|
Name |
Accession |
Description |
Interval |
E-value |
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
148-479 |
3.63e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 53.49 E-value: 3.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654703 148 REKEDMYDEIIELKKSLHVQKSDVDLMRTKLRRLEEENSRKDRQIEQlldpsrGTDFVRTLaeKRPDASWV--------- 218
Cdd:TIGR04523 321 KKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEE------KQNEIEKL--KKENQSYKqeiknlesq 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654703 219 INGLKQRILKLEQQCKEKDGTISKLQ----------TDMKTT---------NLEEMRIAMETYYEEVHR--------LQT 271
Cdd:TIGR04523 393 INDLESKIQNQEKLNQQKDEQIKKLQqekellekeiERLKETiiknnseikDLTNQDSVKELIIKNLDNtresletqLKV 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654703 272 LLASSETTgKKPLGEKKTGAKRQKKMgsaLLSLSRSVQELTEENQSLKEDLDRVLSTSPTISKTqgyvewsKPRLLRRIV 351
Cdd:TIGR04523 473 LSRSINKI-KQNLEQKQKELKSKEKE---LKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESE-------KKEKESKIS 541
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654703 352 ELEKKLSVMESSKshaaepvrshppaclaSSSALHRQPRGdrnKDHErlrgaVRDLKEERTALQEQLLQRDLEVKQLLQA 431
Cdd:TIGR04523 542 DLEDELNKDDFEL----------------KKENLEKEIDE---KNKE-----IEELKQTQKSLKKKQEEKQELIDQKEKE 597
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1034654703 432 KADLEKELecaregeeerrereevlREEIQTLTSKLQELQEMKKEEKE 479
Cdd:TIGR04523 598 KKDLIKEI-----------------EEKEKKISSLEKELEKAKKENEK 628
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
148-479 |
7.72e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 49.30 E-value: 7.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654703 148 REKEDMYDEIIELKKSLHVQKSDVDLMRTKLRRLEEENSRKDRqieqlldpsrgtdFVRTLAEKRPDASWVingLKQRIL 227
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAER-------------YQALLKEKREYEGYE---LLKEKE 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654703 228 KLEQQCKEKDGTISKLQTDmkttnLEEMRIAMETYYEEVHRLQTLLaSSETTGKKPLGEKKTgAKRQKKMGS-------- 299
Cdd:TIGR02169 234 ALERQKEAIERQLASLEEE-----LEKLTEEISELEKRLEEIEQLL-EELNKKIKDLGEEEQ-LRVKEKIGEleaeiasl 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654703 300 --ALLSLSRSVQELTEENQSLKEDLDRVLSTSPTISKTQGYVEWSKPRLLRRIVELEKKLSVMESSkshaaepvrshppa 377
Cdd:TIGR02169 307 erSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAE-------------- 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654703 378 cLASSSALHRQPRgDRNKDherLRGAVRDLKEERTALQEQLLQRDLEVKQLLQAKADLEKELECAREGEEERREREEVLR 457
Cdd:TIGR02169 373 -LEEVDKEFAETR-DELKD---YREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKA 447
|
330 340
....*....|....*....|..
gi 1034654703 458 EEIQTLTSKLQELQEMKKEEKE 479
Cdd:TIGR02169 448 LEIKKQEWKLEQLAADLSKYEQ 469
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
156-481 |
2.52e-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: 47.74 E-value: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654703 156 EIIELKKSLHVQKSDVDLMRTKLRRLEEENSRKDRQIEQLldpsrgtdfVRTLAEKRPDaswvINGLKQRILKLEQQCKE 235
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQL---------RKELEELSRQ----ISALRKDLARLEAEVEQ 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654703 236 KDGTISKLQTDmkttnLEEMRIAMETYYEEVHRLQTLLASSETtgkkplgEKKTGAKRQKKMGSALLSLSRSVQELTEEN 315
Cdd:TIGR02168 745 LEERIAQLSKE-----LTELEAEIEELEERLEEAEEELAEAEA-------EIEELEAQIEQLKEELKALREALDELRAEL 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654703 316 QSLKEDLDRVLSTsptisktqgyvewsKPRLLRRIVELEKKLSVMESSKshaaepvrshppaclasssalhrqprGDRNK 395
Cdd:TIGR02168 813 TLLNEEAANLRER--------------LESLERRIAATERRLEDLEEQI--------------------------EELSE 852
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654703 396 DHERLRGAVRDLKEERTALQEQLlqrdlevKQLLQAKADLEKELECAREGEEERREREEVLREEIQTLTSKLQELQEMKK 475
Cdd:TIGR02168 853 DIESLAAEIEELEELIEELESEL-------EALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLA 925
|
....*.
gi 1034654703 476 EEKEDC 481
Cdd:TIGR02168 926 QLELRL 931
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
148-438 |
5.84e-05 |
|
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: 46.65 E-value: 5.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654703 148 REKEDMY-DEIIELKKSLHVQKSDVDLMRTKLRRLEEENSRKDRQIEQLLDPSRGTDFVRTLAEKRPDASWVIN-GLKQR 225
Cdd:pfam15921 334 REAKRMYeDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDtGNSIT 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654703 226 ILKLEQQCKEKDGTISKLQTDMKTT------NLEEMRIAMETYYEEVHRLQTLLASSETTgkKPLGEKKTGAKRQKKMgs 299
Cdd:pfam15921 414 IDHLRRELDDRNMEVQRLEALLKAMksecqgQMERQMAAIQGKNESLEKVSSLTAQLEST--KEMLRKVVEELTAKKM-- 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654703 300 ALLSLSRSVQELTeenQSLKEDLDRVLSTSPTISKTQGYVEWSKPRL---------LRRIVELEKKLSVMESSKSHAAEP 370
Cdd:pfam15921 490 TLESSERTVSDLT---ASLQEKERAIEATNAEITKLRSRVDLKLQELqhlknegdhLRNVQTECEALKLQMAEKDKVIEI 566
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034654703 371 VRSHppacLASSSALHRQprgdrnkdHERLRGAV--------RDLKEERTALQE-QLL--QRDLEVKQLLQAKADLEKE 438
Cdd:pfam15921 567 LRQQ----IENMTQLVGQ--------HGRTAGAMqvekaqleKEINDRRLELQEfKILkdKKDAKIRELEARVSDLELE 633
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
146-478 |
1.70e-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: 44.96 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654703 146 VYREKEDMYDEIIELKKSLHVQKSDVDLMRTKLRRLEEENSRKDRQIEQlldpSRGTDFVRTLAEKRPDASWVINGLKQR 225
Cdd:pfam02463 694 ILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLK----QKIDEEEEEEEKSRLKKEEKEEEKSEL 769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654703 226 ILKLEQQCKEKDGTISKLQTDMKTTNL------EEMRIAMETYYEEVHRLQTLLASSETTGKKPLGEKKTGAK--RQKKM 297
Cdd:pfam02463 770 SLKEKELAEEREKTEKLKVEEEKEEKLkaqeeeLRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELkeEQKLE 849
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654703 298 GSALLSLSRSVQELTEENQSLKEDLDRVLSTSPTI-SKTQGyvewskprLLRRIVELEKKLSVMESSKSHAAEPVRShpp 376
Cdd:pfam02463 850 KLAEEELERLEEEITKEELLQELLLKEEELEEQKLkDELES--------KEEKEKEEKKELEEESQKLNLLEEKENE--- 918
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654703 377 acLASSSALHRQPRGDRNKDHERLRGAVRDLKEERTALQEQLLQRdleVKQLLQAKADLEKELECAREGEEERREREEVL 456
Cdd:pfam02463 919 --IEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEER---NKRLLLAKEELGKVNLMAIEEFEEKEERYNKD 993
|
330 340
....*....|....*....|....*
gi 1034654703 457 REEIQTLT---SKLQELQEMKKEEK 478
Cdd:pfam02463 994 ELEKERLEeekKKLIRAIIEETCQR 1018
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
201-483 |
2.72e-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: 44.28 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654703 201 GTDFVRTLAEKRPDASwvINGLKQRILKLEQQCKEKDGTISKLQTdmkttNLEEMRIAMETYYEEVHRLQTLLASSETTG 280
Cdd:TIGR02168 656 RPGGVITGGSAKTNSS--ILERRREIEELEEKIEELEEKIAELEK-----ALAELRKELEELEEELEQLRKELEELSRQI 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654703 281 KKPLGEKKTGAKRQKKMGSALLSLSRSVQELTEENQSLKEDLDRVLSTSPTISKTQGYVEWSKPRLLRRIVELEKKLSvm 360
Cdd:TIGR02168 729 SALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALD-- 806
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654703 361 ESSKSHAAepvrshppacLASSSALHRQPRGDRNKDHERLRGAVRDLKEERTALQEQLLQRDLEVKQLLQAKADLEKELE 440
Cdd:TIGR02168 807 ELRAELTL----------LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELE 876
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1034654703 441 CAREGEEERREREEVLREEIQTLTSKLQELQEMKKEEKEDCPE 483
Cdd:TIGR02168 877 ALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEE 919
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
148-483 |
9.41e-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: 42.74 E-value: 9.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654703 148 REKEDMYDEIIELKKSLhvqksdvDLMRTKLRRLEEENSRKDRQIEqlldpsrgtdfvrtlaekrpDASWVINGLKQRIL 227
Cdd:TIGR02168 684 EKIEELEEKIAELEKAL-------AELRKELEELEEELEQLRKELE--------------------ELSRQISALRKDLA 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654703 228 KLEQQCKEKDGTISKLQtdmktTNLEEMRIAMETYYEEVHRLQTLLASSETtgkkplgEKKTGAKRQKKMGSALLSLSRS 307
Cdd:TIGR02168 737 RLEAEVEQLEERIAQLS-----KELTELEAEIEELEERLEEAEEELAEAEA-------EIEELEAQIEQLKEELKALREA 804
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654703 308 VQELTEENQSLKEDLDRVLSTSPTISKTQGYVEWSKPRLLRRIVELEKKLSVMESSKSHAAEPVRSHppaclasssalhr 387
Cdd:TIGR02168 805 LDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEL------------- 871
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654703 388 qprgdrNKDHERLRGAVRDLKEERTALQEQLLQRDLEVKQLLQAKADLEKELECAREGEEERREREEVLREEIQTLTSKL 467
Cdd:TIGR02168 872 ------ESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
|
330
....*....|....*.
gi 1034654703 468 QELQEMKKEEKEDCPE 483
Cdd:TIGR02168 946 SEEYSLTLEEAEALEN 961
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
155-435 |
1.02e-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: 42.74 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654703 155 DEIIELKKSLHVQKSDVDLMRTKLRRLEEENSRKDRQIEQLL-DPSRGTDFVRTLAEKRPDASWVINGLKQRILKLEQQC 233
Cdd:TIGR02168 274 LEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLErQLEELEAQLEELESKLDELAEELAELEEKLEELKEEL 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654703 234 KEKDGTISKLQTDmkttnLEEMRIAMETYYEEVHRLQTLLASsettgkkPLGEKKTGAKRQKKMGSALLSLSRSVQELTE 313
Cdd:TIGR02168 354 ESLEAELEELEAE-----LEELESRLEELEEQLETLRSKVAQ-------LELQIASLNNEIERLEARLERLEDRRERLQQ 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654703 314 ENQSLKEDLDRvlstsPTISKTQGYVEwskpRLLRRIVELEKKLSVMESSKSHAAEpvrshppaclasSSALHRQPRGDR 393
Cdd:TIGR02168 422 EIEELLKKLEE-----AELKELQAELE----ELEEELEELQEELERLEEALEELRE------------ELEEAEQALDAA 480
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1034654703 394 NKDHERLRGAVRDLKeertALQEQLLQRDLEVKQLLQAKADL 435
Cdd:TIGR02168 481 ERELAQLQARLDSLE----RLQENLEGFSEGVKALLKNQSGL 518
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
160-475 |
1.32e-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: 42.12 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654703 160 LKKSL-------HVQKSDVDLMRTklrRLEEENSRKDRQIEQLLDPS--RGTDF--VRTLAEKRPDASWVINGLKQRILK 228
Cdd:pfam10174 329 LKESLtakeqraAILQTEVDALRL---RLEEKESFLNKKTKQLQDLTeeKSTLAgeIRDLKDMLDVKERKINVLQKKIEN 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654703 229 LEQQCKEKDGTISK-------LQTDMKTTN--LEEMRIAMETYYEEVHRLQTLLASSEttgkKPLGEKKTGAKRQKKMGS 299
Cdd:pfam10174 406 LQEQLRDKDKQLAGlkervksLQTDSSNTDtaLTTLEEALSEKERIIERLKEQRERED----RERLEELESLKKENKDLK 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654703 300 ALLSLSRSvqELTEENQSLKEDLDRVLSTSPTISKTQgyvewSKPRLLRriVELEKKL---SVMESS--KSH-AAEPVRS 373
Cdd:pfam10174 482 EKVSALQP--ELTEKESSLIDLKEHASSLASSGLKKD-----SKLKSLE--IAVEQKKeecSKLENQlkKAHnAEEAVRT 552
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654703 374 HPP-----ACLASSSALHRQPRGDRNKDHERLRGAVRD------LKEERTALQEQLLQRDLE-----------VKQLLQA 431
Cdd:pfam10174 553 NPEindriRLLEQEVARYKEESGKAQAEVERLLGILREveneknDKDKKIAELESLTLRQMKeqnkkvanikhGQQEMKK 632
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1034654703 432 KADLEKELECAREGEEERREREEVLREEIQTLTSKLQELQEMKK 475
Cdd:pfam10174 633 KGAQLLEEARRREDNLADNSQQLQLEELMGALEKTRQELDATKA 676
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
156-439 |
1.99e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.57 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654703 156 EIIELKKSLhvqKSDVDLMRTKLRRLEEENSRKDRQIEQLLDPSRGTDFVRTLAEKRpdaswvINGLKQRILKLEQQCKE 235
Cdd:TIGR00606 692 ELQEFISDL---QSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKE------IPELRNKLQKVNRDIQR 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654703 236 KDGTISKLQTDMKTTNLEEMriAMETYYEEVHRLQTLLASSETTgkkplgEKKTGAKRQKKMGSallSLSRSVQELTEEN 315
Cdd:TIGR00606 763 LKNDIEEQETLLGTIMPEEE--SAKVCLTDVTIMERFQMELKDV------ERKIAQQAAKLQGS---DLDRTVQQVNQEK 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654703 316 QSLKEDLDRVLstsptisktqgyvewSKPRLLRRIVELEKKLSVMESSKSHAAEPVRSHPPACLASSSALHRQPRgDRNK 395
Cdd:TIGR00606 832 QEKQHELDTVV---------------SKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLV-ELST 895
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1034654703 396 DHERLRGAVRDLKEERTALqEQLLQRDLEVKQLLQAKADLEKEL 439
Cdd:TIGR00606 896 EVQSLIREIKDAKEQDSPL-ETFLEKDQQEKEELISSKETSNKK 938
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
150-439 |
2.66e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 2.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654703 150 KEDMYDEIIELKKSLHVQKSDVDLMRTKLRRLEEENSRKDRQIEQLldpsrgtdfvRTLAEKrpdaswvINGLKQRILKL 229
Cdd:PRK03918 188 TENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKEL----------EELKEE-------IEELEKELESL 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654703 230 EQQCKEKDGTISKLQtdmktTNLEEMRIAMETYYEEVHRLQTLLASSET--TGKKPLGEKKTGAKRQKKMGSALLSLSRS 307
Cdd:PRK03918 251 EGSKRKLEEKIRELE-----ERIEELKKEIEELEEKVKELKELKEKAEEyiKLSEFYEEYLDELREIEKRLSRLEEEING 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654703 308 VQELTEENQSLKEDLdrvlstsptisktqGYVEWSKPRLLRRIVELEKKLSVMESSKSHAAEPVRshppaclasssalHR 387
Cdd:PRK03918 326 IEERIKELEEKEERL--------------EELKKKLKELEKRLEELEERHELYEEAKAKKEELER-------------LK 378
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1034654703 388 QPRGDRNKdhERLRGAVRDLKEERTALQEQLLQRDLEVKQLLQAKADLEKEL 439
Cdd:PRK03918 379 KRLTGLTP--EKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAI 428
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
188-477 |
3.11e-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: 40.87 E-value: 3.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654703 188 KDRqIEQLLdpSRGTDFVRTLAEKRPDASWVINGLKQRILKLEQQCKEKDGTISKLQTDMKTTNLE---EMRIAMETYYE 264
Cdd:pfam15921 266 QDR-IEQLI--SEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQlrsELREAKRMYED 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654703 265 EVHRL--QTLLASSETTGKKPLGEK--KTGAKRQKKMGSALLSLSRSVQELTEENQSLKEDLDRVLSTSPTISKTqgyve 340
Cdd:pfam15921 343 KIEELekQLVLANSELTEARTERDQfsQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHL----- 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654703 341 wsKPRLLRRIVELEKKLSVMESSKSHAAEPVRSHPPACLASSSALHRQprGDRNKDHERLRGAVRDLKEERTALQEQLLQ 420
Cdd:pfam15921 418 --RRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKV--SSLTAQLESTKEMLRKVVEELTAKKMTLES 493
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034654703 421 RDLEVKQLLQAKADLEKELecaregeeerrereEVLREEIQTLTS----KLQELQEMKKEE 477
Cdd:pfam15921 494 SERTVSDLTASLQEKERAI--------------EATNAEITKLRSrvdlKLQELQHLKNEG 540
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
172-500 |
4.62e-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: 40.48 E-value: 4.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654703 172 DLMRTKLRRLEE-ENSRKDRQIEQLLDPSRGTDFVRTLAEKRPDaswvINGLKqRILKLEQQCKEKDGTISKLQTDMKTT 250
Cdd:pfam05483 363 ELLRTEQQRLEKnEDQLKIITMELQKKSSELEEMTKFKNNKEVE----LEELK-KILAEDEKLLDEKKQFEKIAEELKGK 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654703 251 NlEEMRIAMETYYEEVHRLQ---TLLASSETTGKKPLGEKKTGAKRQKKMGSALLS----LSRSVQELTEENQSL----- 318
Cdd:pfam05483 438 E-QELIFLLQAREKEIHDLEiqlTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAhcdkLLLENKELTQEASDMtlelk 516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654703 319 --KEDL-------DRVLSTSPTISKTQ----GYVEWSKPRLLRRIVELEKKLSVMESSKSHAAEPVRSHPPACLASSSAL 385
Cdd:pfam05483 517 khQEDIinckkqeERMLKQIENLEEKEmnlrDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKC 596
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654703 386 H--RQPRGDRNKDHERLRGAVRDLKEERTALQEQLLQRDLEVK----QLLQAKADLEKELECAREGEEERREREEVLREE 459
Cdd:pfam05483 597 NnlKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNklelELASAKQKFEEIIDNYQKEIEDKKISEEKLLEE 676
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1034654703 460 IQTLTSKLQELQEMKKEEKEDCpevPHKAQELPAPTPSSRH 500
Cdd:pfam05483 677 VEKAKAIADEAVKLQKEIDKRC---QHKIAEMVALMEKHKH 714
|
|
| |
