALNVVKNDLIAKVDQLSGEQEVLKGELEAAKQAKVKLENRIKELEEELK 454
Cdd:pfam16471 1 MGKEVENLIAENTELLATKNALNIVKDDLIARVDELSSEQEQLREELKALQAAKEKLKKRIKELEEELK 69
|
|
| RILP-like |
cd14445 |
Rab interacting lysosomal protein-like 1 and 2 (Rilpl1 and Rilpl2); This domain is found in ... |
32-103 |
5.40e-12 |
|
Rab interacting lysosomal protein-like 1 and 2 (Rilpl1 and Rilpl2); This domain is found in Rab interacting lysosomal protein-like 1 and 2, and appears to be conserved in Bilateria. The Rilp-like proteins regulate the concentration of ciliary membrane proteins in the primary cilium. Rilpl2 interacts with myosin-Va and has been linked to the regulation of cellular morphology in neurons; it forms a complex with Rac1 and activates Rac1-Pak signaling, dependent on myosin-Va.
Pssm-ID: 271220 [Multi-domain] Cd Length: 89 Bit Score: 63.00 E-value: 5.40e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564370964 32 LAGSIYREFERLIHCYDEEVVKELMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLltqyEREKALRKQ 103
Cdd:cd14445 21 IASAIGKEFERLIDRYGPEAVAGLMPKVVRVLELLEALASRNERENLEIEELRLEVDRL----ELEKRERAQ 88
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
61-182 |
4.44e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 51.17 E-value: 4.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 61 NVLENLDSVLSENQEH-----------EVELELLREDNEQL---LTQYERE-KALRKQAEEKFIEFEDaLEQEKKELQIQ 125
Cdd:TIGR04523 321 KKLEEIQNQISQNNKIisqlneqisqlKKELTNSESENSEKqreLEEKQNEiEKLKKENQSYKQEIKN-LESQINDLESK 399
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564370964 126 VEHYEFQTRQLE-------------------LKAKNY--ADQISRLEERESEMKKEYNALHQRhTEMIQTYVEHIERS 182
Cdd:TIGR04523 400 IQNQEKLNQQKDeqikklqqekellekeierLKETIIknNSEIKDLTNQDSVKELIIKNLDNT-RESLETQLKVLSRS 476
|
|
| COG3292 |
COG3292 |
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms]; |
1015-1137 |
1.07e-05 |
|
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
Pssm-ID: 442521 [Multi-domain] Cd Length: 924 Bit Score: 49.99 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 1015 PHHSIRCMAVVDD-----RVWCG-YKNKVHVIQPKTMQIeKSFDAHPRRESQVRQLAWIGDG-VWVSIRlDSTLRLYHAH 1087
Cdd:COG3292 265 SGNSVRSIAEDSDgnlwiRLWIGtYGGGLFRLDPKTGKF-KRYNPNGLPSNSVYSILEDSDGnLWIGTS-GGGLYRYDPK 342
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 564370964 1088 THQhlqdvdIEPYvskmlgTGKLGFSFVRITALLI-AGNRLWVGTGNGVVI 1137
Cdd:COG3292 343 TGK------FTKF------SEDNGLSNNFIRSILEdSDGNLWVGTNGGLYR 381
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
39-185 |
1.33e-05 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 49.47 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 39 EFERLIHCYDEEVvKELMPLVVNVleNLDSVLSENQEHEVELELLREdneqlltQYEREKALRKQAEEKFIEFEDALEQ- 117
Cdd:pfam06160 234 NVDKEIQQLEEQL-EENLALLENL--ELDEAEEALEEIEERIDQLYD-------LLEKEVDAKKYVEKNLPEIEDYLEHa 303
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564370964 118 --EKKELQIQVEH----YEFQTRQLElKAKNYADQISRLEERESEMKKEYNALHQRHTEmIQTYVEHIERSKMQ 185
Cdd:pfam06160 304 eeQNKELKEELERvqqsYTLNENELE-RVRGLEKQLEELEKRYDEIVERLEEKEVAYSE-LQEELEEILEQLEE 375
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
70-160 |
6.05e-05 |
|
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: 46.84 E-value: 6.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 70 LSENQEHEVELELLREDNEQLLTQYEREKALRKQAEEKFIEfedaLEQEKKELQIQVEHYEFQTRQLELKAKNYADQISR 149
Cdd:pfam13868 237 LQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIE----QEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREE 312
|
90
....*....|..
gi 564370964 150 -LEERESEMKKE 160
Cdd:pfam13868 313 eLEEGERLREEE 324
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
79-181 |
8.14e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 8.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 79 ELELLREDNEQLLTQYEREKALRKQAEEKFIEFEDALEQ----EKKELQIQVEHYEFQTRQLELKAKNYADQISRLEERE 154
Cdd:COG4913 296 ELEELRAELARLEAELERLEARLDALREELDELEAQIRGnggdRLEQLEREIERLERELEERERRRARLEALLAALGLPL 375
|
90 100
....*....|....*....|....*..
gi 564370964 155 SEMKKEYNALHQRHTEMIQTYVEHIER 181
Cdd:COG4913 376 PASAEEFAALRAEAAALLEALEEELEA 402
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
33-164 |
8.64e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 8.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 33 AGSIYREFERLIHCYDEEVVKE--LMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRKQAEEKFIE 110
Cdd:PRK03918 167 LGEVIKEIKRRIERLEKFIKRTenIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKE 246
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 564370964 111 FEdALEQEKKELQIQVEHYEFQTRQLELKAKNYADQISRLEEREsEMKKEYNAL 164
Cdd:PRK03918 247 LE-SLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELK-EKAEEYIKL 298
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
41-540 |
9.40e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.98 E-value: 9.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 41 ERLIHCYDEEVvKELMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLLTQY----EREKALRKQAEE---KFIEFED 113
Cdd:TIGR02169 307 ERSIAEKEREL-EDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYaelkEELEDLRAELEEvdkEFAETRD 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 114 ALEQEKKEL-QIQVEHYEFQTRQLELKaknyaDQISRLEERESEMKKEYNALHQRHTEM------IQTYVEHIERSKMQQ 186
Cdd:TIGR02169 386 ELKDYREKLeKLKREINELKRELDRLQ-----EELQRLSEELADLNAAIAGIEAKINELeeekedKALEIKKQEWKLEQL 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 187 VGGGGQTESSLpgRSRKERPTSLNvfpladgmcpnDEMSESgQSSAAATPSTTGTKSNTPTSSvpSAAVTPLNESLQplG 266
Cdd:TIGR02169 461 AADLSKYEQEL--YDLKEEYDRVE-----------KELSKL-QRELAEAEAQARASEERVRGG--RAVEEVLKASIQ--G 522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 267 DYGSVTKNNKRarEKRNSRNMEVQVTQEMRNVSIgmgssDEWSDVQDIIDSTPELDVCPET-----RLDRTGSSPTQGIV 341
Cdd:TIGR02169 523 VHGTVAQLGSV--GERYATAIEVAAGNRLNNVVV-----EDDAVAKEAIELLKRRKAGRATflplnKMRDERRDLSILSE 595
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 342 NKAFGINTDSLYHE--LSTAGSEVIGD------VDEGADLLGEFSvrddFFGMGKEvgnlLLENSQLL----ETKNALNV 409
Cdd:TIGR02169 596 DGVIGFAVDLVEFDpkYEPAFKYVFGDtlvvedIEAARRLMGKYR----MVTLEGE----LFEKSGAMtggsRAPRGGIL 667
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 410 VKNDLIAKVDQLSGEQEVLKGELEAAKQAKVKLENRIKELEEELKRVKSEAVTARRE----------PREEVEDVSSYLc 479
Cdd:TIGR02169 668 FSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEieqleqeeekLKERLEELEEDL- 746
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564370964 480 TELDkipmaQRRRFTRVEMARVLMERNQYKERLMELQEAVrwtEMIRASREHPSVQEKKKS 540
Cdd:TIGR02169 747 SSLE-----QEIENVKSELKELEARIEELEEDLHKLEEAL---NDLEARLSHSRIPEIQAE 799
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
66-167 |
1.07e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.85 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 66 LDSVLSENQEHEVELELLREDNEQLLTQYEREKALRKQAEEKFIEFEDALEQEKKELQI---QVEHYEFQTRQLELKAKN 142
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEllaELARLEQDIARLEERRRE 313
|
90 100
....*....|....*....|....*
gi 564370964 143 YADQISRLEERESEMKKEYNALHQR 167
Cdd:COG1196 314 LEERLEELEEELAELEEELEELEEE 338
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
48-182 |
1.36e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 48 DEEVVKELMPLVVNVLENLDSVLSE--NQEHEVELELLREDNEQLLTQY--EREKALRKQAEEKfiEFEDALEQEKKELQ 123
Cdd:COG4717 331 PPDLSPEELLELLDRIEELQELLREaeELEEELQLEELEQEIAALLAEAgvEDEEELRAALEQA--EEYQELKEELEELE 408
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564370964 124 IQVE-HYEFQTRQLE-LKAKNYADQISRLEERESEMKKEYNALHQRHTEmIQTYVEHIERS 182
Cdd:COG4717 409 EQLEeLLGELEELLEaLDEEELEEELEELEEELEELEEELEELREELAE-LEAELEQLEED 468
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
72-224 |
1.70e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.92 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 72 ENQEHEVELELlREDNEQLLTQYEREKALR----KQAEEKFIEFE-------DALEQEKKELQIQVEHYEFQTRQLELKA 140
Cdd:PRK12704 52 EAIKKEALLEA-KEEIHKLRNEFEKELRERrnelQKLEKRLLQKEenldrklELLEKREEELEKKEKELEQKQQELEKKE 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 141 KNY----ADQISRLEE---------RE---SEMKKEynALHQRhTEMIQTYVEHIE-----RSK------MQQVGGGGQT 193
Cdd:PRK12704 131 EELeeliEEQLQELERisgltaeeaKEillEKVEEE--ARHEA-AVLIKEIEEEAKeeadkKAKeilaqaIQRCAADHVA 207
|
170 180 190
....*....|....*....|....*....|.
gi 564370964 194 EsslpgrsrkerpTSLNVFPLadgmcPNDEM 224
Cdd:PRK12704 208 E------------TTVSVVNL-----PNDEM 221
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
64-160 |
2.43e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.40 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 64 ENLDSVLSENQEHEVELELLREDNEQ--------------LLTQYEREKALRKQAEEKFIEFEDA-------LEQEKKEL 122
Cdd:TIGR04523 412 EQIKKLQQEKELLEKEIERLKETIIKnnseikdltnqdsvKELIIKNLDNTRESLETQLKVLSRSinkikqnLEQKQKEL 491
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 564370964 123 QIQV-EHYEF--QTRQLELKAKNYADQISRLEERESEMKKE 160
Cdd:TIGR04523 492 KSKEkELKKLneEKKELEEKVKDLTKKISSLKEKIEKLESE 532
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
397-523 |
2.49e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.82 E-value: 2.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 397 NSQLLETKNALNVVK---NDLIAKVDQLSGEQEVLKGELEAAKQAKVKLENRIKELEEELKRVKSEAVTARRE------- 466
Cdd:TIGR02168 322 EAQLEELESKLDELAeelAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQiaslnne 401
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 467 ---PREEVEDVSSYLcTELDKIPMAQRRRFTRVEMARVLMERNQYKERLMELQEAVRWTE 523
Cdd:TIGR02168 402 ierLEARLERLEDRR-ERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLE 460
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
380-530 |
2.73e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 44.53 E-value: 2.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 380 RDDFFGMGKEVGNLLLENSQLLETKNALNVVKNDLIAKVDQLSGEQEVLKGELEAAKQAKVKLENRIKELEEE---LKRV 456
Cdd:pfam00038 60 RRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEElafLKKN 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 457 KSEAVtarREPREEVED------VSSYLCTELDKIpMAQRRRFTRVEMARVLME-RNQYKERLMELQEAV-RWTEMIRAS 528
Cdd:pfam00038 140 HEEEV---RELQAQVSDtqvnveMDAARKLDLTSA-LAEIRAQYEEIAAKNREEaEEWYQSKLEELQQAAaRNGDALRSA 215
|
..
gi 564370964 529 RE 530
Cdd:pfam00038 216 KE 217
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
63-521 |
2.96e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 2.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 63 LENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRKQAEEKFIEFEDALE-----QEKKELQIQVEHYEFQTRQLE 137
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllplyQELEALEAELAELPERLEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 138 LKAKNYADQISRLEERESE-------------------------MKKEYNALHQRHTEmIQTYVEHIERSKMQQVGGGGQ 192
Cdd:COG4717 153 ERLEELRELEEELEELEAElaelqeeleelleqlslateeelqdLAEELEELQQRLAE-LEEELEEAQEELEELEEELEQ 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 193 TESSLPGRSRKERPTSLNVFPLAdgmcpndemsesgqssAAATPSTTGTKSNTPTSSVPSAAVTPLNESLQPLGDYGSVt 272
Cdd:COG4717 232 LENELEAAALEERLKEARLLLLI----------------AAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLA- 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 273 knnkRAREKRNSRNMEVQVTQEMRNVsigmgSSDEWSDVQDIIDSTPELDVCPETRLDRTGSSpTQGIVNKAfgintDSL 352
Cdd:COG4717 295 ----REKASLGKEAEELQALPALEEL-----EEEELEELLAALGLPPDLSPEELLELLDRIEE-LQELLREA-----EEL 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 353 YHELSTAGSEvigdvDEGADLLGEFSVRDDffgmgKEVGNLLLENSQLLETKNALNVVKNDLIAKVDQLS-----GEQEV 427
Cdd:COG4717 360 EEELQLEELE-----QEIAALLAEAGVEDE-----EELRAALEQAEEYQELKEELEELEEQLEELLGELEelleaLDEEE 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 428 LKGELEAAKQAKVKLENRIKELEEELKRVKSEavTARREPREEVEDVSSYLCTELDKIpMAQRRRFTRVEMARVLME--R 505
Cdd:COG4717 430 LEEELEELEEELEELEEELEELREELAELEAE--LEQLEEDGELAELLQELEELKAEL-RELAEEWAALKLALELLEeaR 506
|
490
....*....|....*...
gi 564370964 506 NQYKERLME--LQEAVRW 521
Cdd:COG4717 507 EEYREERLPpvLERASEY 524
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
74-183 |
3.56e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 3.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 74 QEHEVELELLREDNEQLLTQYEREKALRKQAEE--KFIEFEDALEQEKKELQIQVEHYEFQTRQLELKAKNYADQISRLE 151
Cdd:PRK03918 262 RELEERIEELKKEIEELEEKVKELKELKEKAEEyiKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLE 341
|
90 100 110
....*....|....*....|....*....|....*..
gi 564370964 152 ERE---SEMKKEYNALHQRHT--EMIQTYVEHIERSK 183
Cdd:PRK03918 342 ELKkklKELEKRLEELEERHElyEEAKAKKEELERLK 378
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
350-541 |
4.03e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.05 E-value: 4.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 350 DSLYHELSTAGSEVIGDVDEGADLLGEFS-VRDDFFGMGKEVGNLLLENSQLLETKNALNVVKNDLIAKVDQLSG----- 423
Cdd:TIGR02168 701 AELRKELEELEEELEQLRKELEELSRQISaLRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEelaea 780
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 424 --EQEVLKGELEAAKQAKVKLENRIKELEEELKRVKSEAVTARREpREEVEDVSSYLCTELDKIpmAQRRRFTRVEMARV 501
Cdd:TIGR02168 781 eaEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER-LESLERRIAATERRLEDL--EEQIEELSEDIESL 857
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 564370964 502 LMERNQYKERLMELQEAV-RWTEMIRASREHPSVQEKKKST 541
Cdd:TIGR02168 858 AAEIEELEELIEELESELeALLNERASLEEALALLRSELEE 898
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
66-185 |
4.04e-04 |
|
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.
Pssm-ID: 462861 [Multi-domain] Cd Length: 302 Bit Score: 44.17 E-value: 4.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 66 LDSVLSENQEH--EVELELLREDNEQLLTQYEREKALRKQAE---EKFIEFEDALEQEKKElqiqvehyeFQTRQLELKa 140
Cdd:pfam09728 172 LQQATEEEEKKaqEKEVAKARELKAQVQTLSETEKELREQLNlyvEKFEEFQDTLNKSNEV---------FTTFKKEME- 241
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 564370964 141 kNYADQISRLEERESEMKKEYNALHQRHTEMI---QTYVEHIERSKMQ 185
Cdd:pfam09728 242 -KMSKKIKKLEKENLTWKRKWEKSNKALLEMAeerQKLKEELEKLQKK 288
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
64-170 |
4.16e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.93 E-value: 4.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 64 ENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRKQAEEKFIEFEDAL-EQEKKELQIQVEHYEFQTRQLELKAK- 141
Cdd:COG1196 323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELaEAEEELEELAEELLEALRAAAELAAQl 402
|
90 100 110
....*....|....*....|....*....|
gi 564370964 142 -NYADQISRLEERESEMKKEYNALHQRHTE 170
Cdd:COG1196 403 eELEEAEEALLERLERLEEELEELEEALAE 432
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
58-186 |
4.66e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 4.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 58 LVVNVLENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRKQAEEKFIEFEDALEQEKKELQIQVEHYEFQTRQLE 137
Cdd:COG4372 25 LIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELE 104
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 564370964 138 LKAKNYADQISRLEEREsemkKEYNALHQRHTEMIQTYVEHIERSKMQQ 186
Cdd:COG4372 105 SLQEEAEELQEELEELQ----KERQDLEQQRKQLEAQIAELQSEIAERE 149
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
86-179 |
6.46e-04 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 41.41 E-value: 6.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 86 DNEQLLTQYEREKALRKQAEEKFIEFEDALEQEKKELQIQVEHYEFQTRQLEL----KAKNYADQISRLEERESEMKKEY 161
Cdd:pfam03938 6 DMQKILEESPEGKAAQAQLEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEereeKEQELQKKEQELQQLQQKAQQEL 85
|
90
....*....|....*...
gi 564370964 162 NALHQRHTEMIQTYVEHI 179
Cdd:pfam03938 86 QKKQQELLQPIQDKINKA 103
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
60-167 |
6.48e-04 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 41.09 E-value: 6.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 60 VNVLENLDSVLSENQEHEVELELLREDNE---QLLTQ----YERE--------KALRK------QAEEKFIEFEDALEQE 118
Cdd:pfam07926 4 SSLQSEIKRLKEEAADAEAQLQKLQEDLEkqaEIAREaqqnYERElvlhaediKALQAlreelnELKAEIAELKAEAESA 83
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 564370964 119 KKELQIQVEHYEFQTRQLElkaknyaDQISRLEERESEMKKEYNALHQR 167
Cdd:pfam07926 84 KAELEESEESWEEQKKELE-------KELSELEKRIEDLNEQNKLLHDQ 125
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
66-185 |
7.56e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 43.37 E-value: 7.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 66 LDSVLSENQEHEVELELLREDNEQLLTQYEREKALRKQAEEKFIEFE---DALEQEKKELQIQVEHYefqTRQLELKAKN 142
Cdd:pfam00038 63 LDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRTSAENDLVGLRkdlDEATLARVDLEAKIESL---KEELAFLKKN 139
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 564370964 143 YADQISRLEERES------EMKkeyNALHQRHT----EMIQTYVEHIERSKMQ 185
Cdd:pfam00038 140 HEEEVRELQAQVSdtqvnvEMD---AARKLDLTsalaEIRAQYEEIAAKNREE 189
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
62-186 |
8.26e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 8.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 62 VLENLDSVLSENQEHEVELELLRED----NEQLLTQYEREKALRKQAEEKFIEFEDA------LEQEKKELQIQVEHYEF 131
Cdd:COG4372 43 LQEELEQLREELEQAREELEQLEEEleqaRSELEQLEEELEELNEQLQAAQAELAQAqeelesLQEEAEELQEELEELQK 122
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564370964 132 QTRQLELKAKNYADQISRLEERESEMKKEYNALH------QRHTEMIQTYVEHIERSKMQQ 186
Cdd:COG4372 123 ERQDLEQQRKQLEAQIAELQSEIAEREEELKELEeqleslQEELAALEQELQALSEAEAEQ 183
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
72-183 |
9.50e-04 |
|
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: 42.98 E-value: 9.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 72 ENQEHEVELELLREDNEQL----LTQYEREKALRKQAEEKFIEFEDALEQEKKELQIQV--EHYEFQTRQLELKAKNyad 145
Cdd:pfam13868 70 ERKRYRQELEEQIEEREQKrqeeYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLreEIDEFNEEQAEWKELE--- 146
|
90 100 110
....*....|....*....|....*....|....*....
gi 564370964 146 qisRLEERESEMK-KEYNALHQRHTEMIQTYVEHIERSK 183
Cdd:pfam13868 147 ---KEEEREEDERiLEYLKEKAEREEEREAEREEIEEEK 182
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
63-187 |
1.05e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 43.29 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 63 LENLDSVLSENQEHEVELEL--LREDNEQLLTQ----Y---EREKALRKQAEEKFIEFEDALE---QEKKELQIQVEH-- 128
Cdd:PRK04778 258 IQDLKEQIDENLALLEELDLdeAEEKNEEIQERidqlYdilEREVKARKYVEKNSDTLPDFLEhakEQNKELKEEIDRvk 337
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564370964 129 --YEFQTRQLElKAKNYADQISRLEERESEMKKEYNALHQRHT---EMIQTYVEHIERSKMQQV 187
Cdd:PRK04778 338 qsYTLNESELE-SVRQLEKQLESLEKQYDEITERIAEQEIAYSelqEELEEILKQLEEIEKEQE 400
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
412-530 |
1.13e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 412 NDLIAKVDQLSGEQEVLKGELEAAKQAKVKLENRIKELEEELKRVKSEAVTArrepREEVEDVSsylcteldkipmaQRR 491
Cdd:COG4372 48 EQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQA----QEELESLQ-------------EEA 110
|
90 100 110
....*....|....*....|....*....|....*....
gi 564370964 492 RFTRVEMARVLMERNQYKERLMELQEAVRWTEMIRASRE 530
Cdd:COG4372 111 EELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAERE 149
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
397-542 |
1.28e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 397 NSQLLETKNALNVVK---NDLIAKVDQLSGEQEVLKGELEAAKQAKVKLENRIKELEEELKRVKSEAVTARREPREEVED 473
Cdd:COG4372 93 QAELAQAQEELESLQeeaEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQE 172
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564370964 474 VSSYLCTELDKIPMAQRRRFTRVEMARVLMERNQYKERLMELQEAVRWTEMIRASREHPSVQEKKKSTI 542
Cdd:COG4372 173 LQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDA 241
|
|
| GreA_GreB_N |
pfam03449 |
Transcription elongation factor, N-terminal; This domain adopts a long alpha-hairpin structure. |
430-457 |
1.30e-03 |
|
Transcription elongation factor, N-terminal; This domain adopts a long alpha-hairpin structure.
Pssm-ID: 460920 [Multi-domain] Cd Length: 71 Bit Score: 38.51 E-value: 1.30e-03
10 20
....*....|....*....|....*...
gi 564370964 430 GELEAAKQAKVKLENRIKELEEELKRVK 457
Cdd:pfam03449 43 AEYDAAKEEQAFIEARIRELEDKLANAE 70
|
|
| DivIVA |
COG3599 |
Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle ... |
39-160 |
1.59e-03 |
|
Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442818 [Multi-domain] Cd Length: 125 Bit Score: 39.84 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 39 EFERLIHCYDEEVVKELMPLVVNVLENLdsvLSENQEHEVELELLREDNEQLLtqyEREKALRK---QAEEkfiEFEDAL 115
Cdd:COG3599 12 EFKKGFRGYDEDEVDEFLDEVAEDYERL---IRENKELKEKLEELEEELEEYR---ELEETLQKtlvVAQE---TAEEVK 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 564370964 116 EQEKKELQIQVEHYEFQTRQLELKAKNYADQISRLEEresEMKKE 160
Cdd:COG3599 83 ENAEKEAELIIKEAELEAEKIIEEAQEKARKIVREIE---ELKRQ 124
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
63-163 |
1.85e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 63 LENLDSVLSENQEhevELELLREDNEQLltqyEREKALRKQAEEKFIEFEDALEQEKKELQIQVEHYEFQTRQLELKAKN 142
Cdd:COG3883 121 LSALSKIADADAD---LLEELKADKAEL----EAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAA 193
|
90 100
....*....|....*....|.
gi 564370964 143 YADQISRLEERESEMKKEYNA 163
Cdd:COG3883 194 AEAQLAELEAELAAAEAAAAA 214
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
72-186 |
1.86e-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: 42.21 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 72 ENQEHEVElELLREDNEQLLTQYEREKALRKQAEEKFIEFEDALEQeKKELQIQVEHYEfQTRQLE----LKAKNYADQI 147
Cdd:pfam13868 30 EKKRIKAE-EKEEERRLDEMMEEERERALEEEEEKEEERKEERKRY-RQELEEQIEERE-QKRQEEyeekLQEREQMDEI 106
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 564370964 148 SRLEERESEMKKEYNALHQRHT--EMIQTYVEHIERSKMQQ 186
Cdd:pfam13868 107 VERIQEEDQAEAEEKLEKQRQLreEIDEFNEEQAEWKELEK 147
|
|
| UPF0242 |
pfam06785 |
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ... |
63-168 |
2.19e-03 |
|
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal transmembrane region and a C-terminal coiled-coil.
Pssm-ID: 429117 [Multi-domain] Cd Length: 194 Bit Score: 40.96 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 63 LENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRK----QAEEKFIEFEDALEQEKKELQIQVEHYEFQTRQLEL 138
Cdd:pfam06785 85 FKILEETLEELQSEEERLEEELSQKEEELRRLTEENQQLQiqlqQISQDFAEFRLESEEQLAEKQLLINEYQQTIEEQRS 164
|
90 100 110
....*....|....*....|....*....|
gi 564370964 139 KAKNYADQISRLEERESEMKKEYNALHQRH 168
Cdd:pfam06785 165 VLEKRQDQIENLESKVRDLNYEIKTLLQLA 194
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
50-163 |
2.21e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.06 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 50 EVVKELMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRKQAEEKFIEFEDALEQEKKELQIQVEhy 129
Cdd:COG4942 139 QYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELA-- 216
|
90 100 110
....*....|....*....|....*....|....
gi 564370964 130 efqtrQLELKAKNYADQISRLEERESEMKKEYNA 163
Cdd:COG4942 217 -----ELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
64-186 |
2.32e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.23 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 64 ENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRKQAEEKFIEFE---DALEQEKKELQIQVEHYEFQTRQLELKA 140
Cdd:COG1196 253 AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEqdiARLEERRRELEERLEELEEELAELEEEL 332
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 564370964 141 KNYADQISRLEERESEMKKEYNALHQRHTEMIQTYVEHIERSKMQQ 186
Cdd:COG1196 333 EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
|
|
| PRK12495 |
PRK12495 |
hypothetical protein; Provisional |
834-938 |
2.33e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 183558 [Multi-domain] Cd Length: 226 Bit Score: 41.01 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 834 SRGDTPVLDKGQG-DVAATANGKVNPSQSTEEATEATEVPDPGPSESEA-------TTVRPGPLTEHVFTDPAPTqsSST 905
Cdd:PRK12495 69 TEDGAAGDDAGDGaEATAPSDAGSQASPDDDAQPAAEAEAADQSAPPEAsstsatdEAATDPPATAAARDGPTPD--PTA 146
|
90 100 110
....*....|....*....|....*....|...
gi 564370964 906 QPASENGSESDGSIVQPQVEPSGESSATTSSAA 938
Cdd:PRK12495 147 QPATPDERRSPRQRPPVSGEPPTPSTPDAHVAG 179
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
58-181 |
2.70e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 58 LVVNVLENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRKQAEEKFIEFE-DALEQEKKELQIQVEHYEFQTRQL 136
Cdd:COG4913 292 LLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREiERLERELEERERRRARLEALLAAL 371
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 564370964 137 ELK----AKNYADQISRLEERESEMKKEYNALHQRHTEMIQTYVEHIER 181
Cdd:COG4913 372 GLPlpasAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRE 420
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
74-164 |
2.92e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.68 E-value: 2.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 74 QEHEVELELLREDNEQLLTQYEREKALRKQAEEKFIEFEDALEQEKKELqiqvehyefqtRQLELKAKNYADQISRLEER 153
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEI-----------KRLELEIEEVEARIKKYEEQ 81
|
90
....*....|...
gi 564370964 154 ESEMK--KEYNAL 164
Cdd:COG1579 82 LGNVRnnKEYEAL 94
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
72-186 |
3.00e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.08 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 72 ENQEHEVElELLREDNEQLLT------QYEREKA-LRKQAEEKfiefedalEQEKKELQIQVEHYEFQTRQLELKAKNYA 144
Cdd:pfam01576 467 ESQLQDTQ-ELLQEETRQKLNlstrlrQLEDERNsLQEQLEEE--------EEAKRNVERQLSTLQAQLSDMKKKLEEDA 537
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 564370964 145 DQISRLEERESEMKKEYNALHQRHTEMIQTYvEHIERSK--MQQ 186
Cdd:pfam01576 538 GTLEALEEGKKRLQRELEALTQQLEEKAAAY-DKLEKTKnrLQQ 580
|
|
| APG6_N |
pfam17675 |
Apg6 coiled-coil region; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. ... |
412-459 |
3.23e-03 |
|
Apg6 coiled-coil region; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. Autophagy is a bulk degradation process induced by starvation in eukaryotic cells. Apg6/Vps30p has two distinct functions in the autophagic process, either associated with the membrane or in a retrieval step of the carboxypeptidase Y sorting pathway.
Pssm-ID: 465452 [Multi-domain] Cd Length: 127 Bit Score: 39.12 E-value: 3.23e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 564370964 412 NDLIAKVDQLSGEQEVLKGELEAAKQAKVKLENRIKELEEELKRVKSE 459
Cdd:pfam17675 44 EELEKELEKLEKEEEELLQELEELEKEREELDAELEALEEELEALDEE 91
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
70-183 |
3.30e-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: 41.44 E-value: 3.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 70 LSENQEHEVELELLREDNEQLLTQYEREKALRKQAEEKFI-EFEDALEQ--EKKELQIQvehyefQTRQLELKAKNYADQ 146
Cdd:pfam13868 90 QEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLReEIDEFNEEqaEWKELEKE------EEREEDERILEYLKE 163
|
90 100 110
....*....|....*....|....*....|....*..
gi 564370964 147 ISRLEERESEMKKEYNALHQRHTEMIQTYVEHIERSK 183
Cdd:pfam13868 164 KAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEK 200
|
|
| PKK |
pfam12474 |
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino ... |
76-171 |
3.48e-03 |
|
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino acids in length. The family is found in association with pfam00069. Polo-like kinase 1 (Plx1) is essential during mitosis for the activation of Cdc25C, for spindle assembly, and for cyclin B degradation. This family is Polo kinase kinase (PKK) which phosphorylates Polo kinase and Polo-like kinase to activate them. PKK is a serine/threonine kinase.
Pssm-ID: 463600 [Multi-domain] Cd Length: 139 Bit Score: 39.08 E-value: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 76 HEVELELLREDNEQLLTQYEREKALRKQAEEKFI---------EFEDALEQEKKELQIQVEhyefqtrqlelkaknyadQ 146
Cdd:pfam12474 23 YEKELEQLERQQKQQIEKLEQRQTQELRRLPKRIraeqkkrlkMFRESLKQEKKELKQEVE------------------K 84
|
90 100
....*....|....*....|....*.
gi 564370964 147 ISRLEERESE-MKKEYNALHQRHTEM 171
Cdd:pfam12474 85 LPKFQRKEAKrQRKEELELEQKHEEL 110
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
63-204 |
3.57e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.85 E-value: 3.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 63 LENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRKQAEEKFIEFEDALEQEKKELQIQVEHYEFQTRQLELKAKN 142
Cdd:COG1196 353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564370964 143 YADQISRLEERESEMKKEYNALHQRHTEMIQTYVEHIERSKMQQVGGGGQTESSLPGRSRKE 204
Cdd:COG1196 433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL 494
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
71-204 |
3.68e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 41.70 E-value: 3.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 71 SENQEHEVELELLREDNEQLLTQYERekalRKQAEEkfiEFEDALEQEKKELQIQVEHYEFQ------TRQ--------L 136
Cdd:pfam01576 57 AEAEEMRARLAARKQELEEILHELES----RLEEEE---ERSQQLQNEKKKMQQHIQDLEEQldeeeaARQklqlekvtT 129
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 137 ELKAKNYADQISRLEERESEMKKEYNALHQRHTEMIQTYVEHIERSKMQQVGGGGQ--TESSLPGRSRKE 204
Cdd:pfam01576 130 EAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHeaMISDLEERLKKE 199
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
67-188 |
3.71e-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: 41.02 E-value: 3.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 67 DSVLSEN-QEHEVELE-LLREDneQLLTQYEREKALRKQAEEkfiefedALEQEKKELQiqvEHYEFQTRQLELKAKNYA 144
Cdd:cd16269 169 EEVLQEFlQSKEAEAEaILQAD--QALTEKEKEIEAERAKAE-------AAEQERKLLE---EQQRELEQKLEDQERSYE 236
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 564370964 145 DQISRLEEresEMKKEYNALHQRHTEMIQTYVEHIERskMQQVG 188
Cdd:cd16269 237 EHLRQLKE---KMEEERENLLKEQERALESKLKEQEA--LLEEG 275
|
|
| DUF4045 |
pfam13254 |
Domain of unknown function (DUF4045); This presumed domain is functionally uncharacterized. ... |
834-918 |
3.73e-03 |
|
Domain of unknown function (DUF4045); This presumed domain is functionally uncharacterized. This domain family is found in bacteria and eukaryotes, and is typically between 384 and 430 amino acids in length.
Pssm-ID: 433066 [Multi-domain] Cd Length: 415 Bit Score: 41.31 E-value: 3.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 834 SRGDTPVldKGQGDVAATANGKVNPSQSTEEATEATEVPD--PGPSESEATTVRPGPLTEH------VFTDPA-PTQSSS 904
Cdd:pfam13254 37 SRQNSFA--SNRGSVAGPSGSLSPGLSPTKLSREGSPESTsrPSSSHSEATIVRHSKDDERpstpdeGFVKPAlPRHSRS 114
|
90
....*....|....
gi 564370964 905 TQPASENGSESDGS 918
Cdd:pfam13254 115 SSALSNTGSEEDSP 128
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
399-519 |
3.79e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.68 E-value: 3.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 399 QLLETK-NALNVVKNDLIAKVDQLSGEQEVLKGELEAAKQAKVKLENRIKELEEELKRVKSEAVTAR------REPReEV 471
Cdd:COG1579 13 QELDSElDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEeqlgnvRNNK-EY 91
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 564370964 472 EDVSSylctELDKIpmAQRRRFTRVEMARVLMERNQYKERLMELQEAV 519
Cdd:COG1579 92 EALQK----EIESL--KRRISDLEDEILELMERIEELEEELAELEAEL 133
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
64-165 |
3.99e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.74 E-value: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 64 ENLDSVL--SENQEHEVE-----LELLREDNEQLLTQYEREKALRKQAEEKFI-----EFEDALEQEKKE---------L 122
Cdd:PRK00409 516 EKLNELIasLEELERELEqkaeeAEALLKEAEKLKEELEEKKEKLQEEEDKLLeeaekEAQQAIKEAKKEadeiikelrQ 595
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 564370964 123 QIQVEHYEFQTRQLELKAKNYADQISRLEERESEMKKEYNALH 165
Cdd:PRK00409 596 LQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELK 638
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
86-181 |
4.10e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 39.10 E-value: 4.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 86 DNEQLLTQYEREKALRKQAEEKFIEFEDALEQEKKELQIQVEhyEFQTRQLELKAKNYADQISRLEERESEMKKEYNA-- 163
Cdd:smart00935 5 DVQKILQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKE--KLQKDAATLSEAAREKKEKELQKKVQEFQRKQQKlq 82
|
90 100
....*....|....*....|
gi 564370964 164 --LHQRHTEMIQTYVEHIER 181
Cdd:smart00935 83 qdLQKRQQEELQKILDKINK 102
|
|
| Med21 |
pfam11221 |
Subunit 21 of Mediator complex; Med21 has been known as Srb7 in yeasts, hSrb7 in humans and ... |
404-474 |
4.17e-03 |
|
Subunit 21 of Mediator complex; Med21 has been known as Srb7 in yeasts, hSrb7 in humans and Trap 19 in Drosophila. The heterodimer of the two subunits Med7 and Med21 appears to act as a hinge between the middle and the tail regions of Mediator.
Pssm-ID: 463241 Cd Length: 134 Bit Score: 38.73 E-value: 4.17e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564370964 404 KNALNVVKNDLIAKVDQLsgeqEVLKGELEAAKQAKVKLENRIKELEEELKRVKSEAVTARREPREEVEDV 474
Cdd:pfam11221 59 EATQRELARDLILKAQQI----EYLIDSLPGIGVSEEEQLQRIKELEEELREAEEERQEAVKEKEELLKKL 125
|
|
| COG3292 |
COG3292 |
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms]; |
1015-1137 |
4.31e-03 |
|
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
Pssm-ID: 442521 [Multi-domain] Cd Length: 924 Bit Score: 41.51 E-value: 4.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 1015 PHHSIRCMAV-VDDRVWCGYKNKVHVIQPKTMQIEKSFDAHPRRESQVRQLAWIGDG-VWVSirLDSTLRLYHAHTHQhl 1092
Cdd:COG3292 79 PSNYIRALLEdSDGRLWIGTDGGLSRYDPKTDKFTRYPLDPGLPNNSIRSIAEDSDGnIWVG--TSNGLYRYDPKTGK-- 154
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 564370964 1093 qdvdIEPYVSKmlgtgklGFSFVRITALLIAGN---------RLWVGT-GNGVVI 1137
Cdd:COG3292 155 ----FKRFTLD-------GLPSNTITSLAEDADgnlwvdsdgNLWIGTdGNGLYR 198
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
59-174 |
4.54e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.29 E-value: 4.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 59 VVNVLENLDSVLSENQEHEVELELLRE----DNEQL--------LTQYERE----KALRKQAEEKFIEFEDALEQEKKEL 122
Cdd:COG1579 47 LEAAKTELEDLEKEIKRLELEIEEVEArikkYEEQLgnvrnnkeYEALQKEieslKRRISDLEDEILELMERIEELEEEL 126
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 564370964 123 QiQVEhyefqtRQLELKAKNYADQISRLEERESEMKKEYNALHQRHTEMIQT 174
Cdd:COG1579 127 A-ELE------AELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
389-542 |
5.23e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 5.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 389 EVGNLLLENSQLLETK----NALNVVKNDLIAKVDQLSGEQEVL---KGELEAAK-------QAKVKLENRIKELEEELK 454
Cdd:PRK03918 190 NIEELIKEKEKELEEVlreiNEISSELPELREELEKLEKEVKELeelKEEIEELEkelesleGSKRKLEEKIRELEERIE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 455 RVKSEAvtarREPREEVEDVssylcTELDKipmaqrrrftRVEMARVLME-RNQYKERLMELQ-EAVRWTEMIRASREHP 532
Cdd:PRK03918 270 ELKKEI----EELEEKVKEL-----KELKE----------KAEEYIKLSEfYEEYLDELREIEkRLSRLEEEINGIEERI 330
|
170
....*....|
gi 564370964 533 SVQEKKKSTI 542
Cdd:PRK03918 331 KELEEKEERL 340
|
|
| PRK10856 |
PRK10856 |
cytoskeleton protein RodZ; |
858-975 |
5.45e-03 |
|
cytoskeleton protein RodZ;
Pssm-ID: 236776 [Multi-domain] Cd Length: 331 Bit Score: 40.39 E-value: 5.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 858 PSQSTEEATEATEVPDPGPSESEATTVRPGPLTehvftdpAPTQSSSTQPASENGSESDGSIVQPQVEPSGESSATTSSA 937
Cdd:PRK10856 170 TDPATTPAPAAPVDTTPTNSQTPAVATAPAPAV-------DPQQNAVVAPSQANVDTAATPAPAAPATPDGAAPLPTDQA 242
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 564370964 938 APTMWLGAQNG---------WLYVHSavANWKKCLHSIKLKDSVLSL 975
Cdd:PRK10856 243 GVSTPAADPNAlvmnftadcWLEVTD--ATGKKLFSGMQRKGGNLNL 287
|
|
| YkyA |
pfam10368 |
Putative cell-wall binding lipoprotein; YkyA is a family of proteins containing a lipoprotein ... |
97-186 |
5.59e-03 |
|
Putative cell-wall binding lipoprotein; YkyA is a family of proteins containing a lipoprotein signal and a hydrolase domain. It is similar to cell wall binding proteins and might also be recognisable by a host immune defence system. It is thus likely to belong to pathways important for pathogenicity.
Pssm-ID: 431235 [Multi-domain] Cd Length: 185 Bit Score: 39.50 E-value: 5.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 97 EKAlrKQAEEKFIEFEDAL-EQEKKELQIQVEHYEFQTRQLElKAKNYADQ-ISRLEERESEMKKEYNALHQRHTEM--I 172
Cdd:pfam10368 11 EEA--VELEKPFEEQQEPLvELEKKEQELYEEIIELGMDEFD-EIKKLSDEaLENVEEREELLEKEKESIEEAKEEFkkI 87
|
90
....*....|....
gi 564370964 173 QTYVEHIERSKMQQ 186
Cdd:pfam10368 88 KEIIEEIEDEELKK 101
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
61-186 |
5.93e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.20 E-value: 5.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 61 NVLENLDSVLSENQEHEVELELLREDNEQLLTQYERE-KALRKQAeekfiefeDALEQEKKELQI-------QVEHYEFQ 132
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEElKALREAL--------DELRAELTLLNEeaanlreRLESLERR 832
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 564370964 133 TRQLELKAKNYADQISRLEERESEMKKEYNALHQRHTEMIQTYVEH-IERSKMQQ 186
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALlNERASLEE 887
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
72-166 |
6.04e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.08 E-value: 6.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 72 ENQEHEVELELLREDNEQLLTQYEREKALRKQAEEKFIEFEDALEQEKKEL--------QIQVEHYEFQTRQLEL--KAK 141
Cdd:COG1196 317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALleaeaelaEAEEELEELAEELLEAlrAAA 396
|
90 100
....*....|....*....|....*
gi 564370964 142 NYADQISRLEERESEMKKEYNALHQ 166
Cdd:COG1196 397 ELAAQLEELEEAEEALLERLERLEE 421
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
65-186 |
6.08e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 6.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 65 NLDSVLSENQEHEVELELLREDN---EQLLTQYEREKALRKQAEEKFIEFEDALEQEKKEL-QIQVEHYEFQTRQLELKA 140
Cdd:COG4913 662 DVASAEREIAELEAELERLDASSddlAALEEQLEELEAELEELEEELDELKGEIGRLEKELeQAEEELDELQDRLEAAED 741
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 564370964 141 KNYADQISRLEER---------ESEMKKEYNALHQRHTEMIQTYVEHIERsKMQQ 186
Cdd:COG4913 742 LARLELRALLEERfaaalgdavERELRENLEERIDALRARLNRAEEELER-AMRA 795
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
72-170 |
7.54e-03 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 37.98 E-value: 7.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 72 ENQEHEVELELLRED----NEQLLTQYEREKAL---RKQAEEKFIEFE---DALEQEKKELQIQVEHYEFQTRQLELKAK 141
Cdd:pfam20492 7 EKQELEERLKQYEEEtkkaQEELEESEETAEELeeeRRQAEEEAERLEqkrQEAEEEKERLEESAEMEAEEKEQLEAELA 86
|
90 100 110
....*....|....*....|....*....|....
gi 564370964 142 NYADQISRLEE----RESEMKK-EYNALHQRHTE 170
Cdd:pfam20492 87 EAQEEIARLEEeverKEEEARRlQEELEEAREEE 120
|
|
| MIC19_MIC25 |
pfam05300 |
MICOS complex subunit MIC19/MIC25; MIC19 (also known as ChChd3) and MIC25 (also known as ... |
79-159 |
7.73e-03 |
|
MICOS complex subunit MIC19/MIC25; MIC19 (also known as ChChd3) and MIC25 (also known as ChChd6) are components of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane. MIC19 plays an important role in the maintenance of the MICOS complex stability and the mitochondrial cristae morphology.
Pssm-ID: 461615 [Multi-domain] Cd Length: 173 Bit Score: 38.91 E-value: 7.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 79 ELELLREDNEQLLTQYEREKALRKQAEEKFIEFE---------DALEQEK----KELQiQVEHY--EFQTRQLELKAKN- 142
Cdd:pfam05300 60 EEELRKKIKEELYKRLEQEQAKVQEELARLAEREreaaqesltRAILRERasteDERL-KAQQLakQLEEKEAELKKQDa 138
|
90
....*....|....*...
gi 564370964 143 -YADQISRLEERESEMKK 159
Cdd:pfam05300 139 fYKEQLARLEEKNAEFYK 156
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
39-234 |
8.84e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 40.33 E-value: 8.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 39 EFERLIHCYDEEVVK---ELMPLVVNVLENLDSVLS--ENQEHEVELELLREDNEQLLTQYEREK----ALRKQAEEKFI 109
Cdd:COG5185 326 ELEESKRETETGIQNltaEIEQGQESLTENLEAIKEeiENIVGEVELSKSSEELDSFKDTIESTKesldEIPQNQRGYAQ 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 110 EFEDALEQEKKELQIQVEHY----EFQTRQLELKAKNYADQISRLEERESEMKKEYNA-LHQRHTEMIQTYVEHIERSKM 184
Cdd:COG5185 406 EILATLEDTLKAADRQIEELqrqiEQATSSNEEVSKLLNELISELNKVMREADEESQSrLEEAYDEINRSVRSKKEDLNE 485
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 564370964 185 ------QQVGGGGQTESSLPGRSRKERPTSLNVFPlADGMCPNDEMSESGQSSAAA 234
Cdd:COG5185 486 eltqieSRVSTLKATLEKLRAKLERQLEGVRSKLD-QVAESLKDFMRARGYAHILA 540
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
420-526 |
8.86e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 8.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 420 QLSGEQEVLKgELEAAKQAKVKLENRIKELEEELKRVKSEAVTARREPREEVEDVSSYLCTELDKIpmAQRRRFTRVEMA 499
Cdd:COG4717 140 ELAELPERLE-ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEEL--QQRLAELEEELE 216
|
90 100
....*....|....*....|....*..
gi 564370964 500 RVLMERNQYKERLMELQEAVRWTEMIR 526
Cdd:COG4717 217 EAQEELEELEEELEQLENELEAAALEE 243
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
63-181 |
9.54e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.31 E-value: 9.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 63 LENLDSVLSENQEhevELELLREDNEQLLTQYEREKALRKQAEEKfiefEDALEQEKKELQIQVEHYEFQTRQLELKAKN 142
Cdd:COG1196 276 LEELELELEEAQA---EEYELLAELARLEQDIARLEERRRELEER----LEELEEELAELEEELEELEEELEELEEELEE 348
|
90 100 110
....*....|....*....|....*....|....*....
gi 564370964 143 YADQISRLEERESEMKKEYNALHQRHTEMIQTYVEHIER 181
Cdd:COG1196 349 AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
404-538 |
9.87e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 9.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 404 KNALNVVKNdliakvdqLSGEQEVLKGELEAAKQakvkLENRIKELEEELKRVK---SEAVTARREPREEVEDVSSYLcT 480
Cdd:PRK03918 165 KNLGEVIKE--------IKRRIERLEKFIKRTEN----IEELIKEKEKELEEVLreiNEISSELPELREELEKLEKEV-K 231
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370964 481 ELDKIpmaqRRRFT--RVEMARVLMERNQYKERLMELQeavrwtEMIRASREHPSVQEKK 538
Cdd:PRK03918 232 ELEEL----KEEIEelEKELESLEGSKRKLEEKIRELE------ERIEELKKEIEELEEK 281
|
|
| |
