|
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 ... |
20-166 |
1.03e-41 |
|
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: 144.29 E-value: 1.03e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 20 VYDLAASIGNDFEKLIDNYGNECVRGIMPKVISALETLEAMAAGNDRENEEIMRLSKAVERLEQEKHQRNQQHLKFEEEL 99
Cdd:pfam09744 1 VYDLASSIGKEFERLIDRYGEDVVKGLMPKVVNVLELLESLASRNQEHNVELEELREDNEQLETQYEREKALRKRAEEEL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 100 EQVEKTYRKDIDDLQQMVKSLVNENRNLSTT-VSSLP-NHADSP-VSTSMREADLKMLLELKEMSSQQKD 166
Cdd:pfam09744 81 EEIEDQWEQETKDLLSQVESLEEENRRLEADhVSRLEeKEAELKkEYSKLHERETEVLRKLKEVVDRQRD 150
|
|
| RILP-like |
cd14445 |
Rab interacting lysosomal protein-like 1 and 2 (Rilpl1 and Rilpl2); This domain is found in ... |
3-91 |
5.53e-35 |
|
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: 124.63 E-value: 5.53e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 3 ARAASPQSPSkQITVVDVYDLAASIGNDFEKLIDNYGNECVRGIMPKVISALETLEAMAAGNDRENEEIMRLSKAVERLE 82
Cdd:cd14445 2 AESALDKSPS-ELTVVDVYDIASAIGKEFERLIDRYGPEAVAGLMPKVVRVLELLEALASRNERENLEIEELRLEVDRLE 80
|
....*....
gi 71982687 83 QEKHQRNQQ 91
Cdd:cd14445 81 LEKRERAQK 89
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
68-230 |
1.29e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 56.38 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 68 NEEIMRLSKAVERLEQEKHQRNQQHLKFEEELEQVEKTYRKDIDDLQQMVKSLvNENRNLSTTVSSLPNhADSP------ 141
Cdd:COG3883 43 QAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAL-YRSGGSVSYLDVLLG-SESFsdfldr 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 142 --VSTSMREADLKMLLELKEMS---SQQKDEIKALQKDVDTYQCQVENLQNSIEKLIRQNEELLrknASLQKQGRMIVEE 216
Cdd:COG3883 121 lsALSKIADADADLLEELKADKaelEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALL---AQLSAEEAAAEAQ 197
|
170
....*....|....
gi 71982687 217 KMEVVRRLEKTEES 230
Cdd:COG3883 198 LAELEAELAAAEAA 211
|
|
| RILP |
pfam11461 |
Rab interacting lysosomal protein; RILP contains a domain which contains two coiled-coil ... |
261-324 |
1.93e-08 |
|
Rab interacting lysosomal protein; RILP contains a domain which contains two coiled-coil regions and is found mainly in the cytosol. RILP is recruited onto late endosomal and lysosomal membranes by Rab7 and acts as a downstream effector of Rab7. This recruitment process is important for phagosome maturation and fusion with late endosomes and lysosomes.
Pssm-ID: 463282 [Multi-domain] Cd Length: 69 Bit Score: 50.67 E-value: 1.93e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71982687 261 TLSELREVIKEKNILKGRVMELEEELDNFKPGA--KKEIMRLDDDDDFDRNPLQPDTSSAQSLGVD 324
Cdd:pfam11461 1 TLQELRDVLQERNELKAQLFLLQEELAYYKSGLlnEEEIPSLRLESPSPRTKPQRSKIKQEESGIK 66
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
92-284 |
1.15e-07 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 54.09 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 92 HLKFEEELEQVEKTYRKDIDdlQQMVKSLVNENRNLSTTVSSLPNhadsPVSTSMREADLKMLLELKEMSSQQKDEIKAL 171
Cdd:COG2433 345 YDAYKNKFERVEKKVPPDVD--RDEVKARVIRGLSIEEALEELIE----KELPEEEPEAEREKEHEERELTEEEEEIRRL 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 172 QKDVDTYQCQVENLQNSIEKLIRQNEELLRKNASLQKQGRMIVEEKMEVVR------RLEKT-EESNIELKKLVKETDRA 244
Cdd:COG2433 419 EEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRKDREISRldreieRLERElEEERERIEELKRKLERL 498
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 71982687 245 CKDMQLANQDNNEP-----RFTLSELREVIKEKNILKGRVMELEE 284
Cdd:COG2433 499 KELWKLEHSGELVPvkvveKFTKEAIRRLEEEYGLKEGDVVYLRD 543
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
53-290 |
2.45e-07 |
|
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: 53.14 E-value: 2.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 53 ALETLEAMAAGND--RENEEIMRLSKAVERLEQEKHQRNQQHLKFEEELEQVEKTYR---KDIDDLQQMVKSLVNE---- 123
Cdd:TIGR02168 221 ELRELELALLVLRleELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSeleEEIEELQKELYALANEisrl 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 124 NRNLSTTVSSLPNHADSPVSTS-MREADLKMLLELKEMSSQQKDEIKALQKDVDTYQCQVENLQNSIEKLIRQNEE---- 198
Cdd:TIGR02168 301 EQQKQILRERLANLERQLEELEaQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEEleeq 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 199 ----------LLRKNASLQKQGRMIVEEKMEVVRRLEKTEESNIELKKLVKETDRACKDMQLAnQDNNEPRFTLSELREV 268
Cdd:TIGR02168 381 letlrskvaqLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELE-ELEEELEELQEELERL 459
|
250 260
....*....|....*....|..
gi 71982687 269 IKEKNILKGRVMELEEELDNFK 290
Cdd:TIGR02168 460 EEALEELREELEEAEQALDAAE 481
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
53-271 |
1.75e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.32 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 53 ALETLEAMAAGNDRENEEIMRLSKAVERLEQEKHQRNQQHLKFEEELEQVEKTYRKDIDDLQQMVKSLVNENRNLSTTVS 132
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 133 SlpnhadspvstsmREADLKMLLELKEMSSQQKDEIKALQKDVDTYQCQVENLQNSIEKLIRQNEELLRKNASLQKQGRM 212
Cdd:COG1196 373 E-------------LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE 439
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 71982687 213 IVEEKMEVVRRLEKTEESNIELKKLVKETDRACKDMQLANQDNNEPRFTLSELREVIKE 271
Cdd:COG1196 440 EEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
68-268 |
5.75e-06 |
|
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: 48.90 E-value: 5.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 68 NEEIMRLSKAVERLEQEKHQRNQQHLKFEEELEQVEKTYRKDIDDLQQMVK---SLVNENRNLSTTVSSLpnHADSPVST 144
Cdd:TIGR02168 294 ANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEkleELKEELESLEAELEEL--EAELEELE 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 145 SMREADLKMLLELKEMSSQQKDEIKALQKDVDTYQCQVENLQNSIEKLIRQNEELLRK--NASLQKQGRMIVEEKMEVVR 222
Cdd:TIGR02168 372 SRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKleEAELKELQAELEELEEELEE 451
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 71982687 223 RLEKTEESNIELKKLVKETDRACKDMQLANQDNNEPRFTLSELREV 268
Cdd:TIGR02168 452 LQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERL 497
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
70-286 |
9.83e-06 |
|
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: 48.14 E-value: 9.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 70 EIMRLSKAVERLEQEKHQRNQQHLKFEEELEQVEKTYRKDIDDLQQMVKSLVNEnrnLSTTVSSLpNHADSPVSTSMREA 149
Cdd:TIGR02169 245 QLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGE---LEAEIASL-ERSIAEKERELEDA 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 150 DlKMLLELKEMSSQQKDEIKALQKDVDTYQCQVENLQNSIEKLIRQNEELLRKNASLQKQGRMIVEEKMEVVRRLEKT-- 227
Cdd:TIGR02169 321 E-ERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLkr 399
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71982687 228 --EESNIELKKLVKETDRacKDMQLANQDNNEPRFtLSELREVIKEKNILKGRVMELEEEL 286
Cdd:TIGR02169 400 eiNELKRELDRLQEELQR--LSEELADLNAAIAGI-EAKINELEEEKEDKALEIKKQEWKL 457
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
70-287 |
1.76e-05 |
|
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: 47.36 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 70 EIMRLSKAVERLEQEKHQRNQQHLKFEEELEQVEK---TYRKDIDDLQQMVKSLVNENRNLSTTVSSLP-----NHADSP 141
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEeleQLRKELEELSRQISALRKDLARLEAEVEQLEeriaqLSKELT 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 142 VSTSMREADLKMLLELKEMSSQQKDEIKALQKDVDTYQcqvENLQNSIEKLIRQNEEL----------LRKNASLQKQGR 211
Cdd:TIGR02168 758 ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLK---EELKALREALDELRAELtllneeaanlRERLESLERRIA 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 212 MIVEEKMEVVRRLEKTEESNIELK-----------KLVKETDRACKDMQLANQDNNEPRFTLSELREVIKEKNilkGRVM 280
Cdd:TIGR02168 835 ATERRLEDLEEQIEELSEDIESLAaeieeleelieELESELEALLNERASLEEALALLRSELEELSEELRELE---SKRS 911
|
....*..
gi 71982687 281 ELEEELD 287
Cdd:TIGR02168 912 ELRRELE 918
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
49-300 |
2.80e-05 |
|
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: 46.59 E-value: 2.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 49 KVISALETLEAMAAGNDRENEEIMRLSKAVERLEQEKHQRNQQHLKFEEELEQVEKTYRKDIDDLQQMVKSLVNENRNLS 128
Cdd:TIGR02168 734 DLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT 813
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 129 TTVSSLpnhADSPVSTSMREADLKMLLELKEMSSQQKDEIKAlqkdvdtyqcQVENLQNSIEKLIRQNEELLRKNASLQK 208
Cdd:TIGR02168 814 LLNEEA---ANLRERLESLERRIAATERRLEDLEEQIEELSE----------DIESLAAEIEELEELIEELESELEALLN 880
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 209 QgRMIVEEKMEVVR-RLEKTEESNIELKKLVKETDRACKDMQL----ANQDNNEPRFTLSELREVIKEK-NILKGRVMEL 282
Cdd:TIGR02168 881 E-RASLEEALALLRsELEELSEELRELESKRSELRRELEELREklaqLELRLEGLEVRIDNLQERLSEEySLTLEEAEAL 959
|
250
....*....|....*...
gi 71982687 283 EEELDNFKPGAKKEIMRL 300
Cdd:TIGR02168 960 ENKIEDDEEEARRRLKRL 977
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
52-286 |
2.96e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 46.35 E-value: 2.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 52 SALETLEAMAAGNDReneeimrlskAVERLeqeKHQRNQQHLKFEEELEQvektYRKDIDDLQQMVKSLVNENRNLSTTV 131
Cdd:pfam10174 436 TALTTLEEALSEKER----------IIERL---KEQREREDRERLEELES----LKKENKDLKEKVSALQPELTEKESSL 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 132 SSLPNHADSPVStSMREADLKmlLELKEMSSQQKDEikalqkDVDTYQCQVENLQNsIEKLIRQNEELLRKNASLQKqgr 211
Cdd:pfam10174 499 IDLKEHASSLAS-SGLKKDSK--LKSLEIAVEQKKE------ECSKLENQLKKAHN-AEEAVRTNPEINDRIRLLEQ--- 565
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 212 miveekmEVVRRLEKTEESNIELKKLVK-----ETDRACKDMQLANQDNNEPRFTLSELREVIKEKNI----LKGRVMEL 282
Cdd:pfam10174 566 -------EVARYKEESGKAQAEVERLLGilrevENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGqqemKKKGAQLL 638
|
....
gi 71982687 283 EEEL 286
Cdd:pfam10174 639 EEAR 642
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
57-297 |
3.82e-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: 46.21 E-value: 3.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 57 LEAMAAGNDRENEEIMRLSKAVERLEQEKHQRNQQHLKFEEELEQVEKT---YRKDIDDLQQM-----VKSLVNENRNLS 128
Cdd:TIGR02169 725 IEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDlhkLEEALNDLEARlshsrIPEIQAELSKLE 804
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 129 TTVSSLPNHADSpvstsmREADLKMLLELKEmssQQKDEIKALQKDVDTYQCQVENLQNSIEKLIRQNEELLRKNASLQK 208
Cdd:TIGR02169 805 EEVSRIEARLRE------IEQKLNRLTLEKE---YLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEA 875
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 209 QgrmiveekmevVRRLEKteesniELKKLVKETDRACKDMQLANQDNNEPRFTLSELREVIKEkniLKGRVMELEEELDN 288
Cdd:TIGR02169 876 A-----------LRDLES------RLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSE---LKAKLEALEEELSE 935
|
....*....
gi 71982687 289 FKPGAKKEI 297
Cdd:TIGR02169 936 IEDPKGEDE 944
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
47-290 |
9.96e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 44.71 E-value: 9.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 47 MPKVISALETLEAMAAGNDRENEEIMRLSKAVERLEQEKHQRNQ--QHLK-FEEELEQVEKTYRKDIDDLQQMVKSLVNE 123
Cdd:pfam05483 386 LQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKiaEELKgKEQELIFLLQAREKEIHDLEIQLTAIKTS 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 124 NRNLSTTVSSLPNHADSPV--STSMREADLKMLLELKEMSSQQKD---EIKALQKDVDTYQCQVENLQNSIEKLIRQNEE 198
Cdd:pfam05483 466 EEHYLKEVEDLKTELEKEKlkNIELTAHCDKLLLENKELTQEASDmtlELKKHQEDIINCKKQEERMLKQIENLEEKEMN 545
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 199 LLRKNASLQKQgrmIVEEKMEVVRRLEKTEESN-------IELKKLVKETDRACKDMQLANQDNNEPRFTLSELREVIKE 271
Cdd:pfam05483 546 LRDELESVREE---FIQKGDEVKCKLDKSEENArsieyevLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKK 622
|
250 260
....*....|....*....|....*..
gi 71982687 272 K--------NILKGRVMELEEELDNFK 290
Cdd:pfam05483 623 KgsaenkqlNAYEIKVNKLELELASAK 649
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
47-288 |
9.97e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 9.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 47 MPKVISALETLEAMAAGNDRENEEIMRLSKAVERLEQEKHQRNQQHLKFEEEL---EQVEKTYRKDIDDLQQMVKSLVNE 123
Cdd:PTZ00121 1594 IEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKkkaEELKKAEEENKIKAAEEAKKAEED 1673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 124 NRNLSTTVSSLPNHADSPVSTSMREADLKMLLELKEMSSQQKDEIKALQKDVDTYQCQVENLQNSIEKLIRQNEELLRKN 203
Cdd:PTZ00121 1674 KKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDE 1753
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 204 ASLQK--QGRMIVEEKMEVVRRL----------EKTEESNIELKKLVKETDRACKDMQLANQDNN-----EPRFTLSELR 266
Cdd:PTZ00121 1754 EEKKKiaHLKKEEEKKAEEIRKEkeavieeeldEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNlvindSKEMEDSAIK 1833
|
250 260
....*....|....*....|..
gi 71982687 267 EVIKEKNILKGRVMELEEELDN 288
Cdd:PTZ00121 1834 EVADSKNMQLEEADAFEKHKFN 1855
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
57-324 |
2.07e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 43.58 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 57 LEAMAAGNDRENEEIMRLSKAVERLEQEKHQRNQQHLK----FEEELEQVEKTYRKDIDDLQQMVKSLVNENRNLSTTVS 132
Cdd:pfam05557 18 KKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKrirlLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKES 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 133 SLPNHADSPVSTSMREADLKMLLELKEMSSQQKD-EIKALQKDVDTYQCQVENLQNSIEKLIRQNEELLRKNASLQkqgr 211
Cdd:pfam05557 98 QLADAREVISCLKNELSELRRQIQRAELELQSTNsELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIK---- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 212 miveekmEVVRRLEKTEESNIELKKLVKETDRAcKDMQlanQDNNEPRFTLSELREVIKEKNILKGRVMELEEELDNFKp 291
Cdd:pfam05557 174 -------ELEFEIQSQEQDSEIVKNSKSELARI-PELE---KELERLREHNKHLNENIENKLLLKEEVEDLKRKLEREE- 241
|
250 260 270
....*....|....*....|....*....|...
gi 71982687 292 GAKKEIMRLDDDDDFDRNPLQPDTSSAQSLGVD 324
Cdd:pfam05557 242 KYREEAATLELEKEKLEQELQSWVKLAQDTGLN 274
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
75-284 |
2.54e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 75 SKAVERLEQEKHQRNQQHLKFEEELEQVEKTYRKDIDDLQQMVKSLVNENRNLSTTVSSLpnhadspvstsmrEADLKML 154
Cdd:PRK03918 167 LGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKL-------------EKEVKEL 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 155 LELKEMSSQQKDEIKALQKDVDTYQCQVENLQNSIEKLIRQNEELLRKNASLQKqgrmiVEEKMEVVRRLEK------TE 228
Cdd:PRK03918 234 EELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKE-----LKEKAEEYIKLSEfyeeylDE 308
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 71982687 229 ESNIE--LKKLVKETDRACKDMQLANQDNNEPRFTLSELREVIKEKNILKGRVMELEE 284
Cdd:PRK03918 309 LREIEkrLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEE 366
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
78-297 |
2.85e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 78 VERLEQEKHQRNQQHLKFEEELEQVEKTYRKDIDDLQQMVKSLVNENRNLSTTVSSLpnhadspvstsmreadlkmllel 157
Cdd:COG4372 40 LDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAEL----------------------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 158 kemsSQQKDEIKALQKDVDTYQCQVENLQNSIEKLIRQNEELLRKNASLQKQGRMIVEEKMEVVRRLEKTEESNIELKKL 237
Cdd:COG4372 97 ----AQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 238 VKETDRACKDMQLANQDNNEPRFTLSELREVIKEKNILKGRVMELEEELDNFKPGAKKEI 297
Cdd:COG4372 173 LQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLG 232
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
65-287 |
5.59e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 5.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 65 DRENEEIMR-LSKAVERLEQEKHQRNQQHLKFEEELEQVEKTYRKDIDDLQQmvKSLVNENRNLSTTVSSlpnhadspVS 143
Cdd:PRK03918 447 EEHRKELLEeYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKL--KELAEQLKELEEKLKK--------YN 516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 144 TSMREADLKMLLELKEMSSQQKDEIKALQKDVDtyqcQVENLQNSIEKLIRQNEELLRKNASLQKQ----GRMIVEEKME 219
Cdd:PRK03918 517 LEELEKKAEEYEKLKEKLIKLKGEIKSLKKELE----KLEELKKKLAELEKKLDELEEELAELLKEleelGFESVEELEE 592
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71982687 220 VVRRLEKTEESNIELKKLVKETDRACKDMQLANQDNNEPRFTLSELREVIKEkniLKGRVMELEEELD 287
Cdd:PRK03918 593 RLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEE---LRKELEELEKKYS 657
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
50-290 |
5.70e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 5.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 50 VISALETLEAMAAGNDRENEEIMRLSKAVERLEQEKHQRNQQHLKFEEELEQVEKTYRKDIDDLQQMVKSLVNENRNLST 129
Cdd:COG4372 33 LRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 130 TVSSLpnhadspvstsmrEADLKMLLELKEMSSQQKDEIKALQKDVDTYQCQVENLQNSIEKLIRQNEELLRKNASLQKQ 209
Cdd:COG4372 113 LQEEL-------------EELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 210 grmiveEKMEVVRRLEKTEESNIELKKLVKETDRACKDMQLANQDNNEPRFTLSELREVIKEKNILKGRVMELEEELDNF 289
Cdd:COG4372 180 ------EAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLE 253
|
.
gi 71982687 290 K 290
Cdd:COG4372 254 E 254
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
74-286 |
6.06e-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: 42.35 E-value: 6.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 74 LSKAVERLEQEKhQRNQQHLKFEEELEQVEKT-YRKDIDDLQQMVKSLVNENRNLSTTVSSLpnhadspvSTSMREADLK 152
Cdd:TIGR02168 198 LERQLKSLERQA-EKAERYKELKAELRELELAlLVLRLEELREELEELQEELKEAEEELEEL--------TAELQELEEK 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 153 mLLELKEMSSQQKDEIKALQKDVDTYQCQVENLQNSI----EKLIRQNEELLRKNASLQKQGRMIVEEKMEVVRRLEKTE 228
Cdd:TIGR02168 269 -LEELRLEVSELEEEIEELQKELYALANEISRLEQQKqilrERLANLERQLEELEAQLEELESKLDELAEELAELEEKLE 347
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71982687 229 ESNIELKKLVKETDRACKDMQLANQDNNEPRFTL----SELREVIKEKNILKGRVMELEEEL 286
Cdd:TIGR02168 348 ELKEELESLEAELEELEAELEELESRLEELEEQLetlrSKVAQLELQIASLNNEIERLEARL 409
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
68-288 |
7.70e-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: 41.93 E-value: 7.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 68 NEEIMRLSKAVERLEQEKHQRNQQhlkfEEELEQVEKTYRKDIDDLQQMVKSLVNENRNLSTTVSSLpnhadspVSTSMR 147
Cdd:TIGR04523 144 LTEIKKKEKELEKLNNKYNDLKKQ----KEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNL-------KKKIQK 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 148 EADL-KMLLELKEMSSQQKDEIKALQKDVDTYQCQVENLQNSIEKLIRQNEE----LLRKNASLQKQGRMIvEEKMEVVR 222
Cdd:TIGR04523 213 NKSLeSQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKikkqLSEKQKELEQNNKKI-KELEKQLN 291
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71982687 223 RLeKTEESNIELKKlVKETDRACKDmQLANQDnNEPRFTLSELREVIKEKNILKGRVMELEEELDN 288
Cdd:TIGR04523 292 QL-KSEISDLNNQK-EQDWNKELKS-ELKNQE-KKLEEIQNQISQNNKIISQLNEQISQLKKELTN 353
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
51-240 |
9.51e-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: 9.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 51 ISALETLEAMAAGNDRENEEIMRLSKAVERLEQEKHQRNQQHLKFEEELEQVEKTYRKDIDDLQQMVKSLVNENRNLSTT 130
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 131 VSSLPNHADSPVSTSMREADLKMLLE-LKEMSSQQKDEIKALQKDVDTYQCQVENLQNSIEKLIRQNEELLRKNASLQKQ 209
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLErLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
|
170 180 190
....*....|....*....|....*....|.
gi 71982687 210 gRMIVEEKMEVVRRLEKTEESNIELKKLVKE 240
Cdd:COG1196 472 -AALLEAALAELLEELAEAAARLLLLLEAEA 501
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
49-243 |
9.55e-04 |
|
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: 41.29 E-value: 9.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 49 KVISALETLEAMAAGNDRENEEIMRLSKAVERLEQEKHQRNQQHLKFEEELEQVEKTYRKDIDDLQQMvkslvNENRNLS 128
Cdd:COG4942 49 EEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRL-----GRQPPLA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 129 TTVSSlpnhaDSPVSTsmreadLKMLLELKEMSSQQKDEIKALQKDVDTYQCQVENLQNSIEKLIRQNEELLRKNASLQK 208
Cdd:COG4942 124 LLLSP-----EDFLDA------VRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEA 192
|
170 180 190
....*....|....*....|....*....|....*.
gi 71982687 209 QgrmiVEEKMEVVRRLEKTEES-NIELKKLVKETDR 243
Cdd:COG4942 193 L----KAERQKLLARLEKELAElAAELAELQQEAEE 224
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
47-226 |
9.76e-04 |
|
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: 9.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 47 MPKVISALETLEAMAAGNDRENEEIMRLSKAVERLEQEKHQRNQQHLKFEEELEQVEKTYRKDIDDLQQmVKSLVNENRN 126
Cdd:COG1579 2 MPEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEE-VEARIKKYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 127 LSTTVSslpnhadspvstSMREAD--LKMLLELKEMSSQQKDEIKALQKDVDTYQCQVENLQNSIEKLIRQNEELLRKN- 203
Cdd:COG1579 81 QLGNVR------------NNKEYEalQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELd 148
|
170 180
....*....|....*....|....*.
gi 71982687 204 ---ASLQKQGRMIVEEKMEVVRRLEK 226
Cdd:COG1579 149 eelAELEAELEELEAEREELAAKIPP 174
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
68-290 |
1.05e-03 |
|
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: 41.54 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 68 NEEIMRLSKAVERLEQEKHQRNQQHLKFEEELEQVE---KTYRKDIDDLQQMVKSLVNENRNLSTTVSS---LPNHADSP 141
Cdd:TIGR04523 334 NKIISQLNEQISQLKKELTNSESENSEKQRELEEKQneiEKLKKENQSYKQEIKNLESQINDLESKIQNqekLNQQKDEQ 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 142 VSTSMREADL--KMLLELKEMSSQQKDEIKALQKDVDTYQCQVENLQNSIEKLIRQNEELLRK----NASLQKQGRMIVE 215
Cdd:TIGR04523 414 IKKLQQEKELleKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSinkiKQNLEQKQKELKS 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 216 EKMEVVRRLEKTEESNIELKKLVKETDRACKDMQLANQDNNEPRFTLSELREVIKE------KNILKGRVMELEEELDNF 289
Cdd:TIGR04523 494 KEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKddfelkKENLEKEIDEKNKEIEEL 573
|
.
gi 71982687 290 K 290
Cdd:TIGR04523 574 K 574
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
49-290 |
1.13e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.57 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 49 KVISALETLEAMAagnDRENEEIMRLSKAVERLEQEKHQRN---QQHLKFEEELEqvekTYRKDIDDLQQMVKSLVNENR 125
Cdd:TIGR00606 840 TVVSKIELNRKLI---QDQQEQIQHLKSKTNELKSEKLQIGtnlQRRQQFEEQLV----ELSTEVQSLIREIKDAKEQDS 912
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 126 NLSTTVSSLPNHADSPVS---TSMREADLK---MLLELKEMSSQQKDEIKALQKDVDTYQCQVENLQNSIEKLIRQNEE- 198
Cdd:TIGR00606 913 PLETFLEKDQQEKEELISskeTSNKKAQDKvndIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKh 992
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 199 ---------LLRKNASLQKQGRMIVEEKMEVVRRLEKTEESNIELKKLVKETDrackDMQLANQDNNEPRFTlSELREVI 269
Cdd:TIGR00606 993 qekinedmrLMRQDIDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMG----QMQVLQMKQEHQKLE-ENIDLIK 1067
|
250 260
....*....|....*....|.
gi 71982687 270 KEKNILKGRVMELEEELDNFK 290
Cdd:TIGR00606 1068 RNHVLALGRQKGYEKEIKHFK 1088
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
70-241 |
1.66e-03 |
|
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: 40.77 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 70 EIMRLSKAVERLEQEKHQRNQQHLKFEEE---LEQVEKTYRKDIDDLQQMVKSLVNENRNLSTTVSSLPNHADSPVSTSM 146
Cdd:TIGR04523 476 SINKIKQNLEQKQKELKSKEKELKKLNEEkkeLEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELK 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 147 READLKMLLELKEMSSQQKDEIKAL-------QKDVDTYQCQVENLQNSIEKLIRQNEELLRKNASLQKQGRMIVEEKME 219
Cdd:TIGR04523 556 KENLEKEIDEKNKEIEELKQTQKSLkkkqeekQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKN 635
|
170 180
....*....|....*....|..
gi 71982687 220 VVRRLEKTEESNIELKKLVKET 241
Cdd:TIGR04523 636 IKSKKNKLKQEVKQIKETIKEI 657
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
72-226 |
2.07e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 40.67 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 72 MRLSKAVERLEQEKHQRN-QQHLkfEEELEQVEKT--YRKDIDDLQQMVKSLVNENRNLSTTVSSLPNHADSPVSTSMRE 148
Cdd:PRK11281 43 AQLDALNKQKLLEAEDKLvQQDL--EQTLALLDKIdrQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETLST 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 149 ADLKmllELKEMSSQQKDEIKALQKDVDTYQCQVENLQN----------------------------------------- 187
Cdd:PRK11281 121 LSLR---QLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTqperaqaalyansqrlqqirnllkggkvggkalrpsqrvll 197
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 71982687 188 -----SIEKLIRQNEELLRKNASLQKQGRMIVEEKMEVVRRLEK 226
Cdd:PRK11281 198 qaeqaLLNAQNDLQRKSLEGNTQLQDLLQKQRDYLTARIQRLEH 241
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
68-214 |
2.46e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.15 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 68 NEEIMRLSkavERLEQEKHQRNQQHLKFEEELEQVEKTYRKDIDDLQQMVKSLVNENRNLSTTVSSLPNhadspVSTSMR 147
Cdd:PRK12704 63 KEEIHKLR---NEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEK-----KEEELE 134
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71982687 148 EADLKMLLELKEMSSQQKDEIKALQKDvdtyqcQVEN-LQNSIEKLIRQNEELLRKNAslQKQGRMIV 214
Cdd:PRK12704 135 ELIEEQLQELERISGLTAEEAKEILLE------KVEEeARHEAAVLIKEIEEEAKEEA--DKKAKEIL 194
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
68-244 |
2.68e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.00 E-value: 2.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 68 NEEIMRLSKAVERLEQ--EKHQRNQQHLKFEEELEQVEKTY----------RKDIDDLQQMVKSLvneNRNLSTTVSSLP 135
Cdd:COG3206 181 EEQLPELRKELEEAEAalEEFRQKNGLVDLSEEAKLLLQQLselesqlaeaRAELAEAEARLAAL---RAQLGSGPDALP 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 136 NHADSPVSTSMREADLKMLLELKEMSSQQKDE---IKALQKdvdtyqcQVENLQNSIEKLIRQNEELLRKN-ASLQKQGR 211
Cdd:COG3206 258 ELLQSPVIQQLRAQLAELEAELAELSARYTPNhpdVIALRA-------QIAALRAQLQQEAQRILASLEAElEALQAREA 330
|
170 180 190
....*....|....*....|....*....|...
gi 71982687 212 MIVEEKMEVVRRLEKTEESNIELKKLVKETDRA 244
Cdd:COG3206 331 SLQAQLAQLEARLAELPELEAELRRLEREVEVA 363
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
69-290 |
4.40e-03 |
|
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: 39.67 E-value: 4.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 69 EEIMRLSKAVERLEQEKHQRNQQHLKFEEELEQVEKtYRKDIDDLQQM--------VKSLVNENRNLSTTVSSLPNH-AD 139
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEKRQQLERLRREREKAER-YQALLKEKREYegyellkeKEALERQKEAIERQLASLEEElEK 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 140 SPVSTSMREADLKMLLEL-----KEMSSQQKDEIKALQKDVDTYQCQVENLQNSIEKLIRQNEELLRKNASLQKQGRMIV 214
Cdd:TIGR02169 256 LTEEISELEKRLEEIEQLleelnKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLL 335
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71982687 215 EEKMEVVRRLektEESNIELKKLVKETDRACKDMQLanqdnneprfTLSELREVIKEKNILKGRVMELEEELDNFK 290
Cdd:TIGR02169 336 AEIEELEREI---EEERKRRDKLTEEYAELKEELED----------LRAELEEVDKEFAETRDELKDYREKLEKLK 398
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
54-299 |
6.33e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 38.89 E-value: 6.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 54 LETLEAMAAGNDRENEEIMRLSKAVERLEQEkhqrnqqhLKFEEELEQVEKTYRKDIDDLQQMVKSLVNENRNLSttVSS 133
Cdd:PRK03918 517 LEELEKKAEEYEKLKEKLIKLKGEIKSLKKE--------LEKLEELKKKLAELEKKLDELEEELAELLKELEELG--FES 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 134 LPNhadspVSTSMREAD--LKMLLELKEMSSQ---QKDEIKALQKDVDTYQCQVENLQNSIEKLIRQNEELLRKNAslQK 208
Cdd:PRK03918 587 VEE-----LEERLKELEpfYNEYLELKDAEKElerEEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYS--EE 659
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 209 QGRMIVEEKMEVVRRLEKTEESNIELKKLVKETDRACKDMQlanqdnnEPRFTLSELREVIKEKNILKGRVMELEEELDN 288
Cdd:PRK03918 660 EYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLK-------EELEEREKAKKELEKLEKALERVEELREKVKK 732
|
250
....*....|.
gi 71982687 289 FKPGAKKEIMR 299
Cdd:PRK03918 733 YKALLKERALS 743
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
149-287 |
8.26e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 38.60 E-value: 8.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 149 ADLKMLLELKEMSSQQKDEIKALQKDVDTYQCQVENLQNSIEKLIRQNEEL--LRKNASLQKQGRMIVEEKMEVVRRLEK 226
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLekLLQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71982687 227 TEESNIELKKLVKETDRACKDM-----QLANQDNNEPRFTLSELREVIKEKNILKGRVMELEEELD 287
Cdd:COG4717 151 LEERLEELRELEEELEELEAELaelqeELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELE 216
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
69-290 |
8.94e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 38.51 E-value: 8.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 69 EEIMRLSKAVE-RLEQEKHQRNQ---QHLKFEEELEQVEKTYrKDIDDLQQMVKSLVNENRNLSTTVSSLpnhadspvst 144
Cdd:PRK03918 189 ENIEELIKEKEkELEEVLREINEissELPELREELEKLEKEV-KELEELKEEIEELEKELESLEGSKRKL---------- 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 145 smrEADLKML--------LELKEMSSQQKdEIKALQKDVDTYQCQVENLQNSIEKLIRQNEELLRKNASLQKQGRMI--- 213
Cdd:PRK03918 258 ---EEKIRELeerieelkKEIEELEEKVK-ELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIkel 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 214 ---VEEKMEVVRRLEKTEESNIELKKLVKETDRACKDMqlANQDNNEPRFTLSELREVIKEKNILKGRVMELEEELDNFK 290
Cdd:PRK03918 334 eekEERLEELKKKLKELEKRLEELEERHELYEEAKAKK--EELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKIT 411
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
148-240 |
9.63e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 38.22 E-value: 9.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982687 148 EADLKMLLELKEMSSQQKDEIKALQKDVDTYQCQVENLQNSIEKLIRQNEELL-RKNASLQKQGRMIVEEKMEVVRRLEK 226
Cdd:PRK12704 46 EAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLdRKLELLEKREEELEKKEKELEQKQQE 125
|
90
....*....|....
gi 71982687 227 TEESNIELKKLVKE 240
Cdd:PRK12704 126 LEKKEEELEELIEE 139
|
|
| |
