|
Name |
Accession |
Description |
Interval |
E-value |
| TMCO5 |
pfam14992 |
TMCO5 family; The TMCO5 family includes human transmembrane and coiled-coil domain-containing ... |
33-311 |
8.56e-142 |
|
TMCO5 family; The TMCO5 family includes human transmembrane and coiled-coil domain-containing proteins 5A and 5B.
Pssm-ID: 464427 [Multi-domain] Cd Length: 278 Bit Score: 401.02 E-value: 8.56e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918709 33 LKYLNSDLEKDLQRLDEANQILLRKIQKKEESIQSLERDIAL--SIGRVPERDDFNEILAQKETALKDLELESAKLEKKN 110
Cdd:pfam14992 1 LNSLNSDLEKDLQRLDEANQVLLLKIQEKEEEIQSLEREITLtrSLAEDEEREELNFTIMEKEDALQELELETAKLEKKN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918709 111 KTLSKNVMELQKKISKGL-KNIASDPETLKKKVTEFKVKLQKSTESCAQQEKEIAKMESDYQSVFQLCEDQAHYIKKYQE 189
Cdd:pfam14992 81 EILVKSVMELQRKLSRKSdKNTGLEQETLKQMLEELKVKLQQSEESCADQEKELAKVESDYQSVHQLCEDQALCIKKYQE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918709 190 ILREMEKEKEVMLLEKEISKAQNDSSQVVKpgstLVETIQSNMEKNIIKKQKRKFWLRHFRYLFFMVMIVIRLLGYVFFH 269
Cdd:pfam14992 161 ILRKMEEEKETRLLEKEVSKAQSNSSQRVK----LVETIQQNMEKTIIKKQKRIFWKRHFRYLFFMVLIFIRLLGYVLFH 236
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 568918709 270 LQYVNPDFLVDTLPMLMSRSSLKWLRDILFPFLTLEVEDVLP 311
Cdd:pfam14992 237 LQYINPDLLVDTLPKMLSRRTLWRLRCFLFPFLTLEVEDLLP 278
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
21-253 |
1.89e-07 |
|
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: 52.38 E-value: 1.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918709 21 TEIPTLEAIKQNLKYLNSDLEKDLQRLDEANQILLRKIQKKEESIQSLERDIALSIGRVPErddFNEILAQKETALKDLE 100
Cdd:TIGR02169 805 EEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEE---LEEELEELEAALRDLE 881
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918709 101 LESAKLEKKNKTLSKNVMELQKKISKglknIASDPETLKKKVTEFKVKLQKSTESCAQQEKEIAKMESDYQSVFQLCEDQ 180
Cdd:TIGR02169 882 SRLGDLKKERDELEAQLRELERKIEE----LEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQ 957
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918709 181 ahyiKKYQEILREMEKEKEV-MLLEKEISKAQNDSSQVVKPGSTLVETIQSNMEK-NIIKKQKRKFWL-------RHFRY 251
Cdd:TIGR02169 958 ----AELQRVEEEIRALEPVnMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERiEEYEKKKREVFMeafeainENFNE 1033
|
..
gi 568918709 252 LF 253
Cdd:TIGR02169 1034 IF 1035
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
26-243 |
6.15e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.75 E-value: 6.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918709 26 LEAIKQNLKYLNSDLEKDLQRLDEANQIL----------LRKIQKKEESIQSLERDIALSIGRVPERDDFNEILAQKETA 95
Cdd:PRK03918 167 LGEVIKEIKRRIERLEKFIKRTENIEELIkekekeleevLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918709 96 LKDLELESAKLEKKNKTLSKNVMELQKKISKgLKNIASDPETLKKKVTEFkVKLQKSTESCAQQEKEIAKMESDYQSVFQ 175
Cdd:PRK03918 247 LESLEGSKRKLEEKIRELEERIEELKKEIEE-LEEKVKELKELKEKAEEY-IKLSEFYEEYLDELREIEKRLSRLEEEIN 324
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568918709 176 LCEDQAHYIKKYQEILREMEKEKEVMLLEKEISKAQNDSSQVVKPGSTLVETIQSNMEKNIIKKQKRK 243
Cdd:PRK03918 325 GIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKE 392
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
4-132 |
3.33e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.15 E-value: 3.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918709 4 EAMEDAGQNPLDDEAEITEIPTLEAIKQNLKYLnSDLEKDLQRLDEANQILLRKIQKKEESIQSLERDIALSigRVPERD 83
Cdd:COG2433 383 EELIEKELPEEEPEAEREKEHEERELTEEEEEI-RRLEEQVERLEAEVEELEAELEEKDERIERLERELSEA--RSEERR 459
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 568918709 84 DfneilAQKETALKDLELESAKLEKKNKTLSKNVMELQKKISKgLKNIA 132
Cdd:COG2433 460 E-----IRKDREISRLDREIERLERELEEERERIEELKRKLER-LKELW 502
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| TMCO5 |
pfam14992 |
TMCO5 family; The TMCO5 family includes human transmembrane and coiled-coil domain-containing ... |
33-311 |
8.56e-142 |
|
TMCO5 family; The TMCO5 family includes human transmembrane and coiled-coil domain-containing proteins 5A and 5B.
Pssm-ID: 464427 [Multi-domain] Cd Length: 278 Bit Score: 401.02 E-value: 8.56e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918709 33 LKYLNSDLEKDLQRLDEANQILLRKIQKKEESIQSLERDIAL--SIGRVPERDDFNEILAQKETALKDLELESAKLEKKN 110
Cdd:pfam14992 1 LNSLNSDLEKDLQRLDEANQVLLLKIQEKEEEIQSLEREITLtrSLAEDEEREELNFTIMEKEDALQELELETAKLEKKN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918709 111 KTLSKNVMELQKKISKGL-KNIASDPETLKKKVTEFKVKLQKSTESCAQQEKEIAKMESDYQSVFQLCEDQAHYIKKYQE 189
Cdd:pfam14992 81 EILVKSVMELQRKLSRKSdKNTGLEQETLKQMLEELKVKLQQSEESCADQEKELAKVESDYQSVHQLCEDQALCIKKYQE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918709 190 ILREMEKEKEVMLLEKEISKAQNDSSQVVKpgstLVETIQSNMEKNIIKKQKRKFWLRHFRYLFFMVMIVIRLLGYVFFH 269
Cdd:pfam14992 161 ILRKMEEEKETRLLEKEVSKAQSNSSQRVK----LVETIQQNMEKTIIKKQKRIFWKRHFRYLFFMVLIFIRLLGYVLFH 236
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 568918709 270 LQYVNPDFLVDTLPMLMSRSSLKWLRDILFPFLTLEVEDVLP 311
Cdd:pfam14992 237 LQYINPDLLVDTLPKMLSRRTLWRLRCFLFPFLTLEVEDLLP 278
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
21-253 |
1.89e-07 |
|
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: 52.38 E-value: 1.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918709 21 TEIPTLEAIKQNLKYLNSDLEKDLQRLDEANQILLRKIQKKEESIQSLERDIALSIGRVPErddFNEILAQKETALKDLE 100
Cdd:TIGR02169 805 EEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEE---LEEELEELEAALRDLE 881
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918709 101 LESAKLEKKNKTLSKNVMELQKKISKglknIASDPETLKKKVTEFKVKLQKSTESCAQQEKEIAKMESDYQSVFQLCEDQ 180
Cdd:TIGR02169 882 SRLGDLKKERDELEAQLRELERKIEE----LEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQ 957
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918709 181 ahyiKKYQEILREMEKEKEV-MLLEKEISKAQNDSSQVVKPGSTLVETIQSNMEK-NIIKKQKRKFWL-------RHFRY 251
Cdd:TIGR02169 958 ----AELQRVEEEIRALEPVnMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERiEEYEKKKREVFMeafeainENFNE 1033
|
..
gi 568918709 252 LF 253
Cdd:TIGR02169 1034 IF 1035
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
26-243 |
6.15e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.75 E-value: 6.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918709 26 LEAIKQNLKYLNSDLEKDLQRLDEANQIL----------LRKIQKKEESIQSLERDIALSIGRVPERDDFNEILAQKETA 95
Cdd:PRK03918 167 LGEVIKEIKRRIERLEKFIKRTENIEELIkekekeleevLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918709 96 LKDLELESAKLEKKNKTLSKNVMELQKKISKgLKNIASDPETLKKKVTEFkVKLQKSTESCAQQEKEIAKMESDYQSVFQ 175
Cdd:PRK03918 247 LESLEGSKRKLEEKIRELEERIEELKKEIEE-LEEKVKELKELKEKAEEY-IKLSEFYEEYLDELREIEKRLSRLEEEIN 324
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568918709 176 LCEDQAHYIKKYQEILREMEKEKEVMLLEKEISKAQNDSSQVVKPGSTLVETIQSNMEKNIIKKQKRK 243
Cdd:PRK03918 325 GIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKE 392
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
38-219 |
1.49e-05 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 45.96 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918709 38 SDLEKDLQRLDEANQILLRKIQKKEESIQSLERDIAlsigrvpERDDFNEILAQKETALKDlelesaklEKKNKTLSKNV 117
Cdd:pfam15905 97 QALEEELEKVEAKLNAAVREKTSLSASVASLEKQLL-------ELTRVNELLKAKFSEDGT--------QKKMSSLSMEL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918709 118 MELQKKISKGLKNIASDPETLKKKVTEFKVKLQKSTESCAQQEKEIAKMESDYQSVFQLCEDQAHYIKKYQEILREMEKE 197
Cdd:pfam15905 162 MKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSEQVEKY 241
|
170 180
....*....|....*....|..
gi 568918709 198 KEVMLLEKEISKAQNDSSQVVK 219
Cdd:pfam15905 242 KLDIAQLEELLKEKNDEIESLK 263
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
21-228 |
2.00e-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: 2.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918709 21 TEIPTLEAIKQNLKYLNSDLEKDLQRLDEANQILLRKIQKKEESIQSLERDIALSIGRvpeRDDFNEILAQKETALKDLE 100
Cdd:TIGR02169 294 EKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKR---RDKLTEEYAELKEELEDLR 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918709 101 LESAKLEKKNKTLSKNVMELQKKISKG-------LKNIASDPETLKKKVTE-------FKVKLQKSTESCAQQEKEIAKM 166
Cdd:TIGR02169 371 AELEEVDKEFAETRDELKDYREKLEKLkreinelKRELDRLQEELQRLSEEladlnaaIAGIEAKINELEEEKEDKALEI 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568918709 167 ESDYQSVFQLCEDQAHYIKKY---QEILREMEKEKEVMLLEKEISKAQNDSSQVVKPGSTLVETI 228
Cdd:TIGR02169 451 KKQEWKLEQLAADLSKYEQELydlKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEV 515
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
4-132 |
3.33e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.15 E-value: 3.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918709 4 EAMEDAGQNPLDDEAEITEIPTLEAIKQNLKYLnSDLEKDLQRLDEANQILLRKIQKKEESIQSLERDIALSigRVPERD 83
Cdd:COG2433 383 EELIEKELPEEEPEAEREKEHEERELTEEEEEI-RRLEEQVERLEAEVEELEAELEEKDERIERLERELSEA--RSEERR 459
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 568918709 84 DfneilAQKETALKDLELESAKLEKKNKTLSKNVMELQKKISKgLKNIA 132
Cdd:COG2433 460 E-----IRKDREISRLDREIERLERELEEERERIEELKRKLER-LKELW 502
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
24-230 |
4.00e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 4.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918709 24 PTLEAIKQNLKYLNSD---LEKDLQRLDEANQILLRKIQKKEESIQSLERDIalsigrvperDDFNEILAQKETALKDLE 100
Cdd:COG3883 16 PQIQAKQKELSELQAEleaAQAELDALQAELEELNEEYNELQAELEALQAEI----------DKLQAEIAEAEAEIEERR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918709 101 lesAKLEKKNKTL---------------SKNV------MELQKKISKGLKNIASDPETLKKKVTEFKVKLQKSTESCAQQ 159
Cdd:COG3883 86 ---EELGERARALyrsggsvsyldvllgSESFsdfldrLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEAL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568918709 160 EKEIAKMESDYQSVFqlcEDQAHYIKKYQEILREMEKEKEVMLLEKEISKAQNDSSQVVKPGSTLVETIQS 230
Cdd:COG3883 163 KAELEAAKAELEAQQ---AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
|
| CAGE1 |
pfam15066 |
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in ... |
63-204 |
4.20e-04 |
|
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in tumour tissues compared with surrounding tissues. CAGE-1 gene showed testis-specific expression among normal tissues and displayed wide expression in a variety of cancer cell lines and cancer tissues. CAGE-1 is predominantly expressed during post-meiotic stages. It localizes to the acrosomal matrix and acrosomal granule showing it to be a component of the acrosome of mammalian spermatids and spermatozoa.
Pssm-ID: 464481 Cd Length: 528 Bit Score: 41.74 E-value: 4.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918709 63 ESIQSLERDIALsigrvperddfNEILAQKETALKDLELESAKLEKKNKTLSKNVMELQKKISK--GLKNIASDpetLKK 140
Cdd:pfam15066 305 ESLQPLEEDMAL-----------NEVLQKLKHTNRKQQMQIQDLQCSNLYLEKKVKELQMKITKqqVFVDIINK---LKE 370
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568918709 141 KVTE-----FKVKLQKStescaqqekEIAKMESDYQSVfqLCEDQAHyikkyqeiLREMEKEKEVMLLE 204
Cdd:pfam15066 371 NVEEliedkYNVILEKN---------DINKTLQNLQEI--LANTQKH--------LQESRKEKETLQLE 420
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
15-216 |
6.50e-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: 6.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918709 15 DDEAEITEIPTLEAIKQNLKYLNSDLEKDLQRLDEANQILLRKIQKKEESIQSLERDIALSIgrvPERDDFNEILAQKET 94
Cdd:COG1196 289 EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE---EELEEAEAELAEAEE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918709 95 ALKDLELESAKLEKKNKTLSKNVMELQKKISKGLKNIASDPETLKKKVTEfKVKLQKSTESCAQQEKEIAKMESDYQSVF 174
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER-LERLEEELEELEEALAELEEEEEEEEEAL 444
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 568918709 175 Q--LCEDQAHYIKKYQEILREMEKEKEVMLLEKEISKAQNDSSQ 216
Cdd:COG1196 445 EeaAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE 488
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
43-206 |
1.07e-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: 39.91 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918709 43 DLQRLDEANQILLRKIQKKEESIQSLERDIAlsigrvperdDFNEILAQKETALKDLELESAKLEKKNKTLSKNVMELQK 122
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELA----------ALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918709 123 KI-----SKGLKNIASDPETLKKKVTEFKVKLQKSTESCAQQEKEIAKMESDYQsvfQLCEDQAHYIKKYQEILREMEKE 197
Cdd:COG1579 81 QLgnvrnNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELA---ELEAELEEKKAELDEELAELEAE 157
|
....*....
gi 568918709 198 KEVMLLEKE 206
Cdd:COG1579 158 LEELEAERE 166
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
31-243 |
2.54e-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: 39.62 E-value: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918709 31 QNLKYLNSDLEKDLQRLDEANQILLRKIQKKEESIQSLERDI----ALSIGRVPERDDFNEILAQKETALKDLELESAKL 106
Cdd:TIGR04523 387 KNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIerlkETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESL 466
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918709 107 EKKNKTLS---KNVMELQKKISKGLKNIASDPETLKKKVTEFKVKLQKSTESCAQQEKEIAKMESDYQSVFQLCEDQAHY 183
Cdd:TIGR04523 467 ETQLKVLSrsiNKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDE 546
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568918709 184 IKKYQEILREMEKEKEVMLLEKEISKAQNDSSQVVKPGSTLVETIQ--SNMEKNIIKKQKRK 243
Cdd:TIGR04523 547 LNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDqkEKEKKDLIKEIEEK 608
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|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
26-136 |
4.61e-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: 38.21 E-value: 4.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918709 26 LEAIKQNLKYLNSDLEKDLQRLDEANQILLRKIQKKEESIQSLERdialsigrvpERDDFNEILAQKETALKDLELESAK 105
Cdd:COG4942 141 LKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEE----------ERAALEALKAERQKLLARLEKELAE 210
|
90 100 110
....*....|....*....|....*....|.
gi 568918709 106 LEKKNKTLSKNVMELQKKISKGLKNIASDPE 136
Cdd:COG4942 211 LAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
22-219 |
5.96e-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: 37.82 E-value: 5.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918709 22 EIPTLEAIKQNLKYLNSDLEKDLQRLDEANQILLRKIQKKEESIQSLERDIALSIGrvpERDDFNEILAQKETALKDLEL 101
Cdd:COG4942 35 EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK---EIAELRAELEAQKEELAELLR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918709 102 ESAKLEKKNKTL----------SKNVMELQKKISKGLKN----IASDPETLKKKVTEFKVKLQKSTESCAQQEKEIAKME 167
Cdd:COG4942 112 ALYRLGRQPPLAlllspedfldAVRRLQYLKYLAPARREqaeeLRADLAELAALRAELEAERAELEALLAELEEERAALE 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 568918709 168 SDYQSVFQLCEDQAHYIKKYQEILREMEKEKEvmLLEKEISKAQNDSSQVVK 219
Cdd:COG4942 192 ALKAERQKLLARLEKELAELAAELAELQQEAE--ELEALIARLEAEAAAAAE 241
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
40-240 |
9.45e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 37.80 E-value: 9.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918709 40 LEKDLQRLDEANQILLRKIQKKEES-----IQSLERDIALSIGRVP----ERDDFNEILAQKETALKDLELESAKLEKKN 110
Cdd:pfam17380 407 LEEERQRKIQQQKVEMEQIRAEQEEarqreVRRLEEERAREMERVRleeqERQQQVERLRQQEEERKRKKLELEKEKRDR 486
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918709 111 KTLSK-NVMELQKKISKGLKNIASdpETLKKKVTEFKVKlQKSTESCAQQEKEIAKMESDYQSVFQ---LCEDQAHYIKK 186
Cdd:pfam17380 487 KRAEEqRRKILEKELEERKQAMIE--EERKRKLLEKEME-ERQKAIYEEERRREAEEERRKQQEMEerrRIQEQMRKATE 563
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 568918709 187 YQEILREMEKEKEVMLLEKEISKAQNDSsqvvkPGSTLVETIQSNMEKNIIKKQ 240
Cdd:pfam17380 564 ERSRLEAMEREREMMRQIVESEKARAEY-----EATTPITTIKPIYRPRISEYQ 612
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