|
Name |
Accession |
Description |
Interval |
E-value |
| Nuf2 |
pfam03800 |
Nuf2 family; Members of this family are components of the mitotic spindle. It has been shown ... |
3-146 |
1.13e-40 |
|
Nuf2 family; Members of this family are components of the mitotic spindle. It has been shown that Nuf2 from yeast is part of a complex called the Ndc80p complex. This complex is thought to bind to the microtubules of the spindle. An arabidopsis protein has been included in this family that has previously not been identified as a member of this family, Swiss:Q9C953. The match is not strong, but in common with other members of this family contains coiled-coil to the C terminus of this region.
Pssm-ID: 461057 Cd Length: 139 Bit Score: 142.30 E-value: 1.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 3 TLSFPRYNVAELVVHIRNKLLTgADGKNLSKsdflpnPKSDVLYMIYMKALQLVYGVRLEHFYMMPMN--IEVTYPHLME 80
Cdd:pfam03800 1 KDSFPRLSVDEIVACLRELGIP-VTEEDLKK------PTPDFVQKLYERFLELLMGITREDIEPPQLAaaALLEYPELHE 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1240700485 81 GFLPVRSLFFYMDSFMPICRVNDFEIVDILNPRTNRTSRFLSGIINFIHFRETCLEKCEEFLLQNK 146
Cdd:pfam03800 74 DSLPLLNLYRHLKRFLKACGVDDFSLKDLLKPDPKRTRRILSALINFARFREERLELYDELLEESE 139
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
185-457 |
3.52e-08 |
|
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: 56.22 E-value: 3.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 185 DDIQELQHLLNEEFRQKTTL-LQ----EEYAKMKSDISEKTKHLneQKLSLVSLKEVEDNLKSKIVDSPEKLKNYKDKMK 259
Cdd:TIGR02168 186 ENLDRLEDILNELERQLKSLeRQaekaERYKELKAELRELELAL--LVLRLEELREELEELQEELKEAEEELEELTAELQ 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 260 GT---VQKLRSAREKVMEQYDIYRDSVDCLpscqleVQLYQKKSQDLADNREKLSSLLKESLNLEDQIESDSSELKKLKT 336
Cdd:TIGR02168 264 ELeekLEELRLEVSELEEEIEELQKELYAL------ANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 337 EENSLIRMTTVKKEKLATARFKINKKQEDVKHYKQAMIEDCNKVQEKRDAVCEqvttVNQEIHKIKSAIQQLRDTKKReI 416
Cdd:TIGR02168 338 ELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ----LELQIASLNNEIERLEARLER-L 412
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1240700485 417 LKSQEIFVNLKSALEKyhEGIEKVAEERSAKLEEKTAELKK 457
Cdd:TIGR02168 413 EDRRERLQQEIEELLK--KLEEAELKELQAELEELEEELEE 451
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
132-448 |
1.11e-07 |
|
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: 54.34 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 132 ETCLEKCEEFLLQNKSSMVRMQQLSNVHQEALMKLE-----------KLNTVPAEEREEFKQFMDDIQELQH--LLNEEF 198
Cdd:pfam05483 411 KKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQarekeihdleiQLTAIKTSEEHYLKEVEDLKTELEKekLKNIEL 490
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 199 RQKTTLLQEEYAKMKSDISEKTKHLNEQKLSLVSLKEVEDNLKSKIVDSPEKLKNYKDKMKGTVQKLRSAREKVMEQYDI 278
Cdd:pfam05483 491 TAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDK 570
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 279 YRDSVDCLPSCQLEVQLYQKKSQDLADNreklssllkeslnLEDQIESDSSELKKLKTEENSLIRMTTVKKEKLATARFK 358
Cdd:pfam05483 571 SEENARSIEYEVLKKEKQMKILENKCNN-------------LKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIK 637
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 359 INKKQEDVKHYKQAMIEDCNKVQEKRDAVCEQVTTVNQEIHKIKSAIQQLRDTKKREILKSQEIFVNLKSALEKYHEGIE 438
Cdd:pfam05483 638 VNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYD 717
|
330
....*....|
gi 1240700485 439 KVAEERSAKL 448
Cdd:pfam05483 718 KIIEERDSEL 727
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
171-404 |
3.95e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.06 E-value: 3.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 171 TVPAEEREEFKQfmDDIQELQHLLNEefrqkttlLQEEYAKMKSDISEKTKHLNEQKLSLVSLKEVEDNLKSKIVDSPEK 250
Cdd:COG3883 11 PAFADPQIQAKQ--KELSELQAELEA--------AQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 251 LKNYKDKMKGTVQklrsarekvmeqyDIYRDSVDclpSCQLEVQLYQKKSQDLADNREKLSSLLKESLNLEDQIESDSSE 330
Cdd:COG3883 81 IEERREELGERAR-------------ALYRSGGS---VSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAE 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1240700485 331 LKKLKTEENSLIRMTTVKKEKLATARFKINKKQEDVKHYKQAMIEDCNKVQEKRDAVCEQVTTVNQEIHKIKSA 404
Cdd:COG3883 145 LEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
175-462 |
4.09e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.29 E-value: 4.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 175 EEREEFKQFMDDIQELQHLLNEEFRQKTTLLQE--EYAKMKSDISEKTKHLNEQKLSLVSLKEVEDNLKSKIvdspEKLK 252
Cdd:PRK03918 176 RRIERLEKFIKRTENIEELIKEKEKELEEVLREinEISSELPELREELEKLEKEVKELEELKEEIEELEKEL----ESLE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 253 NYKDKMKGTVQKLRSAREKVMEQYDIYRDSVDCLPSCQLEVQLYQKKSQDLADNREKLSSLLKESLNLEDQI-------- 324
Cdd:PRK03918 252 GSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEIngieerik 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 325 --ESDSSELKKLKTEENSLIRMTTVKKEK---LATARFKINKKQEDVKHYKQAMIEDCNK-----------VQEKRDAVC 388
Cdd:PRK03918 332 elEEKEERLEELKKKLKELEKRLEELEERhelYEEAKAKKEELERLKKRLTGLTPEKLEKeleelekakeeIEEEISKIT 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 389 EQVTTVNQEIHKIKSAIQQLRDTK------KREILKSQEifvnlKSALEKYHEGIEKVAEERsAKLEEKTAELKKRMVRM 462
Cdd:PRK03918 412 ARIGELKKEIKELKKAIEELKKAKgkcpvcGRELTEEHR-----KELLEEYTAELKRIEKEL-KEIEEKERKLRKELREL 485
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| Nuf2 |
pfam03800 |
Nuf2 family; Members of this family are components of the mitotic spindle. It has been shown ... |
3-146 |
1.13e-40 |
|
Nuf2 family; Members of this family are components of the mitotic spindle. It has been shown that Nuf2 from yeast is part of a complex called the Ndc80p complex. This complex is thought to bind to the microtubules of the spindle. An arabidopsis protein has been included in this family that has previously not been identified as a member of this family, Swiss:Q9C953. The match is not strong, but in common with other members of this family contains coiled-coil to the C terminus of this region.
Pssm-ID: 461057 Cd Length: 139 Bit Score: 142.30 E-value: 1.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 3 TLSFPRYNVAELVVHIRNKLLTgADGKNLSKsdflpnPKSDVLYMIYMKALQLVYGVRLEHFYMMPMN--IEVTYPHLME 80
Cdd:pfam03800 1 KDSFPRLSVDEIVACLRELGIP-VTEEDLKK------PTPDFVQKLYERFLELLMGITREDIEPPQLAaaALLEYPELHE 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1240700485 81 GFLPVRSLFFYMDSFMPICRVNDFEIVDILNPRTNRTSRFLSGIINFIHFRETCLEKCEEFLLQNK 146
Cdd:pfam03800 74 DSLPLLNLYRHLKRFLKACGVDDFSLKDLLKPDPKRTRRILSALINFARFREERLELYDELLEESE 139
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
185-457 |
3.52e-08 |
|
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: 56.22 E-value: 3.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 185 DDIQELQHLLNEEFRQKTTL-LQ----EEYAKMKSDISEKTKHLneQKLSLVSLKEVEDNLKSKIVDSPEKLKNYKDKMK 259
Cdd:TIGR02168 186 ENLDRLEDILNELERQLKSLeRQaekaERYKELKAELRELELAL--LVLRLEELREELEELQEELKEAEEELEELTAELQ 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 260 GT---VQKLRSAREKVMEQYDIYRDSVDCLpscqleVQLYQKKSQDLADNREKLSSLLKESLNLEDQIESDSSELKKLKT 336
Cdd:TIGR02168 264 ELeekLEELRLEVSELEEEIEELQKELYAL------ANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 337 EENSLIRMTTVKKEKLATARFKINKKQEDVKHYKQAMIEDCNKVQEKRDAVCEqvttVNQEIHKIKSAIQQLRDTKKReI 416
Cdd:TIGR02168 338 ELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ----LELQIASLNNEIERLEARLER-L 412
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1240700485 417 LKSQEIFVNLKSALEKyhEGIEKVAEERSAKLEEKTAELKK 457
Cdd:TIGR02168 413 EDRRERLQQEIEELLK--KLEEAELKELQAELEELEEELEE 451
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
174-458 |
7.92e-08 |
|
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: 55.06 E-value: 7.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 174 AEEREEFKQFMDDIQELQHLLNEeFRQKTTLLQEEYAKMKSDISEKTKHLNEQKLSLVSLKEVEDNLKSKIVDSPEKLKN 253
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAE-LRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 254 YKDKMKGTVQKLRSA----------REKVMEQYDIYRDSVDCLPSCQLEVQ-LYQKKSQDLADNREKLSSLLKESLNLED 322
Cdd:TIGR02168 759 LEAEIEELEERLEEAeeelaeaeaeIEELEAQIEQLKEELKALREALDELRaELTLLNEEAANLRERLESLERRIAATER 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 323 QIESDSSELKKLKTEENSLirmtTVKKEKLATARFKINKKQEDVKHYKQAMIEDCNKVQEKRDAVCEQVTTVNQEIHKIK 402
Cdd:TIGR02168 839 RLEDLEEQIEELSEDIESL----AAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELR 914
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1240700485 403 SAIQQLRDTKKREILKSQEIFVNLKSALEKYHEGIE---KVAEERSAKLEEKTAELKKR 458
Cdd:TIGR02168 915 RELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSltlEEAEALENKIEDDEEEARRR 973
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
132-448 |
1.11e-07 |
|
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: 54.34 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 132 ETCLEKCEEFLLQNKSSMVRMQQLSNVHQEALMKLE-----------KLNTVPAEEREEFKQFMDDIQELQH--LLNEEF 198
Cdd:pfam05483 411 KKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQarekeihdleiQLTAIKTSEEHYLKEVEDLKTELEKekLKNIEL 490
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 199 RQKTTLLQEEYAKMKSDISEKTKHLNEQKLSLVSLKEVEDNLKSKIVDSPEKLKNYKDKMKGTVQKLRSAREKVMEQYDI 278
Cdd:pfam05483 491 TAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDK 570
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 279 YRDSVDCLPSCQLEVQLYQKKSQDLADNreklssllkeslnLEDQIESDSSELKKLKTEENSLIRMTTVKKEKLATARFK 358
Cdd:pfam05483 571 SEENARSIEYEVLKKEKQMKILENKCNN-------------LKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIK 637
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 359 INKKQEDVKHYKQAMIEDCNKVQEKRDAVCEQVTTVNQEIHKIKSAIQQLRDTKKREILKSQEIFVNLKSALEKYHEGIE 438
Cdd:pfam05483 638 VNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYD 717
|
330
....*....|
gi 1240700485 439 KVAEERSAKL 448
Cdd:pfam05483 718 KIIEERDSEL 727
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
135-462 |
1.31e-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: 51.22 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 135 LEKCEEFLLQNKSSM--------VRMQQLSNVHQEALMKLEKLNTVPAEEREEFKQFMDDIQELQhllneefrQKTTLLQ 206
Cdd:TIGR02169 686 LKRELSSLQSELRRIenrldelsQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLE--------QEIENVK 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 207 EEYAKMKSDISEKTKHLNEQKLSLVSLKEVEDNLK-SKIVDSPEKLKNYKDKMKGTVQKLRSAREKVMEQYDIYRDSVDC 285
Cdd:TIGR02169 758 SELKELEARIEELEEDLHKLEEALNDLEARLSHSRiPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQE 837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 286 LPSCQLEVQLyQKKS--QDLADNREKLSSLLKESLNLEDQIESDSSELKKLKTEENSL---IRMTTVKKEKLATARFKIN 360
Cdd:TIGR02169 838 LQEQRIDLKE-QIKSieKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELeaqLRELERKIEELEAQIEKKR 916
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 361 KKQEDVKHYKQAMIE-----DCNKVQEKRDAVCEQVT-TVNQEIHKIKSAIQQLRDTKKREIlksqEIFVNLKSALEKYH 434
Cdd:TIGR02169 917 KRLSELKAKLEALEEelseiEDPKGEDEEIPEEELSLeDVQAELQRVEEEIRALEPVNMLAI----QEYEEVLKRLDELK 992
|
330 340 350
....*....|....*....|....*....|
gi 1240700485 435 EGIEKVAEERSAkLEEKTAEL--KKRMVRM 462
Cdd:TIGR02169 993 EKRAKLEEERKA-ILERIEEYekKKREVFM 1021
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
171-404 |
3.95e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.06 E-value: 3.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 171 TVPAEEREEFKQfmDDIQELQHLLNEefrqkttlLQEEYAKMKSDISEKTKHLNEQKLSLVSLKEVEDNLKSKIVDSPEK 250
Cdd:COG3883 11 PAFADPQIQAKQ--KELSELQAELEA--------AQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 251 LKNYKDKMKGTVQklrsarekvmeqyDIYRDSVDclpSCQLEVQLYQKKSQDLADNREKLSSLLKESLNLEDQIESDSSE 330
Cdd:COG3883 81 IEERREELGERAR-------------ALYRSGGS---VSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAE 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1240700485 331 LKKLKTEENSLIRMTTVKKEKLATARFKINKKQEDVKHYKQAMIEDCNKVQEKRDAVCEQVTTVNQEIHKIKSA 404
Cdd:COG3883 145 LEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
175-462 |
4.09e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.29 E-value: 4.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 175 EEREEFKQFMDDIQELQHLLNEEFRQKTTLLQE--EYAKMKSDISEKTKHLNEQKLSLVSLKEVEDNLKSKIvdspEKLK 252
Cdd:PRK03918 176 RRIERLEKFIKRTENIEELIKEKEKELEEVLREinEISSELPELREELEKLEKEVKELEELKEEIEELEKEL----ESLE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 253 NYKDKMKGTVQKLRSAREKVMEQYDIYRDSVDCLPSCQLEVQLYQKKSQDLADNREKLSSLLKESLNLEDQI-------- 324
Cdd:PRK03918 252 GSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEIngieerik 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 325 --ESDSSELKKLKTEENSLIRMTTVKKEK---LATARFKINKKQEDVKHYKQAMIEDCNK-----------VQEKRDAVC 388
Cdd:PRK03918 332 elEEKEERLEELKKKLKELEKRLEELEERhelYEEAKAKKEELERLKKRLTGLTPEKLEKeleelekakeeIEEEISKIT 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 389 EQVTTVNQEIHKIKSAIQQLRDTK------KREILKSQEifvnlKSALEKYHEGIEKVAEERsAKLEEKTAELKKRMVRM 462
Cdd:PRK03918 412 ARIGELKKEIKELKKAIEELKKAKgkcpvcGRELTEEHR-----KELLEEYTAELKRIEKEL-KEIEEKERKLRKELREL 485
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
254-462 |
2.95e-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: 43.51 E-value: 2.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 254 YKDKMKGTVQKLRSAREKVMEQYDIYRDSVDCLPSCQLEVQL---YQKKSQDLadnREKLSSLLKESLN-LEDQIESDSS 329
Cdd:TIGR02168 170 YKERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKaerYKELKAEL---RELELALLVLRLEeLREELEELQE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 330 ELKKLKTEENSLIRMTTVKKEKLATARFKINKKQEDVkhykqamiedcNKVQEKRDAVCEQVTTVNQEIHKIKSAIQQLR 409
Cdd:TIGR02168 247 ELKEAEEELEELTAELQELEEKLEELRLEVSELEEEI-----------EELQKELYALANEISRLEQQKQILRERLANLE 315
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1240700485 410 DTKKReilkSQEIFVNLKSALEKYhegiekvaEERSAKLEEKTAELKKRMVRM 462
Cdd:TIGR02168 316 RQLEE----LEAQLEELESKLDEL--------AEELAELEEKLEELKEELESL 356
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
150-461 |
3.85e-04 |
|
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: 43.13 E-value: 3.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 150 VRMQQLSNVHQEALMKLEKLNTvPAEEREEFKQFMDDIQE-----LQHLLNEEFRQKTTL------LQEEYAKMKSDISE 218
Cdd:TIGR02169 184 ENIERLDLIIDEKRQQLERLRR-EREKAERYQALLKEKREyegyeLLKEKEALERQKEAIerqlasLEEELEKLTEEISE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 219 KTKHLNEqklSLVSLKEVEDNLKSKIVDSPEKLKNYKDKMKGTVQKLRSA-REKVMEQYDIYRDSVdclpscQLEVQLYQ 297
Cdd:TIGR02169 263 LEKRLEE---IEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSiAEKERELEDAEERLA------KLEAEIDK 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 298 KKSQdLADNREKLSSLLKESLNLEDqiesdssELKKLKTEENSLIRMTTVKKEKLATARFKINKKQ---EDVKHYKQAMI 374
Cdd:TIGR02169 334 LLAE-IEELEREIEEERKRRDKLTE-------EYAELKEELEDLRAELEEVDKEFAETRDELKDYReklEKLKREINELK 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 375 EDCNKVQEKRDAVCEQVTTVNQEIHKIKSAIQQLRDTKKREILKSQEIFVNLKSA---LEKYHEGIEKVAEERSaKLEEK 451
Cdd:TIGR02169 406 RELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLaadLSKYEQELYDLKEEYD-RVEKE 484
|
330
....*....|
gi 1240700485 452 TAELKKRMVR 461
Cdd:TIGR02169 485 LSKLQRELAE 494
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
189-451 |
1.60e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 41.26 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 189 ELQHLLNEEFRQKTTLLQEEYAKMKSDISEKTKHLNEQKLSLVSLKEVEDNLKSKIVDSPEKLKNYK-------DKMKGT 261
Cdd:pfam15921 246 QLEALKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNsmymrqlSDLEST 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 262 VQKLRSareKVMEQYDIYRDSVDclpscQLEVQLYQKKSQdLADNREKLSSLLKESLNLEDQIESDSSELKK------LK 335
Cdd:pfam15921 326 VSQLRS---ELREAKRMYEDKIE-----ELEKQLVLANSE-LTEARTERDQFSQESGNLDDQLQKLLADLHKrekelsLE 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 336 TEENS-LIRMTTVKKEKLATARFKINKKQEDVKHYK---QAMIEDCNKVQEKRDAVceqVTTVNQEIHKIKSAIQQLRDT 411
Cdd:pfam15921 397 KEQNKrLWDRDTGNSITIDHLRRELDDRNMEVQRLEallKAMKSECQGQMERQMAA---IQGKNESLEKVSSLTAQLEST 473
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1240700485 412 KkrEILKSqeiFVNLKSALEKYHEGIEKVAEERSAKLEEK 451
Cdd:pfam15921 474 K--EMLRK---VVEELTAKKMTLESSERTVSDLTASLQEK 508
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
151-422 |
1.84e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.69 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 151 RMQQLSNVHQEALMKLEKLNTVPAEEREEFKQFMDDIQELQHLLNEefrqkttlLQEEYAKMKSDISEKTKHLNEQKLSL 230
Cdd:COG1196 247 ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE--------LLAELARLEQDIARLEERRRELEERL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 231 VSLKEVEDNLKSKIVDSPEKLKNYKDKMKGTVQKLRSAREKVMEQYDIYRDsvdclpscqlEVQLYQKKSQDLADNREKL 310
Cdd:COG1196 319 EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE----------AEAELAEAEEELEELAEEL 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 311 SSLLKESLNLEDQIESDSSELKKLKTEENSLIRMTTVKKEKLATARFKINKKQEDVKHYKQAMIEDCNKVQEKRDAVCEQ 390
Cdd:COG1196 389 LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468
|
250 260 270
....*....|....*....|....*....|..
gi 1240700485 391 VTTVNQEIHKIKSAIQQLRDTKKREILKSQEI 422
Cdd:COG1196 469 LEEAALLEAALAELLEELAEAAARLLLLLEAE 500
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
290-458 |
1.89e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.69 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 290 QLEVQLYQKKSQDLADNREKLSSLLKEslnLEDQIESDSSELKKLKTEENSLirmttvkKEKLATARFKINKKQEDVKHY 369
Cdd:COG1196 224 ELEAELLLLKLRELEAELEELEAELEE---LEAELEELEAELAELEAELEEL-------RLELEELELELEEAQAEEYEL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 370 KQAMIE---DCNKVQEKRDAVCEQVTTVNQEIHKIKSAIQQLRDTKKREILKSQEIFVNLKSALEKYHEGIEKVAEERSA 446
Cdd:COG1196 294 LAELARleqDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
|
170
....*....|..
gi 1240700485 447 KLEEKTAELKKR 458
Cdd:COG1196 374 LAEAEEELEELA 385
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
234-451 |
1.97e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.77 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 234 KEVEDNLKSKIVDSPEKLKnyKDKMKGTVQKLRSAREK---VMEQYDIYRDSVDclpscqlevQLYQKKSQDLADNREKL 310
Cdd:PHA02562 154 KLVEDLLDISVLSEMDKLN--KDKIRELNQQIQTLDMKidhIQQQIKTYNKNIE---------EQRKKNGENIARKQNKY 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 311 SSLLKESLNLEDQIESDSSELKKLKTEENSlirmTTVKKEKLATARFKINKK----QEDVKHY---------KQAMIEDC 377
Cdd:PHA02562 223 DELVEEAKTIKAEIEELTDELLNLVMDIED----PSAALNKLNTAAAKIKSKieqfQKVIKMYekggvcptcTQQISEGP 298
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1240700485 378 NKVQEKRDavceQVTTVNQEIHKIKSAIQQLRDtKKREILKSQEIFVNLKSALEKYHEGIekVAEERSAKLEEK 451
Cdd:PHA02562 299 DRITKIKD----KLKELQHSLEKLDTAIDELEE-IMDEFNEQSKKLLELKNKISTNKQSL--ITLVDKAKKVKA 365
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
309-458 |
2.15e-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: 39.52 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 309 KLSSLLKESLNLEDQIESDSSELKKLKTEENSLIRMTTVKKEKLATARFKINKKQEDVKHYKQAMIEDCNKVQEKRDAvc 388
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN-- 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 389 EQVTTVNQEIHKIKSAIQQLRDtkkrEILKSQEIfvnlKSALEKYHEGIEKVAEERSAKLEEKTAELKKR 458
Cdd:COG1579 89 KEYEALQKEIESLKRRISDLED----EILELMER----IEELEEELAELEAELAELEAELEEKKAELDEE 150
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
150-423 |
2.28e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 40.72 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 150 VRMQQLSNVHQEALMKLEKLNTVPAEEREEFKQFMDDIQELQHLLNEEFRQKTTLLQEEYAKMKSDISEK---TKHLNEQ 226
Cdd:TIGR00618 594 VRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHalsIRVLPKE 673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 227 KLSLVSLKEVE-DNLKSKIVDSPEKLKNYKDKMKGTVQKLRSAREKVMEQYDIYRDSVDCLPSCQLEVQLYQKKSQDLAD 305
Cdd:TIGR00618 674 LLASRQLALQKmQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQAR 753
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 306 NREKLSSLLKESLNLEDQIESDS-SELKKLKTEENSLIRMTTVKKEKLATARFKInkkQEDVKHYKQAMIEDCNKVQEKR 384
Cdd:TIGR00618 754 TVLKARTEAHFNNNEEVTAALQTgAELSHLAAEIQFFNRLREEDTHLLKTLEAEI---GQEIPSDEDILNLQCETLVQEE 830
|
250 260 270
....*....|....*....|....*....|....*....
gi 1240700485 385 DAVCEQVTTVNQEIHKIKSAIQQLRDTKKREILKSQEIF 423
Cdd:TIGR00618 831 EQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQA 869
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
185-421 |
2.48e-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: 40.13 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 185 DDIQELQHLLnEEFRQKTTLLQEEYAKMKSDISEKTKHLNEQKLSLVSLKEVEDNLKSKIVDSPEKLKNYKDKMKGTVQK 264
Cdd:COG4942 20 DAAAEAEAEL-EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 265 LRSAREKVMEQ-YDIYRDSvdclPSCQLEVQLYQKKSQDLADNREKLSSLLKESLNLEDQIESDSSELKKLKTEenslir 343
Cdd:COG4942 99 LEAQKEELAELlRALYRLG----RQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE------ 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1240700485 344 mttvkkekLATARFKINKKQEDVKHYKQAMIEDCNKVQEKRDAVCEQVTTVNQEIHKIKSAIQQLRDTKKREILKSQE 421
Cdd:COG4942 169 --------LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
188-458 |
4.40e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.53 E-value: 4.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 188 QELQHLLNEEFRQKTTLLQEEYAKMKSDISEKTKHLNEQKLSLVSLKEVEDNLKskivdspEKLKNYKDKMKGTVQKLRS 267
Cdd:COG1196 220 EELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELR-------LELEELELELEEAQAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 268 AREKVMEQydiyrdsvdclpscQLEVQLYQKKSQDLADNREKLS----SLLKESLNLEDQIESDSSELKKLKTEENSLIR 343
Cdd:COG1196 293 LLAELARL--------------EQDIARLEERRRELEERLEELEeelaELEEELEELEEELEELEEELEEAEEELEEAEA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 344 MTTVKKEKLATARFKINKKQEDVKHYKQAMIEDCNKVQEKRDAVcEQVTTVNQEIHKIKSAIQQLRDTKKREILKSQEIF 423
Cdd:COG1196 359 ELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL-EELEEAEEALLERLERLEEELEELEEALAELEEEE 437
|
250 260 270
....*....|....*....|....*....|....*
gi 1240700485 424 VNLKSALEKYHEGIEKVAEERSAKLEEKTAELKKR 458
Cdd:COG1196 438 EEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
154-457 |
6.79e-03 |
|
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: 38.93 E-value: 6.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 154 QLSNVHQEALMKLEKLNTVPAEEREEFKQFMDDIQEL-----QHLLNEEFRQKttLLQEEYAKMKSDISEKTKHLNEQKL 228
Cdd:pfam05483 328 QLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELlrteqQRLEKNEDQLK--IITMELQKKSSELEEMTKFKNNKEV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 229 SLVSLKEVEDNlKSKIVDSPEKLKNYKDKMKGTVQKLR---SAREKvmEQYDiyrdsvdclpscqLEVQLYQKKSQDlad 305
Cdd:pfam05483 406 ELEELKKILAE-DEKLLDEKKQFEKIAEELKGKEQELIfllQAREK--EIHD-------------LEIQLTAIKTSE--- 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 306 nreklSSLLKESLNLEDQIESDSSELKKLKTEENSLIRMTTVKKEKLATARFKINKKQEDV---KHYKQAMIEDCNKVQE 382
Cdd:pfam05483 467 -----EHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIincKKQEERMLKQIENLEE 541
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 383 KRDAVCEQVTTVNQEIH--------KIKSAIQQLRDTKKREILKSQEIFV------NLKSALEKYHEGIEKVAEERSAKL 448
Cdd:pfam05483 542 KEMNLRDELESVREEFIqkgdevkcKLDKSEENARSIEYEVLKKEKQMKIlenkcnNLKKQIENKNKNIEELHQENKALK 621
|
....*....
gi 1240700485 449 EEKTAELKK 457
Cdd:pfam05483 622 KKGSAENKQ 630
|
|
|