|
Name |
Accession |
Description |
Interval |
E-value |
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
86-507 |
4.75e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.08 E-value: 4.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 86 IEEKCKLLEKfSLIQKEYEGYEVESSLEDASFEKAAAE-EARSLEATCEKLNrsnsELEDEILCLEKDLKEEKSKHSQqd 164
Cdd:PRK03918 191 IEELIKEKEK-ELEEVLREINEISSELPELREELEKLEkEVKELEELKEEIE----ELEKELESLEGSKRKLEEKIRE-- 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 165 elmadISKSIQSLEDESKSLKSQIAEAKIICKtfKMSEERRAIAIKDALNENSQLQTSHKQLFQQEAEVWKGQVSELNKq 244
Cdd:PRK03918 264 -----LEERIEELKKEIEELEEKVKELKELKE--KAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEE- 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 245 kitfedskvhaeqvlndKENHIKTLTGHLPMMKDQAAVLEEDttdddnLELevnsqwenganlddpLKGALKKLIHAAKL 324
Cdd:PRK03918 336 -----------------KEERLEELKKKLKELEKRLEELEER------HEL---------------YEEAKAKKEELERL 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 325 NVSLKSLEGERnhIIIQLSEVDKTKEELTEHIKNLQTQQASLQSEniyfESENQKLQQKLK-----------IMTEFYQE 393
Cdd:PRK03918 378 KKRLTGLTPEK--LEKELEELEKAKEEIEEEISKITARIGELKKE----IKELKKAIEELKkakgkcpvcgrELTEEHRK 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 394 NEMKLYRKltveenyrieeeeKLSRVEEKISRATEGLETYRKLAKDLEEELERtvhfyQKQVISYEKrghdnwlaarTAE 473
Cdd:PRK03918 452 ELLEEYTA-------------ELKRIEKELKEIEEKERKLRKELRELEKVLKK-----ESELIKLKE----------LAE 503
|
410 420 430
....*....|....*....|....*....|....*
gi 511772982 474 RnLSDLRKE-NAHNKQKLTETELKFELLEKDPNAL 507
Cdd:PRK03918 504 Q-LKELEEKlKKYNLEELEKKAEEYEKLKEKLIKL 537
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
95-444 |
6.55e-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: 59.37 E-value: 6.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 95 KFSLIQ--KEYEGYEVESSLEDASFEKAAAEEARSLEATCEKlnrsNSELEDEILCLEKDLKEEKSKHSQQDELMADISK 172
Cdd:pfam05557 8 KARLSQlqNEKKQMELEHKRARIELEKKASALKRQLDRESDR----NQELQKRIRLLEKREAEAEEALREQAELNRLKKK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 173 SIQSLEDESKSLKSQIAEAK--IICKTFKMSEERRAIAIKDalnenSQLQT--SHKQLFQQEAEVWKGQVSELNKQKITF 248
Cdd:pfam05557 84 YLEALNKKLNEKESQLADARevISCLKNELSELRRQIQRAE-----LELQStnSELEELQERLDLLKAKASEAEQLRQNL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 249 EDSkvhaEQVLNDKENHIKTLTGHLPMMKDQAAVLEedttdddnlelevNSQwenganlddplkgalKKLIHAAKLNVSL 328
Cdd:pfam05557 159 EKQ----QSSLAEAEQRIKELEFEIQSQEQDSEIVK-------------NSK---------------SELARIPELEKEL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 329 KSLEGERNHiiiqLSEVDKTKEELTEHIKNLQT---QQASLQSENIYFESENQKLQQKLKIMTEFYQENEMKLYRKLTVE 405
Cdd:pfam05557 207 ERLREHNKH----LNENIENKLLLKEEVEDLKRkleREEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNLRSPEDLS 282
|
330 340 350
....*....|....*....|....*....|....*....
gi 511772982 406 ENYRIEEEEKLSRVEEKISrATEGLETYRKLAKDLEEEL 444
Cdd:pfam05557 283 RRIEQLQQREIVLKEENSS-LTSSARQLEKARRELEQEL 320
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
107-509 |
9.82e-09 |
|
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: 58.96 E-value: 9.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 107 EVESSLEDASFekaaaeearSLEATCEKLNrsnsELEDEILCLEKDLKEEKSKHSQQDELMADISKSIQSLEDESKSLKS 186
Cdd:pfam05483 251 EKENKMKDLTF---------LLEESRDKAN----QLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEE 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 187 --QIAeAKIICKtfkMSEERRAiaikdALNENSQLQTSHKQLfqqeaevwkgqVSELNKQKITFEDSKVHAEQVLNDKEN 264
Cdd:pfam05483 318 dlQIA-TKTICQ---LTEEKEA-----QMEELNKAKAAHSFV-----------VTEFEATTCSLEELLRTEQQRLEKNED 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 265 HIKTLTGHLpmmKDQAAVLEEDTTDDDNLELEV----------------NSQWENganLDDPLKGALKKLIHAaklnvsL 328
Cdd:pfam05483 378 QLKIITMEL---QKKSSELEEMTKFKNNKEVELeelkkilaedeklldeKKQFEK---IAEELKGKEQELIFL------L 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 329 KSLEGERNHIIIQLSEVDKTKEELTEHIKNLQTQQASLQSENIYFES-------ENQKLQQKLKIMT---EFYQEN---- 394
Cdd:pfam05483 446 QAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAhcdklllENKELTQEASDMTlelKKHQEDiinc 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 395 ---EMKLYRKLTVEENYRIEEEEKLSRVEEKISRatEGLETYRKLAKDLE--EELERTVHFYQKQVISYEKRGHDNWLAA 469
Cdd:pfam05483 526 kkqEERMLKQIENLEEKEMNLRDELESVREEFIQ--KGDEVKCKLDKSEEnaRSIEYEVLKKEKQMKILENKCNNLKKQI 603
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 511772982 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 |
1.41e-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: 58.49 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 123 EEARSLEATCEKLNRSNSELEDEILCLEKDLKE-EKSKHSQQDELmADISK----------SIQSLEDESKSLKSQIAEA 191
Cdd:TIGR04523 145 TEIKKKEKELEKLNNKYNDLKKQKEELENELNLlEKEKLNIQKNI-DKIKNkllklelllsNLKKKIQKNKSLESQISEL 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 192 KiicktfkmseerraiaikdalNENSQLQTSHKQLfQQEAEVWKGQVSELNKQKITFEDSKVHAEQVLNDKENHIKTLTG 271
Cdd:TIGR04523 224 K---------------------KQNNQLKDNIEKK-QQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNK 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 272 HLPMMKDQAAVLEEDTTD-----DDNLELEVNSQWENGANLDDPLKGALKKLIHA-AKLNVSLKSLEGERNH-------I 338
Cdd:TIGR04523 282 KIKELEKQLNQLKSEISDlnnqkEQDWNKELKSELKNQEKKLEEIQNQISQNNKIiSQLNEQISQLKKELTNsesenseK 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 339 IIQLSE-------VDKTKEELTEHIKNLQTQQASLQSENIYFESENQKLQQKLKIMtefyQENEMKLYRKLTVEENYRIE 411
Cdd:TIGR04523 362 QRELEEkqneiekLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKL----QQEKELLEKEIERLKETIIK 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 412 EEEKLSRVEEKISrategletyrklAKDLE-EELERTVHFYQKQVISYEKrghdnwlAARTAERNLSDLRKENAHNKQKL 490
Cdd:TIGR04523 438 NNSEIKDLTNQDS------------VKELIiKNLDNTRESLETQLKVLSR-------SINKIKQNLEQKQKELKSKEKEL 498
|
410
....*....|...
gi 511772982 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 |
3.13e-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: 3.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 75 EQKLGATLSGLIEEKCKLLEKFS--------LIQKEYEGYEVESSLEDASFEKAA-------------AEEARSLEATCE 133
Cdd:TIGR04523 252 QTQLNQLKDEQNKIKKQLSEKQKeleqnnkkIKELEKQLNQLKSEISDLNNQKEQdwnkelkselknqEKKLEEIQNQIS 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 134 KLNRSNSELEDEILCLEKDLKEEKSKHSQQDE-------LMADISKSIQSLEDESKSLKSQIAEAKIICKTFKMSEERRA 206
Cdd:TIGR04523 332 QNNKIISQLNEQISQLKKELTNSESENSEKQReleekqnEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKD 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 207 IAIKDALNENSQLQTSHKQLfQQEAEVWKGQVSELNKQKITFEDSKVHAEQVLNDKENHIKTLTGHLPMMKDQaavLEED 286
Cdd:TIGR04523 412 EQIKKLQQEKELLEKEIERL-KETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQN---LEQK 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 287 TTDDDNLELEVNSQWENGANLDDPLKgALKKLIhaAKLNVSLKSLEGERNHIIIQLSEV---------DKTKEELTEHIK 357
Cdd:TIGR04523 488 QKELKSKEKELKKLNEEKKELEEKVK-DLTKKI--SSLKEKIEKLESEKKEKESKISDLedelnkddfELKKENLEKEID 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 358 NLQTQQASLQSENIYFESENQKLQQKLKImtefYQENEMKLYRKLTVEENYRIEEEEKLSRVEEKisraTEGLETYRKLA 437
Cdd:TIGR04523 565 EKNKEIEELKQTQKSLKKKQEEKQELIDQ----KEKEKKDLIKEIEEKEKKISSLEKELEKAKKE----NEKLSSIIKNI 636
|
410
....*....|....*...
gi 511772982 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 |
3.49e-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: 53.92 E-value: 3.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 85 LIEEKCKLLE--KFSLIQKEYEGYEVESSLEDASFEKAAAE-EARSLEATCEKLNRSNSELEDEILCLEKDLKEEKSKHS 161
Cdd:TIGR02169 203 LRREREKAERyqALLKEKREYEGYELLKEKEALERQKEAIErQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIK 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 162 QQ-DELMADISKSIQSLEDESKSLKSQIAEAKiicKTFKMSEERRAIAIKDAlnensqlqtsHKQlfQQEAEVWKGQVSE 240
Cdd:TIGR02169 283 DLgEEEQLRVKEKIGELEAEIASLERSIAEKE---RELEDAEERLAKLEAEI----------DKL--LAEIEELEREIEE 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 241 LNKQKITFEDSKVHAEQVLNDKENHIKtltghlpmmkdqaavlEEDTTdddnlelevnsqwenganlddplkgalkklih 320
Cdd:TIGR02169 348 ERKRRDKLTEEYAELKEELEDLRAELE----------------EVDKE-------------------------------- 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 321 AAKLNVSLKSLEgernhiiiqlSEVDKTKEELTEHIKNLQTQQASLQSENIYFESENQKLQQKLKIMTEFYQENEMKLYr 400
Cdd:TIGR02169 380 FAETRDELKDYR----------EKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKAL- 448
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 511772982 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 |
5.95e-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: 5.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 87 EEKcKLLEKFSLIQKEYEGYEVE-SSLEDASFEKAaaeearsleatcEKLNRSNSELEDeilcLEKDLKEEKSKHSQQDE 165
Cdd:TIGR04523 34 EEK-QLEKKLKTIKNELKNKEKElKNLDKNLNKDE------------EKINNSNNKIKI----LEQQIKDLNDKLKKNKD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 166 LMADISKSIQSLEDESKSLKSQIAEAKIICKTFKMSEERRAIAIKDALNENSQLqtshkqlfQQEAEVWKGQVSELNKQK 245
Cdd:TIGR04523 97 KINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKK--------EKELEKLNNKYNDLKKQK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 246 ITFEDSKVHAEQVLNDKENHIKTLTGHLPMMKDQAAVLEEDTTDDDNLELEV------NSQWENGANLDDPLKGALKKLI 319
Cdd:TIGR04523 169 EELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQIselkkqNNQLKDNIEKKQQEINEKTTEI 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 320 HAAKLNvsLKSLEGERNHIIIQLS----EVDKTKEELTEHIKNLQTQQASLQSENiyfeseNQKLQQKLKIMTEFYQENE 395
Cdd:TIGR04523 249 SNTQTQ--LNQLKDEQNKIKKQLSekqkELEQNNKKIKELEKQLNQLKSEISDLN------NQKEQDWNKELKSELKNQE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 396 MKLyrkltveenyrIEEEEKLSRVEEKISRATEGLETYRKLAKDLE---EELERTVHFYQKQVISYEKRGHDNWLAARTA 472
Cdd:TIGR04523 321 KKL-----------EEIQNQISQNNKIISQLNEQISQLKKELTNSEsenSEKQRELEEKQNEIEKLKKENQSYKQEIKNL 389
|
410 420 430
....*....|....*....|....*....|....*.
gi 511772982 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 |
6.88e-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: 52.72 E-value: 6.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 123 EEARSLEATCEKLNRSNSELEDEILCLEKDLKEEKSKHSQQDELMADISKSIQSLEDESKSLKSQIAEakiicktfKMSE 202
Cdd:TIGR04523 426 KEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKS--------KEKE 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 203 erraiaIKDALNENSQLQTSHKQLFQQEAEvwkgqvSELNKQKITFEDSKVhaEQVLNDKENHIKTLtghlpmmkdqaav 282
Cdd:TIGR04523 498 ------LKKLNEEKKELEEKVKDLTKKISS------LKEKIEKLESEKKEK--ESKISDLEDELNKD------------- 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 283 leEDTTDDDNLELEVNSQWENganlDDPLKGALKKLIHA-AKLNVSLKSLEGERNHIIIQLSEVDKTKEELTEHIKNLQT 361
Cdd:TIGR04523 551 --DFELKKENLEKEIDEKNKE----IEELKQTQKSLKKKqEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKK 624
|
250 260 270
....*....|....*....|....*....|.
gi 511772982 362 QQASLQSENIYFESENQKLQQKLK-IMTEFY 391
Cdd:TIGR04523 625 ENEKLSSIIKNIKSKKNKLKQEVKqIKETIK 655
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
115-393 |
1.16e-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: 52.13 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 115 ASFEKAAAEEARSLEATCEKLNRSNSELEDEILCLEKDLKEEKSKHSQQDELMADISKSIQSLEDESKSLKSQIAEAKII 194
Cdd:pfam10174 439 TTLEEALSEKERIIERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSK 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 195 CKTFKmseerraIAIKDALNENSQLQTSHKQLFQQEAEVWKG-----QVSELNKQKITF--EDSKVHAE-----QVL--- 259
Cdd:pfam10174 519 LKSLE-------IAVEQKKEECSKLENQLKKAHNAEEAVRTNpeindRIRLLEQEVARYkeESGKAQAEverllGILrev 591
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 260 ----NDKENHIKTLTGHLP-MMKDQaavleedTTDDDNLE-LEVNSQWENGANLDDPLKgalkklihaaklnvslKSLEG 333
Cdd:pfam10174 592 enekNDKDKKIAELESLTLrQMKEQ-------NKKVANIKhGQQEMKKKGAQLLEEARR----------------REDNL 648
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 511772982 334 ERNHIIIQLSEV----DKTKEELTEHIKNLQTQQASLQSENIYFESENQKLQQKLKIMTEFYQE 393
Cdd:pfam10174 649 ADNSQQLQLEELmgalEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAERRKQLEEILEMKQE 712
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
118-432 |
1.24e-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: 52.37 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 118 EKAAAEEARSLEATCEKLNRSNSELEDEILCLEKDLKEEKSKHSQQDELMADISKSIQSLEDESKSLKSQIAEAKIICKT 197
Cdd:TIGR02168 248 LKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 198 FkmseERRAIAIKDALNENsqlqtshkqlfQQEAEVWKGQVSELNKQKITFEDSKVHAEQVLNDKENHIKTLTGHLPMMK 277
Cdd:TIGR02168 328 L----ESKLDELAEELAEL-----------EEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 278 DQAAVLEEDTTdddNLELEVNSQWENGANLDDPLKGALKKLIHAAklnvsLKSLEGERNHIIIQLSEVDKTKEELTEHIK 357
Cdd:TIGR02168 393 LQIASLNNEIE---RLEARLERLEDRRERLQQEIEELLKKLEEAE-----LKELQAELEELEEELEELQEELERLEEALE 464
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 511772982 358 NLQTQQASLQSENIYFESENQKLQQKLKiMTEFYQENEMKLYRKLTVEENYRIEEEEKLSRVEEKISrATEGLET 432
Cdd:TIGR02168 465 ELREELEEAEQALDAAERELAQLQARLD-SLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELIS-VDEGYEA 537
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
119-503 |
2.32e-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: 51.17 E-value: 2.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 119 KAAAEEARSLEATCEKLNRSNSELEDEIlclekdlKEEKSKHSQQDELMADISKSIQSLEDESKSLKSQIAEakiicktf 198
Cdd:TIGR04523 207 KKKIQKNKSLESQISELKKQNNQLKDNI-------EKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSE-------- 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 199 KMSE-ERRAIAIKDALNENSQLQTSHKQLFQQEAEVWKGQVSELNKQKitfEDSKVHAEQVLNDKENHIKTLtghlpmmK 277
Cdd:TIGR04523 272 KQKElEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQ---EKKLEEIQNQISQNNKIISQL-------N 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 278 DQAAVLEEDTTDDDNLELEVNSQWENGANlddplkgALKKLIHA-AKLNVSLKSLEGERNHIIIQLSEVDKTKEELTEHI 356
Cdd:TIGR04523 342 EQISQLKKELTNSESENSEKQRELEEKQN-------EIEKLKKEnQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQI 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 357 KNLQTQQASLQSENIYFESENQKLQQKLKIMTEfyQENEMK------------LYRKLTVEENYRIEEEEKLSRVEEKIS 424
Cdd:TIGR04523 415 KKLQQEKELLEKEIERLKETIIKNNSEIKDLTN--QDSVKEliiknldntresLETQLKVLSRSINKIKQNLEQKQKELK 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 425 RATEGLETYRKLAKDLEEELErtvhfYQKQVISYEKRGHDNwLAARTAERN--LSDLRKENAHNKQKLTETELKFELLEK 502
Cdd:TIGR04523 493 SKEKELKKLNEEKKELEEKVK-----DLTKKISSLKEKIEK-LESEKKEKEskISDLEDELNKDDFELKKENLEKEIDEK 566
|
.
gi 511772982 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 |
3.40e-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: 3.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 72 VGREQKLGATLSGLIEEKCKLLEKFSLIQKEYEGYEVESSLEDASFEKAAAEEARSLEATceKLNRSNSELEDEILCLEK 151
Cdd:pfam02463 642 KAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEI--KKKEQREKEELKKLKLEA 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 152 DLKEEKSKHSQQDELMADISKSIQ-----SLEDESKSLKSQIAEAKIICKTFKMsEERRAIAIKDALNENSQLQTSHKQL 226
Cdd:pfam02463 720 EELLADRVQEAQDKINEELKLLKQkideeEEEEEKSRLKKEEKEEEKSELSLKE-KELAEEREKTEKLKVEEEKEEKLKA 798
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 227 FQQEAEVWKGQVSELNKQKITFEDSKVHAEQVLNDKENHIKTLTGHLpmMKDQAAVLEEDTTDDDNLELEVNSQWENGAN 306
Cdd:pfam02463 799 QEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEE--QKLEKLAEEELERLEEEITKEELLQELLLKE 876
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 307 LDDPLKGALKKLIHA-AKLNVSLKSLEGERNHIIIQLSEVDKTKEELTEHIKNLQ-----------TQQASLQSENIYFE 374
Cdd:pfam02463 877 EELEEQKLKDELESKeEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLkyeeepeelllEEADEKEKEENNKE 956
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 375 SENQKLQQKLKIMTEFYQENEMKLYRKLTVEENYRIEEEEKLSRVEEKISRAtegLETYRKLAKDLEEELERTVHFYQKQ 454
Cdd:pfam02463 957 EEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLI---RAIIEETCQRLKEFLELFVSINKGW 1033
|
....*..
gi 511772982 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 |
1.10e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.28 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 146 ILCLEKDLKEEKSKHSQQDELMADISKSIQSLEDESKSLKSQIAEAKIIcktfkmsEERRAIAIKDALNENSQLQTSHKQ 225
Cdd:TIGR02168 672 ILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKE-------LEELSRQISALRKDLARLEAEVEQ 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 226 LFQQEAEVwKGQVSELNKQKITFEDSKVHAEQVLNDKENHIKTLTGHLPMMKDQAAVLEEDTTDddnlelevnsqwenga 305
Cdd:TIGR02168 745 LEERIAQL-SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDE---------------- 807
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 306 nlddpLKGALKKL-IHAAKLNVSLKSLEGERNHIIIQLSEVDKTKEELTEHIKNLQTQQASLQSEniyFESENQKLQQKL 384
Cdd:TIGR02168 808 -----LRAELTLLnEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEEL---IEELESELEALL 879
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 511772982 385 KIMTEfyQENEMKLYRKltveenYRIEEEEKLSRVEEKISRATEGLETYRKLAKDLEEELERT 447
Cdd:TIGR02168 880 NERAS--LEEALALLRS------ELEELSEELRELESKRSELRRELEELREKLAQLELRLEGL 934
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
123-244 |
1.14e-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: 45.32 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 123 EEARSLEATCEKLNRSNSELEDEILCLEKDLKE--EKSKHSQQD---ELM--ADISKSIQSLEDESKSLKSQIAEAKIic 195
Cdd:pfam07926 1 AELSSLQSEIKRLKEEAADAEAQLQKLQEDLEKqaEIAREAQQNyerELVlhAEDIKALQALREELNELKAEIAELKA-- 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 511772982 196 ktfkmseerRAIAIKDALNENSQLQTSHKQLFQQEAEVWKGQVSELNKQ 244
Cdd:pfam07926 79 ---------EAESAKAELEESEESWEEQKKELEKELSELEKRIEDLNEQ 118
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
109-519 |
1.29e-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: 48.95 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 109 ESSLEDASFEKAaaeeaRSLEATCEKLNRSNSELEDEILCLEKDLKEEKSKHSQQDELMADISKSIQSL--EDESKSLK- 185
Cdd:pfam05483 62 QEGLKDSDFENS-----EGLSRLYSKLYKEAEKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELqfENEKVSLKl 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 186 -SQIAEAKIICKTFKMSEERRAIaIKDALNENSQLQTSHKQLFQQEAEVWKGQVSELNKQKITFEDSKVHAEQV------ 258
Cdd:pfam05483 137 eEEIQENKDLIKENNATRHLCNL-LKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENArlemhf 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 259 -------------------LNDKENHI--------------KTLTGHLPMMKDQAAVLEEDTT-DDDNLELEVNSQWENG 304
Cdd:pfam05483 216 klkedhekiqhleeeykkeINDKEKQVsllliqitekenkmKDLTFLLEESRDKANQLEEKTKlQDENLKELIEKKDHLT 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 305 ANLDDpLKGALKKLIHAAK-----LNVSLKSLEGERNHIIIQLSEVDKTKEELTEHIKNLQTQQASLQSeniYFESENQK 379
Cdd:pfam05483 296 KELED-IKMSLQRSMSTQKaleedLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEE---LLRTEQQR 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 380 LQQ---KLKIMTefyqeneMKLYRKLTVEENYRIEEEEKLSRVEE--KISRATEGLETYRKLAKDLEEELERTVHFYQKQ 454
Cdd:pfam05483 372 LEKnedQLKIIT-------MELQKKSSELEEMTKFKNNKEVELEElkKILAEDEKLLDEKKQFEKIAEELKGKEQELIFL 444
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 511772982 455 VISYEKRGHD---NWLAARTAERNLSdlrKENAHNKQKLTETELKFELLEKDPNALDVSNTAFGREHS 519
Cdd:pfam05483 445 LQAREKEIHDleiQLTAIKTSEEHYL---KEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEAS 509
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
94-385 |
2.06e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.39 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 94 EKFSLIQKEYEGYEVEssledasfekAAAEEARSLEATCEKLNRSNSELEDEILCLEKDLKEEKSKHSQQDELMADISKS 173
Cdd:COG1196 213 ERYRELKEELKELEAE----------LLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELE 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 174 IQSLEDESKSLKSQIAEAkiicktfkmsEERRAIAIKDALNENSQLQtshkQLfQQEAEVWKGQVSELNKQKITFEDSKV 253
Cdd:COG1196 283 LEEAQAEEYELLAELARL----------EQDIARLEERRRELEERLE----EL-EEELAELEEELEELEEELEELEEELE 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 254 HAEQVLNDKENHIktltghlpmmKDQAAVLEEDTTDDDNLELEVNSQWENGANLddpLKGALKKLIHAAKLNVSLKSLEG 333
Cdd:COG1196 348 EAEEELEEAEAEL----------AEAEEALLEAEAELAEAEEELEELAEELLEA---LRAAAELAAQLEELEEAEEALLE 414
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 511772982 334 ERNHIIIQLSEVDKTKEELTEHIKNLQTQQASLQSENIYFESENQKLQQKLK 385
Cdd:COG1196 415 RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
135-425 |
2.24e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.13 E-value: 2.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 135 LNRSNseledEILCLEKDLKEEKSKHSQQDELMADISKSIQSLEDESKSLKS-------QIAEAKIICKTFKMSEERRAI 207
Cdd:TIGR02168 673 LERRR-----EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKeleelsrQISALRKDLARLEAEVEQLEE 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 208 AIKDALNENSQLQTSHKQL---------------------------FQQEAEVWKGQVSELNKQKITFEDSKVHAEQVLN 260
Cdd:TIGR02168 748 RIAQLSKELTELEAEIEELeerleeaeeelaeaeaeieeleaqieqLKEELKALREALDELRAELTLLNEEAANLRERLE 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 261 DKENHIKTLTGHLPMMKDQAAVLEEDTTdddNLELEVNSQWENGANLDDPLKGALKKLihaAKLNVSLKSLEGERNHIII 340
Cdd:TIGR02168 828 SLERRIAATERRLEDLEEQIEELSEDIE---SLAAEIEELEELIEELESELEALLNER---ASLEEALALLRSELEELSE 901
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 341 QLSEVDKTKEELTEHIKNLQTQQASLQSENIYFESENQKLQQKLkimTEFYQ---ENEMKLYRKLTveeNYRIEEEEKLS 417
Cdd:TIGR02168 902 ELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL---SEEYSltlEEAEALENKIE---DDEEEARRRLK 975
|
....*...
gi 511772982 418 RVEEKISR 425
Cdd:TIGR02168 976 RLENKIKE 983
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
95-461 |
4.63e-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: 47.09 E-value: 4.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 95 KFSLIQKEYEGYEVESSLEDASFEKAAAEEA-RSLEA---------TCEKLNRSNSE-----LEDEILCLEKDLKEEKSK 159
Cdd:pfam01576 235 RAQLAKKEEELQAALARLEEETAQKNNALKKiRELEAqiselqedlESERAARNKAEkqrrdLGEELEALKTELEDTLDT 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 160 HSQQDELMA----DISKSIQSLEDESKSLKSQIAEAKI--------------ICKTFKMSEERRAIAIKdalNENSQLQT 221
Cdd:pfam01576 315 TAAQQELRSkreqEVTELKKALEEETRSHEAQLQEMRQkhtqaleelteqleQAKRNKANLEKAKQALE---SENAELQA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 222 SHKQLFQQEAEV------WKGQVSELNKQKITFEDSKVHAEQVLNDKENHIKTLTGHLPMMKDQAAVLEEDTTdddnlel 295
Cdd:pfam01576 392 ELRTLQQAKQDSehkrkkLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVS------- 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 296 EVNSQWENGANLddpLKGALKklihaAKLNVS--LKSLEGERNHIIIQLSEVDKTKEELTEHIKNLQTQQASLQseniyf 373
Cdd:pfam01576 465 SLESQLQDTQEL---LQEETR-----QKLNLStrLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMK------ 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 374 esenQKLQQKLKIMtEFYQENEMKLYRKLtveenyrieeEEKLSRVEEKISrATEGLE-TYRKLAKDLEEELERTVHfyQ 452
Cdd:pfam01576 531 ----KKLEEDAGTL-EALEEGKKRLQREL----------EALTQQLEEKAA-AYDKLEkTKNRLQQELDDLLVDLDH--Q 592
|
410
....*....|
gi 511772982 453 KQVIS-YEKR 461
Cdd:pfam01576 593 RQLVSnLEKK 602
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
120-369 |
1.62e-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: 44.75 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 120 AAAEEARSLEATCEKLNRSNSELEDEILCLEKDLKEEKSKHSQQDELMADISKSIQSLEDESKSLKSQIAEAKiicktfk 199
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 200 msEERRAIaikdalneNSQLQTSHKQLFQQEAEVWK-GQVSELNkqkitfedSKVHAEQVlNDKENHIKTLTGHLPMMKD 278
Cdd:COG4942 90 --KEIAEL--------RAELEAQKEELAELLRALYRlGRQPPLA--------LLLSPEDF-LDAVRRLQYLKYLAPARRE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 279 QAAVLEEDTTDDDNLELEVNSQwenganlddplKGALKKLIhaAKLNVSLKSLEGERNHIIIQLSEVDKTKEELTEHIKN 358
Cdd:COG4942 151 QAEELRADLAELAALRAELEAE-----------RAELEALL--AELEEERAALEALKAERQKLLARLEKELAELAAELAE 217
|
250
....*....|.
gi 511772982 359 LQTQQASLQSE 369
Cdd:COG4942 218 LQQEAEELEAL 228
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
135-453 |
3.25e-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: 44.66 E-value: 3.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 135 LNRSNSELEDE----ILCLEKDlkEEKSKHSQQ-DELMADISKSiQSLEDESKSLKSQIAEAKIICKTFK-----MSEER 204
Cdd:TIGR01612 1454 LLFKNIEMADNksqhILKIKKD--NATNDHDFNiNELKEHIDKS-KGCKDEADKNAKAIEKNKELFEQYKkdvteLLNKY 1530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 205 RAIAIKDALNEN--------SQLQTSHKQlFQQEAEVWKGQVSELNKQKITFEDskvhaEQVLNDKENH--------IKT 268
Cdd:TIGR01612 1531 SALAIKNKFAKTkkdseiiiKEIKDAHKK-FILEAEKSEQKIKEIKKEKFRIED-----DAAKNDKSNKaaidiqlsLEN 1604
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 269 LTGHLPMMKDQAAVLEEDTTDDDNLE-----LEVNSQ----WENGANLD------DPLKGAlKKLIHAAK-----LNVSL 328
Cdd:TIGR01612 1605 FENKFLKISDIKKKINDCLKETESIEkkissFSIDSQdtelKENGDNLNslqeflESLKDQ-KKNIEDKKkeldeLDSEI 1683
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 329 KSLEGERNH--------IIIQLSEVDKTKEELTEHIKNL-----QTQQASLQSENIYFESENQKLQQKLKIMTEFYQENe 395
Cdd:TIGR01612 1684 EKIEIDVDQhkknyeigIIEKIKEIAIANKEEIESIKELieptiENLISSFNTNDLEGIDPNEKLEEYNTEIGDIYEEF- 1762
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 511772982 396 MKLYRKL-----TVEENYRIEEEEKLSRV--EEKISRATEGLETYRKLAKDLE-EELERTV-HFYQK 453
Cdd:TIGR01612 1763 IELYNIIagcleTVSKEPITYDEIKNTRInaQNEFLKIIEIEKKSKSYLDDIEaKEFDRIInHFKKK 1829
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
85-232 |
3.39e-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: 3.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 85 LIEEKCKLLEKFSLIQKEYEGYEVESSLEDASFEKAAAEEARSLEATCEKLN--------------RSNSELEDEILCLE 150
Cdd:pfam08614 5 LIDAYNRLLDRTALLEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEqllaqlreelaelyRSRGELAQRLVDLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 151 KDLKEEKSKHSQQDELMADISKSIQSLEDESKSLKSQIAEakiicktfkmseerraiaiKDALNENSQ--LQTSHKQLFQ 228
Cdd:pfam08614 85 EELQELEKKLREDERRLAALEAERAQLEEKLKDREEELRE-------------------KRKLNQDLQdeLVALQLQLNM 145
|
....
gi 511772982 229 QEAE 232
Cdd:pfam08614 146 AEEK 149
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
92-367 |
4.03e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.16 E-value: 4.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 92 LLEKFSLIQKEYEGYEVESSLEDASFEKAAAEeARSLEATCEKLNRSNSELEDEI-------LCLEKDLKEEKSKHSQQD 164
Cdd:COG1196 230 LLLKLRELEAELEELEAELEELEAELEELEAE-LAELEAELEELRLELEELELELeeaqaeeYELLAELARLEQDIARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 165 ELMADISKSIQSLEDESKSLKSQIAEAKIICKTFKMSEERRAIAIKDALNENSQLQTSHKQLFQQEAEvWKGQVSELNKQ 244
Cdd:COG1196 309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE-AEEELEELAEE 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 245 KITFEDSKVHAEQVLNDKENHIKTLTGHLPMMKDQAAVLEEDTTDDDNLELEVNSQwenganLDDPLKGALKKLIHAAKL 324
Cdd:COG1196 388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA------LEEAAEEEAELEEEEEAL 461
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 511772982 325 NVSLKSLEGERNHIIIQLSEVDKTKEELTEHIKNLQTQQASLQ 367
Cdd:COG1196 462 LELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
107-509 |
7.81e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 43.14 E-value: 7.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 107 EVESSLEDASFEKAAA-----EEARSLEATCEKLNRSNSELEdEILCLEKDLKEEKSKHSQQDELMADISKSIQSLEDES 181
Cdd:COG5022 961 EVESKLKETSEEYEDLlkkstILVREGNKANSELKNFKKELA-ELSKQYGALQESTKQLKELPVEVAELQSASKIISSES 1039
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 182 KSLKSQIAEAKIICKTFKMSEERRAiAIKDALNENSQLQTSHKQLFQQEA--------EVWKGQVSELNKQKITFEDSKV 253
Cdd:COG5022 1040 TELSILKPLQKLKGLLLLENNQLQA-RYKALKLRRENSLLDDKQLYQLEStenllktiNVKDLEVTNRNLVKPANVLQFI 1118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 254 HAEQVLNDKENHI----KTLTGHLPMMKDQAAVLEED---TTDDDNLELEVNSQWENGANLDDPLKGALKKLIHAAKLNV 326
Cdd:COG5022 1119 VAQMIKLNLLQEIskflSQLVNTLEPVFQKLSVLQLEldgLFWEANLEALPSPPPFAALSEKRLYQSALYDEKSKLSSSE 1198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 327 sLKSLEGErnhiIIQLSEVDKTKEELTEHIKNLQtqqaslqSENIYFESENQKLQQKLKIMTEFYQENEMKLYRKLTVEE 406
Cdd:COG5022 1199 -VNDLKNE----LIALFSKIFSGWPRGDKLKKLI-------SEGWVPTEYSTSLKGFNNLNKKFDTPASMSNEKLLSLLN 1266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 407 NYRIEEEEKlSRVEEKISRATEGLETYRKLAkdLEEELERTVHFYQ-KQVISYEKRGH--DNWLaaRTAERNLSDLrken 483
Cdd:COG5022 1267 SIDNLLSSY-KLEEEVLPATINSLLQYINVG--LFNALRTKASSLRwKSATEVNYNSEelDDWC--REFEISDVDE---- 1337
|
410 420
....*....|....*....|....*.
gi 511772982 484 ahNKQKLTETELKFELLEKDPNALDV 509
Cdd:COG5022 1338 --ELEELIQAVKVLQLLKDDLNKLDE 1361
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
76-460 |
9.19e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 9.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 76 QKLGATLSGLIEEKCKLLEKFSLIQKEYEgyEVESSLEdasfekaAAEEARSLEATCEKLNRSNSELEDEILclEKDLKE 155
Cdd:PRK03918 327 EERIKELEEKEERLEELKKKLKELEKRLE--ELEERHE-------LYEEAKAKKEELERLKKRLTGLTPEKL--EKELEE 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 156 -EKSKHSQQDELmADISKSIQSLEDESKSLKSQIAE---AKIICKTFK--MSEERRAIAIKDALNENSQLQTSHKQLFQQ 229
Cdd:PRK03918 396 lEKAKEEIEEEI-SKITARIGELKKEIKELKKAIEElkkAKGKCPVCGreLTEEHRKELLEEYTAELKRIEKELKEIEEK 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 230 EAEVWKGQV---SELNKQKITFEDSKVhAEQVLNDKENhiktLTGHlpmmkdQAAVLEEDTTDDDNLELEVNSQWENGAN 306
Cdd:PRK03918 475 ERKLRKELReleKVLKKESELIKLKEL-AEQLKELEEK----LKKY------NLEELEKKAEEYEKLKEKLIKLKGEIKS 543
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 307 LDDPLK--GALKKliHAAKLNVSLKSLEGERNHIIIQLSEVD-KTKEELTEHIKNLQ----------TQQASLQSENIYF 373
Cdd:PRK03918 544 LKKELEklEELKK--KLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEpfyneylelkDAEKELEREEKEL 621
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 374 ESENQKLQQKLKIMTEFYQENEMKLYRKLTVEENYRIEEEEKLSRVEEKISRATEGLETYRKLAKDLEEELERTVHFYQK 453
Cdd:PRK03918 622 KKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKE 701
|
....*..
gi 511772982 454 QVISYEK 460
Cdd:PRK03918 702 ELEEREK 708
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
175-517 |
1.02e-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: 42.70 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 175 QSLEDESKSLKSQI----AEAKIICKTFKMSEERraiaIKDALNENSQLQTSHKQLFQQEAEVwKGQVSELNKQKITF-E 249
Cdd:TIGR04523 36 KQLEKKLKTIKNELknkeKELKNLDKNLNKDEEK----INNSNNKIKILEQQIKDLNDKLKKN-KDKINKLNSDLSKInS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 250 DSKVHAEQVlNDKENHIKTLTGHLPMM-KDQAAVLEEDTTDDDNLElEVNSQWENGANLDDPLKGALKKLIH-AAKLNVS 327
Cdd:TIGR04523 111 EIKNDKEQK-NKLEVELNKLEKQKKENkKNIDKFLTEIKKKEKELE-KLNNKYNDLKKQKEELENELNLLEKeKLNIQKN 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 328 LKSLEGERNHIIIQLSEVDKTKE---ELTEHIKNLQTQQASLQSEniyFESENQKLQQKLKIMtefyQENEMKLyrkltv 404
Cdd:TIGR04523 189 IDKIKNKLLKLELLLSNLKKKIQknkSLESQISELKKQNNQLKDN---IEKKQQEINEKTTEI----SNTQTQL------ 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 405 eenyrIEEEEKLSRVEEKISRATEGLETYRKLAKDLEEELERtvhfYQKQVISYEKRGHDNWLAA-----RTAERNLSDL 479
Cdd:TIGR04523 256 -----NQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQ----LKSEISDLNNQKEQDWNKElkselKNQEKKLEEI 326
|
330 340 350
....*....|....*....|....*....|....*...
gi 511772982 480 RKENAHNKQKLTETELKFELLEKDPNALDVSNTAFGRE 517
Cdd:TIGR04523 327 QNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRE 364
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
100-496 |
1.09e-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: 42.73 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 100 QKEYEGYEVESSLEdaSFEKAAAEEARSLEATCEKLNRSNSEL-------EDEILCLEKDLKEEKSKHSQQDELMADISK 172
Cdd:TIGR00606 688 QTEAELQEFISDLQ--SKLRLAPDKLKSTESELKKKEKRRDEMlglapgrQSIIDLKEKEIPELRNKLQKVNRDIQRLKN 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 173 SIQSLEDESKSLKSQIAEAKI------ICKTFKMS--EERRAIAIKDALNENSQLQTSHKQL---FQQEAEVWKGQVSEL 241
Cdd:TIGR00606 766 DIEEQETLLGTIMPEEESAKVcltdvtIMERFQMElkDVERKIAQQAAKLQGSDLDRTVQQVnqeKQEKQHELDTVVSKI 845
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 242 NKQKITFEDSKvHAEQVLNDKENHIKTLTGHLPMMKDQAAVLEEDTTDDDNLELEVNSQWENGANLDDPLKGALKKLIHA 321
Cdd:TIGR00606 846 ELNRKLIQDQQ-EQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQE 924
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 322 AKLNVSLKSLEGERNHIiiqlsEVDKTKEELTEHIKNLQTQQASLQSeniyfESENQKLQQKLKIMTEFYQENEMKLYRK 401
Cdd:TIGR00606 925 KEELISSKETSNKKAQD-----KVNDIKEKVKNIHGYMKDIENKIQD-----GKDDYLKQKETELNTVNAQLEECEKHQE 994
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 402 LTVEENYRIEEEEKLSRVEEKISRATEGLETYRKLAKDLEEELERTVHFYQKQVISYEKRGHDNwlaartAERNLSDLRK 481
Cdd:TIGR00606 995 KINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQK------LEENIDLIKR 1068
|
410
....*....|....*..
gi 511772982 482 EN--AHNKQKLTETELK 496
Cdd:TIGR00606 1069 NHvlALGRQKGYEKEIK 1085
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
516-775 |
1.10e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 42.62 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 516 REHSPCSPSPLGRPSSETRAFPSPQTLLEDPLRLSPVLPGGGGRGPSSPGNPLDHqitnergepsydrlIDPHRAPSDTG 595
Cdd:PHA03247 2682 RPRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALP--------------AAPAPPAVPAG 2747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 596 SlSSPVEQDRRMMfpPPGQSYPDSTLPPQreDRFYSNSERLSGPAeprsfkMTSLDKMDRSMPSEMESSRNDAKDDLGNL 675
Cdd:PHA03247 2748 P-ATPGGPARPAR--PPTTAGPPAPAPPA--APAAGPPRRLTRPA------VASLSESRESLPSPWDPADPPAAVLAPAA 2816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 676 NVPDSSLPAENEATGPGFIPPPLAPVRGPLFP-------VDTRGPFMRRGPPFPPPPPGTMFGASRGYFPPRDFPGPPHA 748
Cdd:PHA03247 2817 ALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPslplggsVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTE 2896
|
250 260
....*....|....*....|....*..
gi 511772982 749 PFAMRNIYPPRGLPPYLHPRPGFYPNP 775
Cdd:PHA03247 2897 SFALPPDQPERPPQPQAPPPPQPQPQP 2923
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
119-503 |
1.43e-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: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 119 KAAAEEARSLEATCEKLNRSNSELEDEILCLEKDL--KEEKSKH-----SQQDELMADIS--------------KSIQSL 177
Cdd:pfam01576 134 KKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLaeEEEKAKSlsklkNKHEAMISDLEerlkkeekgrqeleKAKRKL 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 178 EDESKSLKSQIAEAKIICKTFKMSEERRAIAIKDALN--ENSQLQTSHKQLFQQEAEvwkGQVSELNKQKITFEDSKVHA 255
Cdd:pfam01576 214 EGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALArlEEETAQKNNALKKIRELE---AQISELQEDLESERAARNKA 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 256 EQVLNDKENHIKTLTGHLpmmkdqaavleEDTTDDDNLELEVNSQWEnganlddplkgalkklihaAKLNVSLKSLEGER 335
Cdd:pfam01576 291 EKQRRDLGEELEALKTEL-----------EDTLDTTAAQQELRSKRE-------------------QEVTELKKALEEET 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 336 NHIIIQLSEVDK----TKEELTEHIKNLQTQQASLQSENIYFESENQKLQQKLKIMTEFYQENEMK----------LYRK 401
Cdd:pfam01576 341 RSHEAQLQEMRQkhtqALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKrkklegqlqeLQAR 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 402 LTVEENYRIEEEEKLSRVEEKISRATEGLETYR----KLAKD---LEEELERTVHFYQ---KQVISY---------EKRG 462
Cdd:pfam01576 421 LSESERQRAELAEKLSKLQSELESVSSLLNEAEgkniKLSKDvssLESQLQDTQELLQeetRQKLNLstrlrqledERNS 500
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 511772982 463 HDNWL-----AARTAERNLSDLRKENAHNKQKLTETELKFELLEKD 503
Cdd:pfam01576 501 LQEQLeeeeeAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEG 546
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
65-507 |
1.52e-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: 42.03 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 65 SVRSRLYVGREQKLGAT------LSGLIEEKCKLLEKFSLIQKEYEGY--EVESSLEDASFEKAAAEEARsleatcEKLN 136
Cdd:pfam15921 296 SIQSQLEIIQEQARNQNsmymrqLSDLESTVSQLRSELREAKRMYEDKieELEKQLVLANSELTEARTER------DQFS 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 137 RSNSELEDEILCLEKDL-KEEK--SKHSQQDELMADI----SKSIQSLEDESKSLKSQIAEAKIICKTFKmSE-----ER 204
Cdd:pfam15921 370 QESGNLDDQLQKLLADLhKREKelSLEKEQNKRLWDRdtgnSITIDHLRRELDDRNMEVQRLEALLKAMK-SEcqgqmER 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 205 RAIAIKDAlNENSQLQTSHKQLFQQEAEVWKGQVSELNKQKITFEDSkvhaeqvlndkENHIKTLTGHLpmmKDQAAVLE 284
Cdd:pfam15921 449 QMAAIQGK-NESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESS-----------ERTVSDLTASL---QEKERAIE 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 285 EDTTDDDNLELEVNsqwenganlddpLKgaLKKLIHAAKLNVSLKSLEGERNHIIIQLSEVDKTKEELTEHIKNLQT--- 361
Cdd:pfam15921 514 ATNAEITKLRSRVD------------LK--LQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQlvg 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 362 ----QQASLQSENIYFESE--NQKLQ-QKLKIMTEfyqENEMKLyRKLtveenyrieeEEKLSRVE-EKISRATEGLETY 433
Cdd:pfam15921 580 qhgrTAGAMQVEKAQLEKEinDRRLElQEFKILKD---KKDAKI-REL----------EARVSDLElEKVKLVNAGSERL 645
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 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 ... |
77-369 |
1.82e-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: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 77 KLGATLSGLIEEKCKLLEKfsLIQKEYEGYEVESSLED-----ASFEKAAAEEARSLEATCEKLNRSNSELEDEILCLEK 151
Cdd:pfam01576 486 NLSTRLRQLEDERNSLQEQ--LEEEEEAKRNVERQLSTlqaqlSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEE 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 152 DL----KEEKSKHSQQ---DELMADISKSIQ---SLEDESKSLKSQIAEAKIIckTFKMSEER------------RAIAI 209
Cdd:pfam01576 564 KAaaydKLEKTKNRLQqelDDLLVDLDHQRQlvsNLEKKQKKFDQMLAEEKAI--SARYAEERdraeaeareketRALSL 641
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 210 KDALNE-----------NSQLQTSHKQLFQQEAEVWKgQVSELnkqkitfEDSKVHAEQVLNDkenhiktltghlpmMKD 278
Cdd:pfam01576 642 ARALEEaleakeelertNKQLRAEMEDLVSSKDDVGK-NVHEL-------ERSKRALEQQVEE--------------MKT 699
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 279 QAAVLEED--TTDDDNLELEVN-----SQWENGANLDDPL----KGALKKLIHA------------AKLNVSLKSLEGER 335
Cdd:pfam01576 700 QLEELEDElqATEDAKLRLEVNmqalkAQFERDLQARDEQgeekRRQLVKQVREleaelederkqrAQAVAAKKKLELDL 779
|
330 340 350
....*....|....*....|....*....|....
gi 511772982 336 NHIIIQLSEVDKTKEELTEHIKNLQTQQASLQSE 369
Cdd:pfam01576 780 KELEAQIDAANKGREEAVKQLKKLQAQMKDLQRE 813
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
86-443 |
1.85e-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: 41.63 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 86 IEEKCKLLEKfSLIQKEYEGYEVESSLED--ASFEKAAAEEaRSLEATCEKLNRSNSELEDEILCLEKDLKEEKSKHS-- 161
Cdd:pfam05483 273 LEEKTKLQDE-NLKELIEKKDHLTKELEDikMSLQRSMSTQ-KALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSfv 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 162 ---------QQDELMADISKSIQSLEDESK----SLKSQIAEAKIICKtFKMSEERRAIAIKDALNENSQLQTSHKQlFQ 228
Cdd:pfam05483 351 vtefeattcSLEELLRTEQQRLEKNEDQLKiitmELQKKSSELEEMTK-FKNNKEVELEELKKILAEDEKLLDEKKQ-FE 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 229 QEAEVWKGQVSEL----NKQKITFEDSKVHAEQVLNDKENHIKTLtghlpmmKDQAAVLEEDTTDddNLELEVNSqweng 304
Cdd:pfam05483 429 KIAEELKGKEQELifllQAREKEIHDLEIQLTAIKTSEEHYLKEV-------EDLKTELEKEKLK--NIELTAHC----- 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 305 anldDPLKGALKKLIH-AAKLNVSLKSLEGERNHiiiqlseVDKTKEELTEHIKNLQTQQASLQSENIYFESENQKLQQK 383
Cdd:pfam05483 495 ----DKLLLENKELTQeASDMTLELKKHQEDIIN-------CKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDE 563
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 384 LKIMTEFYQENEMKLYRKLTVEENYRIEEEEKLSRVEEKISRATEGLETYRKLAKDLEEE 443
Cdd:pfam05483 564 VKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKK 623
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
321-503 |
2.13e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.46 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 321 AAKLNVSLKSLEGERNHIIIQLSEVDKTKEELTEHIKNLQTQQASLQSENIYFESENQKLQQKLKIMTE---FYQENEMK 397
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEErrrELEERLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 398 LYRKLTVEENYRIEEEEKLSRVEEKISRATEGLETYRKLAKDLEEELERTvhfyQKQVISYEKRGHDNWLAARTAERNLS 477
Cdd:COG1196 321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA----EAELAEAEEELEELAEELLEALRAAA 396
|
170 180
....*....|....*....|....*.
gi 511772982 478 DLRKENAHNKQKLTETELKFELLEKD 503
Cdd:COG1196 397 ELAAQLEELEEAEEALLERLERLEEE 422
|
|
| LCD1 |
pfam09798 |
DNA damage checkpoint protein; This is a family of proteins which regulate checkpoint kinases. ... |
134-251 |
2.21e-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: 41.53 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 134 KLNRSNSELEDEILCLEKDLKEEKSKHSQQdelMADISKSIQSLEDESKslksqiaeakiicktFKMSEERRAIAIKDAL 213
Cdd:pfam09798 5 KLELLQQEKEKELEKLKNSYEELKSSHEEE---LEKLKQEVQKLEDEKK---------------FLLNELRSLSATSPAS 66
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 511772982 214 NENSQLQTSHKQLF--------QQEAEVWKGQVSELNKQKITFEDS 251
Cdd:pfam09798 67 SQSHETDTDDSSSVslkkrkieESTAESLKQKYIRLQNNRIVDETS 112
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
87-507 |
2.34e-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: 41.70 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 87 EEKCKLLEKfslIQKEYEGyeVESSLEDASfeKAAAEEARSLEATCEKLNRSNSELEDEILCLEKDLKEEKSKHSQQDEl 166
Cdd:pfam01576 172 EEKAKSLSK---LKNKHEA--MISDLEERL--KKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEE- 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 167 maDISKSIQSLEDES----------KSLKSQIAEAKIICKTFKMSEERRAIAIKDALNENSQLQTSHKQLF-----QQEA 231
Cdd:pfam01576 244 --ELQAALARLEEETaqknnalkkiRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLdttaaQQEL 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 232 EVWKGQ-VSELnkQKITFEDSKVHAEQVLNDKENH---IKTLTGHLPMMKDQAAVLEED--TTDDDNLELEVNSQWENGA 305
Cdd:pfam01576 322 RSKREQeVTEL--KKALEEETRSHEAQLQEMRQKHtqaLEELTEQLEQAKRNKANLEKAkqALESENAELQAELRTLQQA 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 306 NLDDPLKGalkklihaaklnvslKSLEGERNHIIIQLSEVDKTKEELTEHIKNLQTQQASL-------QSENIYFESENQ 378
Cdd:pfam01576 400 KQDSEHKR---------------KKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVssllneaEGKNIKLSKDVS 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 379 KLQQKLKIMTEFYQENEMKlyrKLTVEEnyrieeeeKLSRVEEKISRATEGLEtyrklakdlEEE-----LERTVHFYQK 453
Cdd:pfam01576 465 SLESQLQDTQELLQEETRQ---KLNLST--------RLRQLEDERNSLQEQLE---------EEEeakrnVERQLSTLQA 524
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 511772982 454 QVISYEKRGHDNWLAARTAERNLSDLRKENAHNKQKLTETELKFELLEKDPNAL 507
Cdd:pfam01576 525 QLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRL 578
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
321-509 |
2.70e-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: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 321 AAKLNVSLKSLEGERNHIIIQLSEVDKTKEELTEHIKNLQTQQASLQSENIYFESENQKLQQKLkimtEFYQENEMKLYR 400
Cdd:TIGR02168 693 IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL----TELEAEIEELEE 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 401 KLTVEENYRIEEEEKLSRVEEKISRATEGLETYRKLAKDLEEELERTVHFYQKQ---VISYEKRGHDNWLAARTAERNLS 477
Cdd:TIGR02168 769 RLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLrerLESLERRIAATERRLEDLEEQIE 848
|
170 180 190
....*....|....*....|....*....|..
gi 511772982 478 DLRKENAHNKQKLTETELKFELLEKDPNALDV 509
Cdd:TIGR02168 849 ELSEDIESLAAEIEELEELIEELESELEALLN 880
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
98-379 |
3.23e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 3.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 98 LIQKEYEGYEVESSLEDASFEKAAAEEA-RSLEATCEKLNRSNSELEDEILCLEKDLKEEKSKHSQQDELMADISKSIQS 176
Cdd:COG4372 75 LEQLEEELEELNEQLQAAQAELAQAQEElESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKE 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 177 LEDESKSLKSQIAEAKIICKTFKMSEERRAI-AIKDALNENSQLQTSHKQLFQQEAEVWKGQVSELNKQKITFEDSKVHA 255
Cdd:COG4372 155 LEEQLESLQEELAALEQELQALSEAEAEQALdELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLA 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 256 EQVLNDKENHIKTLTGHLPMMKDQAAVLEEDTTDDD-----NLELEVNSQWENGANLDDPLKGALKKLIHAAKLNVSLKS 330
Cdd:COG4372 235 LSALLDALELEEDKEELLEEVILKEIEELELAILVEkdteeEELEIAALELEALEEAALELKLLALLLNLAALSLIGALE 314
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 511772982 331 LEGERNHIIIQLSEVDKTKEELTEHIKNLQTQQASLQSENIYFESENQK 379
Cdd:COG4372 315 DALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGA 363
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
118-510 |
3.62e-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: 41.11 E-value: 3.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 118 EKAAAEEARSLEATCEKLNRSNSELEDEILCLEKdlKEEKSKHSQQDELMADISKSI----QSLEDESKSLKSQIAE-AK 192
Cdd:TIGR00618 248 KREAQEEQLKKQQLLKQLRARIEELRAQEAVLEE--TQERINRARKAAPLAAHIKAVtqieQQAQRIHTELQSKMRSrAK 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 193 IICKTFKMSEERRAIAIKDALnensqLQTSHKQ--LFQQEAEVWKGQVSELNKQKitfedskvhaeqvlnDKENHIKTLT 270
Cdd:TIGR00618 326 LLMKRAAHVKQQSSIEEQRRL-----LQTLHSQeiHIRDAHEVATSIREISCQQH---------------TLTQHIHTLQ 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 271 GHLPMMKDQAAVLEEDTTDDDNLELEVNSQWENganlDDPLKGalkKLIHA-AKLNVSLKSLEGERNHIIIQLSEVDKTK 349
Cdd:TIGR00618 386 QQKTTLTQKLQSLCKELDILQREQATIDTRTSA----FRDLQG---QLAHAkKQQELQQRYAELCAAAITCTAQCEKLEK 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 350 EELTEHIKNLQTQQASLQSENIYFESENQKLQQKLKIMTEfYQENEMKL---YRKLTVEENYRIEEEEKLSRVEEKISRA 426
Cdd:TIGR00618 459 IHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLE-LQEEPCPLcgsCIHPNPARQDIDNPGPLTRRMQRGEQTY 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 427 TEG----------LETYRKLAKDLEEELERTVHFYQKQVISYEKRGHDNWLAARTAERNLSDLRKENAHNKQKLTETELK 496
Cdd:TIGR00618 538 AQLetseedvyhqLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHAL 617
|
410
....*....|....
gi 511772982 497 FELLEKDPNALDVS 510
Cdd:TIGR00618 618 LRKLQPEQDLQDVR 631
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
64-192 |
5.53e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.28 E-value: 5.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 64 RSVRSRLYVG---REQK--LGATLSGLIEEKCKLLEKFSLIQKEYEGYE----VESSLEDASFE----KAAAEEARSLEA 130
Cdd:COG4913 596 RRIRSRYVLGfdnRAKLaaLEAELAELEEELAEAEERLEALEAELDALQerreALQRLAEYSWDeidvASAEREIAELEA 675
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 511772982 131 TCEKLNRSNSELEDeilcLEKDLKEEKSKHSQQDELMADISKSIQSLEDESKSLKSQIAEAK 192
Cdd:COG4913 676 ELERLDASSDDLAA----LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQ 733
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
133-360 |
5.93e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.00 E-value: 5.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 133 EKLNRSN-SELEDEIlclEKDLKEEKSKHSQQDELMADISKSIQSLEDESKSLKsqiaeaKIICKTFKMSeerraiaikd 211
Cdd:PHA02562 208 RKKNGENiARKQNKY---DELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALN------KLNTAAAKIK---------- 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 212 alnenSQLQTshkqlFQQEAEVW-KGQVSELNKQKITFEDSKvhaeqvLNDKENHIKTLTGHLPMMK---DQAAVLEEDT 287
Cdd:PHA02562 269 -----SKIEQ-----FQKVIKMYeKGGVCPTCTQQISEGPDR------ITKIKDKLKELQHSLEKLDtaiDELEEIMDEF 332
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 511772982 288 TDDDNLELEVNSQWENganlddpLKGALKKLIHAAK-LNVSLKSLEGERnhiIIQLSEVDKTKEELTEHIKNLQ 360
Cdd:PHA02562 333 NEQSKKLLELKNKIST-------NKQSLITLVDKAKkVKAAIEELQAEF---VDNAEELAKLQDELDKIVKTKS 396
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
91-279 |
7.49e-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: 7.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 91 KLLEKFSLIQKEYEGYEVESSLEDASFEKAAAEEarsleatcEKLNRSNSELEDEILCLEKDLKEEKSKhsqqdelMADI 170
Cdd:TIGR02168 334 ELAEELAELEEKLEELKEELESLEAELEELEAEL--------EELESRLEELEEQLETLRSKVAQLELQ-------IASL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 171 SKSIQSLEDESKSLKSQIAeakiicktfKMSEERRAIAIKDALNENSQLQTSHKQLFQQEAEVwKGQVSELNKQKITFED 250
Cdd:TIGR02168 399 NNEIERLEARLERLEDRRE---------RLQQEIEELLKKLEEAELKELQAELEELEEELEEL-QEELERLEEALEELRE 468
|
170 180
....*....|....*....|....*....
gi 511772982 251 SKVHAEQVLNDKENHIKTLTGHLPMMKDQ 279
Cdd:TIGR02168 469 ELEEAEQALDAAERELAQLQARLDSLERL 497
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
140-261 |
8.04e-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: 39.23 E-value: 8.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 140 SELEDEILCLEKDLKEEKSKHSQQDELMADISKSIQSLEDESKSLKsQIAEAKIICKTfkmSEERRAI-AIKDALNENSQ 218
Cdd:smart00787 147 EGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLK-QLEDELEDCDP---TELDRAKeKLKKLLQEIMI 222
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 511772982 219 LQTSHKQLFQQEAEVwKGQVSELNKQKITFEDSKVHAEQVLND 261
Cdd:smart00787 223 KVKKLEELEEELQEL-ESKIEDLTNKKSELNTEIAEAEKKLEQ 264
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
106-519 |
8.09e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 39.81 E-value: 8.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 106 YEVESSLEDASFEKAAAEEARSLEATCEKLNRSNSELEDEILCLEKDLKEEKSkhsqqdeLMADISKSIQSLEDESKSLK 185
Cdd:PTZ00440 512 EKNNIVNNNFKNIEDYYITIEGLKNEIEGLIELIKYYLQSIETLIKDEKLKRS-------MKNDIKNKIKYIEENVDHIK 584
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 186 SQIAEAKIICKTFKMSEE---RRAIAIKDALNENSQLQTSHKQLFQqeaEVWKGQVSELNKQKITFEDSKVHAEQVLNDK 262
Cdd:PTZ00440 585 DIISLNDEIDNIIQQIEElinEALFNKEKFINEKNDLQEKVKYILN---KFYKGDLQELLDELSHFLDDHKYLYHEAKSK 661
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 263 ENhIKTLtghLPMMKDQAAVLEEDTTDDDN-------------LELEVNSQWENGANLD-DPLKGALKKLIHAAKLNVSL 328
Cdd:PTZ00440 662 ED-LQTL---LNTSKNEYEKLEFMKSDNIDniiknlkkelqnlLSLKENIIKKQLNNIEqDISNSLNQYTIKYNDLKSSI 737
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 329 KSLEGERNHIIIQLSEVDKTKEELTEHIKnlQTQQASLQSENIY--FESENQKLQQKLKIMTefyqeNEMKLyrkltvee 406
Cdd:PTZ00440 738 EEYKEEEEKLEVYKHQIINRKNEFILHLY--ENDKDLPDGKNTYeeFLQYKDTILNKENKIS-----NDINI-------- 802
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772982 407 nyrieeeeklsrVEEKISRATEGLETYRKLAKDLEEELERTvhfYQKQVISYEKRGHDNwlaartAERNLSDLRKENAHN 486
Cdd:PTZ00440 803 ------------LKENKKNNQDLLNSYNILIQKLEAHTEKN---DEELKQLLQKFPTED------ENLNLKELEKEFNEN 861
|
410 420 430
....*....|....*....|....*....|...
gi 511772982 487 KQKLTETELKFELLEKDPNALDVSNTAFGREHS 519
Cdd:PTZ00440 862 NQIVDNIIKDIENMNKNINIIKTLNIAINRSNS 894
|
|
| |
