|
Name |
Accession |
Description |
Interval |
E-value |
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
95-444 |
8.54e-09 |
|
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: 58.98 E-value: 8.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 95 KFSLIQ--KEYEGYEVESSLEDASFEKAAAEEARSLEATCEKlnrsNSELEDEILCLEKDLKEEKSKHSQQDELMADISK 172
Cdd:pfam05557 8 KARLSQlqNEKKQMELEHKRARIELEKKASALKRQLDRESDR----NQELQKRIRLLEKREAEAEEALREQAELNRLKKK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 173 SIQSLEDESKSLKSQIAEAK--IICKTFKMSEERRAIAIKDalnenSQLQT--SHKQLFQQEAEVWKGEVSELNKQKITF 248
Cdd:pfam05557 84 YLEALNKKLNEKESQLADARevISCLKNELSELRRQIQRAE-----LELQStnSELEELQERLDLLKAKASEAEQLRQNL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 249 EDSkvhaEQVLNDKENHIKTLTGHLPMMKDQAAVLeedttdddnlelevnsqwenganlddplKGALKKLIHAAKLNVSL 328
Cdd:pfam05557 159 EKQ----QSSLAEAEQRIKELEFEIQSQEQDSEIV----------------------------KNSKSELARIPELEKEL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 329 KSLEGERNHiiiqLSEVDKTKEELTEHIKNLQT---QQASLQSENIYFESENQKLQQKLKIMTEFYQENEMKLYRKLTVE 405
Cdd:pfam05557 207 ERLREHNKH----LNENIENKLLLKEEVEDLKRkleREEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNLRSPEDLS 282
|
330 340 350
....*....|....*....|....*....|....*....
gi 193290160 406 ENYRIEEEEKLSRVEEKISrATEGLETYRKLAKDLEEEL 444
Cdd:pfam05557 283 RRIEQLQQREIVLKEENSS-LTSSARQLEKARRELEQEL 320
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
86-507 |
1.25e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.54 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 86 IEEKCKLLEKfSLIQKEYEGYEVESSLEDASFEKAAAE-EARSLEATCEKLNrsnsELEDEILCLEKDLKEEKSKHSQqd 164
Cdd:PRK03918 191 IEELIKEKEK-ELEEVLREINEISSELPELREELEKLEkEVKELEELKEEIE----ELEKELESLEGSKRKLEEKIRE-- 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 165 elmadISKSIQSLEDESKSLKSQIAEAKIICKtfKMSEERRAIAIKDALNENSQLQTSHKQLFQQEAEVWKGEVSELNKq 244
Cdd:PRK03918 264 -----LEERIEELKKEIEELEEKVKELKELKE--KAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEE- 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 245 kitfedskvhaeqvlndKENHIKTLTGHLPMMKDQAAVLEEDttdddnLELevnsqwenganlddpLKGALKKLIHAAKL 324
Cdd:PRK03918 336 -----------------KEERLEELKKKLKELEKRLEELEER------HEL---------------YEEAKAKKEELERL 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 325 NVSLKSLEGERnhIIIQLSEVDKTKEELTEHIKNLQTQQASLQSEniyfESENQKLQQKLK-----------IMTEFYQE 393
Cdd:PRK03918 378 KKRLTGLTPEK--LEKELEELEKAKEEIEEEISKITARIGELKKE----IKELKKAIEELKkakgkcpvcgrELTEEHRK 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 394 NEMKLYRKltveenyrieeeeKLSRVEEKISRATEGLETYRKLAKDLEEELERtvhfyQKQVISYEKrghdnwlaarTAE 473
Cdd:PRK03918 452 ELLEEYTA-------------ELKRIEKELKEIEEKERKLRKELRELEKVLKK-----ESELIKLKE----------LAE 503
|
410 420 430
....*....|....*....|....*....|....*
gi 193290160 474 RnLSDLRKE-NAHNKQKLTETELKFELLEKDPNAL 507
Cdd:PRK03918 504 Q-LKELEEKlKKYNLEELEKKAEEYEKLKEKLIKL 537
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
107-509 |
1.37e-08 |
|
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: 58.58 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 107 EVESSLEDASFekaaaeearSLEATCEKLNrsnsELEDEILCLEKDLKEEKSKHSQQDELMADISKSIQSLEDESKSLKS 186
Cdd:pfam05483 251 EKENKMKDLTF---------LLEESRDKAN----QLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEE 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 187 --QIAeAKIICKtfkMSEERRAiaikdALNENSQLQTSHKQLfqqeaevwkgeVSELNKQKITFEDSKVHAEQVLNDKEN 264
Cdd:pfam05483 318 dlQIA-TKTICQ---LTEEKEA-----QMEELNKAKAAHSFV-----------VTEFEATTCSLEELLRTEQQRLEKNED 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 265 HIKTLTGHLpmmKDQAAVLEEDTTDDDNLELEV----------------NSQWENganLDDPLKGALKKLIHAaklnvsL 328
Cdd:pfam05483 378 QLKIITMEL---QKKSSELEEMTKFKNNKEVELeelkkilaedeklldeKKQFEK---IAEELKGKEQELIFL------L 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 329 KSLEGERNHIIIQLSEVDKTKEELTEHIKNLQTQQASLQSENIYFES-------ENQKLQQKLKIMT---EFYQEN---- 394
Cdd:pfam05483 446 QAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAhcdklllENKELTQEASDMTlelKKHQEDiinc 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 395 ---EMKLYRKLTVEENYRIEEEEKLSRVEEKISRatEGLETYRKLAKDLE--EELERTVHFYQKQVISYEKRGHDNWLAA 469
Cdd:pfam05483 526 kkqEERMLKQIENLEEKEMNLRDELESVREEFIQ--KGDEVKCKLDKSEEnaRSIEYEVLKKEKQMKILENKCNNLKKQI 603
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 193290160 470 RTAERNLSDLRKENAHNKQKLTETELKFELLEKDPNALDV 509
Cdd:pfam05483 604 ENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLEL 643
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
123-502 |
1.72e-08 |
|
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: 58.11 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 123 EEARSLEATCEKLNRSNSELEDEILCLEKDLKE-EKSKHSQQDELmADISK----------SIQSLEDESKSLKSQIAEA 191
Cdd:TIGR04523 145 TEIKKKEKELEKLNNKYNDLKKQKEELENELNLlEKEKLNIQKNI-DKIKNkllklelllsNLKKKIQKNKSLESQISEL 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 192 KiicktfkmseerraiaikdalNENSQLQTSHKQLfQQEAEVWKGEVSELNKQKITFEDSKVHAEQVLNDKENHIKTLTG 271
Cdd:TIGR04523 224 K---------------------KQNNQLKDNIEKK-QQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNK 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 272 HLPMMKDQAAVLEEDTTD-----DDNLELEVNSQWENGANLDDPLKGALKKLIHA-AKLNVSLKSLEGERNH-------I 338
Cdd:TIGR04523 282 KIKELEKQLNQLKSEISDlnnqkEQDWNKELKSELKNQEKKLEEIQNQISQNNKIiSQLNEQISQLKKELTNsesenseK 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 339 IIQLSE-------VDKTKEELTEHIKNLQTQQASLQSENIYFESENQKLQQKLKIMtefyQENEMKLYRKLTVEENYRIE 411
Cdd:TIGR04523 362 QRELEEkqneiekLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKL----QQEKELLEKEIERLKETIIK 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 412 EEEKLSRVEEKISrategletyrklAKDLE-EELERTVHFYQKQVISYEKrghdnwlAARTAERNLSDLRKENAHNKQKL 490
Cdd:TIGR04523 438 NNSEIKDLTNQDS------------VKELIiKNLDNTRESLETQLKVLSR-------SINKIKQNLEQKQKELKSKEKEL 498
|
410
....*....|...
gi 193290160 491 TE-TELKFELLEK 502
Cdd:TIGR04523 499 KKlNEEKKELEEK 511
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
75-455 |
3.19e-08 |
|
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: 57.34 E-value: 3.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 75 EQKLGATLSGLIEEKCKLLEKFS--------LIQKEYEGYEVESSLEDASFEKAA-------------AEEARSLEATCE 133
Cdd:TIGR04523 252 QTQLNQLKDEQNKIKKQLSEKQKeleqnnkkIKELEKQLNQLKSEISDLNNQKEQdwnkelkselknqEKKLEEIQNQIS 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 134 KLNRSNSELEDEILCLEKDLKEEKSKHSQQDE-------LMADISKSIQSLEDESKSLKSQIAEAKIICKTFKMSEERRA 206
Cdd:TIGR04523 332 QNNKIISQLNEQISQLKKELTNSESENSEKQReleekqnEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKD 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 207 IAIKDALNENSQLQTSHKQLfQQEAEVWKGEVSELNKQKITFEDSKVHAEQVLNDKENHIKTLTGHLPMMKDQaavLEED 286
Cdd:TIGR04523 412 EQIKKLQQEKELLEKEIERL-KETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQN---LEQK 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 287 TTDDDNLELEVNSQWENGANLDDPLKgALKKLIhaAKLNVSLKSLEGERNHIIIQLSEV---------DKTKEELTEHIK 357
Cdd:TIGR04523 488 QKELKSKEKELKKLNEEKKELEEKVK-DLTKKI--SSLKEKIEKLESEKKEKESKISDLedelnkddfELKKENLEKEID 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 358 NLQTQQASLQSENIYFESENQKLQQKLKImtefYQENEMKLYRKLTVEENYRIEEEEKLSRVEEKisraTEGLETYRKLA 437
Cdd:TIGR04523 565 EKNKEIEELKQTQKSLKKKQEEKQELIDQ----KEKEKKDLIKEIEEKEKKISSLEKELEKAKKE----NEKLSSIIKNI 636
|
410
....*....|....*...
gi 193290160 438 KDLEEELERTVHFYQKQV 455
Cdd:TIGR04523 637 KSKKNKLKQEVKQIKETI 654
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
85-446 |
2.53e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 54.30 E-value: 2.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 85 LIEEKCKLLE--KFSLIQKEYEGYEVESSLEDASFEKAAAE-EARSLEATCEKLNRSNSELEDEILCLEKDLKEEKSKHS 161
Cdd:TIGR02169 203 LRREREKAERyqALLKEKREYEGYELLKEKEALERQKEAIErQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIK 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 162 QQ-DELMADISKSIQSLEDESKSLKSQIAEAKiicKTFKMSEERRAIAIKDAlnensqlqtsHKQlfQQEAEVWKGEVSE 240
Cdd:TIGR02169 283 DLgEEEQLRVKEKIGELEAEIASLERSIAEKE---RELEDAEERLAKLEAEI----------DKL--LAEIEELEREIEE 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 241 LNKQKITFEDSKVHAEQVLNDKENHIKtltghlpmmkdqaavlEEDTTdddnlelevnsqwenganlddplkgalkklih 320
Cdd:TIGR02169 348 ERKRRDKLTEEYAELKEELEDLRAELE----------------EVDKE-------------------------------- 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 321 AAKLNVSLKSLEgernhiiiqlSEVDKTKEELTEHIKNLQTQQASLQSENIYFESENQKLQQKLKIMTEFYQENEMKLYr 400
Cdd:TIGR02169 380 FAETRDELKDYR----------EKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKAL- 448
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 193290160 401 KLTVEENYRIEEEEKLSRVEEKISRATEGLETYRKLAKDLEEELER 446
Cdd:TIGR02169 449 EIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAE 494
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
87-508 |
5.51e-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: 53.10 E-value: 5.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 87 EEKcKLLEKFSLIQKEYEGYEVE-SSLEDASFEKAaaeearsleatcEKLNRSNSELEDeilcLEKDLKEEKSKHSQQDE 165
Cdd:TIGR04523 34 EEK-QLEKKLKTIKNELKNKEKElKNLDKNLNKDE------------EKINNSNNKIKI----LEQQIKDLNDKLKKNKD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 166 LMADISKSIQSLEDESKSLKSQIAEAKIICKTFKMSEERRAIAIKDALNENSQLqtshkqlfQQEAEVWKGEVSELNKQK 245
Cdd:TIGR04523 97 KINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKK--------EKELEKLNNKYNDLKKQK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 246 ITFEDSKVHAEQVLNDKENHIKTLTGHLPMMKDQAAVLEEDTTDDDNLELEV------NSQWENGANLDDPLKGALKKLI 319
Cdd:TIGR04523 169 EELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQIselkkqNNQLKDNIEKKQQEINEKTTEI 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 320 HAAKLNvsLKSLEGERNHIIIQLS----EVDKTKEELTEHIKNLQTQQASLQSENiyfeseNQKLQQKLKIMTEFYQENE 395
Cdd:TIGR04523 249 SNTQTQ--LNQLKDEQNKIKKQLSekqkELEQNNKKIKELEKQLNQLKSEISDLN------NQKEQDWNKELKSELKNQE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 396 MKLyrkltveenyrIEEEEKLSRVEEKISRATEGLETYRKLAKDLE---EELERTVHFYQKQVISYEKRGHDNWLAARTA 472
Cdd:TIGR04523 321 KKL-----------EEIQNQISQNNKIISQLNEQISQLKKELTNSEsenSEKQRELEEKQNEIEKLKKENQSYKQEIKNL 389
|
410 420 430
....*....|....*....|....*....|....*.
gi 193290160 473 ERNLSDLRKENAHNKQKLTETELKFELLEKDPNALD 508
Cdd:TIGR04523 390 ESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLE 425
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
123-391 |
9.85e-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: 52.33 E-value: 9.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 123 EEARSLEATCEKLNRSNSELEDEILCLEKDLKEEKSKHSQQDELMADISKSIQSLEDESKSLKSQIAEakiicktfKMSE 202
Cdd:TIGR04523 426 KEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKS--------KEKE 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 203 erraiaIKDALNENSQLQTSHKQLFQQEAEvwkgevSELNKQKITFEDSKVhaEQVLNDKENHIKTLtghlpmmkdqaav 282
Cdd:TIGR04523 498 ------LKKLNEEKKELEEKVKDLTKKISS------LKEKIEKLESEKKEK--ESKISDLEDELNKD------------- 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 283 leEDTTDDDNLELEVNSQWENganlDDPLKGALKKLIHA-AKLNVSLKSLEGERNHIIIQLSEVDKTKEELTEHIKNLQT 361
Cdd:TIGR04523 551 --DFELKKENLEKEIDEKNKE----IEELKQTQKSLKKKqEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKK 624
|
250 260 270
....*....|....*....|....*....|.
gi 193290160 362 QQASLQSENIYFESENQKLQQKLK-IMTEFY 391
Cdd:TIGR04523 625 ENEKLSSIIKNIKSKKNKLKQEVKqIKETIK 655
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
118-432 |
9.97e-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: 52.37 E-value: 9.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 118 EKAAAEEARSLEATCEKLNRSNSELEDEILCLEKDLKEEKSKHSQQDELMADISKSIQSLEDESKSLKSQIAEAKIICKT 197
Cdd:TIGR02168 248 LKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 198 FkmseERRAIAIKDALNENsqlqtshkqlfQQEAEVWKGEVSELNKQKITFEDSKVHAEQVLNDKENHIKTLTGHLPMMK 277
Cdd:TIGR02168 328 L----ESKLDELAEELAEL-----------EEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 278 DQAAVLEEDTTdddNLELEVNSQWENGANLDDPLKGALKKLIHAAklnvsLKSLEGERNHIIIQLSEVDKTKEELTEHIK 357
Cdd:TIGR02168 393 LQIASLNNEIE---RLEARLERLEDRRERLQQEIEELLKKLEEAE-----LKELQAELEELEEELEELQEELERLEEALE 464
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 193290160 358 NLQTQQASLQSENIYFESENQKLQQKLKiMTEFYQENEMKLYRKLTVEENYRIEEEEKLSRVEEKISrATEGLET 432
Cdd:TIGR02168 465 ELREELEEAEQALDAAERELAQLQARLD-SLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELIS-VDEGYEA 537
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
115-393 |
1.04e-06 |
|
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: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 115 ASFEKAAAEEARSLEATCEKLNRSNSELEDEILCLEKDLKEEKSKHSQQDELMADISKSIQSLEDESKSLKSQIAEAKII 194
Cdd:pfam10174 439 TTLEEALSEKERIIERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSK 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 195 CKTFKmseerraIAIKDALNENSQLQTSHKQLFQQEAEVWKGE-----VSELNKQKITF--EDSKVHAE-----QVL--- 259
Cdd:pfam10174 519 LKSLE-------IAVEQKKEECSKLENQLKKAHNAEEAVRTNPeindrIRLLEQEVARYkeESGKAQAEverllGILrev 591
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 260 ----NDKENHIKTLTGHLP-MMKDQaavleedTTDDDNLE-LEVNSQWENGANLDDPLKgalkklihaaklnvslKSLEG 333
Cdd:pfam10174 592 enekNDKDKKIAELESLTLrQMKEQ-------NKKVANIKhGQQEMKKKGAQLLEEARR----------------REDNL 648
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 193290160 334 ERNHIIIQLSEV----DKTKEELTEHIKNLQTQQASLQSENIYFESENQKLQQKLKIMTEFYQE 393
Cdd:pfam10174 649 ADNSQQLQLEELmgalEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAERRKQLEEILEMKQE 712
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
119-503 |
1.11e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 52.33 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 119 KAAAEEARSLEATCEKLNRSNSELEDEIlclekdlKEEKSKHSQQDELMADISKSIQSLEDESKSLKSQIAEakiicktf 198
Cdd:TIGR04523 207 KKKIQKNKSLESQISELKKQNNQLKDNI-------EKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSE-------- 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 199 KMSE-ERRAIAIKDALNENSQLQTSHKQLFQQEAEVWKGEVSELNKQKitfEDSKVHAEQVLNDKENHIKTLtghlpmmK 277
Cdd:TIGR04523 272 KQKElEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQ---EKKLEEIQNQISQNNKIISQL-------N 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 278 DQAAVLEEDTTDDDNLELEVNSQWENGANlddplkgALKKLIHA-AKLNVSLKSLEGERNHIIIQLSEVDKTKEELTEHI 356
Cdd:TIGR04523 342 EQISQLKKELTNSESENSEKQRELEEKQN-------EIEKLKKEnQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQI 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 357 KNLQTQQASLQSENIYFESENQKLQQKLKIMTEfyQENEMK------------LYRKLTVEENYRIEEEEKLSRVEEKIS 424
Cdd:TIGR04523 415 KKLQQEKELLEKEIERLKETIIKNNSEIKDLTN--QDSVKEliiknldntresLETQLKVLSRSINKIKQNLEQKQKELK 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 425 RATEGLETYRKLAKDLEEELErtvhfYQKQVISYEKRGHDNwLAARTAERN--LSDLRKENAHNKQKLTETELKFELLEK 502
Cdd:TIGR04523 493 SKEKELKKLNEEKKELEEKVK-----DLTKKISSLKEKIEK-LESEKKEKEskISDLEDELNKDDFELKKENLEKEIDEK 566
|
.
gi 193290160 503 D 503
Cdd:TIGR04523 567 N 567
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
72-461 |
3.61e-06 |
|
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: 50.74 E-value: 3.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 72 VGREQKLGATLSGLIEEKCKLLEKFSLIQKEYEGYEVESSLEDASFEKAAAEEARSLEATceKLNRSNSELEDEILCLEK 151
Cdd:pfam02463 642 KAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEI--KKKEQREKEELKKLKLEA 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 152 DLKEEKSKHSQQDELMADISKSIQ-----SLEDESKSLKSQIAEAKIICKTFKMsEERRAIAIKDALNENSQLQTSHKQL 226
Cdd:pfam02463 720 EELLADRVQEAQDKINEELKLLKQkideeEEEEEKSRLKKEEKEEEKSELSLKE-KELAEEREKTEKLKVEEEKEEKLKA 798
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 227 FQQEAEVWKGEVSELNKQKITFEDSKVHAEQVLNDKENHIKTLTGHLpmMKDQAAVLEEDTTDDDNLELEVNSQWENGAN 306
Cdd:pfam02463 799 QEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEE--QKLEKLAEEELERLEEEITKEELLQELLLKE 876
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 307 LDDPLKGALKKLIHA-AKLNVSLKSLEGERNHIIIQLSEVDKTKEELTEHIKNLQ-----------TQQASLQSENIYFE 374
Cdd:pfam02463 877 EELEEQKLKDELESKeEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLkyeeepeelllEEADEKEKEENNKE 956
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 375 SENQKLQQKLKIMTEFYQENEMKLYRKLTVEENYRIEEEEKLSRVEEKISRAtegLETYRKLAKDLEEELERTVHFYQKQ 454
Cdd:pfam02463 957 EEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLI---RAIIEETCQRLKEFLELFVSINKGW 1033
|
....*..
gi 193290160 455 VISYEKR 461
Cdd:pfam02463 1034 NKVFFYL 1040
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
146-447 |
4.42e-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: 4.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 146 ILCLEKDLKEEKSKHSQQDELMADISKSIQSLEDESKSLKSQIAEAKIIcktfkmsEERRAIAIKDALNENSQLQTSHKQ 225
Cdd:TIGR02168 672 ILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKE-------LEELSRQISALRKDLARLEAEVEQ 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 226 LFQQEAEVwKGEVSELNKQKITFEDSKVHAEQVLNDKENHIKTLTGHLPMMKDQAAVLEEDTTDddnlelevnsqwenga 305
Cdd:TIGR02168 745 LEERIAQL-SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDE---------------- 807
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 306 nlddpLKGALKKL-IHAAKLNVSLKSLEGERNHIIIQLSEVDKTKEELTEHIKNLQTQQASLQSEniyFESENQKLQQKL 384
Cdd:TIGR02168 808 -----LRAELTLLnEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEEL---IEELESELEALL 879
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 193290160 385 KIMTEfyQENEMKLYRKltveenYRIEEEEKLSRVEEKISRATEGLETYRKLAKDLEEELERT 447
Cdd:TIGR02168 880 NERAS--LEEALALLRS------ELEELSEELRELESKRSELRRELEELREKLAQLELRLEGL 934
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
109-519 |
2.04e-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: 48.18 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 109 ESSLEDASFEKAaaeeaRSLEATCEKLNRSNSELEDEILCLEKDLKEEKSKHSQQDELMADISKSIQSL--EDESKSLK- 185
Cdd:pfam05483 62 QEGLKDSDFENS-----EGLSRLYSKLYKEAEKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELqfENEKVSLKl 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 186 -SQIAEAKIICKtfkmsEERRAIAIKDALNENSQLQTSHKQLFQQEAEVWKGEVSELN----KQKITFEDSKVHAEQV-- 258
Cdd:pfam05483 137 eEEIQENKDLIK-----ENNATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNnnieKMILAFEELRVQAENArl 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 259 -----------------------LNDKENHI--------------KTLTGHLPMMKDQAAVLEEDTT-DDDNLELEVNSQ 300
Cdd:pfam05483 212 emhfklkedhekiqhleeeykkeINDKEKQVsllliqitekenkmKDLTFLLEESRDKANQLEEKTKlQDENLKELIEKK 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 301 WENGANLDDpLKGALKKLIHAAK-----LNVSLKSLEGERNHIIIQLSEVDKTKEELTEHIKNLQTQQASLQSeniYFES 375
Cdd:pfam05483 292 DHLTKELED-IKMSLQRSMSTQKaleedLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEE---LLRT 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 376 ENQKLQQ---KLKIMTefyqeneMKLYRKLTVEENYRIEEEEKLSRVEE--KISRATEGLETYRKLAKDLEEELERTVHF 450
Cdd:pfam05483 368 EQQRLEKnedQLKIIT-------MELQKKSSELEEMTKFKNNKEVELEElkKILAEDEKLLDEKKQFEKIAEELKGKEQE 440
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 193290160 451 YQKQVISYEKRGHD---NWLAARTAERNLSdlrKENAHNKQKLTETELKFELLEKDPNALDVSNTAFGREHS 519
Cdd:pfam05483 441 LIFLLQAREKEIHDleiQLTAIKTSEEHYL---KEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEAS 509
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
94-385 |
2.64e-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: 2.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 94 EKFSLIQKEYEGYEVEssledasfekAAAEEARSLEATCEKLNRSNSELEDEILCLEKDLKEEKSKHSQQDELMADISKS 173
Cdd:COG1196 213 ERYRELKEELKELEAE----------LLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELE 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 174 IQSLEDESKSLKSQIAEAkiicktfkmsEERRAIAIKDALNENSQLQtshkQLfQQEAEVWKGEVSELNKQKITFEDSKV 253
Cdd:COG1196 283 LEEAQAEEYELLAELARL----------EQDIARLEERRRELEERLE----EL-EEELAELEEELEELEEELEELEEELE 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 254 HAEQVLNDKENHIktltghlpmmKDQAAVLEEDTTDDDNLELEVNSQWENGANLddpLKGALKKLIHAAKLNVSLKSLEG 333
Cdd:COG1196 348 EAEEELEEAEAEL----------AEAEEALLEAEAELAEAEEELEELAEELLEA---LRAAAELAAQLEELEEAEEALLE 414
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 193290160 334 ERNHIIIQLSEVDKTKEELTEHIKNLQTQQASLQSENIYFESENQKLQQKLK 385
Cdd:COG1196 415 RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
123-244 |
3.68e-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: 44.17 E-value: 3.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 123 EEARSLEATCEKLNRSNSELEDEILCLEKDLKE--EKSKHSQQD---ELM--ADISKSIQSLEDESKSLKSQIAEAKIic 195
Cdd:pfam07926 1 AELSSLQSEIKRLKEEAADAEAQLQKLQEDLEKqaEIAREAQQNyerELVlhAEDIKALQALREELNELKAEIAELKA-- 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 193290160 196 ktfkmseerRAIAIKDALNENSQLQTSHKQLFQQEAEVWKGEVSELNKQ 244
Cdd:pfam07926 79 ---------EAESAKAELEESEESWEEQKKELEKELSELEKRIEDLNEQ 118
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
95-461 |
2.50e-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: 44.78 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 95 KFSLIQKEYEGYEVESSLEDASFEKAAAEEA-RSLEA---------TCEKLNRSNSE-----LEDEILCLEKDLKEEKSK 159
Cdd:pfam01576 235 RAQLAKKEEELQAALARLEEETAQKNNALKKiRELEAqiselqedlESERAARNKAEkqrrdLGEELEALKTELEDTLDT 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 160 HSQQDELMA----DISKSIQSLEDESKSLKSQIAEAKI--------------ICKTFKMSEERRAIAIKdalNENSQLQT 221
Cdd:pfam01576 315 TAAQQELRSkreqEVTELKKALEEETRSHEAQLQEMRQkhtqaleelteqleQAKRNKANLEKAKQALE---SENAELQA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 222 SHKQLFQQEAEV------WKGEVSELNKQKITFEDSKVHAEQVLNDKENHIKTLTGHLPMMKDQAAVLEEDTTdddnlel 295
Cdd:pfam01576 392 ELRTLQQAKQDSehkrkkLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVS------- 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 296 EVNSQWENGANLddpLKGALKklihaAKLNVS--LKSLEGERNHIIIQLSEVDKTKEELTEHIKNLQTQQASLQseniyf 373
Cdd:pfam01576 465 SLESQLQDTQEL---LQEETR-----QKLNLStrLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMK------ 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 374 esenQKLQQKLKIMtEFYQENEMKLYRKLtveenyrieeEEKLSRVEEKISrATEGLE-TYRKLAKDLEEELERTVHfyQ 452
Cdd:pfam01576 531 ----KKLEEDAGTL-EALEEGKKRLQREL----------EALTQQLEEKAA-AYDKLEkTKNRLQQELDDLLVDLDH--Q 592
|
410
....*....|
gi 193290160 453 KQVIS-YEKR 461
Cdd:pfam01576 593 RQLVSnLEKK 602
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
92-367 |
3.04e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.54 E-value: 3.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 92 LLEKFSLIQKEYEGYEVESSLEDASFEKAAAEeARSLEATCEKLNRSNSELEDEI-------LCLEKDLKEEKSKHSQQD 164
Cdd:COG1196 230 LLLKLRELEAELEELEAELEELEAELEELEAE-LAELEAELEELRLELEELELELeeaqaeeYELLAELARLEQDIARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 165 ELMADISKSIQSLEDESKSLKSQIAEAKIICKTFKMSEERRAIAIKDALNENSQLQTSHKQLFQQEAEvWKGEVSELNKQ 244
Cdd:COG1196 309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE-AEEELEELAEE 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 245 KITFEDSKVHAEQVLNDKENHIKTLTGHLPMMKDQAAVLEEDTTDDDNLELEVNSQwenganLDDPLKGALKKLIHAAKL 324
Cdd:COG1196 388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA------LEEAAEEEAELEEEEEAL 461
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 193290160 325 NVSLKSLEGERNHIIIQLSEVDKTKEELTEHIKNLQTQQASLQ 367
Cdd:COG1196 462 LELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
120-369 |
3.26e-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: 43.60 E-value: 3.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 120 AAAEEARSLEATCEKLNRSNSELEDEILCLEKDLKEEKSKHSQQDELMADISKSIQSLEDESKSLKSQIAEAKiicktfk 199
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 200 msEERRAIaikdalneNSQLQTSHKQLFQQEAEVWK-GEVSELNkqkitfedSKVHAEQVlNDKENHIKTLTGHLPMMKD 278
Cdd:COG4942 90 --KEIAEL--------RAELEAQKEELAELLRALYRlGRQPPLA--------LLLSPEDF-LDAVRRLQYLKYLAPARRE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 279 QAAVLEEDTTDDDNLELEVNSQwenganlddplKGALKKLIhaAKLNVSLKSLEGERNHIIIQLSEVDKTKEELTEHIKN 358
Cdd:COG4942 151 QAEELRADLAELAALRAELEAE-----------RAELEALL--AELEEERAALEALKAERQKLLARLEKELAELAAELAE 217
|
250
....*....|.
gi 193290160 359 LQTQQASLQSE 369
Cdd:COG4942 218 LQQEAEELEAL 228
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
85-232 |
3.46e-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: 42.23 E-value: 3.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 85 LIEEKCKLLEKFSLIQKEYEGYEVESSLEDASFEKAAAEEARSLEATCEKLN--------------RSNSELEDEILCLE 150
Cdd:pfam08614 5 LIDAYNRLLDRTALLEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEqllaqlreelaelyRSRGELAQRLVDLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 151 KDLKEEKSKHSQQDELMADISKSIQSLEDESKSLKSQIAEakiicktfkmseerraiaiKDALNENSQ--LQTSHKQLFQ 228
Cdd:pfam08614 85 EELQELEKKLREDERRLAALEAERAQLEEKLKDREEELRE-------------------KRKLNQDLQdeLVALQLQLNM 145
|
....
gi 193290160 229 QEAE 232
Cdd:pfam08614 146 AEEK 149
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
516-775 |
3.79e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 44.16 E-value: 3.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 516 REHSPCSPSPLGRPSSETRAFPSPQTLLEDPLRLSPVLPGGGGRGPSSPGNPLDHqitnergepsydrlIDPHRAPSDTG 595
Cdd:PHA03247 2682 RPRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALP--------------AAPAPPAVPAG 2747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 596 SlSSPVEQDRRMMfpPPGQSYPDSTLPPQreDRFYSNSERLSGPAeprsfkMTSLDKMDRSMPSEMESSRNDAKDDLGNL 675
Cdd:PHA03247 2748 P-ATPGGPARPAR--PPTTAGPPAPAPPA--APAAGPPRRLTRPA------VASLSESRESLPSPWDPADPPAAVLAPAA 2816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 676 NVPDSSLPAENEATGPGLIPPPLAPISGPLFP-------VDTRGPFMRRGPPFPPPPPGTMFGASRGYFPPRDFPGPPHA 748
Cdd:PHA03247 2817 ALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPslplggsVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTE 2896
|
250 260
....*....|....*....|....*..
gi 193290160 749 PFAMRNIYPPRGLPPYLHPRPGFYPNP 775
Cdd:PHA03247 2897 SFALPPDQPERPPQPQAPPPPQPQPQP 2923
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
135-453 |
4.48e-04 |
|
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: 43.89 E-value: 4.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 135 LNRSNSELEDE----ILCLEKDlkEEKSKHSQQ-DELMADISKSiQSLEDESKSLKSQIAEAKIICKTFK-----MSEER 204
Cdd:TIGR01612 1454 LLFKNIEMADNksqhILKIKKD--NATNDHDFNiNELKEHIDKS-KGCKDEADKNAKAIEKNKELFEQYKkdvteLLNKY 1530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 205 RAIAIKDALNEN--------SQLQTSHKQlFQQEAEVWKGEVSELNKQKITFEDskvhaEQVLNDKENH--------IKT 268
Cdd:TIGR01612 1531 SALAIKNKFAKTkkdseiiiKEIKDAHKK-FILEAEKSEQKIKEIKKEKFRIED-----DAAKNDKSNKaaidiqlsLEN 1604
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 269 LTGHLPMMKDQAAVLEEDTTDDDNLE-----LEVNSQ----WENGANLD------DPLKGAlKKLIHAAK-----LNVSL 328
Cdd:TIGR01612 1605 FENKFLKISDIKKKINDCLKETESIEkkissFSIDSQdtelKENGDNLNslqeflESLKDQ-KKNIEDKKkeldeLDSEI 1683
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 329 KSLEGERNH--------IIIQLSEVDKTKEELTEHIKNL-----QTQQASLQSENIYFESENQKLQQKLKIMTEFYQENe 395
Cdd:TIGR01612 1684 EKIEIDVDQhkknyeigIIEKIKEIAIANKEEIESIKELieptiENLISSFNTNDLEGIDPNEKLEEYNTEIGDIYEEF- 1762
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 193290160 396 MKLYRKL-----TVEENYRIEEEEKLSRV--EEKISRATEGLETYRKLAKDLE-EELERTV-HFYQK 453
Cdd:TIGR01612 1763 IELYNIIagcleTVSKEPITYDEIKNTRInaQNEFLKIIEIEKKSKSYLDDIEaKEFDRIInHFKKK 1829
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
76-460 |
6.88e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 6.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 76 QKLGATLSGLIEEKCKLLEKFSLIQKEYEgyEVESSLEdasfekaAAEEARSLEATCEKLNRSNSELEDEILclEKDLKE 155
Cdd:PRK03918 327 EERIKELEEKEERLEELKKKLKELEKRLE--ELEERHE-------LYEEAKAKKEELERLKKRLTGLTPEKL--EKELEE 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 156 -EKSKHSQQDELmADISKSIQSLEDESKSLKSQIAE---AKIICKTFK--MSEERRAIAIKDALNENSQLQTSHKQLFQQ 229
Cdd:PRK03918 396 lEKAKEEIEEEI-SKITARIGELKKEIKELKKAIEElkkAKGKCPVCGreLTEEHRKELLEEYTAELKRIEKELKEIEEK 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 230 EAEVWKGEV---SELNKQKITFEDSKVhAEQVLNDKENhiktLTGHlpmmkdQAAVLEEDTTDDDNLELEVNSQWENGAN 306
Cdd:PRK03918 475 ERKLRKELReleKVLKKESELIKLKEL-AEQLKELEEK----LKKY------NLEELEKKAEEYEKLKEKLIKLKGEIKS 543
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 307 LDDPLK--GALKKliHAAKLNVSLKSLEGERNHIIIQLSEVD-KTKEELTEHIKNLQ----------TQQASLQSENIYF 373
Cdd:PRK03918 544 LKKELEklEELKK--KLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEpfyneylelkDAEKELEREEKEL 621
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 374 ESENQKLQQKLKIMTEFYQENEMKLYRKLTVEENYRIEEEEKLSRVEEKISRATEGLETYRKLAKDLEEELERTVHFYQK 453
Cdd:PRK03918 622 KKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKE 701
|
....*..
gi 193290160 454 QVISYEK 460
Cdd:PRK03918 702 ELEEREK 708
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
77-369 |
6.92e-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: 6.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 77 KLGATLSGLIEEKCKLLEKfsLIQKEYEGYEVESSLED-----ASFEKAAAEEARSLEATCEKLNRSNSELEDEILCLEK 151
Cdd:pfam01576 486 NLSTRLRQLEDERNSLQEQ--LEEEEEAKRNVERQLSTlqaqlSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEE 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 152 DL----KEEKSKHSQQ---DELMADISKSIQ---SLEDESKSLKSQIAEAKIIckTFKMSEER-RAIAikDALNENSQLQ 220
Cdd:pfam01576 564 KAaaydKLEKTKNRLQqelDDLLVDLDHQRQlvsNLEKKQKKFDQMLAEEKAI--SARYAEERdRAEA--EAREKETRAL 639
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 221 TSHKQLfqQEAEVWKGEVSELNKQ-KITFED---SKVHAEQVLNDKENHIKTLTGHLPMMKDQAAVLEED--TTDDDNLE 294
Cdd:pfam01576 640 SLARAL--EEALEAKEELERTNKQlRAEMEDlvsSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDElqATEDAKLR 717
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 295 LEVN-----SQWENGANLDDPL----KGALKKLIHA------------AKLNVSLKSLEGERNHIIIQLSEVDKTKEELT 353
Cdd:pfam01576 718 LEVNmqalkAQFERDLQARDEQgeekRRQLVKQVREleaelederkqrAQAVAAKKKLELDLKELEAQIDAANKGREEAV 797
|
330
....*....|....*.
gi 193290160 354 EHIKNLQTQQASLQSE 369
Cdd:pfam01576 798 KQLKKLQAQMKDLQRE 813
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
107-509 |
9.74e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 42.76 E-value: 9.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 107 EVESSLEDASFEKAAA-----EEARSLEATCEKLNRSNSELEdEILCLEKDLKEEKSKHSQQDELMADISKSIQSLEDES 181
Cdd:COG5022 961 EVESKLKETSEEYEDLlkkstILVREGNKANSELKNFKKELA-ELSKQYGALQESTKQLKELPVEVAELQSASKIISSES 1039
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 182 KSLKSQIAEAKIICKTFKMSEERRAiAIKDALNENSQLQTSHKQLFQQEA--------EVWKGEVSELNKQKITFEDSKV 253
Cdd:COG5022 1040 TELSILKPLQKLKGLLLLENNQLQA-RYKALKLRRENSLLDDKQLYQLEStenllktiNVKDLEVTNRNLVKPANVLQFI 1118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 254 HAEQVLNDKENHI----KTLTGHLPMMKDQAAVLEED---TTDDDNLELEVNSQWENGANLDDPLKGALKKLIHAAKLNV 326
Cdd:COG5022 1119 VAQMIKLNLLQEIskflSQLVNTLEPVFQKLSVLQLEldgLFWEANLEALPSPPPFAALSEKRLYQSALYDEKSKLSSSE 1198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 327 sLKSLEGErnhiIIQLSEVDKTKEELTEHIKNLQtqqaslqSENIYFESENQKLQQKLKIMTEFYQENEMKLYRKLTVEE 406
Cdd:COG5022 1199 -VNDLKNE----LIALFSKIFSGWPRGDKLKKLI-------SEGWVPTEYSTSLKGFNNLNKKFDTPASMSNEKLLSLLN 1266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 407 NYRIEEEEKlSRVEEKISRATEGLETYRKLAkdLEEELERTVHFYQ-KQVISYEKRGH--DNWLaaRTAERNLSDLrken 483
Cdd:COG5022 1267 SIDNLLSSY-KLEEEVLPATINSLLQYINVG--LFNALRTKASSLRwKSATEVNYNSEelDDWC--REFEISDVDE---- 1337
|
410 420
....*....|....*....|....*.
gi 193290160 484 ahNKQKLTETELKFELLEKDPNALDV 509
Cdd:COG5022 1338 --ELEELIQAVKVLQLLKDDLNKLDE 1361
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
100-496 |
1.32e-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: 42.34 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 100 QKEYEGYEVESSLEdaSFEKAAAEEARSLEATCEKLNRSNSEL-------EDEILCLEKDLKEEKSKHSQQDELMADISK 172
Cdd:TIGR00606 688 QTEAELQEFISDLQ--SKLRLAPDKLKSTESELKKKEKRRDEMlglapgrQSIIDLKEKEIPELRNKLQKVNRDIQRLKN 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 173 SIQSLEDESKSLKSQIAEAKI------ICKTFKMS--EERRAIAIKDALNENSQLQTSHKQL---FQQEAEVWKGEVSEL 241
Cdd:TIGR00606 766 DIEEQETLLGTIMPEEESAKVcltdvtIMERFQMElkDVERKIAQQAAKLQGSDLDRTVQQVnqeKQEKQHELDTVVSKI 845
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 242 NKQKITFEDSKvHAEQVLNDKENHIKTLTGHLPMMKDQAAVLEEDTTDDDNLELEVNSQWENGANLDDPLKGALKKLIHA 321
Cdd:TIGR00606 846 ELNRKLIQDQQ-EQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQE 924
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 322 AKLNVSLKSLEGERNHIiiqlsEVDKTKEELTEHIKNLQTQQASLQSeniyfESENQKLQQKLKIMTEFYQENEMKLYRK 401
Cdd:TIGR00606 925 KEELISSKETSNKKAQD-----KVNDIKEKVKNIHGYMKDIENKIQD-----GKDDYLKQKETELNTVNAQLEECEKHQE 994
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 402 LTVEENYRIEEEEKLSRVEEKISRATEGLETYRKLAKDLEEELERTVHFYQKQVISYEKRGHDNwlaartAERNLSDLRK 481
Cdd:TIGR00606 995 KINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQK------LEENIDLIKR 1068
|
410
....*....|....*..
gi 193290160 482 EN--AHNKQKLTETELK 496
Cdd:TIGR00606 1069 NHvlALGRQKGYEKEIK 1085
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
65-507 |
1.44e-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: 42.41 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 65 SVRSRLYVGREQKLGAT------LSGLIEEKCKLLEKFSLIQKEYEGY--EVESSLEDASFEKAAAEEARsleatcEKLN 136
Cdd:pfam15921 296 SIQSQLEIIQEQARNQNsmymrqLSDLESTVSQLRSELREAKRMYEDKieELEKQLVLANSELTEARTER------DQFS 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 137 RSNSELEDEILCLEKDL-KEEK--SKHSQQDELMADI----SKSIQSLEDESKSLKSQIAEAKIICKTFKmSE-----ER 204
Cdd:pfam15921 370 QESGNLDDQLQKLLADLhKREKelSLEKEQNKRLWDRdtgnSITIDHLRRELDDRNMEVQRLEALLKAMK-SEcqgqmER 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 205 RAIAIKDAlNENSQLQTSHKQLFQQEAEVWKGEVSELNKQKITFEDSkvhaeqvlndkENHIKTLTGHLpmmKDQAAVLE 284
Cdd:pfam15921 449 QMAAIQGK-NESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESS-----------ERTVSDLTASL---QEKERAIE 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 285 EDTTDDDNLELEVNsqwenganlddpLKgaLKKLIHAAKLNVSLKSLEGERNHIIIQLSEVDKTKEELTEHIKNLQT--- 361
Cdd:pfam15921 514 ATNAEITKLRSRVD------------LK--LQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQlvg 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 362 ----QQASLQSENIYFESE--NQKLQ-QKLKIMTEfyqENEMKLyRKLtveenyrieeEEKLSRVE-EKISRATEGLETY 433
Cdd:pfam15921 580 qhgrTAGAMQVEKAQLEKEinDRRLElQEFKILKD---KKDAKI-REL----------EARVSDLElEKVKLVNAGSERL 645
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 434 RKLaKDLEEELERTVHfyqkqvisyEKRGHDNWLAARTAERNLSDLRKENAHNKQKLTETELKFEL------LEKDPNAL 507
Cdd:pfam15921 646 RAV-KDIKQERDQLLN---------EVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLksaqseLEQTRNTL 715
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
87-507 |
1.65e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.08 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 87 EEKCKLLEKfslIQKEYEGyeVESSLEDASfeKAAAEEARSLEATCEKLNRSNSELEDEILCLEKDLKEEKSKHSQQDEl 166
Cdd:pfam01576 172 EEKAKSLSK---LKNKHEA--MISDLEERL--KKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEE- 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 167 maDISKSIQSLEDES----------KSLKSQIAEAKIICKTFKMSEERRAIAIKDALNENSQLQTSHKQLF-----QQEA 231
Cdd:pfam01576 244 --ELQAALARLEEETaqknnalkkiRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLdttaaQQEL 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 232 EVWK-GEVSELnkQKITFEDSKVHAEQVLNDKENH---IKTLTGHLPMMKDQAAVLEED--TTDDDNLELEVNSQWENGA 305
Cdd:pfam01576 322 RSKReQEVTEL--KKALEEETRSHEAQLQEMRQKHtqaLEELTEQLEQAKRNKANLEKAkqALESENAELQAELRTLQQA 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 306 NLDDPLKGalkklihaaklnvslKSLEGERNHIIIQLSEVDKTKEELTEHIKNLQTQQASL-------QSENIYFESENQ 378
Cdd:pfam01576 400 KQDSEHKR---------------KKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVssllneaEGKNIKLSKDVS 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 379 KLQQKLKIMTEFYQENEMKlyrKLTVEEnyrieeeeKLSRVEEKISRATEGLEtyrklakdlEEE-----LERTVHFYQK 453
Cdd:pfam01576 465 SLESQLQDTQELLQEETRQ---KLNLST--------RLRQLEDERNSLQEQLE---------EEEeakrnVERQLSTLQA 524
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 193290160 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 ... |
86-443 |
2.65e-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: 41.25 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 86 IEEKCKLLEKfSLIQKEYEGYEVESSLED--ASFEKAAAEEaRSLEATCEKLNRSNSELEDEILCLEKDLKEEKSKHS-- 161
Cdd:pfam05483 273 LEEKTKLQDE-NLKELIEKKDHLTKELEDikMSLQRSMSTQ-KALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSfv 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 162 ---------QQDELMADISKSIQSLEDESK----SLKSQIAEAKIICKtFKMSEERRAIAIKDALNENSQLQTSHKQlFQ 228
Cdd:pfam05483 351 vtefeattcSLEELLRTEQQRLEKNEDQLKiitmELQKKSSELEEMTK-FKNNKEVELEELKKILAEDEKLLDEKKQ-FE 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 229 QEAEVWKGEVSEL----NKQKITFEDSKVHAEQVLNDKENHIKTLtghlpmmKDQAAVLEEDTTDddNLELEVNSqweng 304
Cdd:pfam05483 429 KIAEELKGKEQELifllQAREKEIHDLEIQLTAIKTSEEHYLKEV-------EDLKTELEKEKLK--NIELTAHC----- 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 305 anldDPLKGALKKLIH-AAKLNVSLKSLEGERNHiiiqlseVDKTKEELTEHIKNLQTQQASLQSENIYFESENQKLQQK 383
Cdd:pfam05483 495 ----DKLLLENKELTQeASDMTLELKKHQEDIIN-------CKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDE 563
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 384 LKIMTEFYQENEMKLYRKLTVEENYRIEEEEKLSRVEEKISRATEGLETYRKLAKDLEEE 443
Cdd:pfam05483 564 VKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKK 623
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
321-509 |
2.94e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.20 E-value: 2.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 321 AAKLNVSLKSLEGERNHIIIQLSEVDKTKEELTEHIKNLQTQQASLQSENIYFESENQKLQQKLkimtEFYQENEMKLYR 400
Cdd:TIGR02168 693 IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL----TELEAEIEELEE 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 401 KLTVEENYRIEEEEKLSRVEEKISRATEGLETYRKLAKDLEEELERTVHFYQKQ---VISYEKRGHDNWLAARTAERNLS 477
Cdd:TIGR02168 769 RLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLrerLESLERRIAATERRLEDLEEQIE 848
|
170 180 190
....*....|....*....|....*....|..
gi 193290160 478 DLRKENAHNKQKLTETELKFELLEKDPNALDV 509
Cdd:TIGR02168 849 ELSEDIESLAAEIEELEELIEELESELEALLN 880
|
|
| LCD1 |
pfam09798 |
DNA damage checkpoint protein; This is a family of proteins which regulate checkpoint kinases. ... |
134-251 |
3.04e-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: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 134 KLNRSNSELEDEILCLEKDLKEEKSKHSQQdelMADISKSIQSLEDESKslksqiaeakiicktFKMSEERRAIAIKDAL 213
Cdd:pfam09798 5 KLELLQQEKEKELEKLKNSYEELKSSHEEE---LEKLKQEVQKLEDEKK---------------FLLNELRSLSATSPAS 66
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 193290160 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 |
3.17e-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: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 140 SELEDEILCLEKDLKEEKSKHSQQDELMADISKSIQSLEDESKSLKsQIAEAKIICKTfkmSEERRAI-AIKDALNENSQ 218
Cdd:smart00787 147 EGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLK-QLEDELEDCDP---TELDRAKeKLKKLLQEIMI 222
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 193290160 219 LQTSHKQLFQQEAEVwKGEVSELNKQKITFEDSKVHAEQVLND 261
Cdd:smart00787 223 KVKKLEELEEELQEL-ESKIEDLTNKKSELNTEIAEAEKKLEQ 264
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
175-517 |
3.62e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.77 E-value: 3.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 175 QSLEDESKSLKSQI----AEAKIICKTFKMSEERraiaIKDALNENSQLQTSHKQLFQQEAEvwkgevselNKQKIT--F 248
Cdd:TIGR04523 36 KQLEKKLKTIKNELknkeKELKNLDKNLNKDEEK----INNSNNKIKILEQQIKDLNDKLKK---------NKDKINklN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 249 EDSKVHAEQVLNDKENHIKtltghlpmMKDQAAVLEEDTTDDDNLELEVNSQWENGANLDDPLKGA---LKKLIHAAKLn 325
Cdd:TIGR04523 103 SDLSKINSEIKNDKEQKNK--------LEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKyndLKKQKEELEN- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 326 vSLKSLEGERNHIiiqLSEVDKTK-------------EELTEHIKNLQTQQASLQSENIYFESENQKLQQKLKIMTEFYQ 392
Cdd:TIGR04523 174 -ELNLLEKEKLNI---QKNIDKIKnkllklelllsnlKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEIS 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 393 ENEMKLyrkltveenyrIEEEEKLSRVEEKISRATEGLETYRKLAKDLEEELERtvhfYQKQVISYEKRGHDNWLAA--- 469
Cdd:TIGR04523 250 NTQTQL-----------NQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQ----LKSEISDLNNQKEQDWNKElks 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 193290160 470 --RTAERNLSDLRKENAHNKQKLTETELKFELLEKDPNALDVSNTAFGRE 517
Cdd:TIGR04523 315 elKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRE 364
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
98-379 |
4.12e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.27 E-value: 4.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 98 LIQKEYEGYEVESSLEDASFEKAAAEEA-RSLEATCEKLNRSNSELEDEILCLEKDLKEEKSKHSQQDELMADISKSIQS 176
Cdd:COG4372 75 LEQLEEELEELNEQLQAAQAELAQAQEElESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKE 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 177 LEDESKSLKSQIAEAKIICKTFKMSEERRAI-AIKDALNENSQLQTSHKQLFQQEAEVWKGEVSELNKQKITFEDSKVHA 255
Cdd:COG4372 155 LEEQLESLQEELAALEQELQALSEAEAEQALdELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLA 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 256 EQVLNDKENHIKTLTGHLPMMKDQAAVLEEDTTDDD-----NLELEVNSQWENGANLDDPLKGALKKLIHAAKLNVSLKS 330
Cdd:COG4372 235 LSALLDALELEEDKEELLEEVILKEIEELELAILVEkdteeEELEIAALELEALEEAALELKLLALLLNLAALSLIGALE 314
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 193290160 331 LEGERNHIIIQLSEVDKTKEELTEHIKNLQTQQASLQSENIYFESENQK 379
Cdd:COG4372 315 DALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGA 363
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
64-241 |
4.32e-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: 4.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 64 RSVRSRLYVG---REQK--LGATLSGLIEEKCKLLEKFSLIQKEYEGYE----VESSLEDASFE----KAAAEEARSLEA 130
Cdd:COG4913 596 RRIRSRYVLGfdnRAKLaaLEAELAELEEELAEAEERLEALEAELDALQerreALQRLAEYSWDeidvASAEREIAELEA 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 131 TCEKLNRSNSE---LEDEILCLEKDLKEEKSKHSQQDELMADISKSIQSLEDESKSLKSQIAEAKIICKT--FKMSEERR 205
Cdd:COG4913 676 ELERLDASSDDlaaLEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLelRALLEERF 755
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 193290160 206 AIAIKDALNE------NSQLQTSHKQLFQQEAEV----------WKGEVSEL 241
Cdd:COG4913 756 AAALGDAVERelrenlEERIDALRARLNRAEEELeramrafnreWPAETADL 807
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
118-510 |
4.56e-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: 4.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 118 EKAAAEEARSLEATCEKLNRSNSELEDEILCLEKdlKEEKSKHSQQDELMADISKSI----QSLEDESKSLKSQIAE-AK 192
Cdd:TIGR00618 248 KREAQEEQLKKQQLLKQLRARIEELRAQEAVLEE--TQERINRARKAAPLAAHIKAVtqieQQAQRIHTELQSKMRSrAK 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 193 IICKTFKMSEERRAIAIKDALnensqLQTSHKQ--LFQQEAEVWKGEVSELNKQKitfedskvhaeqvlnDKENHIKTLT 270
Cdd:TIGR00618 326 LLMKRAAHVKQQSSIEEQRRL-----LQTLHSQeiHIRDAHEVATSIREISCQQH---------------TLTQHIHTLQ 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 271 GHLPMMKDQAAVLEEDTTDDDNLELEVNSQWENganlDDPLKGalkKLIHA-AKLNVSLKSLEGERNHIIIQLSEVDKTK 349
Cdd:TIGR00618 386 QQKTTLTQKLQSLCKELDILQREQATIDTRTSA----FRDLQG---QLAHAkKQQELQQRYAELCAAAITCTAQCEKLEK 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 350 EELTEHIKNLQTQQASLQSENIYFESENQKLQQKLKIMTEfYQENEMKL---YRKLTVEENYRIEEEEKLSRVEEKISRA 426
Cdd:TIGR00618 459 IHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLE-LQEEPCPLcgsCIHPNPARQDIDNPGPLTRRMQRGEQTY 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 427 TEG----------LETYRKLAKDLEEELERTVHFYQKQVISYEKRGHDNWLAARTAERNLSDLRKENAHNKQKLTETELK 496
Cdd:TIGR00618 538 AQLetseedvyhqLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHAL 617
|
410
....*....|....
gi 193290160 497 FELLEKDPNALDVS 510
Cdd:TIGR00618 618 LRKLQPEQDLQDVR 631
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
152-352 |
4.93e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 40.30 E-value: 4.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 152 DLKEEKS--KHSQQDELMADISKSIQSLEDESKSLKsqIAEAKIICKTFKMSEERRAIA----------IKDALNENSQL 219
Cdd:PRK05771 35 DLKEELSneRLRKLRSLLTKLSEALDKLRSYLPKLN--PLREEKKKVSVKSLEELIKDVeeelekiekeIKELEEEISEL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 220 QTSHKQLFQQ--EAEVWKG---EVSELNKQK-ITFEDSKVHAEQVLNDKENH-------IKTLTGHLPMM----KDQAAV 282
Cdd:PRK05771 113 ENEIKELEQEieRLEPWGNfdlDLSLLLGFKyVSVFVGTVPEDKLEELKLESdvenveyISTDKGYVYVVvvvlKELSDE 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 283 LEEDTTDDDNLELEVnsqwenganlddPLKGALKKLIHAAKLNvsLKSLEGERNHIIIQLSEVDKTKEEL 352
Cdd:PRK05771 193 VEEELKKLGFERLEL------------EEEGTPSELIREIKEE--LEEIEKERESLLEELKELAKKYLEE 248
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
100-443 |
6.01e-03 |
|
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: 40.27 E-value: 6.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 100 QKEYEGYE-VESSLEDAsfEKAAAEEARSLeATCEKLNrsnSELEDEILCLEKDLKEEKSKHSQQDELM-ADISKSIQSL 177
Cdd:pfam15964 328 QRESSAYEqVKQAVQMT--EEANFEKTKAL-IQCEQLK---SELERQKERLEKELASQQEKRAQEKEALrKEMKKEREEL 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 178 EDESKSLKSQIAEAKIICKtfKMSEERRAIaikdalneNSQLQTSHKQLFQQEAEVWK--GEVS-ELNKQKItfedSKVH 254
Cdd:pfam15964 402 GATMLALSQNVAQLEAQVE--KVTREKNSL--------VSQLEEAQKQLASQEMDVTKvcGEMRyQLNQTKM----KKDE 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 255 AEQVLNDkenhIKTLTGHLPMMKDQAAVLEEDTTDDDNLELEVNSQWENGANlDDPLKgaLKKLIHAAKLNVSLKSLEGE 334
Cdd:pfam15964 468 AEKEHRE----YRTKTGRQLEIKDQEIEKLGLELSESKQRLEQAQQDAARAR-EECLK--LTELLGESEHQLHLTRLEKE 540
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 335 R------NHIIIQLSEVDKTKEELTEHIKNLQTQQASLQSENIYFESENQKLQQKLKimtefyqENEMKLYRKLTVEENY 408
Cdd:pfam15964 541 SiqqsfsNEAKAQALQAQQREQELTQKMQQMEAQHDKTVNEQYSLLTSQNTFIAKLK-------EECCTLAKKLEEITQK 613
|
330 340 350
....*....|....*....|....*....|....*
gi 193290160 409 RIEEEEKLSRVEEKIsraTEGLETYRKLAKDLEEE 443
Cdd:pfam15964 614 SRSEVEQLSQEKEYL---QDRLEKLQKRNEELEEQ 645
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
119-503 |
6.10e-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: 40.16 E-value: 6.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 119 KAAAEEARSLEATCEKLNRSNSELEDEILCLEKDL--KEEKSKH-----SQQDELMADIS--------------KSIQSL 177
Cdd:pfam01576 134 KKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLaeEEEKAKSlsklkNKHEAMISDLEerlkkeekgrqeleKAKRKL 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 178 EDESKSLKSQIAEAKIICKTFKMSEERRAIAIKDALN--ENSQLQTSHKQLFQQEAEvwkGEVSELNKQKITFEDSKVHA 255
Cdd:pfam01576 214 EGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALArlEEETAQKNNALKKIRELE---AQISELQEDLESERAARNKA 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 256 EQVLNDKENHIKTLTGHLpmmkdqaavleEDTTDDDNLELEVNSQWEnganlddplkgalkklihaAKLNVSLKSLEGER 335
Cdd:pfam01576 291 EKQRRDLGEELEALKTEL-----------EDTLDTTAAQQELRSKRE-------------------QEVTELKKALEEET 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 336 NHIIIQLSEVDK----TKEELTEHIKNLQTQQASLQSENIYFESENQKLQQKLKIMTEFYQENEMK----------LYRK 401
Cdd:pfam01576 341 RSHEAQLQEMRQkhtqALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKrkklegqlqeLQAR 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 402 LTVEENYRIEEEEKLSRVEEKISRATEGLETYR----KLAKD---LEEELERTVHFYQ---KQVISY---------EKRG 462
Cdd:pfam01576 421 LSESERQRAELAEKLSKLQSELESVSSLLNEAEgkniKLSKDvssLESQLQDTQELLQeetRQKLNLstrlrqledERNS 500
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 193290160 463 HDNWL-----AARTAERNLSDLRKENAHNKQKLTETELKFELLEKD 503
Cdd:pfam01576 501 LQEQLeeeeeAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEG 546
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
91-279 |
6.54e-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: 6.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 91 KLLEKFSLIQKEYEGYEVESSLEDASFEKAAAEEarsleatcEKLNRSNSELEDEILCLEKDLKEEKSKhsqqdelMADI 170
Cdd:TIGR02168 334 ELAEELAELEEKLEELKEELESLEAELEELEAEL--------EELESRLEELEEQLETLRSKVAQLELQ-------IASL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 171 SKSIQSLEDESKSLKSQIAeakiicktfKMSEERRAIAIKDALNENSQLQTSHKQLFQQEAEVwKGEVSELNKQKITFED 250
Cdd:TIGR02168 399 NNEIERLEARLERLEDRRE---------RLQQEIEELLKKLEEAELKELQAELEELEEELEEL-QEELERLEEALEELRE 468
|
170 180
....*....|....*....|....*....
gi 193290160 251 SKVHAEQVLNDKENHIKTLTGHLPMMKDQ 279
Cdd:TIGR02168 469 ELEEAEQALDAAERELAQLQARLDSLERL 497
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
106-519 |
7.18e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 40.20 E-value: 7.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 106 YEVESSLEDASFEKAAAEEARSLEATCEKLNRSNSELEDEILCLEKDLKEEKSkhsqqdeLMADISKSIQSLEDESKSLK 185
Cdd:PTZ00440 512 EKNNIVNNNFKNIEDYYITIEGLKNEIEGLIELIKYYLQSIETLIKDEKLKRS-------MKNDIKNKIKYIEENVDHIK 584
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 186 SQIAEAKIICKTFKMSEE---RRAIAIKDALNENSQLQTSHKQLFQqeaEVWKGEVSELNKQKITFEDSKVHAEQVLNDK 262
Cdd:PTZ00440 585 DIISLNDEIDNIIQQIEElinEALFNKEKFINEKNDLQEKVKYILN---KFYKGDLQELLDELSHFLDDHKYLYHEAKSK 661
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 263 ENhIKTLtghLPMMKDQAAVLEEDTTDDDN-------------LELEVNSQWENGANLD-DPLKGALKKLIHAAKLNVSL 328
Cdd:PTZ00440 662 ED-LQTL---LNTSKNEYEKLEFMKSDNIDniiknlkkelqnlLSLKENIIKKQLNNIEqDISNSLNQYTIKYNDLKSSI 737
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 329 KSLEGERNHIIIQLSEVDKTKEELTEHIKnlQTQQASLQSENIY--FESENQKLQQKLKIMTefyqeNEMKLyrkltvee 406
Cdd:PTZ00440 738 EEYKEEEEKLEVYKHQIINRKNEFILHLY--ENDKDLPDGKNTYeeFLQYKDTILNKENKIS-----NDINI-------- 802
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 407 nyrieeeeklsrVEEKISRATEGLETYRKLAKDLEEELERTvhfYQKQVISYEKRGHDNwlaartAERNLSDLRKENAHN 486
Cdd:PTZ00440 803 ------------LKENKKNNQDLLNSYNILIQKLEAHTEKN---DEELKQLLQKFPTED------ENLNLKELEKEFNEN 861
|
410 420 430
....*....|....*....|....*....|...
gi 193290160 487 KQKLTETELKFELLEKDPNALDVSNTAFGREHS 519
Cdd:PTZ00440 862 NQIVDNIIKDIENMNKNINIIKTLNIAINRSNS 894
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
128-502 |
7.34e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 7.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 128 LEATCEKLNRSNSELEDEILCLEKDLKEEkskhsqqdelmADISKSIQSLEDESKSLKSQIAEakiicktfKMSEERRAI 207
Cdd:PRK03918 160 YENAYKNLGEVIKEIKRRIERLEKFIKRT-----------ENIEELIKEKEKELEEVLREINE--------ISSELPELR 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 208 AIKDALNENsqlqtshkqlfQQEAEVWKGEVSELNKQKITFEDSKVHAEQVLNDKENHIKTLTGHLPMMKDQAAVLEEdt 287
Cdd:PRK03918 221 EELEKLEKE-----------VKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKE-- 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 288 tdddnLELEVNSQWENGANLDDPLKGAlkklihaAKLNVSLKSLEGERNHIIIQLSEVDKTK---EELTEHIKNLQTQQA 364
Cdd:PRK03918 288 -----LKEKAEEYIKLSEFYEEYLDEL-------REIEKRLSRLEEEINGIEERIKELEEKEerlEELKKKLKELEKRLE 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 365 SLQSENIYFESENQKLQQKLKIMTEFYQENEMKLYRKLTVEENYRIEEEEKLSRVEEKISRategLETYRKLAKDLEEEL 444
Cdd:PRK03918 356 ELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGE----LKKEIKELKKAIEEL 431
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 193290160 445 E--RTVHFYQKQVISYEKRGhdNWLAARTAErnLSDLRKENAHNKQKLTETELKFELLEK 502
Cdd:PRK03918 432 KkaKGKCPVCGRELTEEHRK--ELLEEYTAE--LKRIEKELKEIEEKERKLRKELRELEK 487
|
|
| |
