|
Name |
Accession |
Description |
Interval |
E-value |
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
133-503 |
2.60e-10 |
|
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: 63.89 E-value: 2.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 133 EKLNRSNSELEDEILclekDLKEEKSKhsqqdelmadISKSIQSLEDESKSLKSQIAEAKIICKTFKMSEERraiaIKDA 212
Cdd:TIGR04523 207 KKKIQKNKSLESQIS----ELKKQNNQ----------LKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNK----IKKQ 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 213 LNEN-SQLQTSHKQLFQQEAEV--WKGEVSELNKQKITFEDSKVHAEqvLNDKENHIKTLTGHLPMMKDQAAVLEEDTTd 289
Cdd:TIGR04523 269 LSEKqKELEQNNKKIKELEKQLnqLKSEISDLNNQKEQDWNKELKSE--LKNQEKKLEEIQNQISQNNKIISQLNEQIS- 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 290 ddNLELEVNSQWENGANLDDPLKGALKKLIHAAKLNVS----LKSLEGERNHIIIQLSEVDKTKEELTEHIKNLQTQQES 365
Cdd:TIGR04523 346 --QLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSykqeIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKEL 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 366 LQSENIYFESENQKLQQKLKIMTEFYQEDEMK----------LYRKLTVEENYRIEEEEKLSKVEEKLSRATEQLETYRK 435
Cdd:TIGR04523 424 LEKEIERLKETIIKNNSEIKDLTNQDSVKELIiknldntresLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNE 503
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 436 LAKDLEEELErtvhfYQKQVISYEKRGHDNwLAARTAERN--LSDLRKENAHNKQKLTETELKFELLEKD 503
Cdd:TIGR04523 504 EKKELEEKVK-----DLTKKISSLKEKIEK-LESEKKEKEskISDLEDELNKDDFELKKENLEKEIDEKN 567
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
107-509 |
2.99e-10 |
|
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: 63.97 E-value: 2.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 107 EVESSLEDASFekaaaeearSLEATCEKLNrsnsELEDEILCLEKDLKEEKSKHSQQDELMADISKSIQSLEDESKSLKS 186
Cdd:pfam05483 251 EKENKMKDLTF---------LLEESRDKAN----QLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEE 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 187 --QIAeAKIICKtfkMSEERRAiaikdALNENSQLQTSHKQLfqqeaevwkgeVSELNKQKITFEDSKVHAEQVLNDKEN 264
Cdd:pfam05483 318 dlQIA-TKTICQ---LTEEKEA-----QMEELNKAKAAHSFV-----------VTEFEATTCSLEELLRTEQQRLEKNED 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 265 HIKTLTGHLpmmKDQAAVLEEDTTDDDNLELEV----------------NSQWENganLDDPLKGALKKLIHAaklnvsL 328
Cdd:pfam05483 378 QLKIITMEL---QKKSSELEEMTKFKNNKEVELeelkkilaedeklldeKKQFEK---IAEELKGKEQELIFL------L 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 329 KSLEGERNHIIIQLSEVDKTKEELTEHIKNLQTQQESLQSENIYFES-------ENQKLQQKLKIMT---EFYQED---- 394
Cdd:pfam05483 446 QAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAhcdklllENKELTQEASDMTlelKKHQEDiinc 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 395 ---EMKLYRKLTVEENYRIEEEEKLSKVEEKLSRATEQLETYRKLAKDLEEELERTVHFYQKQVISYEKRGHDNWLAART 471
Cdd:pfam05483 526 kkqEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIEN 605
|
410 420 430
....*....|....*....|....*....|....*...
gi 146262005 472 AERNLSDLRKENAHNKQKLTETELKFELLEKDPNALDV 509
Cdd:pfam05483 606 KNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLEL 643
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
95-444 |
5.51e-10 |
|
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: 62.84 E-value: 5.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 95 KFSLIQ--KEYEGYEVESSLEDASFEKAAAEEARSLEATCEKlnrsNSELEDEILCLEKDLKEEKSKHSQQDELMADISK 172
Cdd:pfam05557 8 KARLSQlqNEKKQMELEHKRARIELEKKASALKRQLDRESDR----NQELQKRIRLLEKREAEAEEALREQAELNRLKKK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 173 SIQSLEDESKSLKSQIAEAK--IICKTFKMSEERRAIAIKDalnenSQLQT--SHKQLFQQEAEVWKGEVSELNKQKITF 248
Cdd:pfam05557 84 YLEALNKKLNEKESQLADARevISCLKNELSELRRQIQRAE-----LELQStnSELEELQERLDLLKAKASEAEQLRQNL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 249 EDSkvhaEQVLNDKENHIKTLTGHLPMMKDQAAVLeedttdddnlelevnsqwenganlddplKGALKKLIHAAKLNVSL 328
Cdd:pfam05557 159 EKQ----QSSLAEAEQRIKELEFEIQSQEQDSEIV----------------------------KNSKSELARIPELEKEL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 329 KSLEGERNHiiiqLSEVDKTKEELTEHIKNLQT---QQESLQSENIYFESENQKLQQKLKIMTEFYQEDEMKLYRKLTVE 405
Cdd:pfam05557 207 ERLREHNKH----LNENIENKLLLKEEVEDLKRkleREEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNLRSPEDLS 282
|
330 340 350
....*....|....*....|....*....|....*....
gi 146262005 406 ENYRIEEEEKLSKVEEKlSRATEQLETYRKLAKDLEEEL 444
Cdd:pfam05557 283 RRIEQLQQREIVLKEEN-SSLTSSARQLEKARRELEQEL 320
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
75-444 |
2.26e-09 |
|
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: 60.80 E-value: 2.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 75 EQKLGATLSGLIEEKCKLLEKFS--------LIQKEYEGYEVESSLEDASFEKAA-------------AEEARSLEATCE 133
Cdd:TIGR04523 252 QTQLNQLKDEQNKIKKQLSEKQKeleqnnkkIKELEKQLNQLKSEISDLNNQKEQdwnkelkselknqEKKLEEIQNQIS 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 134 KLNRSNSELEDEILCLEKDLKEEKSKHSQQDE-------LMADISKSIQSLEDESKSLKSQIAEAKIICKTFKMSEERRA 206
Cdd:TIGR04523 332 QNNKIISQLNEQISQLKKELTNSESENSEKQReleekqnEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKD 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 207 IAIKDALNENSQLQTSHKQLfQQEAEVWKGEVSELNKQKITFEDSKVHAEQVLNDKENHIKTLTGHLPMMKDQaavLEED 286
Cdd:TIGR04523 412 EQIKKLQQEKELLEKEIERL-KETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQN---LEQK 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 287 TTDDDNLELEVNSQWENGANLDDPLKgALKKLIhaAKLNVSLKSLEGERNHIIIQLSEV---------DKTKEELTEHIK 357
Cdd:TIGR04523 488 QKELKSKEKELKKLNEEKKELEEKVK-DLTKKI--SSLKEKIEKLESEKKEKESKISDLedelnkddfELKKENLEKEID 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 358 NLQTQQESLQSENIYFESENQKLQQKLKImtefyQEDEMKLYRKltveenyrieeeeKLSKVEEKLSRATEQLETYRKLA 437
Cdd:TIGR04523 565 EKNKEIEELKQTQKSLKKKQEEKQELIDQ-----KEKEKKDLIK-------------EIEEKEKKISSLEKELEKAKKEN 626
|
....*..
gi 146262005 438 KDLEEEL 444
Cdd:TIGR04523 627 EKLSSII 633
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
85-446 |
3.21e-09 |
|
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: 60.85 E-value: 3.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 85 LIEEKCKLLE--KFSLIQKEYEGYEVESSLEDASFEKAAAE-EARSLEATCEKLNRSNSELEDEILCLEKDLKEEKSKHS 161
Cdd:TIGR02169 203 LRREREKAERyqALLKEKREYEGYELLKEKEALERQKEAIErQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIK 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 162 QQ-DELMADISKSIQSLEDESKSLKSQIAEAKiicKTFKMSEERRAIAIKDAlnensqlqtsHKQlfQQEAEVWKGEVSE 240
Cdd:TIGR02169 283 DLgEEEQLRVKEKIGELEAEIASLERSIAEKE---RELEDAEERLAKLEAEI----------DKL--LAEIEELEREIEE 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 241 LNKQKITFEDSKVHAEQVLNDKENHIKtltghlpmmkdqaavlEEDTTdddnlelevnsqwenganlddplkgalkklih 320
Cdd:TIGR02169 348 ERKRRDKLTEEYAELKEELEDLRAELE----------------EVDKE-------------------------------- 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 321 AAKLNVSLKSLEgernhiiiqlSEVDKTKEELTEHIKNLQTQQESLQSENIYFESENQKLQQKLKIMTEFyqEDEMKLYR 400
Cdd:TIGR02169 380 FAETRDELKDYR----------EKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINEL--EEEKEDKA 447
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 146262005 401 KltveenyrieeeeKLSKVEEKLSRATEQLETYRKLAKDLEEELER 446
Cdd:TIGR02169 448 L-------------EIKKQEWKLEQLAADLSKYEQELYDLKEEYDR 480
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
86-507 |
1.78e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.15 E-value: 1.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 86 IEEKCKLLEKfSLIQKEYEGYEVESSLEDASFEKAAAE-EARSLEATCEKLNrsnsELEDEILCLEKDLKEEKSKHSQqd 164
Cdd:PRK03918 191 IEELIKEKEK-ELEEVLREINEISSELPELREELEKLEkEVKELEELKEEIE----ELEKELESLEGSKRKLEEKIRE-- 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 165 elmadISKSIQSLEDESKSLKSQIAEAKIICKtfKMSEERRAIAIKDALNENSQLQTSHKQLFQQEAEVWKGEVSELNKq 244
Cdd:PRK03918 264 -----LEERIEELKKEIEELEEKVKELKELKE--KAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEE- 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 245 kitfedskvhaeqvlndKENHIKTLTGHLPMMKDQAAVLEEDttdddnLELevnsqwenganlddpLKGALKKLIHAAKL 324
Cdd:PRK03918 336 -----------------KEERLEELKKKLKELEKRLEELEER------HEL---------------YEEAKAKKEELERL 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 325 NVSLKSLEGERnhIIIQLSEVDKTKEELTEHIKNLQTQQESLQSEniyfESENQKLQQKLK-----------IMTEFYQE 393
Cdd:PRK03918 378 KKRLTGLTPEK--LEKELEELEKAKEEIEEEISKITARIGELKKE----IKELKKAIEELKkakgkcpvcgrELTEEHRK 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 394 DEMKLYRKltveenyrieeeeKLSKVEEKLSRATEQLETYRKLAKDLEEELERtvhfyQKQVISYEKrghdnwlaarTAE 473
Cdd:PRK03918 452 ELLEEYTA-------------ELKRIEKELKEIEEKERKLRKELRELEKVLKK-----ESELIKLKE----------LAE 503
|
410 420 430
....*....|....*....|....*....|....*
gi 146262005 474 RnLSDLRKE-NAHNKQKLTETELKFELLEKDPNAL 507
Cdd:PRK03918 504 Q-LKELEEKlKKYNLEELEKKAEEYEKLKEKLIKL 537
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
123-391 |
2.87e-07 |
|
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: 54.26 E-value: 2.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 123 EEARSLEATCEKLNRSNSELEDEILCLEKDLKEEKSKHSQQDELMADISKSIQSLEDESKSLKSQIAEakiicktfKMSE 202
Cdd:TIGR04523 426 KEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKS--------KEKE 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 203 erraiaIKDALNENSQLQTSHKQLFQQEAEvwkgevSELNKQKITFEDSKVhaEQVLNDKENHIKTLtghlpmmkdqaav 282
Cdd:TIGR04523 498 ------LKKLNEEKKELEEKVKDLTKKISS------LKEKIEKLESEKKEK--ESKISDLEDELNKD------------- 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 283 leEDTTDDDNLELEVNSQWENganlDDPLKGALKKLIHA-AKLNVSLKSLEGERNHIIIQLSEVDKTKEELTEHIKNLQT 361
Cdd:TIGR04523 551 --DFELKKENLEKEIDEKNKE----IEELKQTQKSLKKKqEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKK 624
|
250 260 270
....*....|....*....|....*....|.
gi 146262005 362 QQESLQSENIYFESENQKLQQKLK-IMTEFY 391
Cdd:TIGR04523 625 ENEKLSSIIKNIKSKKNKLKQEVKqIKETIK 655
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
87-508 |
4.68e-07 |
|
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: 53.49 E-value: 4.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 87 EEKcKLLEKFSLIQKEYEGYEVE-SSLEDASFEKAaaeearsleatcEKLNRSNSELEDeilcLEKDLKEEKSKHSQQDE 165
Cdd:TIGR04523 34 EEK-QLEKKLKTIKNELKNKEKElKNLDKNLNKDE------------EKINNSNNKIKI----LEQQIKDLNDKLKKNKD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 166 LMADISKSIQSLEDESKSLKSQIAEAKIICKTFKMSEERRAIAIKDALNENSQLqtshkqlfQQEAEVWKGEVSELNKQK 245
Cdd:TIGR04523 97 KINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKK--------EKELEKLNNKYNDLKKQK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 246 ITFEDSKVHAEQVLNDKENHIKTLTGHLPMMKDQAAVLEEDTTDDDNLELEV------NSQWENGANLDDPLKGALKKLI 319
Cdd:TIGR04523 169 EELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQIselkkqNNQLKDNIEKKQQEINEKTTEI 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 320 HAAKLNvsLKSLEGERNHIIIQLSEVDKTKEELTEHIKNLQTQQESLQSEniYFESENQKLQQKLKIMTEFYQEDEMKLy 399
Cdd:TIGR04523 249 SNTQTQ--LNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSE--ISDLNNQKEQDWNKELKSELKNQEKKL- 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 400 rkltveenyrIEEEEKLSKVEEKLSRATEQLETYRKLAKDLE---EELERTVHFYQKQVISYEKRGHDNWLAARTAERNL 476
Cdd:TIGR04523 324 ----------EEIQNQISQNNKIISQLNEQISQLKKELTNSEsenSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQI 393
|
410 420 430
....*....|....*....|....*....|..
gi 146262005 477 SDLRKENAHNKQKLTETELKFELLEKDPNALD 508
Cdd:TIGR04523 394 NDLESKIQNQEKLNQQKDEQIKKLQQEKELLE 425
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
146-447 |
7.99e-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: 52.75 E-value: 7.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 146 ILCLEKDLKEEKSKHSQQDELMADISKSIQSLEDESKSLKSQIAEAKIIcktfkmsEERRAIAIKDALNENSQLQTSHKQ 225
Cdd:TIGR02168 672 ILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKE-------LEELSRQISALRKDLARLEAEVEQ 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 226 LFQQEAEVwKGEVSELNKQKITFEDSKVHAEQVLNDKENHIKTLTGHLPMMKDQAAVLEEDTTDddnlelevnsqwenga 305
Cdd:TIGR02168 745 LEERIAQL-SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDE---------------- 807
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 306 nlddpLKGALKKL-IHAAKLNVSLKSLEGERNHIIIQLSEVDKTKEELTEHIKNLQTQQESLQSEniyFESENQKLQQKL 384
Cdd:TIGR02168 808 -----LRAELTLLnEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEEL---IEELESELEALL 879
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 146262005 385 KIMTEfyQEDEMKLYRKltveenYRIEEEEKLSKVEEKLSRATEQLETYRKLAKDLEEELERT 447
Cdd:TIGR02168 880 NERAS--LEEALALLRS------ELEELSEELRELESKRSELRRELEELREKLAQLELRLEGL 934
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
115-393 |
8.82e-07 |
|
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: 52.52 E-value: 8.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 115 ASFEKAAAEEARSLEATCEKLNRSNSELEDEILCLEKDLKEEKSKHSQQDELMADISKSIQSLEDESKSLKSQIAEAKII 194
Cdd:pfam10174 439 TTLEEALSEKERIIERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSK 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 195 CKTFKmseerraIAIKDALNENSQLQTSHKQLFQQEAEVWKGE-----VSELNKQKITF--EDSKVHAE-----QVL--- 259
Cdd:pfam10174 519 LKSLE-------IAVEQKKEECSKLENQLKKAHNAEEAVRTNPeindrIRLLEQEVARYkeESGKAQAEverllGILrev 591
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 260 ----NDKENHIKTLTGHLP-MMKDQaavleedTTDDDNLE-LEVNSQWENGANLDDPLKgalkklihaaklnvslKSLEG 333
Cdd:pfam10174 592 enekNDKDKKIAELESLTLrQMKEQ-------NKKVANIKhGQQEMKKKGAQLLEEARR----------------REDNL 648
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 146262005 334 ERNHIIIQLSEV----DKTKEELTEHIKNLQTQQESLQSENIYFESENQKLQQKLKIMTEFYQE 393
Cdd:pfam10174 649 ADNSQQLQLEELmgalEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAERRKQLEEILEMKQE 712
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
118-400 |
4.34e-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: 50.44 E-value: 4.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 118 EKAAAEEARSLEATCEKLNRSNSELEDEILCLEKDLKEEKSKHSQQDELMADISKSIQSLEDESKSLKSQIAEAKIICKT 197
Cdd:TIGR02168 248 LKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 198 FkmseERRAIAIKDALNENsqlqtshkqlfQQEAEVWKGEVSELNKQKITFEDSKVHAEQVLNDKENHIKTLTGHLPMMK 277
Cdd:TIGR02168 328 L----ESKLDELAEELAEL-----------EEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 278 DQAAVLEEDTTdddNLELEVNSQWENGANLDDPLKGALKKLIHAAklnvsLKSLEGERNHIIIQLSEVDKTKEELTEHIK 357
Cdd:TIGR02168 393 LQIASLNNEIE---RLEARLERLEDRRERLQQEIEELLKKLEEAE-----LKELQAELEELEEELEELQEELERLEEALE 464
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 146262005 358 NLQTQQESLQSENIYFESENQKLQQKLKiMTEFYQEDEMKLYR 400
Cdd:TIGR02168 465 ELREELEEAEQALDAAERELAQLQARLD-SLERLQENLEGFSE 506
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
94-385 |
2.15e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.01 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 94 EKFSLIQKEYEGYEVEssledasfekAAAEEARSLEATCEKLNRSNSELEDEILCLEKDLKEEKSKHSQQDELMADISKS 173
Cdd:COG1196 213 ERYRELKEELKELEAE----------LLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELE 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 174 IQSLEDESKSLKSQIAEAkiicktfkmsEERRAIAIKDALNENSQLQtshkQLfQQEAEVWKGEVSELNKQKITFEDSKV 253
Cdd:COG1196 283 LEEAQAEEYELLAELARL----------EQDIARLEERRRELEERLE----EL-EEELAELEEELEELEEELEELEEELE 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 254 HAEQVLNDKENHIktltghlpmmKDQAAVLEEDTTDDDNLELEVNSQWENGANLddpLKGALKKLIHAAKLNVSLKSLEG 333
Cdd:COG1196 348 EAEEELEEAEAEL----------AEAEEALLEAEAELAEAEEELEELAEELLEA---LRAAAELAAQLEELEEAEEALLE 414
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 146262005 334 ERNHIIIQLSEVDKTKEELTEHIKNLQTQQESLQSENIYFESENQKLQQKLK 385
Cdd:COG1196 415 RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
87-507 |
2.90e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 47.86 E-value: 2.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 87 EEKCKLLEKfslIQKEYEGyeVESSLEDASfeKAAAEEARSLEATCEKLNRSNSELEDEILCLEKDLKEEKSKHSQQDEl 166
Cdd:pfam01576 172 EEKAKSLSK---LKNKHEA--MISDLEERL--KKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEE- 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 167 maDISKSIQSLEDES----------KSLKSQIAEAKIICKTFKMSEERRAIAIKDALNENSQLQTSHKQLF-----QQEA 231
Cdd:pfam01576 244 --ELQAALARLEEETaqknnalkkiRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLdttaaQQEL 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 232 EVWK-GEVSELnkQKITFEDSKVHAEQVLNDKENH---IKTLTGHLPMMKDQAAVLEED--TTDDDNLELEVNSQWENGA 305
Cdd:pfam01576 322 RSKReQEVTEL--KKALEEETRSHEAQLQEMRQKHtqaLEELTEQLEQAKRNKANLEKAkqALESENAELQAELRTLQQA 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 306 NLDDPLKGalkklihaaklnvslKSLEGERNHIIIQLSEVDKTKEELTEHIKNLQTQQESL-------QSENIYFESENQ 378
Cdd:pfam01576 400 KQDSEHKR---------------KKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVssllneaEGKNIKLSKDVS 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 379 KLQQKLKIMTEFYQEDEMKlyrKLTVEEnyrieeeeKLSKVEEKLSRATEQLEtyrklakdlEEE-----LERTVHFYQK 453
Cdd:pfam01576 465 SLESQLQDTQELLQEETRQ---KLNLST--------RLRQLEDERNSLQEQLE---------EEEeakrnVERQLSTLQA 524
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 146262005 454 QVISYEKRGHDNWLAARTAERNLSDLRKENAHNKQKLTETELKFELLEKDPNAL 507
Cdd:pfam01576 525 QLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRL 578
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
109-517 |
3.03e-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: 47.41 E-value: 3.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 109 ESSLEDASFEKAaaeeaRSLEATCEKLNRSNSELEDEILCLEKDLKEEKSKHSQQDELMADISKSIQSL--EDESKSLK- 185
Cdd:pfam05483 62 QEGLKDSDFENS-----EGLSRLYSKLYKEAEKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELqfENEKVSLKl 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 186 -SQIAEAKIICKtfkmsEERRAIAIKDALNENSQLQTSHKQLFQQEAEVWKGEVSELN----KQKITFEDSKVHAEQV-- 258
Cdd:pfam05483 137 eEEIQENKDLIK-----ENNATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNnnieKMILAFEELRVQAENArl 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 259 -----------------------LNDKENHI--------------KTLTGHLPMMKDQAAVLEEDTT-DDDNLELEVNSQ 300
Cdd:pfam05483 212 emhfklkedhekiqhleeeykkeINDKEKQVsllliqitekenkmKDLTFLLEESRDKANQLEEKTKlQDENLKELIEKK 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 301 WENGANLDDpLKGALKKLIHAAK-----LNVSLKSLEGERNHIIIQLSEVDKTKEELTEHIKNLQTQQESLQSeniYFES 375
Cdd:pfam05483 292 DHLTKELED-IKMSLQRSMSTQKaleedLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEE---LLRT 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 376 ENQKLQQ---KLKIMTEFYQE--DEMKLYRKLTVEENYRIEEEEKLSKVEEKLSRATEQLEtyrKLAKDLEEELERTVHF 450
Cdd:pfam05483 368 EQQRLEKnedQLKIITMELQKksSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFE---KIAEELKGKEQELIFL 444
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 451 YQKQvisyEKRGHD---NWLAARTAERNLSdlrKENAHNKQKLTETELKFELLEKDPNALDVSNTAFGRE 517
Cdd:pfam05483 445 LQAR----EKEIHDleiQLTAIKTSEEHYL---KEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQE 507
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
70-446 |
3.32e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 47.66 E-value: 3.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 70 LYVGREQKLGATLSGLIEEKCKLLEKFSLIQKEYEGYEVeSSLEDASFEKAAAEEARSLEATCEKLNRSNSELEDEILCL 149
Cdd:pfam02463 613 LEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKG-VSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAK 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 150 EKDLKEEKSKhSQQDELMADISKSIQSLEDESKSLKSQIAEAKIIcKTFKMSEERRAIAIKDALNENSQLQTSHKQLFQQ 229
Cdd:pfam02463 692 EEILRRQLEI-KKKEQREKEELKKLKLEAEELLADRVQEAQDKIN-EELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSEL 769
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 230 EAEVWKGEVSELNKQKITFEDSKVHAEQVLNDKENHIKTltghlpMMKDQAAVLEEDTTDDDNLELEVNSQWENganldd 309
Cdd:pfam02463 770 SLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEE------ELKEEAELLEEEQLLIEQEEKIKEEELEE------ 837
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 310 pLKGALKKLIHAAKLNVSLKSLEGERNHIIIQLSEVDKTKEELTE--HIKNLQTQQESLQSENIYFESENQKLQQKLKIM 387
Cdd:pfam02463 838 -LALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEqkLKDELESKEEKEKEEKKELEEESQKLNLLEEKE 916
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 146262005 388 TEfYQEDEMKLYRKLTVEENYRIEEEEKLSKVEEKLSRATEQLETYRKLAKDLEEELER 446
Cdd:pfam02463 917 NE-IEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGK 974
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
123-244 |
6.38e-05 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 43.40 E-value: 6.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 123 EEARSLEATCEKLNRSNSELEDEILCLEKDLKE--EKSKHSQQD---ELM--ADISKSIQSLEDESKSLKSQIAEAKIic 195
Cdd:pfam07926 1 AELSSLQSEIKRLKEEAADAEAQLQKLQEDLEKqaEIAREAQQNyerELVlhAEDIKALQALREELNELKAEIAELKA-- 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 146262005 196 ktfkmseerRAIAIKDALNENSQLQTSHKQLFQQEAEVWKGEVSELNKQ 244
Cdd:pfam07926 79 ---------EAESAKAELEESEESWEEQKKELEKELSELEKRIEDLNEQ 118
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
86-476 |
6.70e-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: 46.64 E-value: 6.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 86 IEEKCKL--------LEKFSLIQKEYEgyEVESSLEDASFEKAAAEEARSL------------EATCEKLNRSN------ 139
Cdd:pfam05483 273 LEEKTKLqdenlkelIEKKDHLTKELE--DIKMSLQRSMSTQKALEEDLQIatkticqlteekEAQMEELNKAKaahsfv 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 140 -SELEDEILCLEKDLKEEKSKHSQQDE----LMADISKSIQSLEDESKSLKSQIAE----AKIICKTFKMSEERRAI-AI 209
Cdd:pfam05483 351 vTEFEATTCSLEELLRTEQQRLEKNEDqlkiITMELQKKSSELEEMTKFKNNKEVEleelKKILAEDEKLLDEKKQFeKI 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 210 KDALNENSQ-----LQTSHKQLFQQEAEVWKGEVSELNKQKiTFEDSKVHAEqvlNDKENHIKtLTGHLPMMKDQAAVLE 284
Cdd:pfam05483 431 AEELKGKEQeliflLQAREKEIHDLEIQLTAIKTSEEHYLK-EVEDLKTELE---KEKLKNIE-LTAHCDKLLLENKELT 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 285 EDTTDddnLELEVNSQWENGANLDDPLKGALKKLIHAAKLNVSLKS-LEGERNHIIIQLSEV----DKTKEELTEHIKNL 359
Cdd:pfam05483 506 QEASD---MTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDeLESVREEFIQKGDEVkcklDKSEENARSIEYEV 582
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 360 QTQQESLQSENIYFESENQKLQQKLKIMTEFYQEDEmklyrkltveenyrieeeeklsKVEEKLSRATEQLETYRKLAKD 439
Cdd:pfam05483 583 LKKEKQMKILENKCNNLKKQIENKNKNIEELHQENK----------------------ALKKKGSAENKQLNAYEIKVNK 640
|
410 420 430
....*....|....*....|....*....|....*..
gi 146262005 440 LEEELERTVHFYQKQVISYEKRGHDNwlaaRTAERNL 476
Cdd:pfam05483 641 LELELASAKQKFEEIIDNYQKEIEDK----KISEEKL 673
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
175-517 |
1.75e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.01 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 175 QSLEDESKSLKSQI----AEAKIICKTFKMSEERraiaIKDALNENSQLQTSHKQLFQQEAEvwkgevselNKQKIT--F 248
Cdd:TIGR04523 36 KQLEKKLKTIKNELknkeKELKNLDKNLNKDEEK----INNSNNKIKILEQQIKDLNDKLKK---------NKDKINklN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 249 EDSKVHAEQVLNDKENHIKtltghlpmMKDQAAVLEEDTTDDDNLELEVNSQWENGANLDDPLKGA---LKKLIHAAKLn 325
Cdd:TIGR04523 103 SDLSKINSEIKNDKEQKNK--------LEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKyndLKKQKEELEN- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 326 vSLKSLEGERNHIiiqLSEVDKTK-------------EELTEHIKNLQTQQESLQSENIYFESENQKLQQKLKIMTEFYQ 392
Cdd:TIGR04523 174 -ELNLLEKEKLNI---QKNIDKIKnkllklelllsnlKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEIS 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 393 EDEMKLyrkltveenyrIEEEEKLSKVEEKLSRATEQLETYRKLAKDLEEELERtvhfYQKQVISYEKRGHDNWLAA--- 469
Cdd:TIGR04523 250 NTQTQL-----------NQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQ----LKSEISDLNNQKEQDWNKElks 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 146262005 470 --RTAERNLSDLRKENAHNKQKLTETELKFELLEKDPNALDVSNTAFGRE 517
Cdd:TIGR04523 315 elKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRE 364
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
120-369 |
2.60e-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: 43.98 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 120 AAAEEARSLEATCEKLNRSNSELEDEILCLEKDLKEEKSKHSQQDELMADISKSIQSLEDESKSLKSQIAEAKIicktfK 199
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK-----E 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 200 MSEERRAIA-IKDALNEnsQLQTSHKQLFQQEAEVWkgevselnkqkitfedskVHAEQVlNDKENHIKTLTGHLPMMKD 278
Cdd:COG4942 92 IAELRAELEaQKEELAE--LLRALYRLGRQPPLALL------------------LSPEDF-LDAVRRLQYLKYLAPARRE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 279 QAAVLEEDTTDDDNLELEVNSQwenganlddplKGALKKLIhaAKLNVSLKSLEGERNHIIIQLSEVDKTKEELTEHIKN 358
Cdd:COG4942 151 QAEELRADLAELAALRAELEAE-----------RAELEALL--AELEEERAALEALKAERQKLLARLEKELAELAAELAE 217
|
250
....*....|.
gi 146262005 359 LQTQQESLQSE 369
Cdd:COG4942 218 LQQEAEELEAL 228
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
100-443 |
2.87e-04 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 44.51 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 100 QKEYEGYE-VESSLEDAsfEKAAAEEARSLeATCEKLNrsnSELEDEILCLEKDLKEEKSKHSQQDELM-ADISKSIQSL 177
Cdd:pfam15964 328 QRESSAYEqVKQAVQMT--EEANFEKTKAL-IQCEQLK---SELERQKERLEKELASQQEKRAQEKEALrKEMKKEREEL 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 178 EDESKSLKSQIAEAKIICKtfKMSEERRAIaikdalneNSQLQTSHKQLFQQEAEVWK--GEVS-ELNKQKItfedSKVH 254
Cdd:pfam15964 402 GATMLALSQNVAQLEAQVE--KVTREKNSL--------VSQLEEAQKQLASQEMDVTKvcGEMRyQLNQTKM----KKDE 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 255 AEQVLNDkenhIKTLTGHLPMMKDQAAVLEEDTTDDDNLELEVNSQWENGANlDDPLKgaLKKLIHAAKLNVSLKSLEGE 334
Cdd:pfam15964 468 AEKEHRE----YRTKTGRQLEIKDQEIEKLGLELSESKQRLEQAQQDAARAR-EECLK--LTELLGESEHQLHLTRLEKE 540
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 335 R------NHIIIQLSEVDKTKEELTEHIKNLQTQQESLQSENIYFESENQKLQQKLKimtefyqEDEMKLYRKLTVEENY 408
Cdd:pfam15964 541 SiqqsfsNEAKAQALQAQQREQELTQKMQQMEAQHDKTVNEQYSLLTSQNTFIAKLK-------EECCTLAKKLEEITQK 613
|
330 340 350
....*....|....*....|....*....|....*
gi 146262005 409 RIEEEEKLSKVEEKLsraTEQLETYRKLAKDLEEE 443
Cdd:pfam15964 614 SRSEVEQLSQEKEYL---QDRLEKLQKRNEELEEQ 645
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
76-460 |
3.69e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 3.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 76 QKLGATLSGLIEEKCKLLEKFSLIQKEYEgyEVESSLEdasfekaAAEEARSLEATCEKLNRSNSELEDEILclEKDLKE 155
Cdd:PRK03918 327 EERIKELEEKEERLEELKKKLKELEKRLE--ELEERHE-------LYEEAKAKKEELERLKKRLTGLTPEKL--EKELEE 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 156 -EKSKHSQQDELmADISKSIQSLEDESKSLKSQIAE---AKIICKTFK--MSEERRaiaiKDALNEnsqlqtshkqlfqq 229
Cdd:PRK03918 396 lEKAKEEIEEEI-SKITARIGELKKEIKELKKAIEElkkAKGKCPVCGreLTEEHR----KELLEE-------------- 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 230 eaevWKGEVSELNKQKITFEDSKVHAEQVLNDKENHIKTLTGHLPMMK--DQAAVLEEDTTDDDNLELEVNS-QWENGAN 306
Cdd:PRK03918 457 ----YTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKElaEQLKELEEKLKKYNLEELEKKAeEYEKLKE 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 307 LDDPLKGALKKLIHAAKlnvSLKSLEGERNHIIIQLSEVDKTKEELTEHIKNL-----QTQQESLQS-ENIY-------- 372
Cdd:PRK03918 533 KLIKLKGEIKSLKKELE---KLEELKKKLAELEKKLDELEEELAELLKELEELgfesvEELEERLKElEPFYneylelkd 609
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 373 FESENQKLQQKLKIMTEFYQEDEMKLYRKLTV-----------EENYRIEEEEKLSKVEEKLSRATEQLETYRKLAKDLE 441
Cdd:PRK03918 610 AEKELEREEKELKKLEEELDKAFEELAETEKRleelrkeleelEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRR 689
|
410
....*....|....*....
gi 146262005 442 EELERTVHFYQKQVISYEK 460
Cdd:PRK03918 690 EEIKKTLEKLKEELEEREK 708
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
85-232 |
3.94e-04 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 41.84 E-value: 3.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 85 LIEEKCKLLEKFSLIQKEYEGYEVESSLEDASFEKAAAEEARSLEATCEKLN--------------RSNSELEDEILCLE 150
Cdd:pfam08614 5 LIDAYNRLLDRTALLEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEqllaqlreelaelyRSRGELAQRLVDLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 151 KDLKEEKSKHSQQDELMADISKSIQSLEDESKSLKSQIAEakiicktfkmseerraiaiKDALNENSQ--LQTSHKQLFQ 228
Cdd:pfam08614 85 EELQELEKKLREDERRLAALEAERAQLEEKLKDREEELRE-------------------KRKLNQDLQdeLVALQLQLNM 145
|
....
gi 146262005 229 QEAE 232
Cdd:pfam08614 146 AEEK 149
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
119-503 |
4.13e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 4.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 119 KAAAEEARSLEATCEKLNRSNSELEDEILCLEK-----DLKEEKSKHSQQ--------DELMADIsKSIQSLEDESKSLK 185
Cdd:COG4717 91 AELQEELEELEEELEELEAELEELREELEKLEKllqllPLYQELEALEAElaelperlEELEERL-EELRELEEELEELE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 186 SQIAEAKIICKT-FKMSEERRAIAIKDALNENSQLQTSHKQLfQQEAEVWKGEVSELNKQKITFEDSKVHAEqvlndKEN 264
Cdd:COG4717 170 AELAELQEELEElLEQLSLATEEELQDLAEELEELQQRLAEL-EEELEEAQEELEELEEELEQLENELEAAA-----LEE 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 265 HIKTLTGHLPMMkdqAAVLEEDTTDDDNLELEVN---------------------SQWENGANLDDPLKGALKKLIHAAK 323
Cdd:COG4717 244 RLKEARLLLLIA---AALLALLGLGGSLLSLILTiagvlflvlgllallflllarEKASLGKEAEELQALPALEELEEEE 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 324 LNVSLKSLEGERNHIIIQLSEVDKTKEELTEHIKNLQTQQESLQSEniYFESENQKLQQKLKImtefyqEDEMKLYRKLT 403
Cdd:COG4717 321 LEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLE--ELEQEIAALLAEAGV------EDEEELRAALE 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 404 veenyrieEEEKLSKVEEKLSRATEQLETYRKLAKDL-----EEELERTVHFYQKQVISYEKRgHDNWLAARTAERN-LS 477
Cdd:COG4717 393 --------QAEEYQELKEELEELEEQLEELLGELEELlealdEEELEEELEELEEELEELEEE-LEELREELAELEAeLE 463
|
410 420
....*....|....*....|....*...
gi 146262005 478 DLRKEN--AHNKQKLTETELKFELLEKD 503
Cdd:COG4717 464 QLEEDGelAELLQELEELKAELRELAEE 491
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
321-509 |
4.54e-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: 43.89 E-value: 4.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 321 AAKLNVSLKSLEGERNHIIIQLSEVDKTKEELTEHIKNLQTQQESLQSENIYFESENQKLQQKLkimtEFYQEDEMKLYR 400
Cdd:TIGR02168 693 IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL----TELEAEIEELEE 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 401 KLTVEENYRIEEEEKLSKVEEKLSRATEQLETYRKLAKDLEEELERTVHFYQKQ---VISYEKRGHDNWLAARTAERNLS 477
Cdd:TIGR02168 769 RLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLrerLESLERRIAATERRLEDLEEQIE 848
|
170 180 190
....*....|....*....|....*....|..
gi 146262005 478 DLRKENAHNKQKLTETELKFELLEKDPNALDV 509
Cdd:TIGR02168 849 ELSEDIESLAAEIEELEELIEELESELEALLN 880
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
92-367 |
4.82e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.77 E-value: 4.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 92 LLEKFSLIQKEYEGYEVESSLEDASFEKAAAEeARSLEATCEKLNRSNSELEDEI-------LCLEKDLKEEKSKHSQQD 164
Cdd:COG1196 230 LLLKLRELEAELEELEAELEELEAELEELEAE-LAELEAELEELRLELEELELELeeaqaeeYELLAELARLEQDIARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 165 ELMADISKSIQSLEDESKSLKSQIAEAKIICKTFKMSEERRAIAIKDALNENSQLQTSHKQLFQQEAEvWKGEVSELNKQ 244
Cdd:COG1196 309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE-AEEELEELAEE 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 245 KITFEDSKVHAEQVLNDKENHIKTLTGHLPMMKDQAAVLEEDTTDDDNLELEVNSQwenganLDDPLKGALKKLIHAAKL 324
Cdd:COG1196 388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA------LEEAAEEEAELEEEEEAL 461
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 146262005 325 NVSLKSLEGERNHIIIQLSEVDKTKEELTEHIKNLQTQQESLQ 367
Cdd:COG1196 462 LELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
320-538 |
7.25e-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: 43.12 E-value: 7.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 320 HAAKLNVSLKSLEGERNHIIIQLSEVDKTKEELTEHIKNLQTQQESLQSEniYFESenQKLQQKLKIMTEFYQEDEMKLY 399
Cdd:TIGR02168 240 ELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKE--LYAL--ANEISRLEQQKQILRERLANLE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 400 RKLTVEENYRIEEEEKLSKVEEKLSRATEQLETYRKLAKDLEEELERTVHFYQKQVisyekrghdnwLAARTAERNLSDL 479
Cdd:TIGR02168 316 RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELE-----------SRLEELEEQLETL 384
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 146262005 480 RKENAHNKQKLTETELKFELLEKDPNALDVSNTAFGREHAPNGPAPLGQRSSETRAFLS 538
Cdd:TIGR02168 385 RSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELE 443
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
95-461 |
7.47e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 43.24 E-value: 7.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 95 KFSLIQKEYEGYEVESSLEDASFEKAAAEEA-RSLEA---------TCEKLNRSNSE-----LEDEILCLEKDLKEEKSK 159
Cdd:pfam01576 235 RAQLAKKEEELQAALARLEEETAQKNNALKKiRELEAqiselqedlESERAARNKAEkqrrdLGEELEALKTELEDTLDT 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 160 HSQQDELMA----DISKSIQSLEDESKSLKSQIAEAKI--------------ICKTFKMSEERRAIAIKdalNENSQLQT 221
Cdd:pfam01576 315 TAAQQELRSkreqEVTELKKALEEETRSHEAQLQEMRQkhtqaleelteqleQAKRNKANLEKAKQALE---SENAELQA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 222 SHKQLFQQEAEV------WKGEVSELNKQKITFEDSKVHAEQVLNDKENHIKTLTGHLPMMKDQAAVLEEDTTdddnlel 295
Cdd:pfam01576 392 ELRTLQQAKQDSehkrkkLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVS------- 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 296 EVNSQWENGANLddpLKGALKklihaAKLNVS--LKSLEGERNHIIIQLSEVDKTKEELTEHIKNLQTQQeslqseniyf 373
Cdd:pfam01576 465 SLESQLQDTQEL---LQEETR-----QKLNLStrLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQL---------- 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 374 eSENQKLQQKLKIMTEFYQEDEMKLYRKLtveenyrieeEEKLSKVEEKlSRATEQLE-TYRKLAKDLEEELERTVHfyQ 452
Cdd:pfam01576 527 -SDMKKKLEEDAGTLEALEEGKKRLQREL----------EALTQQLEEK-AAAYDKLEkTKNRLQQELDDLLVDLDH--Q 592
|
410
....*....|
gi 146262005 453 KQVIS-YEKR 461
Cdd:pfam01576 593 RQLVSnLEKK 602
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
77-369 |
9.17e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.85 E-value: 9.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 77 KLGATLSGLIEEKCKLLEKfsLIQKEYEGYEVESSLED-----ASFEKAAAEEARSLEATCEKLNRSNSELEDEILCLEK 151
Cdd:pfam01576 486 NLSTRLRQLEDERNSLQEQ--LEEEEEAKRNVERQLSTlqaqlSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEE 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 152 DL----KEEKSKHSQQ---DELMADISKSIQ---SLEDESKSLKSQIAEAKIIckTFKMSEER-RAIAikDALNENSQLQ 220
Cdd:pfam01576 564 KAaaydKLEKTKNRLQqelDDLLVDLDHQRQlvsNLEKKQKKFDQMLAEEKAI--SARYAEERdRAEA--EAREKETRAL 639
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 221 TSHKQLfqQEAEVWKGEVSELNKQ-KITFED---SKVHAEQVLNDKENHIKTLTGHLPMMKDQAAVLEED--TTDDDNLE 294
Cdd:pfam01576 640 SLARAL--EEALEAKEELERTNKQlRAEMEDlvsSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDElqATEDAKLR 717
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 295 LEVN-----SQWENGANLDDPL----KGALKKLIHA------------AKLNVSLKSLEGERNHIIIQLSEVDKTKEELT 353
Cdd:pfam01576 718 LEVNmqalkAQFERDLQARDEQgeekRRQLVKQVREleaelederkqrAQAVAAKKKLELDLKELEAQIDAANKGREEAV 797
|
330
....*....|....*.
gi 146262005 354 EHIKNLQTQQESLQSE 369
Cdd:pfam01576 798 KQLKKLQAQMKDLQRE 813
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
107-509 |
9.57e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 42.76 E-value: 9.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 107 EVESSLEDASFEKAAA-----EEARSLEATCEKLNRSNSELEdEILCLEKDLKEEKSKHSQQDELMADISKSIQSLEDES 181
Cdd:COG5022 961 EVESKLKETSEEYEDLlkkstILVREGNKANSELKNFKKELA-ELSKQYGALQESTKQLKELPVEVAELQSASKIISSES 1039
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 182 KSLKSQIAEAKIICKTFKMSEERRAiAIKDALNENSQLQTSHKQLFQQEA--------EVWKGEVSELNKQKITFEDSKV 253
Cdd:COG5022 1040 TELSILKPLQKLKGLLLLENNQLQA-RYKALKLRRENSLLDDKQLYQLEStenllktiNVKDLEVTNRNLVKPANVLQFI 1118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 254 HAEQVLNDKENHI----KTLTGHLPMMKDQAAVLEED---TTDDDNLELEVNSQWENGANLDDPLKGALKKLIHAAKLNV 326
Cdd:COG5022 1119 VAQMIKLNLLQEIskflSQLVNTLEPVFQKLSVLQLEldgLFWEANLEALPSPPPFAALSEKRLYQSALYDEKSKLSSSE 1198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 327 sLKSLEGErnhiIIQLSEVDKTKEELTEHIKNLQtqqeslqSENIYFESENQKLQQKLKIMTEFYQEDEMKLYRKLTVEE 406
Cdd:COG5022 1199 -VNDLKNE----LIALFSKIFSGWPRGDKLKKLI-------SEGWVPTEYSTSLKGFNNLNKKFDTPASMSNEKLLSLLN 1266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 407 NYRIEEEEKlSKVEEKLSRATEQLETYRKLAkdLEEELERTVHFYQ-KQVISYEKRGH--DNWLaaRTAERNLSDLrken 483
Cdd:COG5022 1267 SIDNLLSSY-KLEEEVLPATINSLLQYINVG--LFNALRTKASSLRwKSATEVNYNSEelDDWC--REFEISDVDE---- 1337
|
410 420
....*....|....*....|....*.
gi 146262005 484 ahNKQKLTETELKFELLEKDPNALDV 509
Cdd:COG5022 1338 --ELEELIQAVKVLQLLKDDLNKLDE 1361
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
274-535 |
9.88e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 9.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 274 PMMKDQAAVLEEDTTDDDNLELEVNSQWENGANLDDPLKGALKKLihaAKLNVSLKSLEGErnhIIIQLSEVDKTKEELT 353
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAEL---EALQAEIDKLQAE---IAEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 354 EHIKNLQTQQESLQSENIYFESEN-----QKLQQKLKIMTefYQEDEMKLYRKLtveenyrieeEEKLSKVEEKLSRATE 428
Cdd:COG3883 90 ERARALYRSGGSVSYLDVLLGSESfsdflDRLSALSKIAD--ADADLLEELKAD----------KAELEAKKAELEAKLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 429 QLETYRKLAKDLEEELERTVHFYQKQVISYEKRghdnwlaARTAERNLSDLRKENAHNKQKLTETELKFELLEKDPNALD 508
Cdd:COG3883 158 ELEALKAELEAAKAELEAQQAEQEALLAQLSAE-------EAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
250 260
....*....|....*....|....*..
gi 146262005 509 VSNTAFGREHAPNGPAPLGQRSSETRA 535
Cdd:COG3883 231 AAAAAAAAAAAAAASAAGAGAAGAAGA 257
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
135-453 |
1.06e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 42.73 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 135 LNRSNSELEDE----ILCLEKDlkEEKSKHSQQ-DELMADISKSiQSLEDESKSLKSQIAEAKIICKTFK-----MSEER 204
Cdd:TIGR01612 1454 LLFKNIEMADNksqhILKIKKD--NATNDHDFNiNELKEHIDKS-KGCKDEADKNAKAIEKNKELFEQYKkdvteLLNKY 1530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 205 RAIAIKDALNEN--------SQLQTSHKQlFQQEAEVWKGEVSELNKQKITFEDskvhaEQVLNDKENH--------IKT 268
Cdd:TIGR01612 1531 SALAIKNKFAKTkkdseiiiKEIKDAHKK-FILEAEKSEQKIKEIKKEKFRIED-----DAAKNDKSNKaaidiqlsLEN 1604
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 269 LTGHLPMMKDQAAVLEEDTTDDDNLE-----LEVNSQ----WENGANLD------DPLKGAlKKLIHAAK-----LNVSL 328
Cdd:TIGR01612 1605 FENKFLKISDIKKKINDCLKETESIEkkissFSIDSQdtelKENGDNLNslqeflESLKDQ-KKNIEDKKkeldeLDSEI 1683
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 329 KSLEGERNH--------IIIQLSEVDKTKEELTEHIKNL-----QTQQESLQSENIYFESENQKLQQKLKIMTEFYQEdE 395
Cdd:TIGR01612 1684 EKIEIDVDQhkknyeigIIEKIKEIAIANKEEIESIKELieptiENLISSFNTNDLEGIDPNEKLEEYNTEIGDIYEE-F 1762
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 146262005 396 MKLYRKL-----TVEENYRIEEEEKLSKV--EEKLSRATEQLETYRKLAKDLE-EELERTV-HFYQK 453
Cdd:TIGR01612 1763 IELYNIIagcleTVSKEPITYDEIKNTRInaQNEFLKIIEIEKKSKSYLDDIEaKEFDRIInHFKKK 1829
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
100-496 |
1.65e-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: 41.96 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 100 QKEYEGYEVESSLEdaSFEKAAAEEARSLEATCEKLNRSNSEL-------EDEILCLEKDLKEEKSKHSQQDELMADISK 172
Cdd:TIGR00606 688 QTEAELQEFISDLQ--SKLRLAPDKLKSTESELKKKEKRRDEMlglapgrQSIIDLKEKEIPELRNKLQKVNRDIQRLKN 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 173 SIQSLEDESKSLKSQIAEAKI------ICKTFKMS--EERRAIAIKDALNENSQLQTSHKQL---FQQEAEVWKGEVSEL 241
Cdd:TIGR00606 766 DIEEQETLLGTIMPEEESAKVcltdvtIMERFQMElkDVERKIAQQAAKLQGSDLDRTVQQVnqeKQEKQHELDTVVSKI 845
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 242 NKQKITFEDSKvHAEQVLNDKENHIKTLTGHLPMMKDQAAVLEEDTTDDDNLELEVNSQWENGANLDDPLKGALKKLIHA 321
Cdd:TIGR00606 846 ELNRKLIQDQQ-EQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQE 924
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 322 AKLNVSLKSLEGERNHIiiqlsEVDKTKEELTEHIKNLQTQQESLQSeniyfESENQKLQQKLKIMTEFYQEDEMKLYRK 401
Cdd:TIGR00606 925 KEELISSKETSNKKAQD-----KVNDIKEKVKNIHGYMKDIENKIQD-----GKDDYLKQKETELNTVNAQLEECEKHQE 994
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 402 LTVEENYRIEEEEKLSKVEEKLSRATEQLETYRKLAKDLEEELERTVHFYQKQVISYEKRGHDNwlaartAERNLSDLRK 481
Cdd:TIGR00606 995 KINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQK------LEENIDLIKR 1068
|
410
....*....|....*..
gi 146262005 482 EN--AHNKQKLTETELK 496
Cdd:TIGR00606 1069 NHvlALGRQKGYEKEIK 1085
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
75-498 |
1.98e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.05 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 75 EQKLGATLSGLIEEKCKLLEKFSLIQKEYEGYEVESSLEDASFEKAAAEEARSLEATCEKLNRSNSELEDEILCLEKDLK 154
Cdd:PTZ00121 1340 EAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKK 1419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 155 EEKSKHSQQDELMADISKSIQSLEDESKSLKSQIAEAKIICKTFKMSEE-RRAIAIKDALNENSQLQTSHKQlfqqeAEV 233
Cdd:PTZ00121 1420 ADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEaKKADEAKKKAEEAKKADEAKKK-----AEE 1494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 234 WKGEVSELNKQkitfEDSKVHAEQVLNDKENHiktltghlpmMKDQAAVLEEDTTDDDNLELEVNSQWENGANLDDPLKG 313
Cdd:PTZ00121 1495 AKKKADEAKKA----AEAKKKADEAKKAEEAK----------KADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKA 1560
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 314 ALKKLIHAAklnvslKSLEGERNHIIIQLSEVDKTKEELTEHIKNLQTQQESLQSENIYFESENQKLQQKLKimtefYQE 393
Cdd:PTZ00121 1561 EEKKKAEEA------KKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELK-----KAE 1629
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 394 DEMKLYRKLTVEENYRIEEEEKLSKVEEKLSRATEQL----ETYRKLAKDL--EEELERTVHFYQKQVISYEKRGHDNWL 467
Cdd:PTZ00121 1630 EEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEakkaEEDKKKAEEAkkAEEDEKKAAEALKKEAEEAKKAEELKK 1709
|
410 420 430
....*....|....*....|....*....|.
gi 146262005 468 AARTAERNLSDLRKENAHNKQKLTETELKFE 498
Cdd:PTZ00121 1710 KEAEEKKKAEELKKAEEENKIKAEEAKKEAE 1740
|
|
| LCD1 |
pfam09798 |
DNA damage checkpoint protein; This is a family of proteins which regulate checkpoint kinases. ... |
134-251 |
2.58e-03 |
|
DNA damage checkpoint protein; This is a family of proteins which regulate checkpoint kinases. In Schizosaccharomyces pombe this protein is called Rad26 and in Saccharomyces cerevisiae it is called LCD1.
Pssm-ID: 462906 Cd Length: 615 Bit Score: 41.15 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 134 KLNRSNSELEDEILCLEKDLKEEKSKHSQQdelMADISKSIQSLEDESKslksqiaeakiicktFKMSEERRAIAIKDAL 213
Cdd:pfam09798 5 KLELLQQEKEKELEKLKNSYEELKSSHEEE---LEKLKQEVQKLEDEKK---------------FLLNELRSLSATSPAS 66
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 146262005 214 NENSQLQTSHKQLF--------QQEAEVWKGEVSELNKQKITFEDS 251
Cdd:pfam09798 67 SQSHETDTDDSSSVslkkrkieESTAESLKQKYIRLQNNRIVDETS 112
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
140-261 |
3.20e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 40.39 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 140 SELEDEILCLEKDLKEEKSKHSQQDELMADISKSIQSLEDESKSLKsQIAEAKIICKTfkmSEERRAI-AIKDALNENSQ 218
Cdd:smart00787 147 EGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLK-QLEDELEDCDP---TELDRAKeKLKKLLQEIMI 222
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 146262005 219 LQTSHKQLFQQEAEVwKGEVSELNKQKITFEDSKVHAEQVLND 261
Cdd:smart00787 223 KVKKLEELEEELQEL-ESKIEDLTNKKSELNTEIAEAEKKLEQ 264
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
106-516 |
3.24e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 41.36 E-value: 3.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 106 YEVESSLEDASFEKAAAEEARSLEATCEKLNRSNSELEDEILCLEKDLKEEKSkhsqqdeLMADISKSIQSLEDESKSLK 185
Cdd:PTZ00440 512 EKNNIVNNNFKNIEDYYITIEGLKNEIEGLIELIKYYLQSIETLIKDEKLKRS-------MKNDIKNKIKYIEENVDHIK 584
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 186 SQIAEAKIICKTFKMSEE---RRAIAIKDALNENSQLQTSHKQLFQqeaEVWKGEVSELNKQKITFEDSKVHAEQVLNDK 262
Cdd:PTZ00440 585 DIISLNDEIDNIIQQIEElinEALFNKEKFINEKNDLQEKVKYILN---KFYKGDLQELLDELSHFLDDHKYLYHEAKSK 661
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 263 ENhIKTLtghLPMMKDQAAVLEEDTTDDDN-------------LELEVNSQWENGANLD-DPLKGALKKLIHAAKLNVSL 328
Cdd:PTZ00440 662 ED-LQTL---LNTSKNEYEKLEFMKSDNIDniiknlkkelqnlLSLKENIIKKQLNNIEqDISNSLNQYTIKYNDLKSSI 737
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 329 KSLEGERNHIIIQLSEVDKTKEELtehIKNLQTQQESL-QSENIY--FESENQKLQQKLKIMTefyqeDEMKLyrkltve 405
Cdd:PTZ00440 738 EEYKEEEEKLEVYKHQIINRKNEF---ILHLYENDKDLpDGKNTYeeFLQYKDTILNKENKIS-----NDINI------- 802
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 406 enyrieeeeklskVEEKLSRATEQLETYRKLAKDLEEELERTvhfYQKQVISYEKRGHDNwlaartAERNLSDLRKENAH 485
Cdd:PTZ00440 803 -------------LKENKKNNQDLLNSYNILIQKLEAHTEKN---DEELKQLLQKFPTED------ENLNLKELEKEFNE 860
|
410 420 430
....*....|....*....|....*....|.
gi 146262005 486 NKQKLTETELKFELLEKDPNALDVSNTAFGR 516
Cdd:PTZ00440 861 NNQIVDNIIKDIENMNKNINIIKTLNIAINR 891
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
512-775 |
3.75e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 41.08 E-value: 3.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 512 TAFGREHAPNGPaPLGQRSSETRAFLSPQTLLEDPLglSPVLPEGGGRGPRGPGNPLDHQITNERGEPSCDRLTDPHRAP 591
Cdd:PHA03247 2668 RRLGRAAQASSP-PQRPRRRAARPTVGSLTSLADPP--PPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAV 2744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 592 SDTGSLSSPVEQDCKmmfpPPGQSYPDSALPPqredrfysnseRLSGSAEPRSF---KMTSLDKMDGSMPSEMESSRNDA 668
Cdd:PHA03247 2745 PAGPATPGGPARPAR----PPTTAGPPAPAPP-----------AAPAAGPPRRLtrpAVASLSESRESLPSPWDPADPPA 2809
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 669 KDDLGNLNVPDSSLPAENEATGPGFIPPPLAPVRGPLFP-------VDTRGPFMRRGPPFPPPPPGTMFGASRGYFPPRD 741
Cdd:PHA03247 2810 AVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPslplggsVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARP 2889
|
250 260 270
....*....|....*....|....*....|....
gi 146262005 742 FPGPPHAPFAMRNIYPPRGLPPYFHPRPGFYPNP 775
Cdd:PHA03247 2890 AVSRSTESFALPPDQPERPPQPQAPPPPQPQPQP 2923
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
98-379 |
4.70e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.89 E-value: 4.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 98 LIQKEYEGYEVESSLEDASFEKAAAEEA-RSLEATCEKLNRSNSELEDEILCLEKDLKEEKSKHSQQDELMADISKSIQS 176
Cdd:COG4372 75 LEQLEEELEELNEQLQAAQAELAQAQEElESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKE 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 177 LEDESKSLKSQIAEAKIICKTFKMSEERRAI-AIKDALNENSQLQTSHKQLFQQEAEVWKGEVSELNKQKITFEDSKVHA 255
Cdd:COG4372 155 LEEQLESLQEELAALEQELQALSEAEAEQALdELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLA 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 256 EQVLNDKENHIKTLTGHLPMMKDQAAVLEEDTTDDD-----NLELEVNSQWENGANLDDPLKGALKKLIHAAKLNVSLKS 330
Cdd:COG4372 235 LSALLDALELEEDKEELLEEVILKEIEELELAILVEkdteeEELEIAALELEALEEAALELKLLALLLNLAALSLIGALE 314
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 146262005 331 LEGERNHIIIQLSEVDKTKEELTEHIKNLQTQQESLQSENIYFESENQK 379
Cdd:COG4372 315 DALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGA 363
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
64-241 |
4.86e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 4.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 64 RSVRSRLYVG---REQK--LGATLSGLIEEKCKLLEKFSLIQKEYEGYE----VESSLEDASFE----KAAAEEARSLEA 130
Cdd:COG4913 596 RRIRSRYVLGfdnRAKLaaLEAELAELEEELAEAEERLEALEAELDALQerreALQRLAEYSWDeidvASAEREIAELEA 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 131 TCEKLNRSNSE---LEDEILCLEKDLKEEKSKHSQQDELMADISKSIQSLEDESKSLKSQIAEAKIICKT--FKMSEERR 205
Cdd:COG4913 676 ELERLDASSDDlaaLEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLelRALLEERF 755
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 146262005 206 AIAIKDALNE------NSQLQTSHKQLFQQEAEV----------WKGEVSEL 241
Cdd:COG4913 756 AAALGDAVERelrenlEERIDALRARLNRAEEELeramrafnreWPAETADL 807
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
128-502 |
6.80e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 6.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 128 LEATCEKLNRSNSELEDEILCLEKDLKEEkskhsqqdelmADISKSIQSLEDESKSLKSQIAEakiicktfKMSEERRAI 207
Cdd:PRK03918 160 YENAYKNLGEVIKEIKRRIERLEKFIKRT-----------ENIEELIKEKEKELEEVLREINE--------ISSELPELR 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 208 AIKDALNENsqlqtshkqlfQQEAEVWKGEVSELNKQKITFEDSKVHAEQVLNDKENHIKTLTGHLPMMKDQAAVLEEdt 287
Cdd:PRK03918 221 EELEKLEKE-----------VKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKE-- 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 288 tdddnLELEVNSQWENGANLDDPLKGAlkklihaAKLNVSLKSLEGERNHIIIQLSEVDKTK---EELTEHIKNLQTQQE 364
Cdd:PRK03918 288 -----LKEKAEEYIKLSEFYEEYLDEL-------REIEKRLSRLEEEINGIEERIKELEEKEerlEELKKKLKELEKRLE 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 365 SLQSENIYFESENQKLQQKLKIMTEFYQEDEMKLYRKLTVEENYRIEEEEKLSKVEEKLSrateQLETYRKLAKDLEEEL 444
Cdd:PRK03918 356 ELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIG----ELKKEIKELKKAIEEL 431
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 445 E--RTVHFYQKQVISYEKRGhdNWLAARTAErnLSDLRKENAHNKQKLTETELKFELLEK 502
Cdd:PRK03918 432 KkaKGKCPVCGRELTEEHRK--ELLEEYTAE--LKRIEKELKEIEEKERKLRKELRELEK 487
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
119-503 |
7.68e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 39.77 E-value: 7.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 119 KAAAEEARSLEATCEKLNRSNSELEDEILCLEKDL--KEEKSKH-----SQQDELMADIS--------------KSIQSL 177
Cdd:pfam01576 134 KKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLaeEEEKAKSlsklkNKHEAMISDLEerlkkeekgrqeleKAKRKL 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 178 EDESKSLKSQIAEAKIICKTFKMSEERRAIAIKDALN--ENSQLQTSHKQLFQQEAEvwkGEVSELNKQKITFEDSKVHA 255
Cdd:pfam01576 214 EGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALArlEEETAQKNNALKKIRELE---AQISELQEDLESERAARNKA 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 256 EQVLNDKENHIKTLTGHLpmmkdqaavleEDTTDDDNLELEVNSQWEnganlddplkgalkklihaAKLNVSLKSLEGER 335
Cdd:pfam01576 291 EKQRRDLGEELEALKTEL-----------EDTLDTTAAQQELRSKRE-------------------QEVTELKKALEEET 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 336 NHIIIQLSEVDK----TKEELTEHIKNLQTQQESLQSENIYFESENQKLQQKLKIMTEFYQEDEMK----------LYRK 401
Cdd:pfam01576 341 RSHEAQLQEMRQkhtqALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKrkklegqlqeLQAR 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 402 LTVEENYRIEEEEKLSKVEEKLSRATEQLETYR----KLAKD---LEEELERTVHFYQ---KQVISY---------EKRG 462
Cdd:pfam01576 421 LSESERQRAELAEKLSKLQSELESVSSLLNEAEgkniKLSKDvssLESQLQDTQELLQeetRQKLNLstrlrqledERNS 500
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 146262005 463 HDNWL-----AARTAERNLSDLRKENAHNKQKLTETELKFELLEKD 503
Cdd:pfam01576 501 LQEQLeeeeeAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEG 546
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
76-279 |
7.82e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 40.04 E-value: 7.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 76 QKLGATLSGLIEEKCKLLEKFSLIQKEYEGYEVESSLEDASFEKAAAEEarsleatcEKLNRSNSELEDEILCLEKDLKE 155
Cdd:TIGR02168 319 EELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAEL--------EELESRLEELEEQLETLRSKVAQ 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146262005 156 EKSKhsqqdelMADISKSIQSLEDESKSLKSQIAeakiicktfKMSEERRAIAIKDALNENSQLQTSHKQLFQQEAEVwK 235
Cdd:TIGR02168 391 LELQ-------IASLNNEIERLEARLERLEDRRE---------RLQQEIEELLKKLEEAELKELQAELEELEEELEEL-Q 453
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 146262005 236 GEVSELNKQKITFEDSKVHAEQVLNDKENHIKTLTGHLPMMKDQ 279
Cdd:TIGR02168 454 EELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERL 497
|
|
| |
