|
Name |
Accession |
Description |
Interval |
E-value |
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
76-407 |
1.74e-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: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654705 76 REKEDMYDEIIELKKSLHVQKSDVDLMRTKLRRLEEENSRKDRQIEQlldpsrGTDFVRTLaeKRPDASWV--------- 146
Cdd:TIGR04523 321 KKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEE------KQNEIEKL--KKENQSYKqeiknlesq 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654705 147 INGLKQRILKLEQQCKEKDGTISKLQ----------TDMKTT---------NLEEMRIAMETYYEEVHR--------LQT 199
Cdd:TIGR04523 393 INDLESKIQNQEKLNQQKDEQIKKLQqekellekeiERLKETiiknnseikDLTNQDSVKELIIKNLDNtresletqLKV 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654705 200 LLASSETTgKKPLGEKKTGAKRQKKMgsaLLSLSRSVQELTEENQSLKEDLDRVLSTSPTISKTqgyvewsKPRLLRRIV 279
Cdd:TIGR04523 473 LSRSINKI-KQNLEQKQKELKSKEKE---LKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESE-------KKEKESKIS 541
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654705 280 ELEKKLSVMESSKshaaepvrshppaclaSSSALHRQPRGdrnKDHErlrgaVRDLKEERTALQEQLLQRDLEVKQLLQA 359
Cdd:TIGR04523 542 DLEDELNKDDFEL----------------KKENLEKEIDE---KNKE-----IEELKQTQKSLKKKQEEKQELIDQKEKE 597
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1034654705 360 KADLEKELecaregeeerrereevlREEIQTLTSKLQELQEMKKEEKE 407
Cdd:TIGR04523 598 KKDLIKEI-----------------EEKEKKISSLEKELEKAKKENEK 628
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
76-407 |
1.22e-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: 48.53 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654705 76 REKEDMYDEIIELKKSLHVQKSDVDLMRTKLRRLEEENSRKDRqieqlldpsrgtdFVRTLAEKRPDASWVingLKQRIL 155
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAER-------------YQALLKEKREYEGYE---LLKEKE 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654705 156 KLEQQCKEKDGTISKLQTDmkttnLEEMRIAMETYYEEVHRLQTLLaSSETTGKKPLGEKKTgAKRQKKMGS-------- 227
Cdd:TIGR02169 234 ALERQKEAIERQLASLEEE-----LEKLTEEISELEKRLEEIEQLL-EELNKKIKDLGEEEQ-LRVKEKIGEleaeiasl 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654705 228 --ALLSLSRSVQELTEENQSLKEDLDRVLSTSPTISKTQGYVEWSKPRLLRRIVELEKKLSVMESSkshaaepvrshppa 305
Cdd:TIGR02169 307 erSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAE-------------- 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654705 306 cLASSSALHRQPRgDRNKDherLRGAVRDLKEERTALQEQLLQRDLEVKQLLQAKADLEKELECAREGEEERREREEVLR 385
Cdd:TIGR02169 373 -LEEVDKEFAETR-DELKD---YREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKA 447
|
330 340
....*....|....*....|..
gi 1034654705 386 EEIQTLTSKLQELQEMKKEEKE 407
Cdd:TIGR02169 448 LEIKKQEWKLEQLAADLSKYEQ 469
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
84-409 |
3.78e-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: 46.97 E-value: 3.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654705 84 EIIELKKSLHVQKSDVDLMRTKLRRLEEENSRKDRQIEQLldpsrgtdfVRTLAEKRPDaswvINGLKQRILKLEQQCKE 163
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQL---------RKELEELSRQ----ISALRKDLARLEAEVEQ 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654705 164 KDGTISKLQTDmkttnLEEMRIAMETYYEEVHRLQTLLASSETtgkkplgEKKTGAKRQKKMGSALLSLSRSVQELTEEN 243
Cdd:TIGR02168 745 LEERIAQLSKE-----LTELEAEIEELEERLEEAEEELAEAEA-------EIEELEAQIEQLKEELKALREALDELRAEL 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654705 244 QSLKEDLDRVLSTsptisktqgyvewsKPRLLRRIVELEKKLSVMESSKshaaepvrshppaclasssalhrqprGDRNK 323
Cdd:TIGR02168 813 TLLNEEAANLRER--------------LESLERRIAATERRLEDLEEQI--------------------------EELSE 852
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654705 324 DHERLRGAVRDLKEERTALQEQLlqrdlevKQLLQAKADLEKELECAREGEEERREREEVLREEIQTLTSKLQELQEMKK 403
Cdd:TIGR02168 853 DIESLAAEIEELEELIEELESEL-------EALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLA 925
|
....*.
gi 1034654705 404 EEKEDC 409
Cdd:TIGR02168 926 QLELRL 931
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
76-366 |
1.25e-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: 45.49 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654705 76 REKEDMY-DEIIELKKSLHVQKSDVDLMRTKLRRLEEENSRKDRQIEQLLDPSRGTDFVRTLAEKRPDASWVIN-GLKQR 153
Cdd:pfam15921 334 REAKRMYeDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDtGNSIT 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654705 154 ILKLEQQCKEKDGTISKLQTDMKTT------NLEEMRIAMETYYEEVHRLQTLLASSETTgkKPLGEKKTGAKRQKKMgs 227
Cdd:pfam15921 414 IDHLRRELDDRNMEVQRLEALLKAMksecqgQMERQMAAIQGKNESLEKVSSLTAQLEST--KEMLRKVVEELTAKKM-- 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654705 228 ALLSLSRSVQELTeenQSLKEDLDRVLSTSPTISKTQGYVEWSKPRL---------LRRIVELEKKLSVMESSKSHAAEP 298
Cdd:pfam15921 490 TLESSERTVSDLT---ASLQEKERAIEATNAEITKLRSRVDLKLQELqhlknegdhLRNVQTECEALKLQMAEKDKVIEI 566
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034654705 299 VRSHppacLASSSALHRQprgdrnkdHERLRGAV--------RDLKEERTALQE-QLL--QRDLEVKQLLQAKADLEKE 366
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 ... |
74-406 |
2.99e-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: 44.19 E-value: 2.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654705 74 VYREKEDMYDEIIELKKSLHVQKSDVDLMRTKLRRLEEENSRKDRQIEQlldpSRGTDFVRTLAEKRPDASWVINGLKQR 153
Cdd:pfam02463 694 ILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLK----QKIDEEEEEEEKSRLKKEEKEEEKSEL 769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654705 154 ILKLEQQCKEKDGTISKLQTDMKTTNL------EEMRIAMETYYEEVHRLQTLLASSETTGKKPLGEKKTGAK--RQKKM 225
Cdd:pfam02463 770 SLKEKELAEEREKTEKLKVEEEKEEKLkaqeeeLRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELkeEQKLE 849
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654705 226 GSALLSLSRSVQELTEENQSLKEDLDRVLSTsptisktQGYVEWSKPRLLRRIVELEKKLSVMESSKSHAAEPVRShppa 305
Cdd:pfam02463 850 KLAEEELERLEEEITKEELLQELLLKEEELE-------EQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENE---- 918
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654705 306 cLASSSALHRQPRGDRNKDHERLRGAVRDLKEERTALQEQLLQRdleVKQLLQAKADLEKELECAREGEEERREREEVLR 385
Cdd:pfam02463 919 -IEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEER---NKRLLLAKEELGKVNLMAIEEFEEKEERYNKDE 994
|
330 340
....*....|....*....|....
gi 1034654705 386 EEIQTLT---SKLQELQEMKKEEK 406
Cdd:pfam02463 995 LEKERLEeekKKLIRAIIEETCQR 1018
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
151-411 |
3.06e-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: 3.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654705 151 KQRILKLEQQCKEKDGTISKLQTdmkttNLEEMRIAMETYYEEVHRLQTLLASSETTGKKPLGEKKTGAKRQKKMGSALL 230
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEK-----ALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIA 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654705 231 SLSRSVQELTEENQSLKEDLDRVLSTSPTISKTQGYVEWSKPRLLRRIVELEKKLSvmESSKSHAAepvrshppacLASS 310
Cdd:TIGR02168 751 QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALD--ELRAELTL----------LNEE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654705 311 SALHRQPRGDRNKDHERLRGAVRDLKEERTALQEQLLQRDLEVKQLLQAKADLEKELECAREGEEERREREEVLREEIQT 390
Cdd:TIGR02168 819 AANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEE 898
|
250 260
....*....|....*....|.
gi 1034654705 391 LTSKLQELQEMKKEEKEDCPE 411
Cdd:TIGR02168 899 LSEELRELESKRSELRRELEE 919
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
76-411 |
1.20e-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: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654705 76 REKEDMYDEIIELKKSLhvqksdvDLMRTKLRRLEEENSRKDRQIEqlldpsrgtdfvrtlaekrpDASWVINGLKQRIL 155
Cdd:TIGR02168 684 EKIEELEEKIAELEKAL-------AELRKELEELEEELEQLRKELE--------------------ELSRQISALRKDLA 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654705 156 KLEQQCKEKDGTISKLQtdmktTNLEEMRIAMETYYEEVHRLQTLLASSETtgkkplgEKKTGAKRQKKMGSALLSLSRS 235
Cdd:TIGR02168 737 RLEAEVEQLEERIAQLS-----KELTELEAEIEELEERLEEAEEELAEAEA-------EIEELEAQIEQLKEELKALREA 804
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654705 236 VQELTEENQSLKEDLDRVLSTSPTISKTQGYVEWSKPRLLRRIVELEKKLSVMESSKSHAAEPVRSHppaclasssalhr 315
Cdd:TIGR02168 805 LDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEL------------- 871
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654705 316 qprgdrNKDHERLRGAVRDLKEERTALQEQLLQRDLEVKQLLQAKADLEKELECAREGEEERREREEVLREEIQTLTSKL 395
Cdd:TIGR02168 872 ------ESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
|
330
....*....|....*.
gi 1034654705 396 QELQEMKKEEKEDCPE 411
Cdd:TIGR02168 946 SEEYSLTLEEAEALEN 961
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
83-363 |
1.46e-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: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654705 83 DEIIELKKSLHVQKSDVDLMRTKLRRLEEENSRKDRQIEQLL-DPSRGTDFVRTLAEKRPDASWVINGLKQRILKLEQQC 161
Cdd:TIGR02168 274 LEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLErQLEELEAQLEELESKLDELAEELAELEEKLEELKEEL 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654705 162 KEKDGTISKLQTDmkttnLEEMRIAMETYYEEVHRLQTLLASsettgkkPLGEKKTGAKRQKKMGSALLSLSRSVQELTE 241
Cdd:TIGR02168 354 ESLEAELEELEAE-----LEELESRLEELEEQLETLRSKVAQ-------LELQIASLNNEIERLEARLERLEDRRERLQQ 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654705 242 ENQSLKEDLDRvlstsPTISKTQGYVEwskpRLLRRIVELEKKLSVMESSKSHAAEpvrshppaclasSSALHRQPRGDR 321
Cdd:TIGR02168 422 EIEELLKKLEE-----AELKELQAELE----ELEEELEELQEELERLEEALEELRE------------ELEEAEQALDAA 480
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1034654705 322 NKDHERLRGAVRDLKeertALQEQLLQRDLEVKQLLQAKADL 363
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 ... |
88-403 |
3.43e-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: 40.58 E-value: 3.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654705 88 LKKSL-------HVQKSDVDLMRTklrRLEEENSRKDRQIEQLLDPS--RGTDF--VRTLAEKRPDASWVINGLKQRILK 156
Cdd:pfam10174 329 LKESLtakeqraAILQTEVDALRL---RLEEKESFLNKKTKQLQDLTeeKSTLAgeIRDLKDMLDVKERKINVLQKKIEN 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654705 157 LEQQCKEKDGTISK-------LQTDMKTTN--LEEMRIAMETYYEEVHRLQTLLASSEttgkKPLGEKKTGAKRQKKMGS 227
Cdd:pfam10174 406 LQEQLRDKDKQLAGlkervksLQTDSSNTDtaLTTLEEALSEKERIIERLKEQRERED----RERLEELESLKKENKDLK 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654705 228 ALLSLSRSvqELTEENQSLKEDLDRVLSTSPTISKTQgyvewSKPRLLRriVELEKKL---SVMESS--KSH-AAEPVRS 301
Cdd:pfam10174 482 EKVSALQP--ELTEKESSLIDLKEHASSLASSGLKKD-----SKLKSLE--IAVEQKKeecSKLENQlkKAHnAEEAVRT 552
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654705 302 HPP-----ACLASSSALHRQPRGDRNKDHERLRGAVRD------LKEERTALQEQLLQRDLE-----------VKQLLQA 359
Cdd:pfam10174 553 NPEindriRLLEQEVARYKEESGKAQAEVERLLGILREveneknDKDKKIAELESLTLRQMKeqnkkvanikhGQQEMKK 632
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1034654705 360 KADLEKELECAREGEEERREREEVLREEIQTLTSKLQELQEMKK 403
Cdd:pfam10174 633 KGAQLLEEARRREDNLADNSQQLQLEELMGALEKTRQELDATKA 676
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
84-367 |
3.54e-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: 40.80 E-value: 3.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654705 84 EIIELKKSLhvqKSDVDLMRTKLRRLEEENSRKDRQIEQLLDPSRGTDFVRTLAEKRpdaswvINGLKQRILKLEQQCKE 163
Cdd:TIGR00606 692 ELQEFISDL---QSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKE------IPELRNKLQKVNRDIQR 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654705 164 KDGTISKLQTDMKTTNLEEMriAMETYYEEVHRLQTLLASSETTgkkplgEKKTGAKRQKKMGSallSLSRSVQELTEEN 243
Cdd:TIGR00606 763 LKNDIEEQETLLGTIMPEEE--SAKVCLTDVTIMERFQMELKDV------ERKIAQQAAKLQGS---DLDRTVQQVNQEK 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654705 244 QSLKEDLDRVLstsptisktqgyvewSKPRLLRRIVELEKKLSVMESSKSHAAEPVRSHPPACLASSSALHRQPRgDRNK 323
Cdd:TIGR00606 832 QEKQHELDTVV---------------SKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLV-ELST 895
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1034654705 324 DHERLRGAVRDLKEERTALqEQLLQRDLEVKQLLQAKADLEKEL 367
Cdd:TIGR00606 896 EVQSLIREIKDAKEQDSPL-ETFLEKDQQEKEELISSKETSNKK 938
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
116-405 |
5.04e-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: 40.10 E-value: 5.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654705 116 KDRqIEQLLdpSRGTDFVRTLAEKRPDASWVINGLKQRILKLEQQCKEKDGTISKLQTDMKTTNLE---EMRIAMETYYE 192
Cdd:pfam15921 266 QDR-IEQLI--SEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQlrsELREAKRMYED 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654705 193 EVHRL--QTLLASSETTGKKPLGEK--KTGAKRQKKMGSALLSLSRSVQELTEENQSLKEDLDRVLSTSPTISKTqgyve 268
Cdd:pfam15921 343 KIEELekQLVLANSELTEARTERDQfsQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHL----- 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654705 269 wsKPRLLRRIVELEKKLSVMESSKSHAAEPVRSHPPACLASSSALHRQprGDRNKDHERLRGAVRDLKEERTALQEQLLQ 348
Cdd:pfam15921 418 --RRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKV--SSLTAQLESTKEMLRKVVEELTAKKMTLES 493
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034654705 349 RDLEVKQLLQAKADLEKELecaregeeerrereEVLREEIQTLTS----KLQELQEMKKEE 405
Cdd:pfam15921 494 SERTVSDLTASLQEKERAI--------------EATNAEITKLRSrvdlKLQELQHLKNEG 540
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
78-367 |
5.39e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 5.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654705 78 KEDMYDEIIELKKSLHVQKSDVDLMRTKLRRLEEENSRKDRQIEQLldpsrgtdfvRTLAEKrpdaswvINGLKQRILKL 157
Cdd:PRK03918 188 TENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKEL----------EELKEE-------IEELEKELESL 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654705 158 EQQCKEKDGTISKLQtdmktTNLEEMRIAMETYYEEVHRLQTLLASSET--TGKKPLGEKKTGAKRQKKMGSALLSLSRS 235
Cdd:PRK03918 251 EGSKRKLEEKIRELE-----ERIEELKKEIEELEEKVKELKELKEKAEEyiKLSEFYEEYLDELREIEKRLSRLEEEING 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654705 236 VQELTEENQSLKEDLdrvlstsptisktqGYVEWSKPRLLRRIVELEKKLSVMESSKSHAAEPVRshppaclasssalHR 315
Cdd:PRK03918 326 IEERIKELEEKEERL--------------EELKKKLKELEKRLEELEERHELYEEAKAKKEELER-------------LK 378
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1034654705 316 QPRGDRNKdhERLRGAVRDLKEERTALQEQLLQRDLEVKQLLQAKADLEKEL 367
Cdd:PRK03918 379 KRLTGLTP--EKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAI 428
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
77-295 |
6.97e-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: 6.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654705 77 EKEDMYDEIIELKKSLHVQKSDVDLMRTKLRRLEEENSRKDRQIEQLLD-------PSRGTDF-VRTLAEKRPDASWVIN 148
Cdd:pfam10174 374 EKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKErvkslqtDSSNTDTaLTTLEEALSEKERIIE 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654705 149 GLKQRILKLEQQckekdgtisklqtdmKTTNLEEMRIAMETYYEEVHRLQTLLASSETTGKKPLGEKKTGAKRQKKMGSA 228
Cdd:pfam10174 454 RLKEQREREDRE---------------RLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSK 518
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034654705 229 LLSLSRSVQELTEENQSLKEDLDRvlstsptiSKTQGYVEWSKPRLLRRIVELEKKLS--VMESSKSHA 295
Cdd:pfam10174 519 LKSLEIAVEQKKEECSKLENQLKK--------AHNAEEAVRTNPEINDRIRLLEQEVAryKEESGKAQA 579
|
|
| |
