|
Name |
Accession |
Description |
Interval |
E-value |
| E_set_AMPKbeta_like_N |
cd02859 |
N-terminal Early set domain, a glycogen binding domain, associated with the catalytic domain ... |
496-574 |
8.07e-23 |
|
N-terminal Early set domain, a glycogen binding domain, associated with the catalytic domain of AMP-activated protein kinase beta subunit; E or "early" set domains are associated with the catalytic domain of AMP-activated protein kinase beta subunit glycogen binding domain at the N-terminal end. AMPK is a metabolic stress sensing protein that senses AMP/ATP and has recently been found to act as a glycogen sensor as well. The protein functions as an alpha-beta-gamma heterotrimer. This N-terminal domain is the glycogen binding domain of the beta subunit. This domain is also a member of the CBM48 (Carbohydrate Binding Module 48) family whose members include pullulanase, maltooligosyl trehalose synthase, starch branching enzyme, glycogen branching enzyme, glycogen debranching enzyme, and isoamylase.
Pssm-ID: 199889 [Multi-domain] Cd Length: 80 Bit Score: 92.28 E-value: 8.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 496 NVTLTISNTE-QEVYLTGSFINWKCTLKCEKLVSGKKGVTVNLTRGRHEFRFMINGEWATSSDYQQVPNGLGGQNNIIFV 574
Cdd:cd02859 1 PVTFRWPGPGgKEVYVTGSFDNWQQPIPLEKSGDGEFSATVELPPGRYEYKFIVDGEWVHDPDLPTVTDEFGNLNNVLEV 80
|
|
| NTD_TDP-43 |
cd19609 |
N-terminal domain of transactive response DNA-binding protein 43; Transactive response ... |
17-82 |
4.96e-22 |
|
N-terminal domain of transactive response DNA-binding protein 43; Transactive response DNA-binding protein of 43 kDa (TDP-43) is a nuclear DNA/RNA-binding protein involved in gene transcription and mRNA processing, transport, and translational regulation. It is vital to pre-mRNA and microRNA processing and regulates stress granule activity through the differential regulation of G3BP and TIA-1. It also forms aggregates implicated in amyotrophic lateral sclerosis. The N-terminal domain of TDP-43 is required for its physiological functions and pathological aggregation.
Pssm-ID: 410991 Cd Length: 74 Bit Score: 89.90 E-value: 4.96e-22
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25151865 17 EIEPVQVSHDQDATLNFATVQSVVPGAHGLYYRDDGERKALLFDNNTGKVYPPPNGWDSVPIFIHL 82
Cdd:cd19609 9 GDEPIEVPLEEDGTLLLSTLQAQFPGATGLKYRNPETGRARGVRLVDGKLYPPEGGWGDRVYYVVF 74
|
|
| TDP43_N |
pfam18694 |
Transactive response DNA-binding protein N-terminal domain; This domain can be found at the ... |
19-82 |
4.86e-20 |
|
Transactive response DNA-binding protein N-terminal domain; This domain can be found at the N-terminal region of transactive response DNA-binding protein 43 kDa (TDP-43), an RNA transporting and processing protein whose aberrant aggregates are implicated in neurodegenerative diseases. TDP-43 N-terminal domain has been shown to play an important role in the aggregation of TDP-43 monomers and its loss of function affects the RNA metabolic levels. Secondary structure of the N-terminal domain consists of six beta-strands and it resembles axin 1.
Pssm-ID: 465833 Cd Length: 74 Bit Score: 84.15 E-value: 4.86e-20
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25151865 19 EPVQVSHDQDATLNFATVQSVVPGAHGLYYR--DDGERKALLFDNntGKVYPPPNGWDSVPIFIHL 82
Cdd:pfam18694 11 EPIEIPLEDDGTLLLSTLQAQFPGACGLKYRnpETGCKRGVRLDD--GKLHPPAGGWGNKVYYVVF 74
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
109-427 |
1.20e-15 |
|
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: 80.50 E-value: 1.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 109 VQKLFAAAGLGGRSQKVYAAGKTRARSTSKKNQPRSQFDAQPENVNISEESEGRDSEKEKNDRQLEKLRNRNDELKIRVK 188
Cdd:TIGR02169 626 VEDIEAARRLMGKYRMVTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLD 705
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 189 EYKSDLSAAQLKVKNLEKKLESAQsaDSEEKFVRIDSEIDEKRSQ------DHDEEINNLHNVIEELRNKLATVESKNKD 262
Cdd:TIGR02169 706 ELSQELSDASRKIGEIEKEIEQLE--QEEEKLKERLEELEEDLSSleqeieNVKSELKELEARIEELEEDLHKLEEALND 783
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 263 LETKFSENQdyLKNAKDKVTFLEnqlnsdahEEVK--STAVRALEVKLGLANNSIRQAEAEKQQLQEANWYANERVGKLE 340
Cdd:TIGR02169 784 LEARLSHSR--IPEIQAELSKLE--------EEVSriEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIE 853
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 341 QENGYLKGITEQLKARADtsHAEKMLKDSEKRVWEINEEKSKLEWRLGELSQWWNDAKWKVGELESSVALQRNLLDTANS 420
Cdd:TIGR02169 854 KEIENLNGKKEELEEELE--ELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEE 931
|
....*..
gi 25151865 421 KIQSLND 427
Cdd:TIGR02169 932 ELSEIED 938
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
163-429 |
6.84e-14 |
|
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: 75.09 E-value: 6.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 163 DSEKEKNDRQLEKLRNRNDELKIRVKEYKSDLSAAQLKVKNLEKKLESAQsadseEKFVRIDSEID--EKRSQDHDEEIN 240
Cdd:TIGR02168 238 REELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQ-----KELYALANEISrlEQQKQILRERLA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 241 NLHNVIEELRNKLATVESKNKDLETKFSENQDYLKNAKDKVTFLENQLNS----------------DAHEEVKStAVRAL 304
Cdd:TIGR02168 313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEEleaeleelesrleeleEQLETLRS-KVAQL 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 305 EVKLGLANNSIRQAEAEKQQLQeanwyanERVGKLEQENGYLKgiTEQLKARADTSHA-----EKMLKDSEKRVWEINEE 379
Cdd:TIGR02168 392 ELQIASLNNEIERLEARLERLE-------DRRERLQQEIEELL--KKLEEAELKELQAeleelEEELEELQEELERLEEA 462
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 25151865 380 KSKLEWRLGELSQWWNDAKWKV----GELESSVALQRNLLDTANSKIQSLNDQS 429
Cdd:TIGR02168 463 LEELREELEEAEQALDAAERELaqlqARLDSLERLQENLEGFSEGVKALLKNQS 516
|
|
| AMPK1_CBM |
pfam16561 |
Glycogen recognition site of AMP-activated protein kinase; AMPK1_CBM is a family found in ... |
507-574 |
1.88e-13 |
|
Glycogen recognition site of AMP-activated protein kinase; AMPK1_CBM is a family found in close association with AMPKBI pfam04739. The surface of AMPK1_CBM reveals a carbohydrate-binding pocket.
Pssm-ID: 465176 [Multi-domain] Cd Length: 85 Bit Score: 66.01 E-value: 1.88e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 507 EVYLTGSFINWKctlKCEKLVSGKKG--VTVNLTRGRHEFRFMINGEWATSSDYQQVPNGLGGQNNIIFV 574
Cdd:pfam16561 13 KVYVTGSFDNWK---KKIPLQKSGGDftTILDLPPGTHQYKFIVDGEWRHDPDLPTATDDMGNLNNYIEV 79
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
161-428 |
6.23e-11 |
|
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: 65.46 E-value: 6.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 161 GRDSEKEKNDRQLEKLRNRNDELKIRVKEYKSDLSAAQLKVKNLEKKLESA--QSADSEEKFVRIDSEID---------E 229
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELsrQISALRKDLARLEAEVEqleeriaqlS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 230 KRSQDHDEEINNLHNVIEELRNKLATVESKNKDLETKfsenqdyLKNAKDKVTFLENQLNSdAHEEVKSTAVRALEVKLG 309
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ-------IEQLKEELKALREALDE-LRAELTLLNEEAANLRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 310 LANNSiRQAEAEKQQLQEANWYANERVGKLEQENGYLKGITEQL-KARADTSHAEKMLKDSEKRVWEINEEKSKLEWRLG 388
Cdd:TIGR02168 826 LESLE-RRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIeELESELEALLNERASLEEALALLRSELEELSEELR 904
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 25151865 389 ELSQWWNDAKWKVGELESSVALQRNLLDTANSKIQSLNDQ 428
Cdd:TIGR02168 905 ELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQER 944
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
155-390 |
2.98e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.08 E-value: 2.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 155 ISEESEGRDSEKEKNDRQLEKLRNRNDELKIRVKEYKSDLSAAQLKVKNLE--KKLESAQSADSE--EKFVRIDSEIdEK 230
Cdd:PRK03918 236 LKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKelKEKAEEYIKLSEfyEEYLDELREI-EK 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 231 RSQDHDEEINNLHNVIEELRNKlatvESKNKDLETKFSENQDYLKNAKDKVtflenqlnsDAHEEVKSTAVRALEVKLGL 310
Cdd:PRK03918 315 RLSRLEEEINGIEERIKELEEK----EERLEELKKKLKELEKRLEELEERH---------ELYEEAKAKKEELERLKKRL 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 311 ANNSIRQAEAEKQQLQEANWYANERVGKLEQENGYLKGITEQLKA----------------RADTSHAEKML-------- 366
Cdd:PRK03918 382 TGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKaieelkkakgkcpvcgRELTEEHRKELleeytael 461
|
250 260
....*....|....*....|....
gi 25151865 367 KDSEKRVWEINEEKSKLEWRLGEL 390
Cdd:PRK03918 462 KRIEKELKEIEEKERKLRKELREL 485
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
157-392 |
7.84e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.79 E-value: 7.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 157 EESEGRDSEKEKNDRQLEKLRNRNDELKIRVKEYKSDLSAAQLKVKNLEKKLESAQ--SADSEEKFVRIDSEIDE--KRS 232
Cdd:COG1196 253 AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEerRRELEERLEELEEELAEleEEL 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 233 QDHDEEINNLHNVIEELRNKLATVESKNKDLETKFSE-NQDYLKNAKDKVTFLENQLNSDAHEEVKSTAVRALEVKLGLA 311
Cdd:COG1196 333 EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEaEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 312 NNSIRQAEAEKQQLQEANwyANERVGKLEQENGYLKGITEQLKARADTSHAEKMLKDSEKRVWEINEEKSKLEWRLGELS 391
Cdd:COG1196 413 LERLERLEEELEELEEAL--AELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAA 490
|
.
gi 25151865 392 Q 392
Cdd:COG1196 491 A 491
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
152-425 |
1.07e-08 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 57.60 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 152 NVNISEESEGRDSEKEKNDRQLEKLRNRNDELKIRVKEYKSDLSAAQLKVKNLEKKLES------AQSADSEEKFVRI-- 223
Cdd:pfam07888 54 NRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEElseekdALLAQRAAHEARIre 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 224 ---DSEIDEKRSQDHDEEINNLHNVIEELRNKLATVESKNKDLETKFSENQDYLKNAKDKVTFLENQL-NSDAHEEVKST 299
Cdd:pfam07888 134 leeDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLaQRDTQVLQLQD 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 300 AVRALEVKLGLANNSIRQAEAEKQQLQEanwyANERVGKLEQENGYLKGITEQLKARADTSHAEkmLKDSEKRVWEINEE 379
Cdd:pfam07888 214 TITTLTQKLTTAHRKEAENEALLEELRS----LQERLNASERKVEGLGEELSSMAAQRDRTQAE--LHQARLQAAQLTLQ 287
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 25151865 380 --KSKLEWRLGElSQWWNDAKwkvgELESSVALQRNLLDTANSKIQSL 425
Cdd:pfam07888 288 laDASLALREGR-ARWAQERE----TLQQSAEADKDRIEKLSAELQRL 330
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
156-406 |
2.33e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.00 E-value: 2.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 156 SEESEGRDSEKEKndrQLEKLRNRNDELKIRVKEYKSDLSAAQLKVKNLEKKLESAQSADSEEKFVridseidEKRSQDH 235
Cdd:PRK03918 188 TENIEELIKEKEK---ELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESL-------EGSKRKL 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 236 DEEINNLHNVIEELRNKLATVESKNKDLETKFSENQDYLKNAKDKVTFLENQLNSDAHEEVKSTAVRALEVKLGLANNSI 315
Cdd:PRK03918 258 EEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 316 RQAEAEKQQLQEANwyanERVGKLE------QENGYLKGITEQLKARA---DTSHAEKMLKDSEKRVWEINEEKSKLEWR 386
Cdd:PRK03918 338 ERLEELKKKLKELE----KRLEELEerhelyEEAKAKKEELERLKKRLtglTPEKLEKELEELEKAKEEIEEEISKITAR 413
|
250 260
....*....|....*....|
gi 25151865 387 LGELSQWWNDAKWKVGELES 406
Cdd:PRK03918 414 IGELKKEIKELKKAIEELKK 433
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
154-384 |
3.20e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.61 E-value: 3.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 154 NISEESEGRDSEK-EKNDRQLEKLRNRNDELKIRVKEYKSDLSaaqlKVKNLEKKLESaqsadseekfvrIDSEIDEKrs 232
Cdd:PRK03918 507 ELEEKLKKYNLEElEKKAEEYEKLKEKLIKLKGEIKSLKKELE----KLEELKKKLAE------------LEKKLDEL-- 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 233 qdhDEEINNLHNVIEELRNK-LATVESKNKDLEtKFSENQDYLKNAKDKVTFLENQLNSDAHEEVKSTAvralevKLGLA 311
Cdd:PRK03918 569 ---EEELAELLKELEELGFEsVEELEERLKELE-PFYNEYLELKDAEKELEREEKELKKLEEELDKAFE------ELAET 638
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25151865 312 NNSIRQAEAEKQQL-----QEANWYANERVGKLEQENGYLKGITEQLKARADTshAEKMLKDSEKRVWEINEEKSKLE 384
Cdd:PRK03918 639 EKRLEELRKELEELekkysEEEYEELREEYLELSRELAGLRAELEELEKRREE--IKKTLEKLKEELEEREKAKKELE 714
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
121-392 |
4.82e-08 |
|
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: 56.23 E-value: 4.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 121 RSQKVYAAGKTRARSTSKKNQPRSQFDAQPENvnISEESEGRDSEKEKNDRQLEKLRNRNDELKIRVKEYKSDLSAA-QL 199
Cdd:TIGR02169 217 LKEKREYEGYELLKEKEALERQKEAIERQLAS--LEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRvKE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 200 KVKNLEKKLESAQSADSEEKFVRIDSEideKRSQDHDEEINN---------------------LHNVIEELRNKLATVES 258
Cdd:TIGR02169 295 KIGELEAEIASLERSIAEKERELEDAE---ERLAKLEAEIDKllaeieelereieeerkrrdkLTEEYAELKEELEDLRA 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 259 KNKDLETKFSENQDYLKNAKDKVTFLENQLNSDAHEEVK-STAVRALEVKLGLANNSIRQAEAEKQQLQEANWYANERVG 337
Cdd:TIGR02169 372 ELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRlQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIK 451
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 25151865 338 KLEQEngylkgiTEQLKAradtshaekMLKDSEKRVWEINEEKSKLEWRLGELSQ 392
Cdd:TIGR02169 452 KQEWK-------LEQLAA---------DLSKYEQELYDLKEEYDRVEKELSKLQR 490
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
138-369 |
5.87e-08 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 55.41 E-value: 5.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 138 KKNQPRSQFDAQPENVNiseesegrdSEKEKNDRQLEKLRNRNDELKIRVKEYKSDLSAAQLKVKNLEKKLESAQSA--D 215
Cdd:PHA02562 189 KIDHIQQQIKTYNKNIE---------EQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAAlnK 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 216 SEEKFVRIDSEID-----EKRSQDHDEEINNLHNvIEELRNKLATVESKNKDLETKFSEnqdyLKNAKDKVTFLENQLN- 289
Cdd:PHA02562 260 LNTAAAKIKSKIEqfqkvIKMYEKGGVCPTCTQQ-ISEGPDRITKIKDKLKELQHSLEK----LDTAIDELEEIMDEFNe 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 290 -SDAHEEVKsTAVRALEVKLGLANNSIRQAEAEKQQLQEANWYANERVGKLEQEngyLKGITEQL----KARADTSHAEK 364
Cdd:PHA02562 335 qSKKLLELK-NKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDE---LDKIVKTKselvKEKYHRGIVTD 410
|
....*
gi 25151865 365 MLKDS 369
Cdd:PHA02562 411 LLKDS 415
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
167-406 |
7.96e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.46 E-value: 7.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 167 EKNDRQLEKLRNRNDELKIRVKEYKSDLSAA---QLKVKNLEKKLESAQSADSE--EKFVRIDSEIDEKRSQdhDEEINN 241
Cdd:PRK03918 158 DDYENAYKNLGEVIKEIKRRIERLEKFIKRTeniEELIKEKEKELEEVLREINEisSELPELREELEKLEKE--VKELEE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 242 LHNVIEELRNKLATVESKNKDLETKFSENQDYLKNAKDKVTFLENQLnsdahEEVKSTAVRALE-VKLGLANNSIRQAEA 320
Cdd:PRK03918 236 LKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKV-----KELKELKEKAEEyIKLSEFYEEYLDELR 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 321 EKQqlqeanwyanERVGKLEQEngyLKGITEQLKAradtshaekmLKDSEKRVWEINEEKSKLEWRLGELSQW---WNDA 397
Cdd:PRK03918 311 EIE----------KRLSRLEEE---INGIEERIKE----------LEEKEERLEELKKKLKELEKRLEELEERhelYEEA 367
|
....*....
gi 25151865 398 KWKVGELES 406
Cdd:PRK03918 368 KAKKEELER 376
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
154-298 |
9.25e-08 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 53.39 E-value: 9.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 154 NISEESEGRDSEKEKNDRQLEKLRNRNDELKIRVKEYKSDLSAAQLKVKNLEKKLESAQSAdseEKFVRIDSEID--EKR 231
Cdd:COG1579 28 ELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN---KEYEALQKEIEslKRR 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25151865 232 SQDHDEEINNLHNVIEELRNKLATVESKNKDLETKFSENQDYLKNAKDKVTFLENQLNSDAHEEVKS 298
Cdd:COG1579 105 ISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
136-392 |
9.27e-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: 55.03 E-value: 9.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 136 TSKKNQPRSQFDAQPE-NVNISEESEGRDSEKEKNDRQLEKLRNRNDELKIRVKEYKSDLSAAQLKVKNLEKKLESAQSA 214
Cdd:TIGR04523 390 ESQINDLESKIQNQEKlNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQ 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 215 DS----EEKFVRIDSEIDEKRSQDHDEEINNLHNVIEELRNKLATVESKN-------KDLETKFSENQDYLKNAKDKVTF 283
Cdd:TIGR04523 470 LKvlsrSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKIsslkekiEKLESEKKEKESKISDLEDELNK 549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 284 LENQLNSDAHEEVKSTAVRALEvKLGLANNSIRQAEAEKQqlqeanwyanERVGKLEQENGYLkgITEQLKARADTSHAE 363
Cdd:TIGR04523 550 DDFELKKENLEKEIDEKNKEIE-ELKQTQKSLKKKQEEKQ----------ELIDQKEKEKKDL--IKEIEEKEKKISSLE 616
|
250 260
....*....|....*....|....*....
gi 25151865 364 KMLKDSEKRVWEINEEKSKLEWRLGELSQ 392
Cdd:TIGR04523 617 KELEKAKKENEKLSSIIKNIKSKKNKLKQ 645
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
150-315 |
1.36e-07 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 54.48 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 150 PENVNISEESEGRDSEKE--KNDRQLEKLRNRNDELKIRVKEYKSdlsaaqlKVKNLEKKLESAQSadseekfvRIDSEI 227
Cdd:COG2433 397 AEREKEHEERELTEEEEEirRLEEQVERLEAEVEELEAELEEKDE-------RIERLERELSEARS--------EERREI 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 228 DEkrsqdhDEEINNLHNVIEELRNKLATVESKNKDLETKFSEnqdyLKNAKDKVtFLENQLNSDAHEEVKSTAVRALEVK 307
Cdd:COG2433 462 RK------DREISRLDREIERLERELEEERERIEELKRKLER----LKELWKLE-HSGELVPVKVVEKFTKEAIRRLEEE 530
|
....*...
gi 25151865 308 LGLANNSI 315
Cdd:COG2433 531 YGLKEGDV 538
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
163-384 |
2.54e-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: 2.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 163 DSEKEKNDRQLEKLRNRNDELKIRVKEYKSDLSAAQLKVKNLEKKLESAQSADSEEKFVRIDSEIDEKRSQDHDEEIN-- 240
Cdd:TIGR02169 783 DLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNgk 862
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 241 --NLHNVIEELRNKLATVESKNKDLETKFSENQDYLKNAKDKvtflENQLNSDAheEVKSTAVRALEVKLGLANNSIRQA 318
Cdd:TIGR02169 863 keELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERK----IEELEAQI--EKKRKRLSELKAKLEALEEELSEI 936
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25151865 319 EAEKQQLQEANwYANERVGKLEQEngyLKGITEQLKARADTSH-AEKMLKDSEKRVWEINEEKSKLE 384
Cdd:TIGR02169 937 EDPKGEDEEIP-EEELSLEDVQAE---LQRVEEEIRALEPVNMlAIQEYEEVLKRLDELKEKRAKLE 999
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
155-358 |
3.88e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.14 E-value: 3.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 155 ISEESEGRDSEKEKNDRQLEKLRNRNDELKIRVKEYKSDLSAAQLKVKNLEKKLES--AQSADSEEKFVRIDSEIDEKRS 232
Cdd:TIGR02168 307 LRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEEleAELEELESRLEELEEQLETLRS 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 233 qdhdeEINNLHNVIEELRNKLATVESKNKDLE---TKFSENQDYLKNAKDKVTFLENQLNSDAHEEVKSTA---VRALEV 306
Cdd:TIGR02168 387 -----KVAQLELQIASLNNEIERLEARLERLEdrrERLQQEIEELLKKLEEAELKELQAELEELEEELEELqeeLERLEE 461
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 25151865 307 KLGLANNSIRQAEAEKQQLQEANWYANERVGKLE--QEN--GYLKGITEQLKARAD 358
Cdd:TIGR02168 462 ALEELREELEEAEQALDAAERELAQLQARLDSLErlQENleGFSEGVKALLKNQSG 517
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
93-390 |
7.30e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.37 E-value: 7.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 93 ADYSKANDAFEKNISAVQKLFAAAglggrSQKVYAAGKTRARSTSKKNQPRSQFD-AQPENVNISEESEGRDSEKEKNDR 171
Cdd:TIGR02168 701 AELRKELEELEEELEQLRKELEEL-----SRQISALRKDLARLEAEVEQLEERIAqLSKELTELEAEIEELEERLEEAEE 775
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 172 QLEKLRNRNDELKIRVKEYKSDLSAAQLKVKNLEKKLeSAQSADSEEKFVRIDSEidEKRSQDHDEEINNLHNVIEELRN 251
Cdd:TIGR02168 776 ELAEAEAEIEELEAQIEQLKEELKALREALDELRAEL-TLLNEEAANLRERLESL--ERRIAATERRLEDLEEQIEELSE 852
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 252 KLATVESKNKDLETKFSENQDYLKNAKDKVTFLENQLNSDAHEEvkstavRALEVKLGLANNSIRQAEAEKQQLQEANWY 331
Cdd:TIGR02168 853 DIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSEL------EELSEELRELESKRSELRRELEELREKLAQ 926
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 25151865 332 ANERVGKLEQEngyLKGITEQLkaradTSHAEKMLKDSEKRVWEINEEKSKLEWRLGEL 390
Cdd:TIGR02168 927 LELRLEGLEVR---IDNLQERL-----SEEYSLTLEEAEALENKIEDDEEEARRRLKRL 977
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
162-359 |
9.69e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.96 E-value: 9.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 162 RDSEKEKNDRQLEKLRNRNDELKIRVKEYKSDLSAAQLKVKNL-----------EKKLESAQSADSEEKFVRIDSEIDEK 230
Cdd:PRK02224 500 RAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELreraaeleaeaEEKREAAAEAEEEAEEAREEVAELNS 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 231 RSQDHDEEINNLHNV------IEELRNKLATVESKNKDLETKFSENQDYLKNAKDKVTFLENQLNSDAHEEVKSTAVRAl 304
Cdd:PRK02224 580 KLAELKERIESLERIrtllaaIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARIEEAREDKERA- 658
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 25151865 305 EVKLGLANNSIRQAEAEKQQLQeanwyanERVGKLEQENGYLKGITEQLKARADT 359
Cdd:PRK02224 659 EEYLEQVEEKLDELREERDDLQ-------AEIGAVENELEELEELRERREALENR 706
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
160-428 |
1.12e-06 |
|
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: 51.97 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 160 EGRDSEKEKNDRQLEKLRNRNDELKIRVKEYKSDLSAAQLKVKNLEKKLESA---------------QSADSEEKFVRID 224
Cdd:TIGR00606 733 PGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAkvcltdvtimerfqmELKDVERKIAQQA 812
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 225 SEIDekrSQDHDEEINNLHNVIEELRNKLATVESKNKDLETKFSENQDYLKNAKDKVTFLEN---QLNSDAHE------- 294
Cdd:TIGR00606 813 AKLQ---GSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSeklQIGTNLQRrqqfeeq 889
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 295 -EVKSTAVRALEVKLGLANNSIRQAEAEKQQLQEANwyaNERVGKLEQENGYLKGITEQLKARADTSHAEkmLKDSEKRV 373
Cdd:TIGR00606 890 lVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEK---EELISSKETSNKKAQDKVNDIKEKVKNIHGY--MKDIENKI 964
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 25151865 374 WEINEE-KSKLEWRLGELSQWWNDAKWKVGELESSVALQRNLLDTANSKIQSLNDQ 428
Cdd:TIGR00606 965 QDGKDDyLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDN 1020
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
163-428 |
1.45e-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: 51.22 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 163 DSEKEKNDRQLEKLRNRNDELKIRVKEYKSDLSAAQ------LKVKNLEKKLE-------SAQSADSEEKFVRIDSEIDE 229
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRrerekaERYQALLKEKReyegyelLKEKEALERQKEAIERQLAS 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 230 KRSQ--DHDEEINNLHNVIEELRNKLATVESKNKDL--------ETKFSENQDYLKNAKDKVTFLENQLnSDAHEEVKST 299
Cdd:TIGR02169 249 LEEEleKLTEEISELEKRLEEIEQLLEELNKKIKDLgeeeqlrvKEKIGELEAEIASLERSIAEKEREL-EDAEERLAKL 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 300 AVRALEVKLGLAN--NSIRQAEAEKQQLQeanwyanERVGKLEQENGYLKGITEQLKARADTSHAEkmLKDSEKRVWEIN 377
Cdd:TIGR02169 328 EAEIDKLLAEIEEleREIEEERKRRDKLT-------EEYAELKEELEDLRAELEEVDKEFAETRDE--LKDYREKLEKLK 398
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25151865 378 EE--------------KSKLEWRLGELSQWWNDAKWKVGELESSVALQRNLLDTANSKIQSLNDQ 428
Cdd:TIGR02169 399 REinelkreldrlqeeLQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAAD 463
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
165-385 |
1.57e-06 |
|
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: 51.27 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 165 EKEKNDRQLEKlrnrnDELKIRVKEYKSDLSAAQLKVKNLEkkLESAQSADSEEKFVRIDSEIDEKRSQDHDE------E 238
Cdd:pfam15921 596 EKEINDRRLEL-----QEFKILKDKKDAKIRELEARVSDLE--LEKVKLVNAGSERLRAVKDIKQERDQLLNEvktsrnE 668
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 239 INNLHNVIEEL----RNKLATVESKNKDLETKFSENQDYLKNAKDKVTFLENqlnSDAHE-----------EVKSTAVRA 303
Cdd:pfam15921 669 LNSLSEDYEVLkrnfRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEG---SDGHAmkvamgmqkqiTAKRGQIDA 745
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 304 LEVKLGLANNSIRQAEAEKQQLQEANWYANERVGKLEQENGYLKGITEQLKARadtshaEKMLKDSEKRVwEINEEKSKL 383
Cdd:pfam15921 746 LQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQ------ERRLKEKVANM-EVALDKASL 818
|
..
gi 25151865 384 EW 385
Cdd:pfam15921 819 QF 820
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
170-384 |
1.72e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.09 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 170 DRQLEKLRN------RNDELKIRVKEYKSDLSAAQLKVKNLEKKLESAQSADSEEKFVR-------IDSEIDEKRSQDH- 235
Cdd:COG1196 199 ERQLEPLERqaekaeRYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEEleaelaeLEAELEELRLELEe 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 236 -DEEINNLHNVIEELRNKLATVESKNKDLETKFSENQDYLKNAKDKVTFLENQLNSDAHEEVKSTA-VRALEVKLGLANN 313
Cdd:COG1196 279 lELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEeLEEAEEELEEAEA 358
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25151865 314 SIRQAEAEKQQLQEAnwyANERVGKLEQEN-GYLKGITEQLKARADTSHAEKMLKDSEKRVWEINEEKSKLE 384
Cdd:COG1196 359 ELAEAEEALLEAEAE---LAEAEEELEELAeELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELE 427
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
151-436 |
2.28e-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: 50.79 E-value: 2.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 151 ENVNISEESEGRDSEKEKNDRQLEKLRNRNDELKIRVKEYKSDlsaaqlKVKNLEKKLESaQSADSEEKFVRIDSEIDEK 230
Cdd:TIGR04523 261 EQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQ------KEQDWNKELKS-ELKNQEKKLEEIQNQISQN 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 231 RSQdhdeeINNLHNVIEELRNKLATVESKNKDLETKFSENQDYLKNAKDkvtflENQLNSDAHEEVKSTaVRALEVKL-- 308
Cdd:TIGR04523 334 NKI-----ISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKK-----ENQSYKQEIKNLESQ-INDLESKIqn 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 309 -----GLANNSIRQAEAEKQQLQ-------EANWYANERVGKLEQENGYLKGITEQLKARadTSHAEKMLKDSEKrvwEI 376
Cdd:TIGR04523 403 qeklnQQKDEQIKKLQQEKELLEkeierlkETIIKNNSEIKDLTNQDSVKELIIKNLDNT--RESLETQLKVLSR---SI 477
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 377 NEEKSKLEWRLGELSQwwndakwKVGELESSVALQRNLldtaNSKIQSLNDQSHSSTMTI 436
Cdd:TIGR04523 478 NKIKQNLEQKQKELKS-------KEKELKKLNEEKKEL----EEKVKDLTKKISSLKEKI 526
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
162-428 |
2.55e-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: 50.40 E-value: 2.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 162 RDSEKEKNDRQLEKLRNRNDELKIRVKEYKSDLSAAQLKVKNLEKKLESAQSADSEEKFVRIDSEIDEKRSqdhdeEINN 241
Cdd:TIGR04523 169 EELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQ-----EINE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 242 LHNVIEELRNKLATVESKNKDLETKFSENQDYLKNAKDKVTFLENQLN--------------SDAHEEVKS------TAV 301
Cdd:TIGR04523 244 KTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNqlkseisdlnnqkeQDWNKELKSelknqeKKL 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 302 RALEVKLGLANNSIRQ--------------AEAEKQQLQEANWYANERVGKLEQENGYLKGITEQLKARADT-----SHA 362
Cdd:TIGR04523 324 EEIQNQISQNNKIISQlneqisqlkkeltnSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDleskiQNQ 403
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25151865 363 EKMLKDSEKRVWEINEEKSKLEWRLGELSQWWNDAKWKVGELESSVALQRNLLDTANSKIQSLNDQ 428
Cdd:TIGR04523 404 EKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQ 469
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
222-384 |
3.30e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.38 E-value: 3.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 222 RIDSEIDEKRSQ--DHDEEINNLHNVIEELRNKLATVESKNKDLETKFSENQDYLKNAKDKVTFLENQLNSdaheeVKST 299
Cdd:COG1579 14 ELDSELDRLEHRlkELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGN-----VRNN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 300 -AVRALEVKLGLANNsiRQAEAEKQQLQeanwyANERVGKLEQEngyLKGITEQLKARADTSHAEKmlKDSEKRVWEINE 378
Cdd:COG1579 89 kEYEALQKEIESLKR--RISDLEDEILE-----LMERIEELEEE---LAELEAELAELEAELEEKK--AELDEELAELEA 156
|
....*.
gi 25151865 379 EKSKLE 384
Cdd:COG1579 157 ELEELE 162
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
154-427 |
3.88e-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: 50.02 E-value: 3.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 154 NISEESEGRDSEKEKNDRQLEKLRNRNDELKIRVKEYKSDLSA-AQLKVKNLEKKLESaQSADSEEKFVRIDSEIDEKRS 232
Cdd:TIGR04523 257 QLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDlNNQKEQDWNKELKS-ELKNQEKKLEEIQNQISQNNK 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 233 QdhdeeINNLHNVIEELRNKLATVESKNKDLETKFSENQDYLKNAKDkvtflENQLNSDAHEEVKSTaVRALEVKL---- 308
Cdd:TIGR04523 336 I-----ISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKK-----ENQSYKQEIKNLESQ-INDLESKIqnqe 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 309 ---GLANNSIRQAEAEKQQLQ-------EANWYANERVGKLEQENGYLKGITEQL-------------------KARADT 359
Cdd:TIGR04523 405 klnQQKDEQIKKLQQEKELLEkeierlkETIIKNNSEIKDLTNQDSVKELIIKNLdntresletqlkvlsrsinKIKQNL 484
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25151865 360 SHAEKMLKDSEKRVWEINEEKSKLEWRLGELSQWWNDAKWKVGELESSVALQRNLLDTANSKIQSLND 427
Cdd:TIGR04523 485 EQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDF 552
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
166-367 |
3.94e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 3.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 166 KEKNDRQLEKLRNRNDELKIRVKEYKsdlsAAQLKVKNLEKKLESAQSADSEekfvrIDSEIDEKRSQdhdEEINNLHNV 245
Cdd:COG4717 66 PELNLKELKELEEELKEAEEKEEEYA----ELQEELEELEEELEELEAELEE-----LREELEKLEKL---LQLLPLYQE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 246 IEELRNKLATVESKNKDLETKFSEnqdyLKNAKDKVTFLENQLnsdahEEVKSTAVRALEVKLGLANNSIRQAEAEKQQL 325
Cdd:COG4717 134 LEALEAELAELPERLEELEERLEE----LRELEEELEELEAEL-----AELQEELEELLEQLSLATEEELQDLAEELEEL 204
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 25151865 326 QEANWYANERVGKLEQENGYLKGITEQLKARADTSHAEKMLK 367
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLK 246
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
171-425 |
4.23e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.94 E-value: 4.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 171 RQLEKLRNRNDELKIRVKEYKSDLSAAQLKVKNLEKKLESAQSADSE---------EKFVRIDSEID--EKRSQDHDEEI 239
Cdd:COG1196 232 LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEEleleleeaqAEEYELLAELArlEQDIARLEERR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 240 NNLHNVIEELRNKLATVESKNKDLETKFSENQDYLKNAKDKVTFLENQLnsdahEEVKSTAVRALEVKLGLANNSIRQAE 319
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL-----AEAEEALLEAEAELAEAEEELEELAE 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 320 AEKQQLQEANWYANERVGKLEQENGYLKGITEQLKARAdtSHAEKMLKDSEKRVWEINEEKSKLEWRLGELSQwWNDAKW 399
Cdd:COG1196 387 ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELE--ELEEALAELEEEEEEEEEALEEAAEEEAELEEE-EEALLE 463
|
250 260
....*....|....*....|....*.
gi 25151865 400 KVGELESSVALQRNLLDTANSKIQSL 425
Cdd:COG1196 464 LLAELLEEAALLEAALAELLEELAEA 489
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
181-388 |
9.26e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.88 E-value: 9.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 181 DELKIRVKEYKSDLSAAQLKVKNLEKKLESAQSADSEEKfvRIDS-----EIDEKRSQDHDEEINNLHNVIEELRNKLAT 255
Cdd:PRK02224 471 EEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAED--RIERleerrEDLEELIAERRETIEEKRERAEELRERAAE 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 256 VESKNKDLETKFSENQDYLKNAKDKVTFLENQLnsdahEEVKST--AVRALEVKLGLANNSIRQAEA--EK-QQLQEANw 330
Cdd:PRK02224 549 LEAEAEEKREAAAEAEEEAEEAREEVAELNSKL-----AELKERieSLERIRTLLAAIADAEDEIERlrEKrEALAELN- 622
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25151865 331 yaNERVGKLEQENGYLKGITEQL------KARADTSHAEKMLKDSEKRVWEINEEKSKLEWRLG 388
Cdd:PRK02224 623 --DERRERLAEKRERKRELEAEFdearieEAREDKERAEEYLEQVEEKLDELREERDDLQAEIG 684
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
155-422 |
9.58e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.50 E-value: 9.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 155 ISEESEGRDSEKEKNDRQLEKLRNRNDELKIRVKEYKSDLSAAQLKVKNLEKKLESAQSADSEekfvrIDSEIDEKR--S 232
Cdd:PRK02224 263 LRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEE-----LRDRLEECRvaA 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 233 QDHDEEinnlhnvIEELRNKLATVESKNKDLETKFSENQDYLKNAKDKVTFLENQLnsdahEEVKStAVRALEVKLGLAN 312
Cdd:PRK02224 338 QAHNEE-------AESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEI-----EELEE-EIEELRERFGDAP 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 313 NSIRQAEAEKQQLQEANWYANERVGKLEQEngyLKGITEQL-KARA---------------DTSHAEKmLKDSEKRVWEI 376
Cdd:PRK02224 405 VDLGNAEDFLEELREERDELREREAELEAT---LRTARERVeEAEAlleagkcpecgqpveGSPHVET-IEEDRERVEEL 480
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 25151865 377 NEEKSKLEWRLGELSQWWNDAKwKVGELESSVALQRNLLDTANSKI 422
Cdd:PRK02224 481 EAELEDLEEEVEEVEERLERAE-DLVEAEDRIERLEERREDLEELI 525
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
186-428 |
1.06e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.50 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 186 RVKEYKSDLSAAQLKVKNLEkklesaqsADSEEKFVRIDSEIDEKRSQDhdeeinnLHNVIEELRNKLATVESknkDLEt 265
Cdd:PRK02224 163 KLEEYRERASDARLGVERVL--------SDQRGSLDQLKAQIEEKEEKD-------LHERLNGLESELAELDE---EIE- 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 266 KFSENQDYLKNAKDkvtflENQLNSDAHEEvKSTAVRALEVKLGLANNSIRQAEAEKQQLQEANWYANERVGKLEQENGY 345
Cdd:PRK02224 224 RYEEQREQARETRD-----EADEVLEEHEE-RREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDD 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 346 LKGIT-------EQLKARADT-----SHAEKMLKDSEKRVWEINEEKSKLEWRLGELSQWWNDAKWKVGELESSVALQRN 413
Cdd:PRK02224 298 LLAEAglddadaEAVEARREEledrdEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEARE 377
|
250
....*....|....*
gi 25151865 414 LLDTANSKIQSLNDQ 428
Cdd:PRK02224 378 AVEDRREEIEELEEE 392
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
171-327 |
1.73e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 171 RQLEKLRNRNDELKIRVKEYKSDLSAAQLKVKNLEKKLESAQSADSEEKFVRIDSEIDEKRSQ--DHDEEINNLHNV--- 245
Cdd:COG4913 255 EPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARldALREELDELEAQirg 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 246 -----IEELRNKLATVESKNKDLETKFSENQDYLKNAK-----DKVTFLENQLNSDAHEEVKSTAVRALEVKLGLANNSI 315
Cdd:COG4913 335 nggdrLEQLEREIERLERELEERERRRARLEALLAALGlplpaSAEEFAALRAEAAALLEALEEELEALEEALAEAEAAL 414
|
170
....*....|..
gi 25151865 316 RQAEAEKQQLQE 327
Cdd:COG4913 415 RDLRRELRELEA 426
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
164-419 |
2.05e-05 |
|
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: 47.07 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 164 SEKEKNDRQLEKLRNRNDELKIRVKEYKSDLSAAQLKVKNLEKKLESAqsadseekfvridseidEKRSQDHDEEINNLH 243
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAAL-----------------ARRIRALEQELAALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 244 NVIEELRNKLATVESKNKDLETKFSE--NQDYLKNAKDKVTFLenqLNSDAHEEvkstAVRALEVKLGLANNSIRQAEAE 321
Cdd:COG4942 83 AELAELEKEIAELRAELEAQKEELAEllRALYRLGRQPPLALL---LSPEDFLD----AVRRLQYLKYLAPARREQAEEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 322 KQQLQEanwyANERVGKLEQENGYLKGITEQLKARADTshAEKMLKDSEKRVWEINEEKSKLEWRLGELSQWWNDAKWKV 401
Cdd:COG4942 156 RADLAE----LAALRAELEAERAELEALLAELEEERAA--LEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
|
250
....*....|....*...
gi 25151865 402 GELESSVALQRNLLDTAN 419
Cdd:COG4942 230 ARLEAEAAAAAERTPAAG 247
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
157-289 |
3.32e-05 |
|
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: 46.16 E-value: 3.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 157 EESEGRDSEKEKNDRQLEKLrnrnDELKIRVKEYKSDLS--AAQLKvkNLEKKLESAQSADSE---EKFVRIDSEIDEKR 231
Cdd:smart00787 151 ENLEGLKEDYKLLMKELELL----NSIKPKLRDRKDALEeeLRQLK--QLEDELEDCDPTELDrakEKLKKLLQEIMIKV 224
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25151865 232 SQ--DHDEEINNLHNVIEELRNKLATVESKNKDLETKFSENQDY----LKNAKDKVTFLENQLN 289
Cdd:smart00787 225 KKleELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGFtfkeIEKLKEQLKLLQSLTG 288
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
170-327 |
4.83e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.92 E-value: 4.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 170 DRQLEKLRNRNDELKIRVKEYKSDLSAAQLKVKNLEKKLEsaqsaDSEEKFVRIDSEIDEKRSQ-DHDEE-INNLHNV-- 245
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELE-----DLEKEIKRLELEIEEVEARiKKYEEqLGNVRNNke 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 246 IEELRNKLATVESKNKDLETKFSENQDYLKNAKDKVTFLENQLnsDAHEEVKSTAVRALEVKLGLANNSIRQAEAEKQQL 325
Cdd:COG1579 91 YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAEL--AELEAELEEKKAELDEELAELEAELEELEAEREEL 168
|
..
gi 25151865 326 QE 327
Cdd:COG1579 169 AA 170
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
169-387 |
5.39e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 5.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 169 NDRQLEKLRNRNDELKIRVKEYKSDLSAAQLKVKNLEKKLESAQSADsEEKFVRIDseidekrSQDHDEEINNLHNVIEE 248
Cdd:COG4913 608 NRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLA-EYSWDEID-------VASAEREIAELEAELER 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 249 LRnklatvesknkdletkfsENQDYLKNAKDKVTFLENQLNsDAHEEvkstaVRALEVKLGLANNSIRQAEAEKQQLQEA 328
Cdd:COG4913 680 LD------------------ASSDDLAALEEQLEELEAELE-ELEEE-----LDELKGEIGRLEKELEQAEEELDELQDR 735
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 25151865 329 NWYANERVGKLEQENgylkgITEQLKARADTSHAEKMLKDSEKRVWEINEEKSKLEWRL 387
Cdd:COG4913 736 LEAAEDLARLELRAL-----LEERFAAALGDAVERELRENLEERIDALRARLNRAEEEL 789
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
233-390 |
5.90e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.92 E-value: 5.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 233 QDHDEEINNLHNVIEELRNKLATVESKNKDLETKFSENQDYLKNAKDKVTFLENQLnsdahEEVKSTAVRaLEVKLGLAN 312
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEI-----EEVEARIKK-YEEQLGNVR 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 25151865 313 NSiRQAEAEKQQLQeanwYANERVGKLEQEngyLKGITEQL-KARADTSHAEKMLKDSEKrvwEINEEKSKLEWRLGEL 390
Cdd:COG1579 87 NN-KEYEALQKEIE----SLKRRISDLEDE---ILELMERIeELEEELAELEAELAELEA---ELEEKKAELDEELAEL 154
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
154-406 |
9.46e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 9.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 154 NISEESEGRdsEKEKNDRQLEKLRNRNDELKIRVKEYKSDLSAAQLKVKNLEKKLESAQSADSEEKFVRidSEIDEkrsq 233
Cdd:PRK03918 376 RLKKRLTGL--TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCG--RELTE---- 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 234 DHDEEInnlhnvIEELRNKLATVESKNKDLETKFSEnqdyLKNAKDKV-TFLENQLNSDAHEEVkSTAVRALEVKLGLAN 312
Cdd:PRK03918 448 EHRKEL------LEEYTAELKRIEKELKEIEEKERK----LRKELRELeKVLKKESELIKLKEL-AEQLKELEEKLKKYN 516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 313 nsIRQAEAEKQQLQEANwyanERVGKLEQEngyLKGITEQLKARADTshaEKMLKDSEKRVWEINEEKSKLEWRLGELS- 391
Cdd:PRK03918 517 --LEELEKKAEEYEKLK----EKLIKLKGE---IKSLKKELEKLEEL---KKKLAELEKKLDELEEELAELLKELEELGf 584
|
250
....*....|....*
gi 25151865 392 QWWNDAKWKVGELES 406
Cdd:PRK03918 585 ESVEELEERLKELEP 599
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
155-428 |
1.03e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 45.60 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 155 ISEESEGRDSEKEKNDRQLEKLRNRNDELKIRVKEYKSDLSAAQLKVKNLEKKLESAqsadsEEKFVRIDSEIDEKRSQD 234
Cdd:pfam12128 271 ETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEAL-----EDQHGAFLDADIETAAAD 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 235 HDEEiNNLHNVIEELRNKLATVESKNKDLETKFseNQDYLKNAKDKVTFLENqlNSDAHEEVKSTAVRALEVklglANNS 314
Cdd:pfam12128 346 QEQL-PSWQSELENLEERLKALTGKHQDVTAKY--NRRRSKIKEQNNRDIAG--IKDKLAKIREARDRQLAV----AEDD 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 315 IRQAEAE-KQQLQEANWYANERVGKLEQENGYLKG------ITEQLKARADTS-----HAEKMLKDSEKRVWEINEEKSK 382
Cdd:pfam12128 417 LQALESElREQLEAGKLEFNEEEYRLKSRLGELKLrlnqatATPELLLQLENFderieRAREEQEAANAEVERLQSELRQ 496
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 25151865 383 LEWRLGELSQWWNDAKWKVGELESSVA-LQRNLLDTANSKIQSLNDQ 428
Cdd:pfam12128 497 ARKRRDQASEALRQASRRLEERQSALDeLELQLFPQAGTLLHFLRKE 543
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
155-423 |
1.27e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.51 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 155 ISEESEGRDSEKEKNDRQLEKLRNRNDELKIRVKEYKSDLSAAQLKVKNLEKKLESAQS--ADSEEKFVRIDSEIDEKRS 232
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEqlQAAQAELAQAQEELESLQE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 233 Q--DHDEEINNLHNVIEELRNKLATVESKNKDLETKFSENQDYLKNAKDKVTFLENQ---LNSDAHEEVKSTAVRALEVK 307
Cdd:COG4372 109 EaeELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEElaaLEQELQALSEAEAEQALDEL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 308 LGLAN-NSIRQAEAEKQQLQEANWYANERVGKLEQENGYLKGITEQLKARADTSHAEKMLKDSEKRVWEINEEKSKLEWR 386
Cdd:COG4372 189 LKEANrNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAIL 268
|
250 260 270
....*....|....*....|....*....|....*..
gi 25151865 387 LGELSQWWNDAKWKVGELESSVALQRNLLDTANSKIQ 423
Cdd:COG4372 269 VEKDTEEEELEIAALELEALEEAALELKLLALLLNLA 305
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
154-416 |
1.47e-04 |
|
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: 44.71 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 154 NISEESEGRDSEKEKNdRQLEKLRNRNDELKIRVKEYKSDLSAAQLKVKnlekklesAQSADSEEKF-VRIDSEIDEKRS 232
Cdd:pfam05483 158 NLLKETCARSAEKTKK-YEYEREETRQVYMDLNNNIEKMILAFEELRVQ--------AENARLEMHFkLKEDHEKIQHLE 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 233 QDHDEEINNLHNVIEELRNKLATVESKNKDLETKFSENQDYLKNAKDKVTFL-EN--QLNSDAH------EEVKSTAVR- 302
Cdd:pfam05483 229 EEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQdENlkELIEKKDhltkelEDIKMSLQRs 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 303 -----ALEVKLGLANNSIRQAEAEKQ-QLQEANwyanervgKLEQENGYLkgITEqlkARADTSHAEKMLKDSEKRVwEI 376
Cdd:pfam05483 309 mstqkALEEDLQIATKTICQLTEEKEaQMEELN--------KAKAAHSFV--VTE---FEATTCSLEELLRTEQQRL-EK 374
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 25151865 377 NEEKSKL--------EWRLGELSQWWNDAKWKVGELESSVALQRNLLD 416
Cdd:pfam05483 375 NEDQLKIitmelqkkSSELEEMTKFKNNKEVELEELKKILAEDEKLLD 422
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
165-280 |
1.63e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 165 EKEKNDRQLEKLRNRNDELKIRVKEYKSdlsaAQLKVKNLEKKLESAQSADSEEKfvRIDSEIDEKRSQDHDEEINNLHN 244
Cdd:COG4717 133 ELEALEAELAELPERLEELEERLEELRE----LEEELEELEAELAELQEELEELL--EQLSLATEEELQDLAEELEELQQ 206
|
90 100 110
....*....|....*....|....*....|....*.
gi 25151865 245 VIEELRNKLATVESKNKDLETKFSENQDYLKNAKDK 280
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| E_set_Isoamylase_like_N |
cd07184 |
N-terminal Early set domain associated with the catalytic domain of isoamylase-like (also ... |
497-569 |
1.95e-04 |
|
N-terminal Early set domain associated with the catalytic domain of isoamylase-like (also called glycogen 6-glucanohydrolase) proteins; E or "early" set domains are associated with the catalytic domain of isoamylase-like proteins at the N-terminal end. Isoamylase is one of the starch-debranching enzymes that catalyze the hydrolysis of alpha-1,6-glucosidic linkages specific in alpha-glucans such as amylopectin or glycogen. Isoamylase contains a bound calcium ion, but this is not in the same position as the conserved calcium ion that has been reported in other alpha-amylase family enzymes. The N-terminal domain of isoamylase may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end and may be involved in homodimeric/tetrameric/dodecameric interactions. Members of this family include members of the alpha amylase family, sialidase, galactose oxidase, cellulase, cellulose, hyaluronate lyase, chitobiase, and chitinase. This domain is also a member of the CBM48 (Carbohydrate Binding Module 48) family whose members include pullulanase, maltooligosyl trehalose synthase, starch branching enzyme, glycogen branching enzyme, glycogen debranching enzyme, and the beta subunit of AMP-activated protein kinase.
Pssm-ID: 199892 [Multi-domain] Cd Length: 86 Bit Score: 40.30 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 497 VTLTISNTE--QEVYLTGSFINWkcTLKCEKLVSGKKG---VTVNLTRG-RHEFRFMINGE-WATssDYQQ---VPNGLG 566
Cdd:cd07184 3 VTFELPAEQgaDSVSLVGDFNDW--DPQATPMKKLKNGtfsATLDLPAGrEYQFRYLIDGErWVN--DPEAdayAPNGFG 78
|
...
gi 25151865 567 GQN 569
Cdd:cd07184 79 EEN 81
|
|
| E_set |
cd02688 |
Early set domain associated with the catalytic domain of sugar utilizing enzymes at either the ... |
497-572 |
2.10e-04 |
|
Early set domain associated with the catalytic domain of sugar utilizing enzymes at either the N or C terminus; The E or "early" set domains of sugar utilizing enzymes are associated with different types of catalytic domains at either the N-terminal or C-terminal end. These domains may be related to the immunoglobulin and/or fibronectin type III superfamilies. Members of this family include alpha amylase, sialidase, galactose oxidase, cellulase, cellulose, hyaluronate lyase, chitobiase, and chitinase. A subset of these members were recently identified as members of the CBM48 (Carbohydrate Binding Module 48) family. Members of the CBM48 family include pullulanase, maltooligosyl trehalose synthase, starch branching enzyme, glycogen branching enzyme, glycogen debranching enzyme, isoamylase, and the beta subunit of AMP-activated protein kinase.
Pssm-ID: 199878 [Multi-domain] Cd Length: 82 Bit Score: 40.22 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 497 VTLTISNTEQE-VYLTGSFINWK--CTLKCEKLVSGKKGVTVNLTRGRHEFRFMING--EWATSSDYQQVPNGLGGQNNI 571
Cdd:cd02688 2 VTFRIFAPGAKsVYLIGSFNGWWqaQALPMTKNGGGVWSATIPLPLGTYEYKYVIDGgkNVLPYFDPYYVAGDGNSGASI 81
|
.
gi 25151865 572 I 572
Cdd:cd02688 82 V 82
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
96-269 |
2.58e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.88 E-value: 2.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 96 SKANDAFEKNISAVQKLFAAAGLGGRSQKVyaagktrARSTSKKNQPRSQFDAQPENVNISEESegrDSEKEKNDRQLEK 175
Cdd:PRK02224 541 ELRERAAELEAEAEEKREAAAEAEEEAEEA-------REEVAELNSKLAELKERIESLERIRTL---LAAIADAEDEIER 610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 176 LRNRNDELKIRVKEYKSDLSAAQLKVKNLEKK-----LESAQS--ADSEEKFVRIDSEIDEKRSQDHD--EEINNLHNVI 246
Cdd:PRK02224 611 LREKREALAELNDERRERLAEKRERKRELEAEfdearIEEAREdkERAEEYLEQVEEKLDELREERDDlqAEIGAVENEL 690
|
170 180
....*....|....*....|....*.
gi 25151865 247 ---EELRNKLATVESKNKDLETKFSE 269
Cdd:PRK02224 691 eelEELRERREALENRVEALEALYDE 716
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
166-379 |
2.83e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 43.76 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 166 KEKNDRQLEKLRNRN----DELKI--------RVKEYKSDLSAAQLKVKNLEKKLESAQSADSEEKFVRIDS--EIDEKR 231
Cdd:PRK05771 15 KSYKDEVLEALHELGvvhiEDLKEelsnerlrKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVKSLEEliKDVEEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 232 SQDHDEEINNLHNVIEELRNKLATVESKNKDLE--TKFSENQDYLKNAKDKVTFL----ENQLNSDAHEEVKSTAVRALE 305
Cdd:PRK05771 95 LEKIEKEIKELEEEISELENEIKELEQEIERLEpwGNFDLDLSLLLGFKYVSVFVgtvpEDKLEELKLESDVENVEYIST 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 306 VK-------LGLANNS------IRQAEAEKQQLQEANwYANERVGKLEQENGYLKGITEQLKARadtshAEKMLKDSEKR 372
Cdd:PRK05771 175 DKgyvyvvvVVLKELSdeveeeLKKLGFERLELEEEG-TPSELIREIKEELEEIEKERESLLEE-----LKELAKKYLEE 248
|
....*..
gi 25151865 373 VWEINEE 379
Cdd:PRK05771 249 LLALYEY 255
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
157-285 |
3.63e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 3.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 157 EESEGRDSEKEKNDRQLEKLRNRNDELKIRVKEYKS----------DLSAAQLKVKNLEKKLESAQSADSEEKFVRIDSE 226
Cdd:PRK03918 588 EELEERLKELEPFYNEYLELKDAEKELEREEKELKKleeeldkafeELAETEKRLEELRKELEELEKKYSEEEYEELREE 667
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 25151865 227 IDEKRSqdhdeEINNLHNVIEELRNKLATVESKNKDLEtkfsENQDYLKNAKDKVTFLE 285
Cdd:PRK03918 668 YLELSR-----ELAGLRAELEELEKRREEIKKTLEKLK----EELEEREKAKKELEKLE 717
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
103-261 |
5.94e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 42.80 E-value: 5.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 103 EKNISAVQKLFAAaglggRSQKVYAAGKTRARSTSKKNQPR---SQFDAQPENVNISEESEGRDSEK---EKNDRQ--LE 174
Cdd:pfam17380 389 QKNERVRQELEAA-----RKVKILEEERQRKIQQQKVEMEQiraEQEEARQREVRRLEEERAREMERvrlEEQERQqqVE 463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 175 KLRNRNDELKIRV----KEYKSDLSAAQLKVKNLEKKLESAQSADSEEKFVR--IDSEIDEKRSQDHDEEinnLHNVIEE 248
Cdd:pfam17380 464 RLRQQEEERKRKKleleKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRklLEKEMEERQKAIYEEE---RRREAEE 540
|
170
....*....|...
gi 25151865 249 LRNKLATVESKNK 261
Cdd:pfam17380 541 ERRKQQEMEERRR 553
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
194-428 |
7.71e-04 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 41.72 E-value: 7.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 194 LSAAQLKVKNLEKKLESAQSADSEEKFVRIDSEI---------DEKRSQDHDEEINNLHNVIE-------ELRNKLATVE 257
Cdd:pfam15905 49 TPATARKVKSLELKKKSQKNLKESKDQKELEKEIralvqergeQDKRLQALEEELEKVEAKLNaavrektSLSASVASLE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 258 SKNKD-------LETKFSE--NQDYLKNAKDKVTFLENQLnsDAHEEVKSTAVRALEVKLGLANNSIRQAEAEKQQLQEA 328
Cdd:pfam15905 129 KQLLEltrvnelLKAKFSEdgTQKKMSSLSMELMKLRNKL--EAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEK 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 329 NWYAN-------ERVGKLEQENGYLKGITEQL-KARADTSHAEKMLKDSEKrvwEINEEKSKLEWRLGELSQWWNDAKWK 400
Cdd:pfam15905 207 LVSTEkekieekSETEKLLEYITELSCVSEQVeKYKLDIAQLEELLKEKND---EIESLKQSLEEKEQELSKQIKDLNEK 283
|
250 260 270
....*....|....*....|....*....|..
gi 25151865 401 VGELESS----VALQRNLLDTANSKIQSLNDQ 428
Cdd:pfam15905 284 CKLLESEkeelLREYEEKEQTLNAELEELKEK 315
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
171-423 |
9.25e-04 |
|
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.
Pssm-ID: 464838 [Multi-domain] Cd Length: 384 Bit Score: 41.97 E-value: 9.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 171 RQLEKLRNRNDeLKIRVKEYKSDLSAAQLKVKNLEKKLESAQSADSEEKFV----RIDSEI-------DEKRSQDHDEEI 239
Cdd:pfam15742 101 KQAQSIKSQNS-LQEKLAQEKSRVADAEEKILELQQKLEHAHKVCLTDTCIlekkQLEERIkeaseneAKLKQQYQEEQQ 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 240 NN--LHNVIEELRNKLATVESKNKDLETKFSENQDYLKNAKDKVTFLENQLnSDAHEEVKSTavRALEVKL-GLANNSIR 316
Cdd:pfam15742 180 KRklLDQNVNELQQQVRSLQDKEAQLEMTNSQQQLRIQQQEAQLKQLENEK-RKSDEHLKSN--QELSEKLsSLQQEKEA 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 317 QAEA----------------EKQQLQEANWYA------------NERVGKLEQENGYLKGITEQLKARAD--TSHAEKML 366
Cdd:pfam15742 257 LQEElqqvlkqldvhvrkynEKHHHHKAKLRRakdrlvheveqrDERIKQLENEIGILQQQSEKEKAFQKqvTAQNEILL 336
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 25151865 367 kdsekrvweinEEKSKLEWRLGELSQWWNDAKWKVgeleSSVALQRNLLDTANSKIQ 423
Cdd:pfam15742 337 -----------LEKRKLLEQLTEQEELIKNNKRTI----SSVQNRVNFLDEENKQLQ 378
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
246-436 |
1.04e-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: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 246 IEELRNKLATVESKNKDLETKfsenqdyLKNAKDKVTFLENQLnsdaheEVKSTAVRALEVKLGLANNSIRQAEAEKQQL 325
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKA-------LAELRKELEELEEEL------EQLRKELEELSRQISALRKDLARLEAEVEQL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 326 QEANWYANERVGKLEQEngylkgITEQLKARADTSHAEKmlkdsekrvwEINEEKSKLEWRLGELSQWWNDAKWKVGELE 405
Cdd:TIGR02168 746 EERIAQLSKELTELEAE------IEELEERLEEAEEELA----------EAEAEIEELEAQIEQLKEELKALREALDELR 809
|
170 180 190
....*....|....*....|....*....|.
gi 25151865 406 SSVALQRNLLDTANSKIQSLNDQSHSSTMTI 436
Cdd:TIGR02168 810 AELTLLNEEAANLRERLESLERRIAATERRL 840
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
171-430 |
1.43e-03 |
|
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: 41.88 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 171 RQLEKLRNRNDELkIRVKEYKSDLSAAQLKVKNLEKKLEsAQSADSEEKFVRIDSEIDEKRSQDHDEEiNNLHNVIEELR 250
Cdd:pfam02463 166 RLKRKKKEALKKL-IEETENLAELIIDLEELKLQELKLK-EQAKKALEYYQLKEKLELEEEYLLYLDY-LKLNEERIDLL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 251 NKLATVESKNKDLETKFSENQDYLKNAKDKVTFLENQLNSDAHEEVKSTAVRALEVKLGLANNsIRQAEAEKQQLQEanw 330
Cdd:pfam02463 243 QELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKL-ERRKVDDEEKLKE--- 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 331 yANERVGKLEQengylkgitEQLKARADTSHAEKMLKDSEKRVWEINEEKSKLEWRLGELSQWWNDAKWKVGE----LES 406
Cdd:pfam02463 319 -SEKEKKKAEK---------ELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLeserLSS 388
|
250 260
....*....|....*....|....
gi 25151865 407 SVALQRNLLDTANSKIQSLNDQSH 430
Cdd:pfam02463 389 AAKLKEEELELKSEEEKEAQLLLE 412
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
144-328 |
1.98e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.16 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 144 SQFDAQPENVNISEESEGRDSEKEKNDRQLEKLRnrndelkirvkeykSDLSAAQLKVKNLEKKLESAQSADSEEkfvri 223
Cdd:COG3206 199 EEFRQKNGLVDLSEEAKLLLQQLSELESQLAEAR--------------AELAEAEARLAALRAQLGSGPDALPEL----- 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 224 dseidekrSQDhdeeinnlhNVIEELRNKLATVESKNKDLETKFSENQDYLKNAKDKVTFLENQLNSDAHEEVKS--TAV 301
Cdd:COG3206 260 --------LQS---------PVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASleAEL 322
|
170 180
....*....|....*....|....*..
gi 25151865 302 RALEVKLGLANNSIRQAEAEKQQLQEA 328
Cdd:COG3206 323 EALQAREASLQAQLAQLEARLAELPEL 349
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
202-324 |
2.66e-03 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 40.81 E-value: 2.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 202 KNLEKKLESAQSA--DSEEKFVRIDSEIDEKRSQDHDEEINnlhnvIEELRNKLATV-ESK-------------NKDLET 265
Cdd:pfam05911 684 KRLKEEFEQLKSEkeNLEVELASCTENLESTKSQLQESEQL-----IAELRSELASLkESNslaetqlkcmaesYEDLET 758
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25151865 266 KFSENQDYLKNAKDKVTFLENQLN--SDAHEEVKSTAvRALEVKL------GLANNSIRQAEAEKQQ 324
Cdd:pfam05911 759 RLTELEAELNELRQKFEALEVELEeeKNCHEELEAKC-LELQEQLernekkESSNCDADQEDKKLQQ 824
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
264-428 |
2.67e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.20 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 264 ETKFSENQDYLKNAKDKVTFLENQLNS-DAHEEVKSTAVRALEVKLGLANNSIRQAEAEKQQLQEANWYANERVGKL--- 339
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDAlQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERara 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 340 EQENGYLKGITEQLK---------ARAD-----TSHAEKMLKDSEKRVWEINEEKSKLEWRLGELSQWWNDAKWKVGELE 405
Cdd:COG3883 95 LYRSGGSVSYLDVLLgsesfsdflDRLSalskiADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180
....*....|....*....|...
gi 25151865 406 SSVALQRNLLDTANSKIQSLNDQ 428
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQ 197
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
151-428 |
2.76e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 151 ENVNISEESEGRDSEKEKNDRQLEKLRNRNDELKIRVKEYKSDLSAAQLKVKNLEKKLESAQSADSEEKFVRIDSEIDEK 230
Cdd:PRK03918 280 EKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEE 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 231 RSQDHdEEINNLHNVIEELRNKLA-----TVESKNKDLETKFSENQDYLKNAKDKVTFLENQLNS--DAHEEVKS----- 298
Cdd:PRK03918 360 RHELY-EEAKAKKEELERLKKRLTgltpeKLEKELEELEKAKEEIEEEISKITARIGELKKEIKElkKAIEELKKakgkc 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 299 -TAVRAL--EVKLGLANN---SIRQAEAEKQQLQEANWYANERVGKLEQEngylkgITEQLKARADTSHAEKmLKDSEKR 372
Cdd:PRK03918 439 pVCGRELteEHRKELLEEytaELKRIEKELKEIEEKERKLRKELRELEKV------LKKESELIKLKELAEQ-LKELEEK 511
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25151865 373 VWEINEEKSKLEWRL------------GELSQWWNDAKwKVGELESSVALQRNLLDTANSKIQSLNDQ 428
Cdd:PRK03918 512 LKKYNLEELEKKAEEyeklkekliklkGEIKSLKKELE-KLEELKKKLAELEKKLDELEEELAELLKE 578
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
156-271 |
3.09e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 39.95 E-value: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 156 SEESEGRDSEKEKNDRQLEKL-------RNRNDELKIRVKEYKSDLSAAQLKVKNLEKKLE--SAQSADSEEKFVRIDSE 226
Cdd:PRK09039 45 SREISGKDSALDRLNSQIAELadllsleRQGNQDLQDSVANLRASLSAAEAERSRLQALLAelAGAGAAAEGRAGELAQE 124
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 25151865 227 IDEKR--SQDHDEEINNLHNVIEELRNKLATVESKNKDLETKFSENQ 271
Cdd:PRK09039 125 LDSEKqvSARALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQ 171
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
158-433 |
3.87e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.16 E-value: 3.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 158 ESEGRDSEKEKNDRQLEKLRNRND----ELKIRV-KEYKSDLSAAQLKvknleKKLEsAQSADSEEKFVRIDSEIDEKRS 232
Cdd:pfam01576 163 EFTSNLAEEEEKAKSLSKLKNKHEamisDLEERLkKEEKGRQELEKAK-----RKLE-GESTDLQEQIAELQAQIAELRA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 233 Q--DHDEEINNLHNVIEELRNKLATVESKNKDLETKFSENQDYLKNAKDKVTFLENQlNSDAHEEVKstAVRA-LEVKLG 309
Cdd:pfam01576 237 QlaKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQ-RRDLGEELE--ALKTeLEDTLD 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 310 LAN-----NSIRQAEAE--KQQLQEANWYANERVGKLEQE-NGYLKGITEQL-KARADTSHAEKMLKDSEKRVWEINEE- 379
Cdd:pfam01576 314 TTAaqqelRSKREQEVTelKKALEEETRSHEAQLQEMRQKhTQALEELTEQLeQAKRNKANLEKAKQALESENAELQAEl 393
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25151865 380 -------------KSKLEWRLGELSQWWNDAKWKVGELESSVALQRNLLDTANSKIQSLNDQSHSST 433
Cdd:pfam01576 394 rtlqqakqdsehkRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLS 460
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
165-380 |
4.19e-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: 40.09 E-value: 4.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 165 EKEKNDRQLEKLRNRNDELKIRVKEYKSDLSAAQLKVK-NLEKKLESAQSADSEekfvridSEIDEKRSQDHDEEINNLH 243
Cdd:pfam05483 528 QEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKcKLDKSEENARSIEYE-------VLKKEKQMKILENKCNNLK 600
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 244 NVIEELRNKLATVESKNKDLETKFSENQDYLKNAKDKVTFLENQLNSDAH--EEVKSTAVRALEVKLGLANNSIRQAEAE 321
Cdd:pfam05483 601 KQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQkfEEIIDNYQKEIEDKKISEEKLLEEVEKA 680
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 25151865 322 KQQLQEANWYANERVGKLEQENGYLKGITEQLKARADTSHAEkmlKDSEKRVWEINEEK 380
Cdd:pfam05483 681 KAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEE---RDSELGLYKNKEQE 736
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
156-391 |
5.16e-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: 39.81 E-value: 5.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 156 SEESEGR-DSEKEKNDRQLEKLRNRNDELKIRVKEYKSDLSAAQLKVKNLEKKLES---------------AQSADSEEK 219
Cdd:pfam10174 114 TEENFRRlQSEHERQAKELFLLRKTLEEMELRIETQKQTLGARDESIKKLLEMLQSkglpkksgeedwertRRIAEAEMQ 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 220 FVRIDSEIDEK-------------RSQDHDE--EINNLHNVIEELRNKLATVESKNKDLE-----TKFS------ENQDY 273
Cdd:pfam10174 194 LGHLEVLLDQKekenihlreelhrRNQLQPDpaKTKALQTVIEMKDTKISSLERNIRDLEdevqmLKTNgllhteDREEE 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 274 LKNA---KDKVTFLEN---QLNSDAHEevKSTAVRALEVKLGLANNsirQAEAEKQQLQeanwYANERVGKLEQENGYLK 347
Cdd:pfam10174 274 IKQMevyKSHSKFMKNkidQLKQELSK--KESELLALQTKLETLTN---QNSDCKQHIE----VLKESLTAKEQRAAILQ 344
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 25151865 348 GITEQLKARADtsHAEKMLKDSEKRVWEINEEKSKLEwrlGELS 391
Cdd:pfam10174 345 TEVDALRLRLE--EKESFLNKKTKQLQDLTEEKSTLA---GEIR 383
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
165-330 |
5.98e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.37 E-value: 5.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 165 EKEKNDRQLEKLRNRNDELKIRVKEYKSDLSAAQL--KVKNLEKKLesaqsADSEEKFVRIDSEIDEKRSQDHD-----E 237
Cdd:COG4717 96 ELEELEEELEELEAELEELREELEKLEKLLQLLPLyqELEALEAEL-----AELPERLEELEERLEELRELEEEleeleA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 238 EINNLHNVIEELRNKLATVESKN-KDLETKFSENQDYLKNAKDKVTFLENQLNSdaheevKSTAVRALEVKLglannsir 316
Cdd:COG4717 171 ELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELEE------LEEELEQLENEL-------- 236
|
170
....*....|....
gi 25151865 317 QAEAEKQQLQEANW 330
Cdd:COG4717 237 EAAALEERLKEARL 250
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
170-372 |
8.35e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 38.66 E-value: 8.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 170 DRQLEKLRNRNDELKIRVKEYKSDLSAAQLKVKNLEKKLESAQsadseEKFVRIDSEIDEKRsqdhdEEINNLHNVIEEL 249
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQ-----AELEALQAEIDKLQ-----AEIAEAEAEIEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 250 RNKL---ATVESKNKDLETKFsenqDYLKNAKDKVTFLENQLNSDAHEEVKSTAVRALEVKLGLANNSIRQAEAEKQQLQ 326
Cdd:COG3883 85 REELgerARALYRSGGSVSYL----DVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 25151865 327 EANWYANERVGKLEQENGYLKGITEQLKARADTSHAEKMLKDSEKR 372
Cdd:COG3883 161 ALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELA 206
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
103-384 |
8.52e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.35 E-value: 8.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 103 EKNISAVQKLFAA--AGLGGRSQKVYAAGKTRARSTSKKNQPRSQFDA-QPENVNISEESEGRDSEKEKND---RQLEKL 176
Cdd:PTZ00121 1248 ERNNEEIRKFEEArmAHFARRQAAIKAEEARKADELKKAEEKKKADEAkKAEEKKKADEAKKKAEEAKKADeakKKAEEA 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 177 RNRNDELKIRVKEYK-------SDLSAAQLKVKNLEKKLESAQSADSEEKfvridSEIDEKRSQdhDEEINNlhnvIEEL 249
Cdd:PTZ00121 1328 KKKADAAKKKAEEAKkaaeaakAEAEAAADEAEAAEEKAEAAEKKKEEAK-----KKADAAKKK--AEEKKK----ADEA 1396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 250 RNKLATVESKNKDLETKFSENQ--DYLKNAKDKVTFLEnQLNSDAHEEVKSTAVRALEVKLGLANNSIRQAEaEKQQLQE 327
Cdd:PTZ00121 1397 KKKAEEDKKKADELKKAAAAKKkaDEAKKKAEEKKKAD-EAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAE-EAKKADE 1474
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25151865 328 ANWYANE--RVGKLEQENGYLKGITEQLKARADT-SHAEKMLKDSEKRVWE---INEEKSKLE 384
Cdd:PTZ00121 1475 AKKKAEEakKADEAKKKAEEAKKKADEAKKAAEAkKKADEAKKAEEAKKADeakKAEEAKKAD 1537
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
154-269 |
9.04e-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: 38.85 E-value: 9.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 154 NISEESEGRDSEKEKNDRQLEKLRNRNDELKIRVKEYKSD-------LSAAQLKVKNLEKKLESAqsadsEEKFVRIDSE 226
Cdd:TIGR04523 558 NLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEkkdlikeIEEKEKKISSLEKELEKA-----KKENEKLSSI 632
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 25151865 227 ID--EKRSQDHDEEINNLHNVIEELRNKLATVESKNKDLETKFSE 269
Cdd:TIGR04523 633 IKniKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDD 677
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
145-429 |
9.27e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 38.84 E-value: 9.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 145 QFDAQPENVNISEESEGRDSEKEKNDrQLEKLRNRN------DELKIRVKEYKSDLSAAQLkVKNLEKKLESAQSADSEE 218
Cdd:COG3206 60 LVEPQSSDVLLSGLSSLSASDSPLET-QIEILKSRPvlervvDKLNLDEDPLGEEASREAA-IERLRKNLTVEPVKGSNV 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 219 KFVRIDSEiDEKRSQDhdeeINNLhnVIEELRNklATVESKNKDLE--TKFSENQdyLKNAKDKVTFLENQL-------- 288
Cdd:COG3206 138 IEISYTSP-DPELAAA----VANA--LAEAYLE--QNLELRREEARkaLEFLEEQ--LPELRKELEEAEAALeefrqkng 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151865 289 --NSDAHEEVKSTAVRALEVKLGLANNSIRQAEAEKQQLQEANWYANERVGKLEQENGYLKGITEQLKARADTSHAEKML 366
Cdd:COG3206 207 lvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARY 286
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25151865 367 KDSEKRVWEINEEKSKLEWRL-GELSQWWNDAKWKVGELESSVALQRNLLDTANSKIQSLNDQS 429
Cdd:COG3206 287 TPNHPDVIALRAQIAALRAQLqQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELE 350
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|
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