|
Name |
Accession |
Description |
Interval |
E-value |
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
125-456 |
1.51e-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: 51.56 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559830 125 REKEDMYDEIIELKKSLHVQKSDVDLMRTKLRRLEEENSRKDRQIEQlldpsrGTDFVRTLaeKRPDASWV--------- 195
Cdd:TIGR04523 321 KKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEE------KQNEIEKL--KKENQSYKqeiknlesq 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559830 196 INGLKQRILKLEQQCKEKDGTISKLQ----------TDMKTT---------NLEEMRIAMETYYEEVHR--------LQT 248
Cdd:TIGR04523 393 INDLESKIQNQEKLNQQKDEQIKKLQqekellekeiERLKETiiknnseikDLTNQDSVKELIIKNLDNtresletqLKV 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559830 249 LLASSETTgKKPLGEKKTGAKRQKKMgsaLLSLSRSVQELTEENQSLKEDLDRVLSTSPTISKTqgyvewsKPRLLRRIV 328
Cdd:TIGR04523 473 LSRSINKI-KQNLEQKQKELKSKEKE---LKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESE-------KKEKESKIS 541
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559830 329 ELEKKLSVMESSKshaaepvrshppaclaSSSALHRQPRGdrnKDHErlrgaVRDLKEERTALQEQLLQRDLEVKQLLQA 408
Cdd:TIGR04523 542 DLEDELNKDDFEL----------------KKENLEKEIDE---KNKE-----IEELKQTQKSLKKKQEEKQELIDQKEKE 597
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 566559830 409 KADLEKELecaregeeerrereevlREEIQTLTSKLQELQEMKKEEKE 456
Cdd:TIGR04523 598 KKDLIKEI-----------------EEKEKKISSLEKELEKAKKENEK 628
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
125-456 |
1.97e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.14 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559830 125 REKEDMYDEIIELKKSLHVQKSDVDLMRTKLRRLEEENSRKDRqieqlldpsrgtdFVRTLAEKRPDASWVingLKQRIL 204
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAER-------------YQALLKEKREYEGYE---LLKEKE 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559830 205 KLEQQCKEKDGTISKLQTDmkttnLEEMRIAMETYYEEVHRLQTLLaSSETTGKKPLGEKKTgAKRQKKMGS-------- 276
Cdd:TIGR02169 234 ALERQKEAIERQLASLEEE-----LEKLTEEISELEKRLEEIEQLL-EELNKKIKDLGEEEQ-LRVKEKIGEleaeiasl 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559830 277 --ALLSLSRSVQELTEENQSLKEDLDRVLSTSPTISKTQGYVEWSKPRLLRRIVELEKKLSVMESSkshaaepvrshppa 354
Cdd:TIGR02169 307 erSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAE-------------- 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559830 355 cLASSSALHRQPRgDRNKDherLRGAVRDLKEERTALQEQLLQRDLEVKQLLQAKADLEKELECAREGEEERREREEVLR 434
Cdd:TIGR02169 373 -LEEVDKEFAETR-DELKD---YREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKA 447
|
330 340
....*....|....*....|..
gi 566559830 435 EEIQTLTSKLQELQEMKKEEKE 456
Cdd:TIGR02169 448 LEIKKQEWKLEQLAADLSKYEQ 469
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
133-458 |
5.40e-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: 46.59 E-value: 5.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559830 133 EIIELKKSLHVQKSDVDLMRTKLRRLEEENSRKDRQIEQLldpsrgtdfVRTLAEKRPDaswvINGLKQRILKLEQQCKE 212
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQL---------RKELEELSRQ----ISALRKDLARLEAEVEQ 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559830 213 KDGTISKLQTDmkttnLEEMRIAMETYYEEVHRLQTLLASSETtgkkplgEKKTGAKRQKKMGSALLSLSRSVQELTEEN 292
Cdd:TIGR02168 745 LEERIAQLSKE-----LTELEAEIEELEERLEEAEEELAEAEA-------EIEELEAQIEQLKEELKALREALDELRAEL 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559830 293 QSLKEDLDRVLSTsptisktqgyvewsKPRLLRRIVELEKKLSVMESSKshaaepvrshppaclasssalhrqprGDRNK 372
Cdd:TIGR02168 813 TLLNEEAANLRER--------------LESLERRIAATERRLEDLEEQI--------------------------EELSE 852
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559830 373 DHERLRGAVRDLKEERTALQEQLlqrdlevKQLLQAKADLEKELECAREGEEERREREEVLREEIQTLTSKLQELQEMKK 452
Cdd:TIGR02168 853 DIESLAAEIEELEELIEELESEL-------EALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLA 925
|
....*.
gi 566559830 453 EEKEDC 458
Cdd:TIGR02168 926 QLELRL 931
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
125-415 |
1.04e-04 |
|
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: 45.88 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559830 125 REKEDMY-DEIIELKKSLHVQKSDVDLMRTKLRRLEEENSRKDRQIEQLLDPSRGTDFVRTLAEKRPDASWVIN-GLKQR 202
Cdd:pfam15921 334 REAKRMYeDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDtGNSIT 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559830 203 ILKLEQQCKEKDGTISKLQTDMKTT------NLEEMRIAMETYYEEVHRLQTLLASSETTgkKPLGEKKTGAKRQKKMgs 276
Cdd:pfam15921 414 IDHLRRELDDRNMEVQRLEALLKAMksecqgQMERQMAAIQGKNESLEKVSSLTAQLEST--KEMLRKVVEELTAKKM-- 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559830 277 ALLSLSRSVQELTeenQSLKEDLDRVLSTSPTISKTQGYVEWSKPRL---------LRRIVELEKKLSVMESSKSHAAEP 347
Cdd:pfam15921 490 TLESSERTVSDLT---ASLQEKERAIEATNAEITKLRSRVDLKLQELqhlknegdhLRNVQTECEALKLQMAEKDKVIEI 566
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 566559830 348 VRSHppacLASSSALHRQprgdrnkdHERLRGAV--------RDLKEERTALQE-QLL--QRDLEVKQLLQAKADLEKE 415
Cdd:pfam15921 567 LRQQ----IENMTQLVGQ--------HGRTAGAMqvekaqleKEINDRRLELQEfKILkdKKDAKIRELEARVSDLELE 633
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
200-460 |
3.80e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.89 E-value: 3.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559830 200 KQRILKLEQQCKEKDGTISKLQTdmkttNLEEMRIAMETYYEEVHRLQTLLASSETTGKKPLGEKKTGAKRQKKMGSALL 279
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEK-----ALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIA 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559830 280 SLSRSVQELTEENQSLKEDLDRVLSTSPTISKTQGYVEWSKPRLLRRIVELEKKLSvmESSKSHAAepvrshppacLASS 359
Cdd:TIGR02168 751 QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALD--ELRAELTL----------LNEE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559830 360 SALHRQPRGDRNKDHERLRGAVRDLKEERTALQEQLLQRDLEVKQLLQAKADLEKELECAREGEEERREREEVLREEIQT 439
Cdd:TIGR02168 819 AANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEE 898
|
250 260
....*....|....*....|.
gi 566559830 440 LTSKLQELQEMKKEEKEDCPE 460
Cdd:TIGR02168 899 LSEELRELESKRSELRRELEE 919
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
123-455 |
4.96e-04 |
|
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: 43.42 E-value: 4.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559830 123 VYREKEDMYDEIIELKKSLHVQKSDVDLMRTKLRRLEEENSRKDRQIEQlldpSRGTDFVRTLAEKRPDASWVINGLKQR 202
Cdd:pfam02463 694 ILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLK----QKIDEEEEEEEKSRLKKEEKEEEKSEL 769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559830 203 ILKLEQQCKEKDGTISKLQTDMKTTNL------EEMRIAMETYYEEVHRLQTLLASSETTGKKPLGEKKTGAK--RQKKM 274
Cdd:pfam02463 770 SLKEKELAEEREKTEKLKVEEEKEEKLkaqeeeLRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELkeEQKLE 849
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559830 275 GSALLSLSRSVQELTEENQSLKEDLDRVLSTsptisktQGYVEWSKPRLLRRIVELEKKLSVMESSKSHAAEPVRShppa 354
Cdd:pfam02463 850 KLAEEELERLEEEITKEELLQELLLKEEELE-------EQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENE---- 918
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559830 355 cLASSSALHRQPRGDRNKDHERLRGAVRDLKEERTALQEQLLQRdleVKQLLQAKADLEKELECAREGEEERREREEVLR 434
Cdd:pfam02463 919 -IEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEER---NKRLLLAKEELGKVNLMAIEEFEEKEERYNKDE 994
|
330 340
....*....|....*....|....
gi 566559830 435 EEIQTLT---SKLQELQEMKKEEK 455
Cdd:pfam02463 995 LEKERLEeekKKLIRAIIEETCQR 1018
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
125-460 |
1.55e-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: 41.97 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559830 125 REKEDMYDEIIELKKSLhvqksdvDLMRTKLRRLEEENSRKDRQIEqlldpsrgtdfvrtlaekrpDASWVINGLKQRIL 204
Cdd:TIGR02168 684 EKIEELEEKIAELEKAL-------AELRKELEELEEELEQLRKELE--------------------ELSRQISALRKDLA 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559830 205 KLEQQCKEKDGTISKLQtdmktTNLEEMRIAMETYYEEVHRLQTLLASSETtgkkplgEKKTGAKRQKKMGSALLSLSRS 284
Cdd:TIGR02168 737 RLEAEVEQLEERIAQLS-----KELTELEAEIEELEERLEEAEEELAEAEA-------EIEELEAQIEQLKEELKALREA 804
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559830 285 VQELTEENQSLKEDLDRVLSTSPTISKTQGYVEWSKPRLLRRIVELEKKLSVMESSKSHAAEPVRSHppaclasssalhr 364
Cdd:TIGR02168 805 LDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEL------------- 871
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559830 365 qprgdrNKDHERLRGAVRDLKEERTALQEQLLQRDLEVKQLLQAKADLEKELECAREGEEERREREEVLREEIQTLTSKL 444
Cdd:TIGR02168 872 ------ESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
|
330
....*....|....*.
gi 566559830 445 QELQEMKKEEKEDCPE 460
Cdd:TIGR02168 946 SEEYSLTLEEAEALEN 961
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
132-412 |
2.17e-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: 41.58 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559830 132 DEIIELKKSLHVQKSDVDLMRTKLRRLEEENSRKDRQIEQLL-DPSRGTDFVRTLAEKRPDASWVINGLKQRILKLEQQC 210
Cdd:TIGR02168 274 LEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLErQLEELEAQLEELESKLDELAEELAELEEKLEELKEEL 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559830 211 KEKDGTISKLQTDmkttnLEEMRIAMETYYEEVHRLQTLLASsettgkkPLGEKKTGAKRQKKMGSALLSLSRSVQELTE 290
Cdd:TIGR02168 354 ESLEAELEELEAE-----LEELESRLEELEEQLETLRSKVAQ-------LELQIASLNNEIERLEARLERLEDRRERLQQ 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559830 291 ENQSLKEDLDRvlstsPTISKTQGYVEwskpRLLRRIVELEKKLSVMESSKSHAAEpvrshppaclasSSALHRQPRGDR 370
Cdd:TIGR02168 422 EIEELLKKLEE-----AELKELQAELE----ELEEELEELQEELERLEEALEELRE------------ELEEAEQALDAA 480
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 566559830 371 NKDHERLRGAVRDLKeertALQEQLLQRDLEVKQLLQAKADL 412
Cdd:TIGR02168 481 ERELAQLQARLDSLE----RLQENLEGFSEGVKALLKNQSGL 518
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
165-454 |
4.32e-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: 40.49 E-value: 4.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559830 165 KDRqIEQLLdpSRGTDFVRTLAEKRPDASWVINGLKQRILKLEQQCKEKDGTISKLQTDMKTTNLE---EMRIAMETYYE 241
Cdd:pfam15921 266 QDR-IEQLI--SEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQlrsELREAKRMYED 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559830 242 EVHRL--QTLLASSETTGKKPLGEK--KTGAKRQKKMGSALLSLSRSVQELTEENQSLKEDLDRVLSTSPTISKTqgyve 317
Cdd:pfam15921 343 KIEELekQLVLANSELTEARTERDQfsQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHL----- 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559830 318 wsKPRLLRRIVELEKKLSVMESSKSHAAEPVRSHPPACLASSSALHRQprGDRNKDHERLRGAVRDLKEERTALQEQLLQ 397
Cdd:pfam15921 418 --RRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKV--SSLTAQLESTKEMLRKVVEELTAKKMTLES 493
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 566559830 398 RDLEVKQLLQAKADLEKELecaregeeerrereEVLREEIQTLTS----KLQELQEMKKEE 454
Cdd:pfam15921 494 SERTVSDLTASLQEKERAI--------------EATNAEITKLRSrvdlKLQELQHLKNEG 540
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
133-416 |
4.37e-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: 40.42 E-value: 4.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559830 133 EIIELKKSLhvqKSDVDLMRTKLRRLEEENSRKDRQIEQLLDPSRGTDFVRTLAEKRpdaswvINGLKQRILKLEQQCKE 212
Cdd:TIGR00606 692 ELQEFISDL---QSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKE------IPELRNKLQKVNRDIQR 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559830 213 KDGTISKLQTDMKTTNLEEMriAMETYYEEVHRLQTLLASSETTgkkplgEKKTGAKRQKKMGSallSLSRSVQELTEEN 292
Cdd:TIGR00606 763 LKNDIEEQETLLGTIMPEEE--SAKVCLTDVTIMERFQMELKDV------ERKIAQQAAKLQGS---DLDRTVQQVNQEK 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559830 293 QSLKEDLDRVLstsptisktqgyvewSKPRLLRRIVELEKKLSVMESSKSHAAEPVRSHPPACLASSSALHRQPRgDRNK 372
Cdd:TIGR00606 832 QEKQHELDTVV---------------SKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLV-ELST 895
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 566559830 373 DHERLRGAVRDLKEERTALqEQLLQRDLEVKQLLQAKADLEKEL 416
Cdd:TIGR00606 896 EVQSLIREIKDAKEQDSPL-ETFLEKDQQEKEELISSKETSNKK 938
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
137-452 |
4.90e-03 |
|
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: 40.19 E-value: 4.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559830 137 LKKSL-------HVQKSDVDLMRTklrRLEEENSRKDRQIEQLLDPS--RGTDF--VRTLAEKRPDASWVINGLKQRILK 205
Cdd:pfam10174 329 LKESLtakeqraAILQTEVDALRL---RLEEKESFLNKKTKQLQDLTeeKSTLAgeIRDLKDMLDVKERKINVLQKKIEN 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559830 206 LEQQCKEKDGTISK-------LQTDMKTTN--LEEMRIAMETYYEEVHRLQTLLASSEttgkKPLGEKKTGAKRQKKMGS 276
Cdd:pfam10174 406 LQEQLRDKDKQLAGlkervksLQTDSSNTDtaLTTLEEALSEKERIIERLKEQRERED----RERLEELESLKKENKDLK 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559830 277 ALLSLSRSvqELTEENQSLKEDLDRVLSTSPTISKTQgyvewSKPRLLRriVELEKKL---SVMESS--KSH-AAEPVRS 350
Cdd:pfam10174 482 EKVSALQP--ELTEKESSLIDLKEHASSLASSGLKKD-----SKLKSLE--IAVEQKKeecSKLENQlkKAHnAEEAVRT 552
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559830 351 HPP-----ACLASSSALHRQPRGDRNKDHERLRGAVRD------LKEERTALQEQLLQRDLE-----------VKQLLQA 408
Cdd:pfam10174 553 NPEindriRLLEQEVARYKEESGKAQAEVERLLGILREveneknDKDKKIAELESLTLRQMKeqnkkvanikhGQQEMKK 632
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 566559830 409 KADLEKELECAREGEEERREREEVLREEIQTLTSKLQELQEMKK 452
Cdd:pfam10174 633 KGAQLLEEARRREDNLADNSQQLQLEELMGALEKTRQELDATKA 676
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
126-344 |
9.22e-03 |
|
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: 39.42 E-value: 9.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559830 126 EKEDMYDEIIELKKSLHVQKSDVDLMRTKLRRLEEENSRKDRQIEQLLD-------PSRGTDF-VRTLAEKRPDASWVIN 197
Cdd:pfam10174 374 EKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKErvkslqtDSSNTDTaLTTLEEALSEKERIIE 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559830 198 GLKQRILKLEQQckekdgtisklqtdmKTTNLEEMRIAMETYYEEVHRLQTLLASSETTGKKPLGEKKTGAKRQKKMGSA 277
Cdd:pfam10174 454 RLKEQREREDRE---------------RLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSK 518
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 566559830 278 LLSLSRSVQELTEENQSLKEDLDRvlstsptiSKTQGYVEWSKPRLLRRIVELEKKLS--VMESSKSHA 344
Cdd:pfam10174 519 LKSLEIAVEQKKEECSKLENQLKK--------AHNAEEAVRTNPEINDRIRLLEQEVAryKEESGKAQA 579
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
127-416 |
9.96e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.28 E-value: 9.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559830 127 KEDMYDEIIELKKSLHVQKSDVDLMRTKLRRLEEENSRKDRQIEQLldpsrgtdfvRTLAEKrpdaswvINGLKQRILKL 206
Cdd:PRK03918 188 TENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKEL----------EELKEE-------IEELEKELESL 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559830 207 EQQCKEKDGTISKLQtdmktTNLEEMRIAMETYYEEVHRLQTLLASSET--TGKKPLGEKKTGAKRQKKMGSALLSLSRS 284
Cdd:PRK03918 251 EGSKRKLEEKIRELE-----ERIEELKKEIEELEEKVKELKELKEKAEEyiKLSEFYEEYLDELREIEKRLSRLEEEING 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559830 285 VQELTEENQSLKEDLdrvlstsptisktqGYVEWSKPRLLRRIVELEKKLSVMESSKSHAAEPVRshppaclasssalHR 364
Cdd:PRK03918 326 IEERIKELEEKEERL--------------EELKKKLKELEKRLEELEERHELYEEAKAKKEELER-------------LK 378
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 566559830 365 QPRGDRNKdhERLRGAVRDLKEERTALQEQLLQRDLEVKQLLQAKADLEKEL 416
Cdd:PRK03918 379 KRLTGLTP--EKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAI 428
|
|
| |
