|
Name |
Accession |
Description |
Interval |
E-value |
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
47-352 |
1.48e-180 |
|
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.
Pssm-ID: 461455 [Multi-domain] Cd Length: 309 Bit Score: 524.20 E-value: 1.48e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 47 EEQLPHYKLRADTIY-GYDHDDW-LHTPL-ISPDANIDLTTEQIEETLKYFLLCAERVGQMTKTYNDIDAVTRLLEEKER 123
Cdd:pfam04849 1 EEQIPPYKLRADTLGtGYANQDWkIPSPAgRPPEVSLPLSPEQIRETLNYFLLCSDRVSQMTKTYNDIEAVTRLLEEKER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 124 DLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEPESVCSTPLKRNESSSSV 203
Cdd:pfam04849 81 DLELAARIGQSLLKQNSVLTERNEALEEQLGSAREEILQLRHELSKKDDLLQIYSNDAEESETESSCSTPLRRNESFSSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 204 QNYFHLDSLQKKLKDLEEENVVLRSEACQLKTETITYEEKEQQLVNDCVKELRDANVQIASISEELAKKTEDAARQQEEI 283
Cdd:pfam04849 161 HGCVQLDALQEKLRGLEEENLKLRSEASHLKTETDTYEEKEQQLMSDCVEQLSEANQQMAELSEELARKMEENLRQQEEI 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124517685 284 THLLSQIVDLQKKAKSCAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQEELKNLRNK 352
Cdd:pfam04849 241 TSLLAQIVDLQHKCKELGIENEELQQHLQASKEAQRQLTSELQELQDRYAECLGMLHEAQEELKELRKK 309
|
|
| Milton |
pfam12448 |
Kinesin associated protein; This domain family is found in eukaryotes, and is typically ... |
411-580 |
1.87e-74 |
|
Kinesin associated protein; This domain family is found in eukaryotes, and is typically between 143 and 173 amino acids in length. The family is found in association with pfam04849. This family is a region of the protein milton. Milton recruits the heavy chain of kinesin to mitochondria to allow the motor movement function of kinesin.
Pssm-ID: 463588 Cd Length: 171 Bit Score: 241.80 E-value: 1.87e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 411 KQRSLTPSPMNIPGSNQSSAMNSLLSSCVSTPRSSFYGSDVSNVVLDNKTNSILLETEAADLGNEDHNKKPGTPGTPGSH 490
Cdd:pfam12448 1 RQRSLTPSPMNIPGSNQSSSLTSMRSSSSSTPRSSYYGGDGSSISLDNRTNSILSETSSSQDSGYDRPKKPGTPGTPGAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 491 DLETALRRLSLRRENYLSERRFFEEEQERKLRELAE----KGELHSGSLTPTESIMSLGTHSRfSEFTGFSGmsFSSRSY 566
Cdd:pfam12448 81 DLEAALRRLSLRRQNYLSERRFFEEERERKLLALAGtynyDEGEHGGSLTPNDSIMSLGSNHS-GSSSHSSG--FSSRSY 157
|
170
....*....|....
gi 124517685 567 LPEKLQIVKPLEGS 580
Cdd:pfam12448 158 LPEKLQIVKPLEGS 171
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
111-352 |
1.46e-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: 78.56 E-value: 1.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 111 IDAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEPEsvc 190
Cdd:TIGR02168 700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEE--- 776
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 191 stpLKRNESsssvqnyfHLDSLQKKLKDLEEENVVLRSEACQLKTETITYEEKEQQL---VNDCVKELRDANVQIASISE 267
Cdd:TIGR02168 777 ---LAEAEA--------EIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLrerLESLERRIAATERRLEDLEE 845
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 268 ELAKKTEDAARQQEEITHLLSQIVDLQKKAKSCAVENEELVQHLGAAKDAQRQLTAELRELEDK-------YAECMEMLH 340
Cdd:TIGR02168 846 QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKrselrreLEELREKLA 925
|
250
....*....|..
gi 124517685 341 EAQEELKNLRNK 352
Cdd:TIGR02168 926 QLELRLEGLEVR 937
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
78-351 |
1.71e-12 |
|
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: 71.63 E-value: 1.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 78 ANIDLTTEQIEETLKyfllcaervgQMTKTYNDIDAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIR 157
Cdd:TIGR02168 684 EKIEELEEKIAELEK----------ALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 158 EEVSQLRHELSMKDELLQFYTSAAEESEPESVCSTPLKRNESSSSVQNYFHLDSLQKKLKDLEEENVVLRSEACQLKTET 237
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 238 ityEEKEQQLVnDCVKELRDANVQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKSCAVENEELVQHLGAAKDA 317
Cdd:TIGR02168 834 ---AATERRLE-DLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESK 909
|
250 260 270
....*....|....*....|....*....|....
gi 124517685 318 QRQLTAELRELEDKYAEcmemLHEAQEELKNLRN 351
Cdd:TIGR02168 910 RSELRRELEELREKLAQ----LELRLEGLEVRID 939
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
98-352 |
1.72e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.42 E-value: 1.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 98 AERVGQMTKTYNDIDAVTRLL--EEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQ 175
Cdd:COG1196 212 AERYRELKEELKELEAELLLLklRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 176 FYTSAAEESEPESVCSTPLKRNESSSSVQNYFHLDSLQKKLKDLEEEnvvLRSEACQLKTETITYEEKEQQLvNDCVKEL 255
Cdd:COG1196 292 ELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE---LEELEEELEEAEEELEEAEAEL-AEAEEAL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 256 RDANVQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKSCAVENEELVQHLGAAKDAQRQLTAELRELEDKYAEC 335
Cdd:COG1196 368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447
|
250
....*....|....*..
gi 124517685 336 MEMLHEAQEELKNLRNK 352
Cdd:COG1196 448 AEEEAELEEEEEALLEL 464
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
99-389 |
6.75e-11 |
|
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: 66.63 E-value: 6.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 99 ERVGQMTKTYNDID-AVTRLLEEKERDLELAARIGQslLKKnktltERNELLEEQvEHIREEVSQLRHELS--------- 168
Cdd:TIGR02169 650 EKSGAMTGGSRAPRgGILFSRSEPAELQRLRERLEG--LKR-----ELSSLQSEL-RRIENRLDELSQELSdasrkigei 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 169 MKD-ELLQFYTSAA----EESEPE-SVCSTPLKRNESSssvqnyfhLDSLQKKLKDLEEENVVLRSEACQLKTETITYEE 242
Cdd:TIGR02169 722 EKEiEQLEQEEEKLkerlEELEEDlSSLEQEIENVKSE--------LKELEARIEELEEDLHKLEEALNDLEARLSHSRI 793
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 243 KE-QQLVNDCVKELRDANVQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKSCAVENEELVQHLGAAKDAQRQL 321
Cdd:TIGR02169 794 PEiQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEEL 873
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124517685 322 TAELRELEDKYAECMEMLHEAQEELKNLRNKtmptsrryhslglfpMDSLAAEIEgtmRKELQLEELE 389
Cdd:TIGR02169 874 EAALRDLESRLGDLKKERDELEAQLRELERK---------------IEELEAQIE---KKRKRLSELK 923
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
98-389 |
1.28e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.47 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 98 AERVGQMTKTYNDIDAVTRLLEEKERDLElaarigqSLLKKNKTLTERNELLEEQVEHIREEVSQLRH------ELSMKD 171
Cdd:PRK03918 220 REELEKLEKEVKELEELKEEIEELEKELE-------SLEGSKRKLEEKIRELEERIEELKKEIEELEEkvkelkELKEKA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 172 E----LLQFYTSAAEESEPESVCSTPLkRNESSSSVQNYFHLDSLQKKLKDLEEENVVLRSEACQLKTETITYEEKEQQL 247
Cdd:PRK03918 293 EeyikLSEFYEEYLDELREIEKRLSRL-EEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKK 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 248 VN--------------DCVKELRDANVQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKSCAVENEELVQHlgA 313
Cdd:PRK03918 372 EElerlkkrltgltpeKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEE--H 449
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124517685 314 AKDAQRQLTAELRELEDKYAECMEMLHEAQEELKNLRNKTMPTSRryhslgLFPMDSLAAEIEGTMRK--ELQLEELE 389
Cdd:PRK03918 450 RKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESE------LIKLKELAEQLKELEEKlkKYNLEELE 521
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
208-389 |
3.81e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.72 E-value: 3.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 208 HLDSLQKKLKDLEEENVVLRSEACQLKTETITYEEKEQQLVndcvKELRDANVQIASISEELAKKTEDAARQQEEITHLL 287
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELR----LELEELELELEEAQAEEYELLAELARLEQDIARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 288 SQIVDLQKKAKSCAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQEELKNLRNKTMPTSRRYHSLglfp 367
Cdd:COG1196 309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL---- 384
|
170 180
....*....|....*....|..
gi 124517685 368 MDSLAAEIEGTMRKELQLEELE 389
Cdd:COG1196 385 AEELLEALRAAAELAAQLEELE 406
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
85-390 |
4.73e-09 |
|
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: 60.46 E-value: 4.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 85 EQIEETLKyfllcaervgQMTKTYNDIDAVTRLLEEKERDLELaarigqslLKKNKTLTERNELLEEQVEHIREEVSQLR 164
Cdd:TIGR02168 172 ERRKETER----------KLERTRENLDRLEDILNELERQLKS--------LERQAEKAERYKELKAELRELELALLVLR 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 165 HElSMKDELLQFYTSAAEESEpesvcstplkrnessssvqnyfHLDSLQKKLKDLEEENVVLRSEACQLKTEtityEEKE 244
Cdd:TIGR02168 234 LE-ELREELEELQEELKEAEE----------------------ELEELTAELQELEEKLEELRLEVSELEEE----IEEL 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 245 QQLVNDCVKELRDANVQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKSCAVENEELVQHLGAAKDAQRQLTAE 324
Cdd:TIGR02168 287 QKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAE 366
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124517685 325 LRELEDKYAECMEMLHEAQEELKNLRNKtmptsrryhslglfpMDSLAAEIEgtmRKELQLEELES 390
Cdd:TIGR02168 367 LEELESRLEELEEQLETLRSKVAQLELQ---------------IASLNNEIE---RLEARLERLED 414
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
116-390 |
4.87e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.46 E-value: 4.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 116 RLLEEKERdLELAARIGQSLLKKNKTLTErnelLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEesepesvcstpLK 195
Cdd:PRK03918 443 RELTEEHR-KELLEEYTAELKRIEKELKE----IEEKERKLRKELRELEKVLKKESELIKLKELAEQ-----------LK 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 196 RNESSSSVqnyFHLDSLQKKLKDLEEenvvLRSEACQLKTETITYEEKEQQLvNDCVKELRDANVQIASISEELAK---- 271
Cdd:PRK03918 507 ELEEKLKK---YNLEELEKKAEEYEK----LKEKLIKLKGEIKSLKKELEKL-EELKKKLAELEKKLDELEEELAEllke 578
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 272 --------KTEDAARQQE---------EITHLLSQIVDLQKKAKSCAVENEELVQHLGAAKDAQRQLTAELRELEDKYAE 334
Cdd:PRK03918 579 leelgfesVEELEERLKElepfyneylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE 658
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 124517685 335 cmemlheaqEELKNLRNKTMPTSRRYHSL--GLFPMDSLAAEIEGTMRK-ELQLEELES 390
Cdd:PRK03918 659 ---------EEYEELREEYLELSRELAGLraELEELEKRREEIKKTLEKlKEELEEREK 708
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
209-390 |
1.48e-08 |
|
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: 58.91 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 209 LDSLQKKLKDLEEENVVLRSEACQLKTETityEEKEQQLVNDcVKELRDANVQIASISEELAKKTEDAARQQEEITHLLS 288
Cdd:TIGR02168 693 IAELEKALAELRKELEELEEELEQLRKEL---EELSRQISAL-RKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEE 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 289 QIVDLQKKAKSCAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQEELKNLRNKTMPTSRRyhslglfpM 368
Cdd:TIGR02168 769 RLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERR--------L 840
|
170 180
....*....|....*....|..
gi 124517685 369 DSLAAEIEgtmRKELQLEELES 390
Cdd:TIGR02168 841 EDLEEQIE---ELSEDIESLAA 859
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
111-414 |
3.65e-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: 57.77 E-value: 3.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 111 IDAVTRLLEEKERDLELAArigqslLKKNKTLTERNELLEEqVEHIREEVSQLRHELSMKDELLQFYTSAAEESEpesvc 190
Cdd:TIGR02169 197 RQQLERLRREREKAERYQA------LLKEKREYEGYELLKE-KEALERQKEAIERQLASLEEELEKLTEEISELE----- 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 191 stplKRNESSSSVqnyfhLDSLQKKLKDL-EEENVVLRSEACQLKTETI----TYEEKEQQLvNDCVKELRDANVQIASI 265
Cdd:TIGR02169 265 ----KRLEEIEQL-----LEELNKKIKDLgEEEQLRVKEKIGELEAEIAslerSIAEKEREL-EDAEERLAKLEAEIDKL 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 266 SEELAKKTEDAARQQEEITHLLSQIVDLQKKAKSCAVENEELVQHLGAAKDAQRQLTAELreledkyaecmEMLHEAQEE 345
Cdd:TIGR02169 335 LAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKL-----------EKLKREINE 403
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124517685 346 LKNLRNKTMPTSRRYHSLGLFpmdsLAAEIEgtmRKELQLEELESPDITHQKRVFETVRNVNQVVKQRS 414
Cdd:TIGR02169 404 LKRELDRLQEELQRLSEELAD----LNAAIA---GIEAKINELEEEKEDKALEIKKQEWKLEQLAADLS 465
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
81-398 |
3.74e-08 |
|
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: 57.42 E-value: 3.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 81 DLTTEQIEETLKYFLL---CAERVGQMTKTYNDIDAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIR 157
Cdd:pfam05483 475 DLKTELEKEKLKNIELtahCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVR 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 158 EEVSQLRHELSMKDEllqfytsaAEESEPESVCSTPLKRNESSSSVQNYFH-----LDSLQKKLKDLEEENVVLRSEAC- 231
Cdd:pfam05483 555 EEFIQKGDEVKCKLD--------KSEENARSIEYEVLKKEKQMKILENKCNnlkkqIENKNKNIEELHQENKALKKKGSa 626
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 232 -------------QLKTETITYEEKEQQLVNDCVKELRDANVQIASISEELAKK---TEDAARQQEEI----THLLSQIV 291
Cdd:pfam05483 627 enkqlnayeikvnKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAkaiADEAVKLQKEIdkrcQHKIAEMV 706
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 292 DLQKKAKSCAVE-NEELVQHLGAAKDAQRQLTAELRELEdkyaecmemlheaqEELKNLRNKTMPTSRRYhslglfpmds 370
Cdd:pfam05483 707 ALMEKHKHQYDKiIEERDSELGLYKNKEQEQSSAKAALE--------------IELSNIKAELLSLKKQL---------- 762
|
330 340
....*....|....*....|....*...
gi 124517685 371 laaEIEGTMRKELQLEELESPDITHQKR 398
Cdd:pfam05483 763 ---EIEKEEKEKLKMEAKENTAILKDKK 787
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
118-298 |
9.26e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.93 E-value: 9.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 118 LEEKERDLELAarigQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEpesvcstplKRN 197
Cdd:COG4717 73 LKELEEELKEA----EEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEA---------LEA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 198 ESSSSVQNYFHLDSLQKKLKDLEEENVVLRSEACQLKTETITYEEK----EQQLVNDCVKELRDANVQIASISEELAKKT 273
Cdd:COG4717 140 ELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQlslaTEEELQDLAEELEELQQRLAELEEELEEAQ 219
|
170 180
....*....|....*....|....*
gi 124517685 274 EDAARQQEEITHLLSQIVDLQKKAK 298
Cdd:COG4717 220 EELEELEEELEQLENELEAAALEER 244
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
83-352 |
1.03e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.84 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 83 TTEQIEETLKYFLLCAERVgqmtKTYNDIDAvtrLLEEKER-DLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVS 161
Cdd:PRK03918 343 LKKKLKELEKRLEELEERH----ELYEEAKA---KKEELERlKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIG 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 162 QLRHELSMKDELLQFYTSAAEESepeSVCSTPLKRNESSSSVQNY-FHLDSLQKKLKDLEEENVVLRSEACQLktETITY 240
Cdd:PRK03918 416 ELKKEIKELKKAIEELKKAKGKC---PVCGRELTEEHRKELLEEYtAELKRIEKELKEIEEKERKLRKELREL--EKVLK 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 241 EEKEQQLVNDCVKELRDANVQIASIS-EELAKKTEDAARQQEEITHLLSQIVDLQKKAKSCAVENEELVQHLGAAKDAQR 319
Cdd:PRK03918 491 KESELIKLKELAEQLKELEEKLKKYNlEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEE 570
|
250 260 270
....*....|....*....|....*....|...
gi 124517685 320 QLTAELRELEDKYAECMEMLHEAQEELKNLRNK 352
Cdd:PRK03918 571 ELAELLKELEELGFESVEELEERLKELEPFYNE 603
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
103-389 |
1.48e-07 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 54.15 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 103 QMTKTYNDIDAVTRLLEE-KERDLELaarigQSLLKKNKTltERNELLEEqvehIREEVSQLRHELSMKDELLQFYTSAA 181
Cdd:COG1340 9 SLEELEEKIEELREEIEElKEKRDEL-----NEELKELAE--KRDELNAQ----VKELREEAQELREKRDELNEKVKELK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 182 EEsepesvcstplkRNESSSSVQNYFH------------------LDSLQKKLKDLEEEnvvlrseacqLKTETITyEEK 243
Cdd:COG1340 78 EE------------RDELNEKLNELREeldelrkelaelnkaggsIDKLRKEIERLEWR----------QQTEVLS-PEE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 244 EQQLVNdcvkelrdanvQIASISEELaKKTEDAARQQEEITHLLSQIVDLQKKAKSCAVENEELVQHLGAAKDaqrQLTA 323
Cdd:COG1340 135 EKELVE-----------KIKELEKEL-EKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHE---EMIE 199
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124517685 324 ELRELEDKYAEcMEMLH----EAQEELKNLRNKTMPTSRRYHSLglfpMDSLAAEIEGT--MRKELQLEELE 389
Cdd:COG1340 200 LYKEADELRKE-ADELHkeivEAQEKADELHEEIIELQKELREL----RKELKKLRKKQraLKREKEKEELE 266
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
36-349 |
2.94e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 54.26 E-value: 2.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 36 NLPEVEIISLlEEQLPHYKLRADTIYgyDHDDWLHTPLISPDANIDLTTEQIEETLKYFLLCAERVGQMTKTYNDIdavt 115
Cdd:TIGR04523 120 NKLEVELNKL-EKQKKENKKNIDKFL--TEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKI---- 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 116 rllEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQFYTS---AAEESEPESVcsT 192
Cdd:TIGR04523 193 ---KNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTqlnQLKDEQNKIK--K 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 193 PLKRNEsSSSVQNYFHLDSLQKKLKDLEEENVVLRSEACQ-----LKTETITYEEKEQQLVNDCV---KELRDANVQIAS 264
Cdd:TIGR04523 268 QLSEKQ-KELEQNNKKIKELEKQLNQLKSEISDLNNQKEQdwnkeLKSELKNQEKKLEEIQNQISqnnKIISQLNEQISQ 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 265 ISEELAKKTEDAARQQEEITHLLSQIVDLQKkakscavENEELvqhlgaaKDAQRQLTAELRELEDKYAECMEMLHEAQE 344
Cdd:TIGR04523 347 LKKELTNSESENSEKQRELEEKQNEIEKLKK-------ENQSY-------KQEIKNLESQINDLESKIQNQEKLNQQKDE 412
|
....*
gi 124517685 345 ELKNL 349
Cdd:TIGR04523 413 QIKKL 417
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
122-363 |
4.64e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.15 E-value: 4.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 122 ERDLELAARIgQSLlKKNKTLTE--RNELLEEQ---------VEH------IREEVSQLRHELSMKDELLQFYTSAAEES 184
Cdd:COG4913 191 EKALRLLHKT-QSF-KPIGDLDDfvREYMLEEPdtfeaadalVEHfddlerAHEALEDAREQIELLEPIRELAERYAAAR 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 185 EpesvcstplkRNESSSSVQNYFHLDSLQKKLKDLEEENVVLRSEACQLKTEtitYEEKEQQLvNDCVKELRDANVQIAS 264
Cdd:COG4913 269 E----------RLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAE---LERLEARL-DALREELDELEAQIRG 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 265 IS----EELAKKTEDAARQQEEITHLLSQIVDLQKKAKSCAVENEE--------LVQHLGAAKDAQRQLTAELRELEDKY 332
Cdd:COG4913 335 NGgdrlEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEefaalraeAAALLEALEEELEALEEALAEAEAAL 414
|
250 260 270
....*....|....*....|....*....|.
gi 124517685 333 AECMEMLHEAQEELKNLRNKTMPTSRRYHSL 363
Cdd:COG4913 415 RDLRRELRELEAEIASLERRKSNIPARLLAL 445
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
28-349 |
6.51e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 53.43 E-value: 6.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 28 SCDVCNSTNlPEVEIISLLEEQLPHYKLRAdtiyGYDHDDWLHTPLISPDANIDLTTEQIEETLKYFLLCAERVgqmtkt 107
Cdd:TIGR00618 583 KEDIPNLQN-ITVRLQDLTEKLSEAEDMLA----CEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHAL------ 651
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 108 yndidaVTRLLEEKERDLELAARIGQsllkknKTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEPE 187
Cdd:TIGR00618 652 ------QLTLTQERVREHALSIRVLP------KELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDRE 719
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 188 svcstplkRNE----SSSSVQNY-FHLDSLQKKLKDLEEEnvvlRSEACQLKTETitYEEKEQQLVndcVKELRDANVQi 262
Cdd:TIGR00618 720 --------FNEienaSSSLGSDLaAREDALNQSLKELMHQ----ARTVLKARTEA--HFNNNEEVT---AALQTGAELS- 781
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 263 asiseELAKKTEDAARQQEEITHLLSQI-VDLQKKAKS----CAVENEELVQHLGAAKDAQRQLTA---ELRELEDKYAE 334
Cdd:TIGR00618 782 -----HLAAEIQFFNRLREEDTHLLKTLeAEIGQEIPSdediLNLQCETLVQEEEQFLSRLEEKSAtlgEITHQLLKYEE 856
|
330
....*....|....*
gi 124517685 335 CMEMLHEAQEELKNL 349
Cdd:TIGR00618 857 CSKQLAQLTQEQAKI 871
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
85-375 |
7.73e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.14 E-value: 7.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 85 EQIEETLKYFLLcaERVGQMTKTYndidavtRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLR 164
Cdd:PRK03918 506 KELEEKLKKYNL--EELEKKAEEY-------EKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELL 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 165 HELsmkdELLQFYTSAAEESEPESVCSTPLKRNESSSSVQNyfhLDSLQKKLKDLEEEnvvlrseacqlktetITYEEKE 244
Cdd:PRK03918 577 KEL----EELGFESVEELEERLKELEPFYNEYLELKDAEKE---LEREEKELKKLEEE---------------LDKAFEE 634
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 245 QQLVNDCVKELRDanvQIasisEELAKK--TEDAARQQEEITHLLSQIVDLQKkakscavENEELVQHLGAAKDAQRQLT 322
Cdd:PRK03918 635 LAETEKRLEELRK---EL----EELEKKysEEEYEELREEYLELSRELAGLRA-------ELEELEKRREEIKKTLEKLK 700
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 124517685 323 AELRELEdKYAECMEMLHEAQEELKNLRNKTmptsRRYHSL----GLFPMDSLAAEI 375
Cdd:PRK03918 701 EELEERE-KAKKELEKLEKALERVEELREKV----KKYKALlkerALSKVGEIASEI 752
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
69-341 |
1.84e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.96 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 69 LHTPLISPDANIDLTTEQIEEtlkyfllCAERVGQMTKTYNDIDAVTRLLEEKERDLE-LAARIGQSLLKKNKTLTERNE 147
Cdd:PRK02224 204 LHERLNGLESELAELDEEIER-------YEEQREQARETRDEADEVLEEHEERREELEtLEAEIEDLRETIAETEREREE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 148 LLEEqVEHIREEVSQLRHELsmkDELLQfyTSAAEESEPESVCStplkrnessssvqnyfHLDSLQKKLKDLEEENVVLR 227
Cdd:PRK02224 277 LAEE-VRDLRERLEELEEER---DDLLA--EAGLDDADAEAVEA----------------RREELEDRDEELRDRLEECR 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 228 SEACQLKTETITYEEKEQQLvNDCVKELRDanvQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKSCAVE---- 303
Cdd:PRK02224 335 VAAQAHNEEAESLREDADDL-EERAEELRE---EAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDlgna 410
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 124517685 304 ---NEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHE 341
Cdd:PRK02224 411 edfLEELREERDELREREAELEATLRTARERVEEAEALLEA 451
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
79-351 |
2.30e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 51.56 E-value: 2.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 79 NIDLTTEQIEETLKYFLlcaervGQMTKTYNDIDAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIRE 158
Cdd:TIGR04523 458 NLDNTRESLETQLKVLS------RSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLES 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 159 EVSQLRHELS-MKDELLQFYTSAAEESEPESVCStplKRNESSSSVQNYFHLDS----LQKKLKDLEEENVVLRSEacqL 233
Cdd:TIGR04523 532 EKKEKESKISdLEDELNKDDFELKKENLEKEIDE---KNKEIEELKQTQKSLKKkqeeKQELIDQKEKEKKDLIKE---I 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 234 KTETITYEEKEQQLvNDCVKELRDANVQIASISE---------ELAKKTEDAARQQ--------EEITHLLSQIVDLQKK 296
Cdd:TIGR04523 606 EEKEKKISSLEKEL-EKAKKENEKLSSIIKNIKSkknklkqevKQIKETIKEIRNKwpeiikkiKESKTKIDDIIELMKD 684
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 124517685 297 AkscaveNEELVQHLgaAKDAQRQL-TAELRELEDKYAECMEMLHEAQEELKNLRN 351
Cdd:TIGR04523 685 W------LKELSLHY--KKYITRMIrIKDLPKLEEKYKEIEKELKKLDEFSKELEN 732
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
106-387 |
3.20e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.22 E-value: 3.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 106 KTYNDIDAVTRLLEEKERDLE-LAARIG--QSLLKKNKtltERNELLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAE 182
Cdd:PRK03918 162 NAYKNLGEVIKEIKRRIERLEkFIKRTEniEELIKEKE---KELEEVLREINEISSELPELREELEKLEKEVKELEELKE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 183 ESEpesvcstPLKRNESsssvqnyfhldSLQKKLKDLEEENVVLRSEACQLKTETITYEEKEQQLvndcvKELRDANVQI 262
Cdd:PRK03918 239 EIE-------ELEKELE-----------SLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKEL-----KELKEKAEEY 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 263 ASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKscavENEELVQHLGAAKDAQRQLTAELRELEdKYAECMEMLHEA 342
Cdd:PRK03918 296 IKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK----ELEEKEERLEELKKKLKELEKRLEELE-ERHELYEEAKAK 370
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 124517685 343 QEELKNLRNKtmptsrryhsLGLFPMDSLAAEIEGTMRKELQLEE 387
Cdd:PRK03918 371 KEELERLKKR----------LTGLTPEKLEKELEELEKAKEEIEE 405
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
208-352 |
3.96e-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: 49.15 E-value: 3.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 208 HLDSLQKKLKDLEEENVVLRSEACQLKTEtitYEEKEQQLvNDCVKELRDANVQIASISEELAKKTE--DAARQQEEITH 285
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEAR---LEAAKTEL-EDLEKEIKRLELEIEEVEARIKKYEEqlGNVRNNKEYEA 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124517685 286 LLSQIVDLQKKAKSCAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECM----EMLHEAQEELKNLRNK 352
Cdd:COG1579 94 LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKaeldEELAELEAELEELEAE 164
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
131-348 |
4.96e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.68 E-value: 4.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 131 IGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEPEsvcstplkrnESSSSVQNyfHLD 210
Cdd:COG4913 604 LGFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDE----------IDVASAER--EIA 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 211 SLQKKLKDLEEENVVLRseacQLKTEtitYEEKEQQLvNDCVKELRDANVQIASISEELakktEDAARQQEEITHLLSQI 290
Cdd:COG4913 672 ELEAELERLDASSDDLA----ALEEQ---LEELEAEL-EELEEELDELKGEIGRLEKEL----EQAEEELDELQDRLEAA 739
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124517685 291 VDLQKKAkscavENEELVQHLGAA------KDAQRQLTAELRELEDKYAECMEMLHEAQEELKN 348
Cdd:COG4913 740 EDLARLE-----LRALLEERFAAAlgdaveRELRENLEERIDALRARLNRAEEELERAMRAFNR 798
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
104-414 |
5.38e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 50.36 E-value: 5.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 104 MTKTYNDIDAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMK-------DELLQF 176
Cdd:pfam02463 179 IEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELlrdeqeeIESSKQ 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 177 YTSAAEESEPESvcstpLKRNESSSSVQNYfhLDSLQKKLKDLEEEnvvLRSEACQLKTETITYEEKEQQLVNDCVKELR 256
Cdd:pfam02463 259 EIEKEEEKLAQV-----LKENKEEEKEKKL--QEEELKLLAKEEEE---LKSELLKLERRKVDDEEKLKESEKEKKKAEK 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 257 DANVQIASISEELAKKTEDAARQQEEIThllsQIVDLQKKAKScavENEELVQHLGAAKDAQRQLTAELRELEDKYAECM 336
Cdd:pfam02463 329 ELKKEKEEIEELEKELKELEIKREAEEE----EEEELEKLQEK---LEQLEEELLAKKKLESERLSSAAKLKEEELELKS 401
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124517685 337 EMLHEAQEELKNLRNKTMPTSRRyhslglfpmDSLAAEIEGTMRKELQLEELESPDITHQKRVFETVRNVNQVVKQRS 414
Cdd:pfam02463 402 EEEKEAQLLLELARQLEDLLKEE---------KKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKS 470
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
105-354 |
5.90e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.45 E-value: 5.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 105 TKTYNDIDAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEeQVEHIREEVSQLR-HELSMKDELLQFYTSAAEE 183
Cdd:PRK03918 458 TAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAE-QLKELEEKLKKYNlEELEKKAEEYEKLKEKLIK 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 184 SEPE-SVCSTPLKRNESSSSvqnyfHLDSLQKKLKDLEEENVVLRSEACQLKTETIT-YEEKEQQL---------VNDCV 252
Cdd:PRK03918 537 LKGEiKSLKKELEKLEELKK-----KLAELEKKLDELEEELAELLKELEELGFESVEeLEERLKELepfyneyleLKDAE 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 253 KELRDANVQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKScaVENEELVQHLGAAKDAQRQLTAELRELEDKY 332
Cdd:PRK03918 612 KELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE--EEYEELREEYLELSRELAGLRAELEELEKRR 689
|
250 260
....*....|....*....|..
gi 124517685 333 AECMEMLHEAQEELKNLRNKTM 354
Cdd:PRK03918 690 EEIKKTLEKLKEELEEREKAKK 711
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
99-412 |
8.04e-06 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 49.47 E-value: 8.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 99 ERVGQMTKTYNDIdaVTRLLEEKERDL----ELAARIgqSLLKKNKTLTERNELL---EEQVEHIREEVSQLR--HELSM 169
Cdd:pfam06160 45 EKFEEWRKKWDDI--VTKSLPDIEELLfeaeELNDKY--RFKKAKKALDEIEELLddiEEDIKQILEELDELLesEEKNR 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 170 K--DELLQFYtsaaeesepESVCSTPLKRNESSSSVqnyfhLDSLQKKLKDLEEE-----------------NVVLrsea 230
Cdd:pfam06160 121 EevEELKDKY---------RELRKTLLANRFSYGPA-----IDELEKQLAEIEEEfsqfeeltesgdylearEVLE---- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 231 cQLKTETITYEEK-EQ--QLVNDCVKELRDANVQIASISEELAKK----TEDAArqQEEITHLLSQIVDLQKKAKSCAVE 303
Cdd:pfam06160 183 -KLEEETDALEELmEDipPLYEELKTELPDQLEELKEGYREMEEEgyalEHLNV--DKEIQQLEEQLEENLALLENLELD 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 304 N-EELVQHLGAAKDA-QRQLTAEL---RELEDKYAECMEMLHEAQEELKNLRNKTMPTSRRYHslglfpmdsLAAEIEGT 378
Cdd:pfam06160 260 EaEEALEEIEERIDQlYDLLEKEVdakKYVEKNLPEIEDYLEHAEEQNKELKEELERVQQSYT---------LNENELER 330
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 124517685 379 MRK-ELQLEELES------PDITHQKRVFETVR-NVNQVVKQ 412
Cdd:pfam06160 331 VRGlEKQLEELEKrydeivERLEEKEVAYSELQeELEEILEQ 372
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
118-352 |
8.31e-06 |
|
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.
Pssm-ID: 462861 [Multi-domain] Cd Length: 302 Bit Score: 48.80 E-value: 8.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 118 LEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELS----MKDELlqfytsaaeesepESVCSTp 193
Cdd:pfam09728 13 LDSPEEKLAALCKKYAELLEEMKRLQKDLKKLKKKQDQLQKEKDQLQSELSkailAKSKL-------------EKLCRE- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 194 lkrnessssvqnyfhldsLQKKLKDLEEENVVLRSEACQLKTETItyeEKEQQLVND---CVKELRDANVQIASISEELA 270
Cdd:pfam09728 79 ------------------LQKQNKKLKEESKKLAKEEEEKRKELS---EKFQSTLKDiqdKMEEKSEKNNKLREENEELR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 271 KKTEDAARQQEeithLLSQIVDLQKKAKscaveneELVQHLGAAKDAQRQLTAELRELEDKYAECMEM---LHEAQEELK 347
Cdd:pfam09728 138 EKLKSLIEQYE----LRELHFEKLLKTK-------ELEVQLAEAKLQQATEEEEKKAQEKEVAKARELkaqVQTLSETEK 206
|
....*
gi 124517685 348 NLRNK 352
Cdd:pfam09728 207 ELREQ 211
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
140-349 |
1.67e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.80 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 140 KTLTERNEL------LEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEPESV--CSTPLKRNESSSSvqnyfHLDS 211
Cdd:PRK04863 841 QLNRRRVELeraladHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLADETLADRVeeIREQLDEAEEAKR-----FVQQ 915
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 212 LQKKLKDLEEENVVLRSEACQLKTETITYEEKEQQLvndcvkelRDANVQIASISEELAKKT----EDAARQQEEITHLL 287
Cdd:PRK04863 916 HGNALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQ--------RDAKQQAFALTEVVQRRAhfsyEDAAEMLAKNSDLN 987
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124517685 288 SQivdLQKKAKSCAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQEELKNL 349
Cdd:PRK04863 988 EK---LRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDL 1046
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
253-413 |
2.05e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 253 KELRDANVQIasisEELAKKTEDAARQQEEITHLLSQIVDLQKKAKSCAVENEELVQHLGAAKDAQR--QLTAELRELED 330
Cdd:COG4717 71 KELKELEEEL----KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQEleALEAELAELPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 331 KYAEcmemLHEAQEELKNLRNKtmptsrryhslglfpMDSLAAEIEgTMRKELQlEELESPDITHQKRVFETVRNVNQVV 410
Cdd:COG4717 147 RLEE----LEERLEELRELEEE---------------LEELEAELA-ELQEELE-ELLEQLSLATEEELQDLAEELEELQ 205
|
...
gi 124517685 411 KQR 413
Cdd:COG4717 206 QRL 208
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
141-388 |
2.10e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.50 E-value: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 141 TLTERnellEEQVEHIREEVSQLRHELSMKDELLQFYTSAAE-ESEPESvcstpLKRNESSSSVQNYFHLDSLQKKLKDL 219
Cdd:PRK02224 469 TIEED----RERVEELEAELEDLEEEVEEVEERLERAEDLVEaEDRIER-----LEERREDLEELIAERRETIEEKRERA 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 220 EEenvvLRSEACQLKTETITYEEKEQQL---VNDCVKELRDANVQIASISEELaKKTEDAARQQEEITHLLSQIVDLQKK 296
Cdd:PRK02224 540 EE----LRERAAELEAEAEEKREAAAEAeeeAEEAREEVAELNSKLAELKERI-ESLERIRTLLAAIADAEDEIERLREK 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 297 AKSCAVENEELVQHLGAAKDAQRQLTAE-----LRELEDKYAECMEMLHEAQEELKNLRNKTmptsrryhslglfpmDSL 371
Cdd:PRK02224 615 REALAELNDERRERLAEKRERKRELEAEfdearIEEAREDKERAEEYLEQVEEKLDELREER---------------DDL 679
|
250
....*....|....*...
gi 124517685 372 AAEIeGTMRKELQ-LEEL 388
Cdd:PRK02224 680 QAEI-GAVENELEeLEEL 696
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
113-389 |
2.29e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.59 E-value: 2.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 113 AVTRLLEEKERDLELAARIGQSL---LKKNKTLTERNELLEEQVEHIREEVSQLRHEL-SMKDELLQfytsAAEESEpes 188
Cdd:COG4372 11 ARLSLFGLRPKTGILIAALSEQLrkaLFELDKLQEELEQLREELEQAREELEQLEEELeQARSELEQ----LEEELE--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 189 vcstplKRNESSSSVQNYfhLDSLQKKLKDLEEENVVLRSEACQLKTETITYEEKEQQLvndcvkelrdaNVQIASISEE 268
Cdd:COG4372 84 ------ELNEQLQAAQAE--LAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQL-----------EAQIAELQSE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 269 LAKKTEDAARQQEEITHLLSQIVDLQKKAKscAVENEELVQHLGAA-KDAQRQLTAELRELEDKYAECMEMLHEAQEELK 347
Cdd:COG4372 145 IAEREEELKELEEQLESLQEELAALEQELQ--ALSEAEAEQALDELlKEANRNAEKEEELAEAEKLIESLPRELAEELLE 222
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 124517685 348 NLRNKTMPTSRRYHSLGLFPMDSLAAEIEGTMRKELQLEELE 389
Cdd:COG4372 223 AKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELE 264
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
113-349 |
2.32e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.50 E-value: 2.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 113 AVTRLLEEKERDLE-LAARIGQsllKKNKTLTER-NEL------LEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEES 184
Cdd:PRK02224 177 GVERVLSDQRGSLDqLKAQIEE---KEEKDLHERlNGLeselaeLDEEIERYEEQREQARETRDEADEVLEEHEERREEL 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 185 EP---------ESVCSTPLKRNESSSSVQnyfhldSLQKKLKDLEEENVVLRSEAcqlktetiTYEEKEQQLVNDCVKEL 255
Cdd:PRK02224 254 ETleaeiedlrETIAETEREREELAEEVR------DLRERLEELEEERDDLLAEA--------GLDDADAEAVEARREEL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 256 RDanvQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKSCAVENEELVQHLGAAKDAQRQLTAELRELEDKYAEC 335
Cdd:PRK02224 320 ED---RDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEEL 396
|
250
....*....|....
gi 124517685 336 MEMLHEAQEELKNL 349
Cdd:PRK02224 397 RERFGDAPVDLGNA 410
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
253-413 |
2.62e-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: 47.45 E-value: 2.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 253 KELRDANVQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKSCAVENEELVQHLGAAKDAQRQLTAELRELEDKY 332
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 333 AECMEML--HEAQEELKNLRNKTMP--TSRRYHSLGLFpMDSLAAEIEGTMRKELQLEELESpDITHQKRVFETVRNVNQ 408
Cdd:COG4942 107 AELLRALyrLGRQPPLALLLSPEDFldAVRRLQYLKYL-APARREQAEELRADLAELAALRA-ELEAERAELEALLAELE 184
|
....*
gi 124517685 409 VVKQR 413
Cdd:COG4942 185 EERAA 189
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
118-352 |
3.46e-05 |
|
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: 47.71 E-value: 3.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 118 LEEKERDLEL----AARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELS-MKDEL---------LQFYTSAAEE 183
Cdd:TIGR04523 389 LESQINDLESkiqnQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKdLTNQDsvkeliiknLDNTRESLET 468
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 184 SEpeSVCSTPLKRNESSSS------VQNYFHLDSLQKKLKDLEEENVVLRSEACQLKtetityeEKEQQLVNdcvkELRD 257
Cdd:TIGR04523 469 QL--KVLSRSINKIKQNLEqkqkelKSKEKELKKLNEEKKELEEKVKDLTKKISSLK-------EKIEKLES----EKKE 535
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 258 ANVQIASISEELAKKTEDAARQQ--EEITHLLSQIVDLQKKAKSCAVENEELVQHLGAAKDAQRQLTAELRELEDKYAEC 335
Cdd:TIGR04523 536 KESKISDLEDELNKDDFELKKENleKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSL 615
|
250 260
....*....|....*....|....
gi 124517685 336 MEMLHEAQEE-------LKNLRNK 352
Cdd:TIGR04523 616 EKELEKAKKEneklssiIKNIKSK 639
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
234-415 |
3.73e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.20 E-value: 3.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 234 KTETITYEEKEQQLVNDCVKELRDANVQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKSCAVENEELVQHLGA 313
Cdd:COG4372 12 RLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 314 AKDAQRQLTAELRELEDKYAECMEMLHEAQEELKNLRNKTMPTSRRYhslglfpmDSLAAEIEgtmRKELQLEELESpDI 393
Cdd:COG4372 92 AQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQI--------AELQSEIA---EREEELKELEE-QL 159
|
170 180
....*....|....*....|..
gi 124517685 394 THQKRVFETVRNVNQVVKQRSL 415
Cdd:COG4372 160 ESLQEELAALEQELQALSEAEA 181
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
214-352 |
4.70e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 4.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 214 KKLKDLEEENVVLRSEACQLKTETITYEEKEQQLVN---------------DCVKELRDANVQIASISEELA---KKTED 275
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEEleaeleelreeleklEKLLQLLPLYQELEALEAELAelpERLEE 150
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124517685 276 AARQQEEITHLLSQIVDLQKKAKSCAVENEELVQHLGAAKDAQ-RQLTAELRELEDKYAECMEMLHEAQEELKNLRNK 352
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELEELEEE 228
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
85-382 |
4.87e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 47.27 E-value: 4.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 85 EQIEETLKYFLLCAERVGQMT-KTYNDIDAVTRLLEEKERDLELAArigqSLLKKNKTLTERNELLEEQVEHIREEVSQL 163
Cdd:TIGR00618 472 EQQLQTKEQIHLQETRKKAVVlARLLELQEEPCPLCGSCIHPNPAR----QDIDNPGPLTRRMQRGEQTYAQLETSEEDV 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 164 RHELSMKDELLQFYtSAAEESEPESVCSTPLKRNESSSSvqnyfhLDSLQKKLKDLEEENVVLRSEACQLKTETITYEEK 243
Cdd:TIGR00618 548 YHQLTSERKQRASL-KEQMQEIQQSFSILTQCDNRSKED------IPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRK 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 244 EQQLVNDCVKELRDANVQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKaKSCAVENEelvqhLGAAKDAQRQLTA 323
Cdd:TIGR00618 621 LQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKE-LLASRQLA-----LQKMQSEKEQLTY 694
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124517685 324 ELRELEdkyaECMEMLHEAQEELKNLRNKTMPTSRRYHSLG--LFPMDSLAAEIEGTMRKE 382
Cdd:TIGR00618 695 WKEMLA----QCQTLLRELETHIEEYDREFNEIENASSSLGsdLAAREDALNQSLKELMHQ 751
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
115-349 |
5.74e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 47.09 E-value: 5.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 115 TRLLEEKERDLELAARIGQSLLKKNKTL-TERNELLEE--QVEHIREEVSQLRHELSMKDELLQFYTSAAEESEPEsvcs 191
Cdd:pfam01576 355 TQALEELTEQLEQAKRNKANLEKAKQALeSENAELQAElrTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAE---- 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 192 tplkRNESSSSVQNyfHLDSLQKKLKDLEEENVVLRSEACQLK-----TETITYEEKEQQLVNDcvKELRDANVQIASIS 266
Cdd:pfam01576 431 ----LAEKLSKLQS--ELESVSSLLNEAEGKNIKLSKDVSSLEsqlqdTQELLQEETRQKLNLS--TRLRQLEDERNSLQ 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 267 EELAKKTEDAARQQEEITHLLSQIVDLQKKAKSCAVENEELVQhlgAAKDAQRQLTAELRELEDKyAECMEMLHEA---- 342
Cdd:pfam01576 503 EQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEE---GKKRLQRELEALTQQLEEK-AAAYDKLEKTknrl 578
|
....*..
gi 124517685 343 QEELKNL 349
Cdd:pfam01576 579 QQELDDL 585
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
157-354 |
7.57e-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: 45.78 E-value: 7.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 157 REEVSQLRHELsMKDE--LLQFYTSAAEEsepesvcsTPLKRNESSSSVQNYFHLDS----------LQKKLKDLEEENV 224
Cdd:smart00787 83 RDLFKEIEEET-LINNppLFKEYFSASPD--------VKLLMDKQFQLVKTFARLEAkkmwyewrmkLLEGLKEGLDENL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 225 -VLRSEACQLKtetityeeKEQQLVNDCVKELRDAN-------VQIASISEELAK-KTEDAARQQEEITHLLSQIVDLQK 295
Cdd:smart00787 154 eGLKEDYKLLM--------KELELLNSIKPKLRDRKdaleeelRQLKQLEDELEDcDPTELDRAKEKLKKLLQEIMIKVK 225
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124517685 296 KAKSCAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEM-LHEA---QEELKNLRNKTM 354
Cdd:smart00787 226 KLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGFtFKEIeklKEQLKLLQSLTG 288
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
85-389 |
8.11e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 8.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 85 EQIEETLKYFLLCAERVGQMTKTY----NDIDAVTRLLEEKERDLELAARIG--------QSLLKKNKTLTERNELLEEQ 152
Cdd:COG4717 135 EALEAELAELPERLEELEERLEELreleEELEELEAELAELQEELEELLEQLslateeelQDLAEELEELQQRLAELEEE 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 153 VEHIREEVSQLRHELsmkDELLQFYTSAAEESEPESVCST--------------------------------------PL 194
Cdd:COG4717 215 LEEAQEELEELEEEL---EQLENELEAAALEERLKEARLLlliaaallallglggsllsliltiagvlflvlgllallFL 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 195 KRNESSSSVQNYFHLDSLQKKLKDLEEENVVLRSEACQLKtETITYEEKEQQLvnDCVKELRDANVQIASISEELAKKTE 274
Cdd:COG4717 292 LLAREKASLGKEAEELQALPALEELEEEELEELLAALGLP-PDLSPEELLELL--DRIEELQELLREAEELEEELQLEEL 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 275 DAARQQ----------EEITHLLSQIVDLQKKAKSCAVENEELVQHLGAAKDAQR-----QLTAELRELEDKYAECMEML 339
Cdd:COG4717 369 EQEIAAllaeagvedeEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEaldeeELEEELEELEEELEELEEEL 448
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 124517685 340 HEAQEELKNLRN--KTMPTSRRYhslglfpmDSLAAEIEgtmRKELQLEELE 389
Cdd:COG4717 449 EELREELAELEAelEQLEEDGEL--------AELLQELE---ELKAELRELA 489
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
82-352 |
8.13e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 46.61 E-value: 8.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 82 LTTEQIEETLKYFLLCAERVGQMTKTYNdidaVTRLLEEKERDL---ELAARIGQSLLKKNKTLTERNELLEEQ----VE 154
Cdd:COG5022 803 LSLLGSRKEYRSYLACIIKLQKTIKREK----KLRETEEVEFSLkaeVLIQKFGRSLKAKKRFSLLKKETIYLQsaqrVE 878
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 155 HIREEVSQLRHELSMKDEL-LQFYTSAAEESEpesvcstpLKRNESSSSVQNYFHLDSLQKKLKDLEEENVVLRSEACQL 233
Cdd:COG5022 879 LAERQLQELKIDVKSISSLkLVNLELESEIIE--------LKKSLSSDLIENLEFKTELIARLKKLLNNIDLEEGPSIEY 950
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 234 --KTETITYEEKEQQLvNDCVKELRDANVQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKSCAVENEElVQHL 311
Cdd:COG5022 951 vkLPELNKLHEVESKL-KETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPVE-VAEL 1028
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 124517685 312 GAAKDAQRQLTAELR---ELEDKYAECMEMLHEAQEELKNLRNK 352
Cdd:COG5022 1029 QSASKIISSESTELSilkPLQKLKGLLLLENNQLQARYKALKLR 1072
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
129-342 |
8.88e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 46.43 E-value: 8.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 129 ARIgQSLLKKNKTLTERnelleeqvEHIREEVSQLRHELSMKDEllQFYTSAAEESEPESVCSTPLK-RNE-SSSSVQNY 206
Cdd:PLN02939 150 ARL-QALEDLEKILTEK--------EALQGKINILEMRLSETDA--RIKLAAQEKIHVEILEEQLEKlRNElLIRGATEG 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 207 FHLDSLQKKLKDLEEENVVLRSEACQLKTETITYEEKEQQLVNdCVKE--LRDANVQiasiseELAKKTEDAarqQEEIt 284
Cdd:PLN02939 219 LCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAETEERVFK-LEKErsLLDASLR------ELESKFIVA---QEDV- 287
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124517685 285 hllSQIVDLQKKAKSCAVENEELVqhLGAAKDAQRQLTAEL---RELEDKYAECMEMLHEA 342
Cdd:PLN02939 288 ---SKLSPLQYDCWWEKVENLQDL--LDRATNQVEKAALVLdqnQDLRDKVDKLEASLKEA 343
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
150-332 |
1.01e-04 |
|
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.
Pssm-ID: 427715 [Multi-domain] Cd Length: 360 Bit Score: 45.46 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 150 EEQVEHIREEVSQLRHEL-----SMKDELLQFYTSAAEesePESVCSTPLKRNESSSSVQNYFH-LDSLQKKLKDLeeen 223
Cdd:pfam04108 111 EDSVEILRDALKELIDELqaaqeSLDSDLKRFDDDLRD---LQKELESLSSPSESISLIPTLLKeLESLEEEMASL---- 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 224 vvLRS-----EACQL--------KTETITYEEKEQQLVNDCVKELRDANVQIASISEELAKKTEDAARQQEEITHLLSQI 290
Cdd:pfam04108 184 --LESltnhyDQCVTavklteggRAEMLEVLENDARELDDVVPELQDRLDEMENNYERLQKLLEQKNSLIDELLSALQLI 261
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 124517685 291 VDLQKKAKSCAVENEELVQHLGAAKDAQRQLTAELRELEDKY 332
Cdd:pfam04108 262 AEIQSRLPEYLAALKEFEERWEEEKETIEDYLSELEDLREFY 303
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
109-349 |
1.01e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.53 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 109 NDIDAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELsmkdellqfytsAAEESEpes 188
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQEL------------AALEAE--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 189 vcstpLKRNESSssvqnyfhLDSLQKKLKDLEEENVVLRSEACQLKTETITYEEKEQQLVNDCVKELRDanvqIASISEE 268
Cdd:COG4942 85 -----LAELEKE--------IAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQY----LKYLAPA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 269 LAKKTEDAARQQEEITHLLSQIVDLQKKAKSCAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQEELKN 348
Cdd:COG4942 148 RREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
.
gi 124517685 349 L 349
Cdd:COG4942 228 L 228
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
110-353 |
1.39e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 45.60 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 110 DIDAVTRLLEEkerdlELAARigQSLLKKNKTLTErnelleeQVEHIREEVSQLRHELsmkDELLQFYTSAAEESEpesv 189
Cdd:PRK04778 290 RIDQLYDILER-----EVKAR--KYVEKNSDTLPD-------FLEHAKEQNKELKEEI---DRVKQSYTLNESELE---- 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 190 cstplkrnessssvqnyfHLDSLQKKLKDLEEENVVLRSEacqLKTETITYEEKEQQLvNDCVKELRDANVQIASISEEL 269
Cdd:PRK04778 349 ------------------SVRQLEKQLESLEKQYDEITER---IAEQEIAYSELQEEL-EEILKQLEEIEKEQEKLSEML 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 270 AKKTEDAARQQEEITHLLSQIVDLQKKakscaVEN-------EELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEA 342
Cdd:PRK04778 407 QGLRKDELEAREKLERYRNKLHEIKRY-----LEKsnlpglpEDYLEMFFEVSDEIEALAEELEEKPINMEAVNRLLEEA 481
|
250
....*....|.
gi 124517685 343 QEELKNLRNKT 353
Cdd:PRK04778 482 TEDVETLEEET 492
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
116-284 |
1.46e-04 |
|
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: 44.53 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 116 RLLEEKERDLELA--ARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEpesvcstp 193
Cdd:COG1579 8 ALLDLQELDSELDrlEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE-------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 194 lkrnESSSSVQNYFHLDSLQKKLKDLEEENVVLRSEACQLKTEtityEEKEQQLVNDCVKELRDANVQIASISEELAKKT 273
Cdd:COG1579 80 ----EQLGNVRNNKEYEALQKEIESLKRRISDLEDEILELMER----IEELEEELAELEAELAELEAELEEKKAELDEEL 151
|
170
....*....|.
gi 124517685 274 EDAARQQEEIT 284
Cdd:COG1579 152 AELEAELEELE 162
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
147-352 |
1.52e-04 |
|
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: 45.81 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 147 ELLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEPESVCSTPL---------KRNESSSSVQNYF-----HLDSL 212
Cdd:TIGR00606 635 QDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVcqrvfqteaELQEFISDLQSKLrlapdKLKST 714
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 213 QKKLKDLEEEnvvlrseacqlKTETITYEEKEQQLVNDCVKELRDANVQIASISEELAKKTEDAARQQEeithLLSQIVD 292
Cdd:TIGR00606 715 ESELKKKEKR-----------RDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQET----LLGTIMP 779
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124517685 293 LQKKAKSCAVENEELVQHLGAAKDAQR---QLTAELR--ELEDKYAECMEMLHEAQEELKNLRNK 352
Cdd:TIGR00606 780 EEESAKVCLTDVTIMERFQMELKDVERkiaQQAAKLQgsDLDRTVQQVNQEKQEKQHELDTVVSK 844
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
103-299 |
2.17e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.75 E-value: 2.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 103 QMTKTYNDIDAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSmkdELLQFYTSAAE 182
Cdd:COG4942 42 ELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELA---ELLRALYRLGR 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 183 ESEPESVcstpLKRNESSSSVQNYFHLDSLQKKLKDLEEENVVLRSEACQLKTETITYEEKEQQLVNDCVKELRDANVQI 262
Cdd:COG4942 119 QPPLALL----LSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALK 194
|
170 180 190
....*....|....*....|....*....|....*..
gi 124517685 263 ASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKS 299
Cdd:COG4942 195 AERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
78-405 |
2.43e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.83 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 78 ANIDlttEQIEETLKYfllcAERVgQMTKTYNDIDAVTRLLEEKERDLelaarigQSLLKKNKTLTERNELLEEQVEHIR 157
Cdd:PRK04778 82 PDIE---EQLFEAEEL----NDKF-RFRKAKHEINEIESLLDLIEEDI-------EQILEELQELLESEEKNREEVEQLK 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 158 EEVSQLRHELSMKDELlqfYTSAAEE-----SEPESVCSTPLKRNESSSSVQNYFHLDSLQKKLKDLE-----------E 221
Cdd:PRK04778 147 DLYRELRKSLLANRFS---FGPALDElekqlENLEEEFSQFVELTESGDYVEAREILDQLEEELAALEqimeeipellkE 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 222 ENVVLRSEACQLKTetiTYEE-KEQQLV---NDCVKELRDANVQIASISEELA----KKTEDAARQ-QEEITHLLSQI-- 290
Cdd:PRK04778 224 LQTELPDQLQELKA---GYRElVEEGYHldhLDIEKEIQDLKEQIDENLALLEeldlDEAEEKNEEiQERIDQLYDILer 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 291 -VDLQKKAKScavENEELVQHLGAAKDAQRQLTAELRELEDKY---AECMEMLHEAQEELKNLRNKTMPTSRRYHSlGLF 366
Cdd:PRK04778 301 eVKARKYVEK---NSDTLPDFLEHAKEQNKELKEEIDRVKQSYtlnESELESVRQLEKQLESLEKQYDEITERIAE-QEI 376
|
330 340 350
....*....|....*....|....*....|....*....
gi 124517685 367 PMDSLAAEIEGTMRkelQLEELEspdiTHQKRVFETVRN 405
Cdd:PRK04778 377 AYSELQEELEEILK---QLEEIE----KEQEKLSEMLQG 408
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
109-299 |
3.03e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.37 E-value: 3.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 109 NDIDAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELS--------MKDELLQF---- 176
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAelraeleaQKEELAELlral 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 177 YTSAAEESEPESVCSTPLKRNESSSSVQNYF------HLDSLQKKLKDLEEENVVLRSEACQLKTETITYEEKEQQL--- 247
Cdd:COG4942 114 YRLGRQPPLALLLSPEDFLDAVRRLQYLKYLaparreQAEELRADLAELAALRAELEAERAELEALLAELEEERAALeal 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 124517685 248 VNDCVKELRDANVQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKS 299
Cdd:COG4942 194 KAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
253-352 |
3.18e-04 |
|
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: 43.37 E-value: 3.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 253 KELRDANVQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKSCAVENEELVQH-------LGAAKDAqRQLTA-- 323
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARikkyeeqLGNVRNN-KEYEAlq 95
|
90 100 110
....*....|....*....|....*....|....*..
gi 124517685 324 --------ELRELEDKYAECMEMLHEAQEELKNLRNK 352
Cdd:COG1579 96 keieslkrRISDLEDEILELMERIEELEEELAELEAE 132
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
209-352 |
3.65e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 3.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 209 LDSLQKKLKDLEEENVVLRSEACQLKTETITYEEKEQQLVNDCVKELRDANVQIASIS--EEL--AKKTEDAARQQEEIT 284
Cdd:COG3883 46 LEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSylDVLlgSESFSDFLDRLSALS 125
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124517685 285 HLLSQ---IVDLQKKAKscavenEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQEELKNLRNK 352
Cdd:COG3883 126 KIADAdadLLEELKADK------AELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAE 190
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
112-346 |
3.65e-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: 44.44 E-value: 3.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 112 DAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEPESVCS 191
Cdd:pfam12128 269 SDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQ 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 192 TPLKRNESSSSVQNyfhLDSLQKKLKDLEEEnvvlrseacqlktetitYEEKEQQLVNDCVKElrdanvqIASISEELAK 271
Cdd:pfam12128 349 LPSWQSELENLEER---LKALTGKHQDVTAK-----------------YNRRRSKIKEQNNRD-------IAGIKDKLAK 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 272 KTEDAARQQEEITHLLSQI-----VDLQKKAKSCAVENEELVQHLGAAKDAQRQLTAELRELEDKyAECMEMLHEAQEEL 346
Cdd:pfam12128 402 IREARDRQLAVAEDDLQALeselrEQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQL-ENFDERIERAREEQ 480
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
209-388 |
3.83e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.98 E-value: 3.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 209 LDSLQKKLKDLEEENVVLRSEACQLKTETITYEEKEQQL---VNDCVKELRDANVQIASISEELAKKTEDAARQ------ 279
Cdd:COG4942 36 IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALeqeLAALEAELAELEKEIAELRAELEAQKEELAELlralyr 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 280 ---QEEITHLLSQ--IVDLQKKAKSCAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQEELKNL----- 349
Cdd:COG4942 116 lgrQPPLALLLSPedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALealka 195
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 124517685 350 -RNKTMPTSRRyhslglfPMDSLAAEIEGTMRKELQLEEL 388
Cdd:COG4942 196 eRQKLLARLEK-------ELAELAAELAELQQEAEELEAL 228
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
85-358 |
4.27e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 4.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 85 EQIEETLKYFLLCAERVGQMTKTYNDIDAVTRLLEEKERDLElaarigqSLLKKNKTLTErnelLEEQVEHIREEVSQLR 164
Cdd:COG4913 637 EAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELE-------RLDASSDDLAA----LEEQLEELEAELEELE 705
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 165 HELsmkDELLQFYTSAAEEsepesvcstpLKRNESSssvqnyfhLDSLQKKLKDLEEENVVLRSEACQlktetityEEKE 244
Cdd:COG4913 706 EEL---DELKGEIGRLEKE----------LEQAEEE--------LDELQDRLEAAEDLARLELRALLE--------ERFA 756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 245 QQLVNDCVKELRDAnvqiasISEELAKKTEDAARQQEEITHLLSQIVDLQKkakscaveneELVQHLGAAKDAQRQLTAE 324
Cdd:COG4913 757 AALGDAVERELREN------LEERIDALRARLNRAEEELERAMRAFNREWP----------AETADLDADLESLPEYLAL 820
|
250 260 270
....*....|....*....|....*....|....
gi 124517685 325 LRELEDkyaecmEMLHEAQEELKNLRNKTMPTSR 358
Cdd:COG4913 821 LDRLEE------DGLPEYEERFKELLNENSIEFV 848
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
194-328 |
4.87e-04 |
|
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, microtubule-binding protein consisting of two 1,600-amino acid-long coils, is essential for the full functioning of the mitotic checkpoint pathway. There are several leucine-rich repeats along the sequence of LEK1 that are considered to be zippers, though they do not appear to be binding DNA directly in this instance.
Pssm-ID: 463102 [Multi-domain] Cd Length: 140 Bit Score: 41.13 E-value: 4.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 194 LKRNES-SSSVQNyfHLDSLQKKLKDLEEENVVLRSEACQLKTETITYEEKEQQLVndcvKELRDANVQIASISEELAKK 272
Cdd:pfam10473 12 LKESERkADSLKD--KVENLERELEMSEENQELAILEAENSKAEVETLKAEIEEMA----QNLRDLELDLVTLRSEKENL 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 124517685 273 TEDAARQQEEITHLLSQIVDLQKKAKscaVENEELVQHLGAAKDAQRQLTAELREL 328
Cdd:pfam10473 86 TKELQKKQERVSELESLNSSLENLLE---EKEQEKVQMKEESKTAVEMLQTQLKEL 138
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
87-382 |
5.81e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 43.79 E-value: 5.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 87 IEETLKYFLLCAERVGQMtKTYNDidAVTRLLEEKErDLELAARIGQSLLKKNktLTERNELLEEQVEHIREEVSQLRHE 166
Cdd:COG5185 231 IEEALKGFQDPESELEDL-AQTSD--KLEKLVEQNT-DLRLEKLGENAESSKR--LNENANNLIKQFENTKEKIAEYTKS 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 167 LSMKDELLQF--YTSAAEES-EPESvcstplKRNESSSSVQNYFHldSLQKKLKDLEEENVVLRSEACQLKTETITYEEK 243
Cdd:COG5185 305 IDIKKATESLeeQLAAAEAEqELEE------SKRETETGIQNLTA--EIEQGQESLTENLEAIKEEIENIVGEVELSKSS 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 244 EqqlvndcvkELRDANVQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKakscavENEELVQHLGAA----KDAQR 319
Cdd:COG5185 377 E---------ELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADR------QIEELQRQIEQAtssnEEVSK 441
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124517685 320 QLTAELRELEDKYAECMEMLHEAQEELKNLRNKTMPTSRRYHSLGLFPMDSLAAEIEGTMRKE 382
Cdd:COG5185 442 LLNELISELNKVMREADEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKL 504
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
126-349 |
6.02e-04 |
|
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: 43.63 E-value: 6.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 126 ELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSmkDELLQFytsaaeesepesvcstplKRNESSssvqn 205
Cdd:pfam01576 320 ELRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELT--EQLEQA------------------KRNKAN----- 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 206 yfhldsLQKKLKDLEEENVVLRSEA---CQLKTETITYEEKEQQLVNDCVKELRDANVQiasiSEELAKKTEDAARQQEE 282
Cdd:pfam01576 375 ------LEKAKQALESENAELQAELrtlQQAKQDSEHKRKKLEGQLQELQARLSESERQ----RAELAEKLSKLQSELES 444
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124517685 283 ITHLLSQI-VDLQKKAKSCAVENEEL--VQHLGAAKDAQR-QLTAELRELEDKYAECMEMLHEAQEELKNL 349
Cdd:pfam01576 445 VSSLLNEAeGKNIKLSKDVSSLESQLqdTQELLQEETRQKlNLSTRLRQLEDERNSLQEQLEEEEEAKRNV 515
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
117-401 |
6.61e-04 |
|
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: 43.63 E-value: 6.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 117 LLEEKERDLELAARIGQsLLKKNKTLTERNELLEEQVEHIRE---EVSQLRHELSMK----DELLQFYTSAAEESEpESV 189
Cdd:pfam01576 14 LQKVKERQQKAESELKE-LEKKHQQLCEEKNALQEQLQAETElcaEAEEMRARLAARkqelEEILHELESRLEEEE-ERS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 190 CSTPLKRNESSSSVQNY-FHLD--------------SLQKKLKDLEEENVVLRSEACQLKTETITYEEKEQQLVNDCVKE 254
Cdd:pfam01576 92 QQLQNEKKKMQQHIQDLeEQLDeeeaarqklqlekvTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 255 ---------LRDANVQIASISEELAKKTEDAARQQE--------EITHLLSQIVDLQKKAKSCAVENEELVQHLGAAKDA 317
Cdd:pfam01576 172 eekakslskLKNKHEAMISDLEERLKKEEKGRQELEkakrklegESTDLQEQIAELQAQIAELRAQLAKKEEELQAALAR 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 318 QRQLTAELRELEDKYAECMEMLHEAQEELKNLRNKTMPTSRRYHSLGLfPMDSLAAEIEGTMRKELQLEELESP---DIT 394
Cdd:pfam01576 252 LEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGE-ELEALKTELEDTLDTTAAQQELRSKreqEVT 330
|
....*..
gi 124517685 395 HQKRVFE 401
Cdd:pfam01576 331 ELKKALE 337
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
206-354 |
7.20e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 7.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 206 YFHLDSLQKKLKDLEEENVVLRSEAcQLKTETITYE------EKEQQLVNDCVKELRDANVQIASISEELAKKTEDAARQ 279
Cdd:PRK12704 23 FVRKKIAEAKIKEAEEEAKRILEEA-KKEAEAIKKEalleakEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRK 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124517685 280 QEeithllsqivDLQKKakscaveNEELVQHlgaakdaQRQLTAELRELEDKYAECMEMLHEAQEELKNLRNKTM 354
Cdd:PRK12704 102 LE----------LLEKR-------EEELEKK-------EKELEQKQQELEKKEEELEELIEEQLQELERISGLTA 152
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
114-386 |
8.26e-04 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 43.14 E-value: 8.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 114 VTRLLEEKerdlelaarigQSLLKKNKTLTERNE-----------------LLEEQVEHIREEVSQL---RHELSMKDEL 173
Cdd:pfam05622 23 VSLLQEEK-----------NSLQQENKKLQERLDqlesgddsgtpggkkylLLQKQLEQLQEENFRLetaRDDYRIKCEE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 174 L-----------QFYTSAAEES-----EPESVCSTPLKRNESSSSVQNYFH----LDSLQKKLKDLEEENVVLRSEACQl 233
Cdd:pfam05622 92 LekevlelqhrnEELTSLAEEAqalkdEMDILRESSDKVKKLEATVETYKKkledLGDLRRQVKLLEERNAEYMQRTLQ- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 234 ktetitYEEkeqqlvndcvkELRDANvqiasiseelakktedAARQQEEIthLLSQIVDLQKKAKSCAVENEELVQHLga 313
Cdd:pfam05622 171 ------LEE-----------ELKKAN----------------ALRGQLET--YKRQVQELHGKLSEESKKADKLEFEY-- 213
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124517685 314 aKDAQRQLTAELRELEDKYAECmEMLHEAQEELK--NLRNKTMPTSRRYHSLGLFPMDSLAAEIEGTMRKE----LQLE 386
Cdd:pfam05622 214 -KKLEEKLEALQKEKERLIIER-DTLRETNEELRcaQLQQAELSQADALLSPSSDPGDNLAAEIMPAEIREklirLQHE 290
|
|
| PRK14160 |
PRK14160 |
heat shock protein GrpE; Provisional |
241-349 |
1.02e-03 |
|
heat shock protein GrpE; Provisional
Pssm-ID: 237629 [Multi-domain] Cd Length: 211 Bit Score: 41.66 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 241 EEKEQQLVNDCVKELRDANVQiASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKScavENEELVQHLGAAKDAQRQ 320
Cdd:PRK14160 11 ENMEEDCCKENENKEEDKGKE-EDLEFEEIEKEEIIEDSEESNEVKIEELKDENNKLKE---ENKKLENELEALKDRLLR 86
|
90 100 110
....*....|....*....|....*....|....*...
gi 124517685 321 LTAEL--------RELEDKYAE-CMEMLHEAQEELKNL 349
Cdd:PRK14160 87 TVAEYdnyrkrtaKEKEGIYSDaCEDVLKELLPVLDNL 124
|
|
| PRK08476 |
PRK08476 |
F0F1 ATP synthase subunit B'; Validated |
263-355 |
1.43e-03 |
|
F0F1 ATP synthase subunit B'; Validated
Pssm-ID: 181442 [Multi-domain] Cd Length: 141 Bit Score: 40.06 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 263 ASISEELAKKTEDAArqqeEITHLLSQIVDLQKKAKSCAveNEELVQHLGAAKD-AQRQLTAELRELEDKYAECMEMLHE 341
Cdd:PRK08476 41 ASIKNDLEKVKTNSS----DVSEIEHEIETILKNAREEA--NKIRQKAIAKAKEeAEKKIEAKKAELESKYEAFAKQLAN 114
|
90
....*....|....
gi 124517685 342 AQEELKNLRNKTMP 355
Cdd:PRK08476 115 QKQELKEQLLSQMP 128
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
113-350 |
1.47e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 113 AVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRhelsmKDELLQFYTSAAEEsepesvcst 192
Cdd:COG4717 320 ELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQE-----IAALLAEAGVEDEE--------- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 193 plkrnESSSSVQNYFHLDSLQKKLKDLEEEnvvLRSEACQLKTETITYEEKEQQlvndcvKELRDANVQIASISEELAKK 272
Cdd:COG4717 386 -----ELRAALEQAEEYQELKEELEELEEQ---LEELLGELEELLEALDEEELE------EELEELEEELEELEEELEEL 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 273 TEDAARQQEEITHLlsqivdlqkkakscavENEELVQHLgaaKDAQRQLTAELRELEDKYAECM---EMLHEAQEELKNL 349
Cdd:COG4717 452 REELAELEAELEQL----------------EEDGELAEL---LQELEELKAELRELAEEWAALKlalELLEEAREEYREE 512
|
.
gi 124517685 350 R 350
Cdd:COG4717 513 R 513
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
213-350 |
1.58e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.33 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 213 QKKLKDLEEENVVLRSEACQLKTETITYEEKEQQLV------NDCVKELRDANVQIASISEELAKKTEDAARQQEEITHL 286
Cdd:PRK02224 198 EKEEKDLHERLNGLESELAELDEEIERYEEQREQARetrdeaDEVLEEHEERREELETLEAEIEDLRETIAETEREREEL 277
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124517685 287 LSQIVDLQKKAKSCAVENEELVQHLG-------AAKDAQRQLTAELRELEDKYAECMEMLHEAQEELKNLR 350
Cdd:PRK02224 278 AEEVRDLRERLEELEEERDDLLAEAGlddadaeAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLR 348
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
209-352 |
1.72e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.23 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 209 LDSLQKKLKDLEEE-NVVLRseACQLKTEtitYEEKEQQLVndcVKELRDANVQIASISEELAKKTEDAARQQEEITHLL 287
Cdd:COG1196 195 LGELERQLEPLERQaEKAER--YRELKEE---LKELEAELL---LLKLRELEAELEELEAELEELEAELEELEAELAELE 266
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124517685 288 SQIVDLQKKAKSCAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQEELKNLRNK 352
Cdd:COG1196 267 AELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEE 331
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
143-349 |
1.82e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 42.25 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 143 TERNEL------LEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEPESVCSTplkRNESSSSVQNYFHLDSLQKKL 216
Cdd:COG3096 843 QRRSELerelaqHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLLADETLADRLEEL---REELDAAQEAQAFIQQHGKAL 919
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 217 KDLEEENVVLRSEACQLKTETITYEEKEQQLvndcvkelRDANVQIASISEELAKKT----EDAARQQEEITHLlsqivd 292
Cdd:COG3096 920 AQLEPLVAVLQSDPEQFEQLQADYLQAKEQQ--------RRLKQQIFALSEVVQRRPhfsyEDAVGLLGENSDL------ 985
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124517685 293 lqkkakscaveNEELVQHLGAAKDAQRQLTAELRELEDKYAECM--------------EMLHEAQEELKNL 349
Cdd:COG3096 986 -----------NEKLRARLEQAEEARREAREQLRQAQAQYSQYNqvlaslkssrdakqQTLQELEQELEEL 1045
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
44-353 |
1.96e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 42.13 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 44 SLLEEQLPHYKLRADTIYGYDHddwlhtpLISPDANIdltTEQIEETLKYFLLCAERVGQMTKTYN-----DIDAVTRLL 118
Cdd:PTZ00440 379 NLFNKLFGDLKEKIETLLDSEY-------FISKYTNI---ISLSEHTLKAAEDVLKENSQKIADYAlysnlEIIEIKKKY 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 119 EEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEPESVCSTPLKR-- 196
Cdd:PTZ00440 449 DEKINELKKSINQLKTLISIMKSFYDLIISEKDSMDSKEKKESSDSNYQEKVDELLQIINSIKEKNNIVNNNFKNIEDyy 528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 197 ----------NESSSSVQNYfhLDSlQKKLKDLEEENVVLRSeacQLKTETITYEEKeqqlvNDCVKELRDANVQIASIS 266
Cdd:PTZ00440 529 itieglkneiEGLIELIKYY--LQS-IETLIKDEKLKRSMKN---DIKNKIKYIEEN-----VDHIKDIISLNDEIDNII 597
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 267 EELAKKTEDAARQQEEITHllsQIVDLQKKAKSCAVEneelvQHLGAAKDAQRQLTAELRELEDKYAEcmemlHEAQEEL 346
Cdd:PTZ00440 598 QQIEELINEALFNKEKFIN---EKNDLQEKVKYILNK-----FYKGDLQELLDELSHFLDDHKYLYHE-----AKSKEDL 664
|
....*..
gi 124517685 347 KNLRNKT 353
Cdd:PTZ00440 665 QTLLNTS 671
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
204-388 |
2.22e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 40.27 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 204 QNYF------HLDsLQKKLKDleeenvvlrsEACQLKTEtityEEKEQQLVNDCVKE-------LRDANVQIasisEELA 270
Cdd:pfam13851 14 KNYYnditrnNLE-LIKSLKE----------EIAELKKK----EERNEKLMSEIQQEnkrltepLQKAQEEV----EELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 271 KKTEDAARQQEEITHLLSQIVDLQKKAKSCAVENEELVQHLgaakdaqRQLTAELRELEDKYAecmEMLHEAQE--ELKN 348
Cdd:pfam13851 75 KQLENYEKDKQSLKNLKARLKVLEKELKDLKWEHEVLEQRF-------EKVERERDELYDKFE---AAIQDVQQktGLKN 144
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 124517685 349 LRNKTMptsrryhslglfpMDSLAAEIEgtmRKELQLEEL 388
Cdd:pfam13851 145 LLLEKK-------------LQALGETLE---KKEAQLNEV 168
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
135-351 |
2.60e-03 |
|
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular sites as centrioles, basal bodies, and along ciliary and flagellar doublet microtubules. Tektins form unique protofilaments, organized as longitudinal polymers of tektin heterodimers with axial periodicity matching tubulin. Tektin polypeptides consist of several alpha-helical regions that are predicted to form coiled coils. Indeed, tektins share considerable structural similarities with intermediate filament proteins. Possible functional roles for tektins are: stabilization of tubulin protofilaments; attachment of A and B-tubules in ciliary/flagellar microtubule doublets and C-tubules in centrioles; binding of axonemal components.
Pssm-ID: 460827 [Multi-domain] Cd Length: 383 Bit Score: 41.38 E-value: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 135 LLKKNKT-LTERNELLEEQVEHIREEVSQLRHELSMKDELLQFytsaaeesepESVCSTpLKRNesSSSVQNYFHLDSLQ 213
Cdd:pfam03148 127 LIEGIQElLQRTLEQAWEQLRLLRAARHKLEKDLSDKKEALEI----------DEKCLS-LNNT--SPNISYKPGPTRIP 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 214 KKLKDLEE-----ENVVLRSEACQLKTETITyeEKEQQLVNDCVKELRDanvQIASISEELAKK---TEDA--------A 277
Cdd:pfam03148 194 PNSSTPEEwekftQDNIERAEKERAASAQLR--ELIDSILEQTANDLRA---QADAVNFALRKRieeTEDAknklewqlK 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 278 RQQEEITHLLSQIVDLQK--KAKSCAV-------------ENEELVqhlgaaKD-AQRQLTAELRELEDKYAECMEMLHE 341
Cdd:pfam03148 269 KTLQEIAELEKNIEALEKaiRDKEAPLklaqtrlenrtyrPNVELC------RDeAQYGLVDEVKELEETIEALKQKLAE 342
|
250
....*....|
gi 124517685 342 AQEELKNLRN 351
Cdd:pfam03148 343 AEASLQALER 352
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
117-413 |
2.89e-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: 41.35 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 117 LLEEKERDLELaarigqsLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMKDELLqfytSAAEE--SEPESVCSTpL 194
Cdd:pfam10174 388 MLDVKERKINV-------LQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTAL----TTLEEalSEKERIIER-L 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 195 KRNESSSSVQNYFHLDSLQKKLKDLEEENVVLRSEACQLKTETITYEEKEQQLVNDCVKE---LRDANVQIASISEEL-- 269
Cdd:pfam10174 456 KEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKdskLKSLEIAVEQKKEECsk 535
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 270 -------AKKTEDAARQQEEITHLLSQI-VDLQKKAKSCAVENEELVQHLGAAKDAQRQltaelRELEDKYAECMEMLHE 341
Cdd:pfam10174 536 lenqlkkAHNAEEAVRTNPEINDRIRLLeQEVARYKEESGKAQAEVERLLGILREVENE-----KNDKDKKIAELESLTL 610
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124517685 342 AQ--EELKNLRN-KTMPTSRRYHSLGLFPMDSLAAEIEGTMRKELQLEELESpdithqkrVFETVRNVNQVVKQR 413
Cdd:pfam10174 611 RQmkEQNKKVANiKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEELMG--------ALEKTRQELDATKAR 677
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
111-351 |
2.93e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.56 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 111 IDAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHEL-SMKDELLQFYTSAAE-----ES 184
Cdd:PRK02224 316 REELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELeEAREAVEDRREEIEEleeeiEE 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 185 EPESVCSTPLKRNESSSsvqnyfHLDSLQKKLKDLEEENVVLRSEacqLKTETITYEEKEQ-----------QLVNDC-- 251
Cdd:PRK02224 396 LRERFGDAPVDLGNAED------FLEELREERDELREREAELEAT---LRTARERVEEAEAlleagkcpecgQPVEGSph 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 252 VKELRDANVQIASISEELakktEDAARQQEEITHLLSQIVDLQKKAK--SCAVENEELVQHLGAAK----DAQRQLTAEL 325
Cdd:PRK02224 467 VETIEEDRERVEELEAEL----EDLEEEVEEVEERLERAEDLVEAEDriERLEERREDLEELIAERretiEEKRERAEEL 542
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 124517685 326 RELEDKY-------------------------AECMEMLHEAQEELKNLRN 351
Cdd:PRK02224 543 RERAAELeaeaeekreaaaeaeeeaeeareevAELNSKLAELKERIESLER 593
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
132-401 |
3.17e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 41.21 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 132 GQSLLKKNKTLT-ERNELLEEQvEHIREEVSQLRHELSMKDELLQFYTSAAEESEPESVCSTPLKRNEssssvqnyfhld 210
Cdd:pfam05622 213 YKKLEEKLEALQkEKERLIIER-DTLRETNEELRCAQLQQAELSQADALLSPSSDPGDNLAAEIMPAE------------ 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 211 sLQKKLKDLEEENVVLRSEAcqlktetityEEKEQQLVNDCVKELRDANVQIASISEELAKktedaarQQEEITHLLSQI 290
Cdd:pfam05622 280 -IREKLIRLQHENKMLRLGQ----------EGSYRERLTELQQLLEDANRRKNELETQNRL-------ANQRILELQQQV 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 291 VDLQKKAKSCAVENEELVQhlgaakdaqrqltaelreLEDKYAECMEMLHEAQEELknlrnktmptsrryhslglfpmds 370
Cdd:pfam05622 342 EELQKALQEQGSKAEDSSL------------------LKQKLEEHLEKLHEAQSEL------------------------ 379
|
250 260 270
....*....|....*....|....*....|..
gi 124517685 371 laaeiegtMRKELQLEELESP-DITHQKRVFE 401
Cdd:pfam05622 380 --------QKKKEQIEELEPKqDSNLAQKIDE 403
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
85-337 |
3.46e-03 |
|
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: 41.21 E-value: 3.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 85 EQIEETLKYFLLCAERV-GQMTKTYNDIDAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHI------- 156
Cdd:TIGR02169 304 ASLERSIAEKERELEDAeERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVdkefaet 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 157 REEVSQLRHELSM-KDELlqfytsaaeesepesvcsTPLKRNES---SSSVQNYFHLDSLQKKLKDLEEENVVLRSEACQ 232
Cdd:TIGR02169 384 RDELKDYREKLEKlKREI------------------NELKRELDrlqEELQRLSEELADLNAAIAGIEAKINELEEEKED 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 233 LKTETITYEEKEQQLVNDcvkelrdanvqIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKscAVENEEL----- 307
Cdd:TIGR02169 446 KALEIKKQEWKLEQLAAD-----------LSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQAR--ASEERVRggrav 512
|
250 260 270
....*....|....*....|....*....|
gi 124517685 308 VQHLGAAKDAQRQLTAELRELEDKYAECME 337
Cdd:TIGR02169 513 EEVLKASIQGVHGTVAQLGSVGERYATAIE 542
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
103-334 |
5.58e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.27 E-value: 5.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 103 QMTKTYNDIDAVTRLLEEKERDLElaarigqsllKKNKTLTERNElleeQVEHIREEVSQLRHELsmkDELLQFYTSAAE 182
Cdd:COG4372 39 ELDKLQEELEQLREELEQAREELE----------QLEEELEQARS----ELEQLEEELEELNEQL---QAAQAELAQAQE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 183 ESEpesvcstplKRNESSSSVQNYfhLDSLQKKLKDLEEENVVLRSEACQLKTEtitYEEKEQQLvndcvKELRDanvQI 262
Cdd:COG4372 102 ELE---------SLQEEAEELQEE--LEELQKERQDLEQQRKQLEAQIAELQSE---IAEREEEL-----KELEE---QL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124517685 263 ASISEELAKKTEDaaRQQEEITHLLSQIVDLQKKAKSCAVENEELVQHLGAAKDAQRQLTAELRELEDKYAE 334
Cdd:COG4372 160 ESLQEELAALEQE--LQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEA 229
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
140-352 |
5.62e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.38 E-value: 5.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 140 KTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEPESVCSTPLKRNESSSSVQNY--FH--LDSLQKK 215
Cdd:PHA02562 163 SVLSEMDKLNKDKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAktIKaeIEELTDE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 216 LKDLEEENV-------VLRSEACQLKT--ETITYEEK---EQQLVNDCVKELRDANVQIASISE---ELAKKTEDAARQQ 280
Cdd:PHA02562 243 LLNLVMDIEdpsaalnKLNTAAAKIKSkiEQFQKVIKmyeKGGVCPTCTQQISEGPDRITKIKDklkELQHSLEKLDTAI 322
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124517685 281 EEITHLLSQIVDLQKKAKSCAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQEELKNLRNK 352
Cdd:PHA02562 323 DELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKT 394
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
258-349 |
6.33e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.81 E-value: 6.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 258 ANVQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKSCAVENEELVQHLGAAKDAQRQLTAELRELEDKYAecme 337
Cdd:COG3883 7 AAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIE---- 82
|
90
....*....|..
gi 124517685 338 mlhEAQEELKNL 349
Cdd:COG3883 83 ---ERREELGER 91
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
103-414 |
6.60e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.42 E-value: 6.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 103 QMTKTYNDIDAVTRLLEEKERDLELAarigqSLLKKNKTLTERnelLEEQVEHIREEVSQLRHELSMKDeLLQFYTSAAE 182
Cdd:TIGR00606 759 DIQRLKNDIEEQETLLGTIMPEEESA-----KVCLTDVTIMER---FQMELKDVERKIAQQAAKLQGSD-LDRTVQQVNQ 829
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 183 ESEPesvcstplKRNESSSSVQNyfhLDSLQKKLKDLEEENVVLRSEACQLKTETITYEEKEQQL-------------VN 249
Cdd:TIGR00606 830 EKQE--------KQHELDTVVSK---IELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRqqfeeqlvelsteVQ 898
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 250 DCVKELRDANVQIASISEELAK----KTEDAARQQEEITHLLSQIVDLQKKAKSCAVENEELVQHLGAAKDAQ-RQLTAE 324
Cdd:TIGR00606 899 SLIREIKDAKEQDSPLETFLEKdqqeKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYlKQKETE 978
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 325 LRELEDKYAECMEMLHEAQEELKNLRNKTMPTSRRYHSLglfpMDSLAaeiegTMRKELQLEELESPDITHQKRVfetvr 404
Cdd:TIGR00606 979 LNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWL----QDNLT-----LRKRENELKEVEEELKQHLKEM----- 1044
|
330
....*....|
gi 124517685 405 NVNQVVKQRS 414
Cdd:TIGR00606 1045 GQMQVLQMKQ 1054
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
109-318 |
7.15e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.81 E-value: 7.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 109 NDIDAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELsmKDELLQFYTSAAEESEPES 188
Cdd:COG3883 30 AELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL--GERARALYRSGGSVSYLDV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 189 VcstpLkrneSSSSVQNYFH-LDSLQK----------KLKDLEEENVVLRSEACQLKTETITYEEKEQQLVNDCVKELRD 257
Cdd:COG3883 108 L----L----GSESFSDFLDrLSALSKiadadadlleELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAE 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124517685 258 ANVQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKSCAVENEELVQHLGAAKDAQ 318
Cdd:COG3883 180 QEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
208-388 |
7.77e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.28 E-value: 7.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 208 HLDSLQKKLKDLEEE--NVVLRSEACQLKTETI-----------TYEEKEQQLvndcvKELRDANVQIASISEELAKKTE 274
Cdd:COG4913 625 ELAEAEERLEALEAEldALQERREALQRLAEYSwdeidvasaerEIAELEAEL-----ERLDASSDDLAALEEQLEELEA 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 275 DAARQQEEITHLLSQIVDLQKKAKSCAVENEEL-VQHLGAAKDAQRQLTAELREL------EDKYAECMEMLHE----AQ 343
Cdd:COG4913 700 ELEELEEELDELKGEIGRLEKELEQAEEELDELqDRLEAAEDLARLELRALLEERfaaalgDAVERELRENLEEridaLR 779
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 124517685 344 EELKNLRNKTMPTSRRYHSLGLFPMDSLAAEIEGT-----MRKELQLEEL 388
Cdd:COG4913 780 ARLNRAEEELERAMRAFNREWPAETADLDADLESLpeylaLLDRLEEDGL 829
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
254-352 |
7.98e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 38.65 E-value: 7.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 254 ELRDANVQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKScAVE--NEELvqhlgaAKDA---QRQLTAELREL 328
Cdd:COG1842 31 AIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARL-ALEkgREDL------AREAlerKAELEAQAEAL 103
|
90 100
....*....|....*....|....
gi 124517685 329 EDKYAECMEMLHEAQEELKNLRNK 352
Cdd:COG1842 104 EAQLAQLEEQVEKLKEALRQLESK 127
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
83-345 |
8.09e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 39.94 E-value: 8.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 83 TTEQIEETLKyfllcaerVGQMTKTYNDIDAVTRLLEE--------KERDLELAARIgQSLLKKNKTLTERNELLEEQVE 154
Cdd:COG5185 294 TKEKIAEYTK--------SIDIKKATESLEEQLAAAEAeqeleeskRETETGIQNLT-AEIEQGQESLTENLEAIKEEIE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 155 HIREEV--SQLRHEL-SMKDELlqfytsaaeESEPESVcstPLKRNESSSSVQNYfhLDSLQKKLKDLEEENVVLRSEAC 231
Cdd:COG5185 365 NIVGEVelSKSSEELdSFKDTI---------ESTKESL---DEIPQNQRGYAQEI--LATLEDTLKAADRQIEELQRQIE 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 232 QLKTETITYEEKEQQLVNDCVKELRDANVQIASISEELAKKTEDAARQQEEIthLLSQIVDLQKKAKSCAVENEELVQHL 311
Cdd:COG5185 431 QATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEINRSVRSKKED--LNEELTQIESRVSTLKATLEKLRAKL 508
|
250 260 270
....*....|....*....|....*....|....
gi 124517685 312 GAAKDAQRQLTAELRELEDKYAECMEMLHEAQEE 345
Cdd:COG5185 509 ERQLEGVRSKLDQVAESLKDFMRARGYAHILALE 542
|
|
| DUF2046 |
pfam09755 |
Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues ... |
181-350 |
9.37e-03 |
|
Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues of a family of proteins of unknown function possibly containing a coiled-coil domain.
Pssm-ID: 401633 [Multi-domain] Cd Length: 304 Bit Score: 39.04 E-value: 9.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 181 AEESEPESVCSTPLKRNESSSSVQNyfhldsLQKKLKDLEEENVVLRSEACQLKTETITYEEKEqqlvndcvKELRDANV 260
Cdd:pfam09755 1 ASESDTSSVDGGPTLAPPSPVTREQ------LQKRIESLQQENRVLKMELETYKLRCKALQEEN--------RALRQASV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517685 261 QIAS--------ISEELAKKTEDAARQQEEITHLLSQ-----IVDLQKKAKSCAVENEELVQHLGaaKDAQRQLTAELRE 327
Cdd:pfam09755 67 NIQAkaeqeeefISNTLLKKIQALKKEKETLAMNYEQeeeflTNDLSRKLTQLRQEKVELEQTLE--QEQEYQVNKLMRK 144
|
170 180
....*....|....*....|...
gi 124517685 328 LEDKYAEcmemLHEAQEELKNLR 350
Cdd:pfam09755 145 IEKLEAE----TLNKQTNLEQLR 163
|
|
| |
