|
Name |
Accession |
Description |
Interval |
E-value |
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
24-307 |
3.42e-146 |
|
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: 433.68 E-value: 3.42e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 24 RDSESITVLGTDRVEQMTKTYNDIDMVTHLLAERDRDLELAARIGQALLKRNHVLSEQNEALEEQLGQAFDQVNQLQHEL 103
Cdd:pfam04849 45 RETLNYFLLCSDRVSQMTKTYNDIEAVTRLLEEKERDLELAARIGQSLLKQNSVLTERNEALEEQLGSAREEILQLRHEL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 104 SKKDELLRIVSIASEESETDSSCSTPLRFNESFSLSQGLLQLDMLHEKLRELEEENMALRSkvqfaslssnalwaalgda 183
Cdd:pfam04849 125 SKKDDLLQIYSNDAEESETESSCSTPLRRNESFSSLHGCVQLDALQEKLRGLEEENLKLRS------------------- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 184 EACHIKTETFTYEEKEQQLVNDCVKELRETNAQMSRMTEELSGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELR 263
Cdd:pfam04849 186 EASHLKTETDTYEEKEQQLMSDCVEQLSEANQQMAELSEELARKMEENLRQQEEITSLLAQIVDLQHKCKELGIENEELQ 265
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1907070336 264 LHLQASKDAQRQLTMELHELQDRNMECLGMLHESQEEIKELRSK 307
Cdd:pfam04849 266 QHLQASKEAQRQLTSELQELQDRYAECLGMLHEAQEELKELRKK 309
|
|
| Milton |
pfam12448 |
Kinesin associated protein; This domain family is found in eukaryotes, and is typically ... |
368-519 |
2.45e-25 |
|
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: 103.52 E-value: 2.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 368 RGRSVTfPVLLPIPGSNRSSViMTAKPFESGVQP-------------AEDKTL--LSPGGSTEVPGNSQPTNP--PGSPE 430
Cdd:pfam12448 1 RQRSLT-PSPMNIPGSNQSSS-LTSMRSSSSSTPrssyyggdgssisLDNRTNsiLSETSSSQDSGYDRPKKPgtPGTPG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 431 DSDLATALHRLSLRRQNYLSEKQFFAEEWERKIQILAE----QEEEVSSCDAPTENLASVCTDQSETTDLGSASCLRGFM 506
Cdd:pfam12448 79 ARDLEAALRRLSLRRQNYLSERRFFEEERERKLLALAGtynyDEGEHGGSLTPNDSIMSLGSNHSGSSSHSSGFSSRSYL 158
|
170
....*....|...
gi 1907070336 507 PEKLQIVKPLEGS 519
Cdd:pfam12448 159 PEKLQIVKPLEGS 171
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
47-304 |
2.02e-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: 58.14 E-value: 2.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 47 IDMVTHLLAERDRDLELAARIGQALLKRNHVLSEQNEALEEQLGQAFDQVNQLQHELSKKDELLRIVSIASEESETDSSC 126
Cdd:TIGR02168 700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE 779
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 127 STPLRFNESFSLSQGLLQLDMLHEKLRELEEENMALRSKVQFASLSSNALWAALGDAEachiKTETFTYEEKEQ--QLVN 204
Cdd:TIGR02168 780 AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATE----RRLEDLEEQIEElsEDIE 855
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 205 DCVKELRETNAQMSRMTEELSGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQ 284
Cdd:TIGR02168 856 SLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLE 935
|
250 260
....*....|....*....|....
gi 1907070336 285 DRNMECLGMLHE----SQEEIKEL 304
Cdd:TIGR02168 936 VRIDNLQERLSEeyslTLEEAEAL 959
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
54-305 |
1.44e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.45 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 54 LAERDRDLELAARIGQALLKRnhvLSEQNEALEEQLGQAFDQVNQLQHELSKKDELLrivSIASEESETDSSCSTPLRFN 133
Cdd:TIGR02168 682 LEEKIEELEEKIAELEKALAE---LRKELEELEEELEQLRKELEELSRQISALRKDL---ARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 134 ESFSLSQGLLQLDMLHE---KLRELEEENMALRSKVQFASLSSNALWAALGDAEAchiktETFTYEEKEQQLVNDCVKEL 210
Cdd:TIGR02168 756 LTELEAEIEELEERLEEaeeELAEAEAEIEELEAQIEQLKEELKALREALDELRA-----ELTLLNEEAANLRERLESLE 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 211 RETNAQmSRMTEELSGKSDELlryQEEISSLLSQIVDLQ-------HKLKEHVIEKEELRLHLQASKDAQRQLTMELHEL 283
Cdd:TIGR02168 831 RRIAAT-ERRLEDLEEQIEEL---SEDIESLAAEIEELEelieeleSELEALLNERASLEEALALLRSELEELSEELREL 906
|
250 260
....*....|....*....|..
gi 1907070336 284 QDRNMECLGMLHESQEEIKELR 305
Cdd:TIGR02168 907 ESKRSELRRELEELREKLAQLE 928
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
55-352 |
1.32e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 52.38 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 55 AERDRDL--ELAARIGQALLKRNHVLSEQNEALEEQLGQAFDQVNQLQHELSKKDEllRIVSIASEesetdsscstplrf 132
Cdd:TIGR02169 210 AERYQALlkEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEK--RLEEIEQL-------------- 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 133 nesfslsqgllqLDMLHEKLRELEEENMaLRSKVQFASLSSNAlwAALGDAEAchiktetftyeEKEQQLvNDCVKELRE 212
Cdd:TIGR02169 274 ------------LEELNKKIKDLGEEEQ-LRVKEKIGELEAEI--ASLERSIA-----------EKEREL-EDAEERLAK 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 213 TNAQMSRMTEELSGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQDRNMECLG 292
Cdd:TIGR02169 327 LEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKR 406
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 293 MLHESQEEIKELRSKsgpsahlcfsqsygvftGESLAAEIEGTMRKKLSLDEESVSKQKA 352
Cdd:TIGR02169 407 ELDRLQEELQRLSEE-----------------LADLNAAIAGIEAKINELEEEKEDKALE 449
|
|
| UPF0242 |
pfam06785 |
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ... |
209-307 |
1.51e-06 |
|
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal transmembrane region and a C-terminal coiled-coil.
Pssm-ID: 429117 [Multi-domain] Cd Length: 194 Bit Score: 49.43 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 209 ELRETNAQMSRMTEELSGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEElrlhlqasKDAQRQLtmELHELQDRNM 288
Cdd:pfam06785 91 TLEELQSEEERLEEELSQKEEELRRLTEENQQLQIQLQQISQDFAEFRLESEE--------QLAEKQL--LINEYQQTIE 160
|
90
....*....|....*....
gi 1907070336 289 ECLGMLHESQEEIKELRSK 307
Cdd:pfam06785 161 EQRSVLEKRQDQIENLESK 179
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
78-307 |
2.11e-06 |
|
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: 51.60 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 78 LSEQNEALEEQLGQAFDQVNQLQHELSKKDELLRIVSIASEESETDSSCSTPLRFNESFSLSQGLLQLDMLHEKLRELEE 157
Cdd:TIGR02168 682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 158 ENMALRSKVQFASLSSNAL---WAAL-----GDAEACHIKTETFTYEEKEQQLVNDCVKELRETnaqMSRMTEELSGKSD 229
Cdd:TIGR02168 762 EIEELEERLEEAEEELAEAeaeIEELeaqieQLKEELKALREALDELRAELTLLNEEAANLRER---LESLERRIAATER 838
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907070336 230 ELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQDRnmeclgmLHESQEEIKELRSK 307
Cdd:TIGR02168 839 RLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSE-------LEELSEELRELESK 909
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
78-307 |
3.33e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.22 E-value: 3.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 78 LSEQNEALEEQLGQAFDQVNQLQHELskkDELLRIVSIASEESETDSSCSTPL-----RFNESfsLSQGLLQLDMLHEKL 152
Cdd:TIGR02169 679 LRERLEGLKRELSSLQSELRRIENRL---DELSQELSDASRKIGEIEKEIEQLeqeeeKLKER--LEELEEDLSSLEQEI 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 153 RELEEENMALRSKVQFASLSSNALWAALGDAEAcHIKTETFTYEEKEQQLVNDCVKE----LRETNAQMSRMTEELSGKS 228
Cdd:TIGR02169 754 ENVKSELKELEARIEELEEDLHKLEEALNDLEA-RLSHSRIPEIQAELSKLEEEVSRiearLREIEQKLNRLTLEKEYLE 832
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907070336 229 DELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQDRNMECLGMLHESQEEIKELRSK 307
Cdd:TIGR02169 833 KEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQ 911
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
144-356 |
5.56e-06 |
|
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: 50.44 E-value: 5.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 144 QLDMLHEKLRELEEENMALRSKVQFASLSSNALWAALGDAEACHiktetftyeEKEQQLVNDCVKELRETNAQMSRMTEE 223
Cdd:TIGR02168 699 ALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEV---------EQLEERIAQLSKELTELEAEIEELEER 769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 224 LSGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQDRNMECLGMLHESQEEIKE 303
Cdd:TIGR02168 770 LEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEE 849
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1907070336 304 LRSKsgpsahlcfsqsygvftGESLAAEIE--GTMRKKLSLDEESVSKQKAQQKR 356
Cdd:TIGR02168 850 LSED-----------------IESLAAEIEelEELIEELESELEALLNERASLEE 887
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
35-401 |
6.47e-06 |
|
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: 50.06 E-value: 6.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 35 DRVEQMTKTYNDIDMVTHLLAERDRDLELAARIGQALLKRnhvLSEQNEALEEQLgqafdqvnqlQHELSKKDELLRIVS 114
Cdd:TIGR02168 274 LEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN---LERQLEELEAQL----------EELESKLDELAEELA 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 115 IASEESETDSSCSTplRFNESFSLSQGLLQldMLHEKLRELEEENMALRSKVQFASLSSNALwaalgdaeachikTETFT 194
Cdd:TIGR02168 341 ELEEKLEELKEELE--SLEAELEELEAELE--ELESRLEELEEQLETLRSKVAQLELQIASL-------------NNEIE 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 195 YEEKEQQLVNDCVKELRETNAQMSRMTEELsgksdELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQR 274
Cdd:TIGR02168 404 RLEARLERLEDRRERLQQEIEELLKKLEEA-----ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALD 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 275 QLTMELHELQDRNMECLGML--HES-QEEIKEL-RSKSGPSAHL-CFSQSYGVFTGESLAAEI--EGTMRKKLSLDEESV 347
Cdd:TIGR02168 479 AAERELAQLQARLDSLERLQenLEGfSEGVKALlKNQSGLSGILgVLSELISVDEGYEAAIEAalGGRLQAVVVENLNAA 558
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907070336 348 S------KQKAQQKRVFDTVKVANDTRGRSVTFPVLLPIPG--SNRSSVIMTAKPFESGVQP 401
Cdd:TIGR02168 559 KkaiaflKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGflGVAKDLVKFDPKLRKALSY 620
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
78-285 |
8.26e-06 |
|
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: 48.92 E-value: 8.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 78 LSEQN-EALEEQLGQAFDQVNQLQHELSKkdELLRIVSIASEESETDSSCSTPLRFNESFSlsqgllqlDMLHEkLRELE 156
Cdd:pfam04108 109 IDEDSvEILRDALKELIDELQAAQESLDS--DLKRFDDDLRDLQKELESLSSPSESISLIP--------TLLKE-LESLE 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 157 EEnMA--LRSKVQFASLSSNALWAALGDaeachiKTETFTYEEKEQQLVNDCVKELRETNAQMSRMTEELSGKSDELLRY 234
Cdd:pfam04108 178 EE-MAslLESLTNHYDQCVTAVKLTEGG------RAEMLEVLENDARELDDVVPELQDRLDEMENNYERLQKLLEQKNSL 250
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1907070336 235 QEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQD 285
Cdd:pfam04108 251 IDELLSALQLIAEIQSRLPEYLAALKEFEERWEEEKETIEDYLSELEDLRE 301
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
88-307 |
1.18e-05 |
|
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 (LZTFL1) and Leucine zipper protein 2 (LUZP2).
Pssm-ID: 464620 [Multi-domain] Cd Length: 276 Bit Score: 47.78 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 88 QLGQAFDQVNQ----LQHELSKKD--ELLRIVSIAsEESETDSSCSTPlrfneSFSLSQGLLQ-------LDMLHEKLRE 154
Cdd:pfam15294 64 LLRQLFSQAEKwhlkLQADISELEnrELLEQIAEF-EEREFTSSNKKP-----NFELNKPKLEplnegggSALLHMEIER 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 155 LEEENMALRSkvQFASLSSNALwAALGDAEACHIKTETFTYEEKEQQLVNDCVKELRETNAQMSRMTEELSGKSDEllrY 234
Cdd:pfam15294 138 LKEENEKLKE--RLKTLESQAT-QALDEKSKLEKALKDLQKEQGAKKDVKSNLKEISDLEEKMAALKSDLEKTLNA---S 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 235 QEEISSLLSQIVDLQHKLkehviekeeLRLhlqaskdaQRQLTMELHEL--------QDRNMEclGMLHESQEEIKELRS 306
Cdd:pfam15294 212 TALQKSLEEDLASTKHEL---------LKV--------QEQLEMAEKELekkfqqtaAYRNMK--EMLTKKNEQIKELRK 272
|
.
gi 1907070336 307 K 307
Cdd:pfam15294 273 R 273
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
6-345 |
2.73e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.14 E-value: 2.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 6 NAIFkSRTGEAN--LMSSNHRDSESITVLGTDRVEqmtKTYNDIDMVTHLLAERDRDLElaarigqALLKRNHVLSEQNE 83
Cdd:PRK03918 128 NAIY-IRQGEIDaiLESDESREKVVRQILGLDDYE---NAYKNLGEVIKEIKRRIERLE-------KFIKRTENIEELIK 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 84 ALEEQLGQAFDQVNQLQHELSKKDELLRIVSIASEESEtdsscSTPLRFNESFSLSQGLLQ-LDMLHEKLRELEEENMAL 162
Cdd:PRK03918 197 EKEKELEEVLREINEISSELPELREELEKLEKEVKELE-----ELKEEIEELEKELESLEGsKRKLEEKIRELEERIEEL 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 163 RSKVQfaslssnalwaalgdaeachiktetfTYEEKEQQLvndcvKELRETNAQMSRMTEELSGKSDELLRYQEEISSLL 242
Cdd:PRK03918 272 KKEIE--------------------------ELEEKVKEL-----KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLE 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 243 SQIVDLQHKLKEhvIEKEELRLhlqaskdaqRQLTMELHELQDRNMEclgmLHESQEEIKELRSKSGPSAHLcfSQSYGV 322
Cdd:PRK03918 321 EEINGIEERIKE--LEEKEERL---------EELKKKLKELEKRLEE----LEERHELYEEAKAKKEELERL--KKRLTG 383
|
330 340
....*....|....*....|...
gi 1907070336 323 FTGESLAAEIEGTMRKKLSLDEE 345
Cdd:PRK03918 384 LTPEKLEKELEELEKAKEEIEEE 406
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
55-306 |
5.29e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.24 E-value: 5.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 55 AERDRDL--ELAARIGQALLKRNHVLSEQNEALEEQLGQAFDQVNQLQHELSKKDELLRIVSIASEESEtdsscstplrf 132
Cdd:COG1196 212 AERYRELkeELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELE----------- 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 133 nesfslsqglLQLDMLHEKLRELEEENMALRSKVQFASLSSNALwaalgdaeachiktetftyEEKEQQLVndcvKELRE 212
Cdd:COG1196 281 ----------LELEEAQAEEYELLAELARLEQDIARLEERRREL-------------------EERLEELE----EELAE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 213 TNAQMSRMTEELSGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQDRNMECLG 292
Cdd:COG1196 328 LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE 407
|
250
....*....|....
gi 1907070336 293 MLHESQEEIKELRS 306
Cdd:COG1196 408 AEEALLERLERLEE 421
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
198-308 |
1.04e-04 |
|
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: 45.39 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 198 KEQQLVNDCVKELRETNAQMSRMTEEL--------SGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQAS 269
Cdd:smart00787 165 KELELLNSIKPKLRDRKDALEEELRQLkqledeleDCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDL 244
|
90 100 110
....*....|....*....|....*....|....*....
gi 1907070336 270 KDAQRQLTMELHELQDRNMECLGMlheSQEEIKELRSKS 308
Cdd:smart00787 245 TNKKSELNTEIAEAEKKLEQCRGF---TFKEIEKLKEQL 280
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
48-307 |
1.18e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 45.88 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 48 DMVTHLLAERDRDLE-LAARIGQALLKRNHVLSE----------QNEALEEQLGQAFDQVNQLQHEL--------SKKDE 108
Cdd:pfam15921 267 DRIEQLISEHEVEITgLTEKASSARSQANSIQSQleiiqeqarnQNSMYMRQLSDLESTVSQLRSELreakrmyeDKIEE 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 109 LLRIVSIASEESeTDSSCSTPLRFNESFSLSQGLLQLDM-LHEKLREL---EEENMALRSKVQFASLSSNALWAALGDae 184
Cdd:pfam15921 347 LEKQLVLANSEL-TEARTERDQFSQESGNLDDQLQKLLAdLHKREKELsleKEQNKRLWDRDTGNSITIDHLRRELDD-- 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 185 achiktetftyEEKEQQLVNDCVKELR-ETNAQMSRMTEELSGKSDELlryqEEISSLLSQIVDLQHKLKEHVIEKEELR 263
Cdd:pfam15921 424 -----------RNMEVQRLEALLKAMKsECQGQMERQMAAIQGKNESL----EKVSSLTAQLESTKEMLRKVVEELTAKK 488
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1907070336 264 LHLQASKDAQRQLTMELHElQDRNMEClgmlheSQEEIKELRSK 307
Cdd:pfam15921 489 MTLESSERTVSDLTASLQE-KERAIEA------TNAEITKLRSR 525
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
54-244 |
2.27e-04 |
|
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: 45.06 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 54 LAERDRDLE-LAARIGQALLKRNHVLSEQnEALEEQLGQAFDQVNQLQHEL-SKKDELLRIVSIASEESEtdsscstplR 131
Cdd:TIGR02169 310 IAEKERELEdAEERLAKLEAEIDKLLAEI-EELEREIEEERKRRDKLTEEYaELKEELEDLRAELEEVDK---------E 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 132 FNESF-SLSQGLLQLDMLHEKLRELEEENMALRSKVQFASLSSNALWAALGDAEACHIKTETFT------YEEKEQQLvN 204
Cdd:TIGR02169 380 FAETRdELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKedkaleIKKQEWKL-E 458
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1907070336 205 DCVKELRETNAQMSRMTEELSGKSDELLRYQEEISSLLSQ 244
Cdd:TIGR02169 459 QLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQ 498
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
189-307 |
4.42e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 4.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 189 KTETFTYEEKEQQLVNDCVKELRETNAQMSRMTEELSGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQA 268
Cdd:COG4372 12 RLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQA 91
|
90 100 110
....*....|....*....|....*....|....*....
gi 1907070336 269 SKDAQRQLTMELHELQDRNMECLGMLHESQEEIKELRSK 307
Cdd:COG4372 92 AQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQ 130
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
34-284 |
4.62e-04 |
|
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: 43.90 E-value: 4.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 34 TDRVEQMTKTYNDIDMVTHLLAERDRDL--ELAARIGQALLKrnhvLSEQNEALEEQLGQAFDQVNQLQHELSKKDELLR 111
Cdd:TIGR02169 257 TEEISELEKRLEEIEQLLEELNKKIKDLgeEEQLRVKEKIGE----LEAEIASLERSIAEKERELEDAEERLAKLEAEID 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 112 IVSIASEESETDsscstplrfnesfsLSQGLLQLDMLHEKLRELEEENMALRSKVQFASLSSNALWAALGDAEAchiKTE 191
Cdd:TIGR02169 333 KLLAEIEELERE--------------IEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYRE---KLE 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 192 TFTYEEKEQQLVND-CVKELRETNAQMSRMTEELSGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASK 270
Cdd:TIGR02169 396 KLKREINELKRELDrLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLK 475
|
250
....*....|....
gi 1907070336 271 DAQRQLTMELHELQ 284
Cdd:TIGR02169 476 EEYDRVEKELSKLQ 489
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
59-472 |
9.75e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 43.14 E-value: 9.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 59 RDLELAARIGQALLKRNHVLSEQNEALEEQLGQAFDQVNQLQHELSKKDELLRIVSIASEESEtdsscSTPLRFNESFSL 138
Cdd:COG5022 843 KAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSISSLKLVNLELE-----SEIIELKKSLSS 917
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 139 SQgLLQLDMLHEKLRELEEENMALRSKVQfaslssnalwaalgdaeachiKTETFTYEEKEQQLVNDCvKELRETNAQMS 218
Cdd:COG5022 918 DL-IENLEFKTELIARLKKLLNNIDLEEG---------------------PSIEYVKLPELNKLHEVE-SKLKETSEEYE 974
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 219 RM-------TEELSGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASK-----DAQRQLTMELHELQDR 286
Cdd:COG5022 975 DLlkkstilVREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPVEVAELQSASKiisseSTELSILKPLQKLKGL 1054
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 287 NMEclgMLHESQEEIKELRSKSgPSAHLCFSQSYGVFTGESLAAEIEgtMRKKLSLDEESVSKQKAQQKRVFDTVKVAND 366
Cdd:COG5022 1055 LLL---ENNQLQARYKALKLRR-ENSLLDDKQLYQLESTENLLKTIN--VKDLEVTNRNLVKPANVLQFIVAQMIKLNLL 1128
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 367 TRgrsvtfpvllpIPGSNRSSVIMTAKPFESgvqpaEDKTLLSPGGSTEVPGNSQPTNPP---GSPEDSDLATALH---- 439
Cdd:COG5022 1129 QE-----------ISKFLSQLVNTLEPVFQK-----LSVLQLELDGLFWEANLEALPSPPpfaALSEKRLYQSALYdeks 1192
|
410 420 430
....*....|....*....|....*....|....*...
gi 1907070336 440 RLSLRRQNYLSEK-----QFFAEEWERKIQILAEQEEE 472
Cdd:COG5022 1193 KLSSSEVNDLKNElialfSKIFSGWPRGDKLKKLISEG 1230
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
197-307 |
1.08e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.62 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 197 EKEQQLVNDCVKELRETNAQMSRMTEELSGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQL 276
Cdd:COG1196 249 EELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL 328
|
90 100 110
....*....|....*....|....*....|.
gi 1907070336 277 TMELHELQDRNMECLGMLHESQEEIKELRSK 307
Cdd:COG1196 329 EEELEELEEELEELEEELEEAEEELEEAEAE 359
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
182-307 |
1.12e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.69 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 182 DAEACHIKTETFTYeekeqqlvNDCVKELRETNAQMsrmTEELSGKSDELLryqEEISSLLSQIVDLQHKLKEHVIEKEE 261
Cdd:PHA02562 187 DMKIDHIQQQIKTY--------NKNIEEQRKKNGEN---IARKQNKYDELV---EEAKTIKAEIEELTDELLNLVMDIED 252
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1907070336 262 LRLHLQASKDAQRQLTMELHELQ-DRNM--------ECLGMLHESQEEIKELRSK 307
Cdd:PHA02562 253 PSAALNKLNTAAAKIKSKIEQFQkVIKMyekggvcpTCTQQISEGPDRITKIKDK 307
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
144-286 |
1.56e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 144 QLDMLHEKLRELEEENMALRSKVQFASLSSNALWAALGDAeachiKTETFTYEEKEQQLVndcvKELRETNAQMSRMTEE 223
Cdd:COG4372 32 QLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQA-----RSELEQLEEELEELN----EQLQAAQAELAQAQEE 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907070336 224 LSGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQDR 286
Cdd:COG4372 103 LESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
10-346 |
1.60e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 42.20 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 10 KSRTGEANLMSSNHRDSESITVLGTDRVEQMtKTYNDI------DMVTHLL-AERDRDLELAARIgQALLKRNHVLSEQn 82
Cdd:PLN02939 89 KSTSSDDDHNRASMQRDEAIAAIDNEQQTNS-KDGEQLsdfqleDLVGMIQnAEKNILLLNQARL-QALEDLEKILTEK- 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 83 EALEEQlgqafdqVNQLQHELSKKDELLRIVSIASEESETDSSCSTPLRFNESFSLSQGLLQLDMLHEKLRELEEENMAL 162
Cdd:PLN02939 166 EALQGK-------INILEMRLSETDARIKLAAQEKIHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLL 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 163 RSKVQFASlssnalwaalgdAEACHIK-TETFTYE-EKEQQLVNDCVKELRetnAQMSRMTEELSgKSDELlryqeEISS 240
Cdd:PLN02939 239 KDDIQFLK------------AELIEVAeTEERVFKlEKERSLLDASLRELE---SKFIVAQEDVS-KLSPL-----QYDC 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 241 LLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQDRNM--ECLGMLHESQEEIKELRSKSGPSAHLCFSQ 318
Cdd:PLN02939 298 WWEKVENLQDLLDRATNQVEKAALVLDQNQDLRDKVDKLEASLKEANVskFSSYKVELLQQKLKLLEERLQASDHEIHSY 377
|
330 340
....*....|....*....|....*...
gi 1907070336 319 sygVFTGESLAAEIEGTMRKklsLDEES 346
Cdd:PLN02939 378 ---IQLYQESIKEFQDTLSK---LKEES 399
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
146-356 |
1.67e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 146 DMLHEKLRELEEENMALRSKV-QFASLSSNALWAALGDAEAchIKTETFTYEEKEQQL---VNDCVKELRETNAQMSRMT 221
Cdd:COG4372 2 DRLGEKVGKARLSLFGLRPKTgILIAALSEQLRKALFELDK--LQEELEQLREELEQAreeLEQLEEELEQARSELEQLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 222 EELSGKSDELLRYQEEISSLLSQIVDLQHklkehviEKEELRLHLQASKDAQRQLTMELHELQDRNMECLGMLHESQEEI 301
Cdd:COG4372 80 EELEELNEQLQAAQAELAQAQEELESLQE-------EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEEL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1907070336 302 KELRSKSgpsahlcfsqsygvftgESLAAEIEGTMRKKLSLDEESVSKQKAQQKR 356
Cdd:COG4372 153 KELEEQL-----------------ESLQEELAALEQELQALSEAEAEQALDELLK 190
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
111-356 |
2.68e-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: 41.59 E-value: 2.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 111 RIVSIASEESETDSSC---STPLRFNESFSLSQgLLQLDMLHEKLRELEEENMALRSKVQfaslssnalwaalgdaeacH 187
Cdd:TIGR02169 640 RMVTLEGELFEKSGAMtggSRAPRGGILFSRSE-PAELQRLRERLEGLKRELSSLQSELR-------------------R 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 188 IKTETFTYeekeQQLVNDCVKELRETNAQMSRMTEELSGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQ 267
Cdd:TIGR02169 700 IENRLDEL----SQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLH 775
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 268 ASKDAqrqltmeLHELQDR-NMECLGMLHESQEEIKELRSKSgpsahlcfsqsygvftgESLAAEIEGTMrKKLSLDEES 346
Cdd:TIGR02169 776 KLEEA-------LNDLEARlSHSRIPEIQAELSKLEEEVSRI-----------------EARLREIEQKL-NRLTLEKEY 830
|
250
....*....|..
gi 1907070336 347 VSK--QKAQQKR 356
Cdd:TIGR02169 831 LEKeiQELQEQR 842
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
54-321 |
3.24e-03 |
|
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: 40.90 E-value: 3.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 54 LAERDRDLELAARIGQALLKRNHVLSEQNEALEEQLGQAFDQVNQLQHELSKKDEllRIVSIASEESEtdsscstplrfn 133
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEA--ELAELEKEIAE------------ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 134 esfslsqgllqldmLHEKLRELEEEnmaLRSKVQFASLSSNALWAALGdaeachIKTETFTYEEKEQQLVNDCVKELRET 213
Cdd:COG4942 95 --------------LRAELEAQKEE---LAELLRALYRLGRQPPLALL------LSPEDFLDAVRRLQYLKYLAPARREQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 214 NAQMSRMTEELSGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQltmELHELQDRNMECLGM 293
Cdd:COG4942 152 AEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAA---ELAELQQEAEELEAL 228
|
250 260
....*....|....*....|....*...
gi 1907070336 294 LHESQEEIKELRSKSGPSAhlcFSQSYG 321
Cdd:COG4942 229 IARLEAEAAAAAERTPAAG---FAALKG 253
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
54-307 |
3.38e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 3.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 54 LAERDRDLELAARIGQALLKRnhvLSEQNEALEEQLGQAFDQ--VNQLQHELSKKDELLRIVS-IASEESETDSSCSTPL 130
Cdd:COG4717 197 LAEELEELQQRLAELEEELEE---AQEELEELEEELEQLENEleAAALEERLKEARLLLLIAAaLLALLGLGGSLLSLIL 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 131 RFNESFSLSQGLLQLDMLH------------------EKLRELEEEN-MALRSKVQFASLSSNALWAALGDAEAcHIKTE 191
Cdd:COG4717 274 TIAGVLFLVLGLLALLFLLlarekaslgkeaeelqalPALEELEEEElEELLAALGLPPDLSPEELLELLDRIE-ELQEL 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 192 TFTYEEKEQQLvndcvkELRETNAQMSRMTEELSGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKD 271
Cdd:COG4717 353 LREAEELEEEL------QLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALD 426
|
250 260 270
....*....|....*....|....*....|....*.
gi 1907070336 272 AQrQLTMELHELQDRnmeclgmLHESQEEIKELRSK 307
Cdd:COG4717 427 EE-ELEEELEELEEE-------LEELEEELEELREE 454
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
39-284 |
4.20e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 40.81 E-value: 4.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 39 QMTKTYNDIDMVTHLLAERDRDLELAARigQA-LLKRNHVLSEQNEALEEQLgqafdQVNQLQHELSKKDELLRIVSIAS 117
Cdd:TIGR02168 180 KLERTRENLDRLEDILNELERQLKSLER--QAeKAERYKELKAELRELELAL-----LVLRLEELREELEELQEELKEAE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 118 EESETDSScstplrfnesfslsqgllQLDMLHEKLRELEEENMALRSKVQFASLSSNALWAALGDAEAcHIKTetftYEE 197
Cdd:TIGR02168 253 EELEELTA------------------ELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQ-QKQI----LRE 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 198 KEQQLVNDcVKELRETNAQMSRMTEELSgksDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQLT 277
Cdd:TIGR02168 310 RLANLERQ-LEELEAQLEELESKLDELA---EELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLR 385
|
....*..
gi 1907070336 278 MELHELQ 284
Cdd:TIGR02168 386 SKVAQLE 392
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
183-304 |
4.38e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 40.59 E-value: 4.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 183 AEACHIKtETFTYEEKEQQLVNDCVKELRETNAQMSRMTEELSGKS---DELLRYQEEISSLLSQIVDLQHKLKEHV--I 257
Cdd:PRK04778 331 EEIDRVK-QSYTLNESELESVRQLEKQLESLEKQYDEITERIAEQEiaySELQEELEEILKQLEEIEKEQEKLSEMLqgL 409
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1907070336 258 EKEELRLHlQASKDAQRQLTMELHELQDRNM-----ECLGMLHESQEEIKEL 304
Cdd:PRK04778 410 RKDELEAR-EKLERYRNKLHEIKRYLEKSNLpglpeDYLEMFFEVSDEIEAL 460
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
35-307 |
4.68e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 40.66 E-value: 4.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 35 DRVEQMTKTYNDIDMVTHLLAERDRDLELAARIGQALLKRNHVLSEQNEALEEQLGQAFDQVNQLQHELSKKDELLRIVS 114
Cdd:PRK01156 173 DVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKN 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 115 iaseesetdsscstplRFNESFSLSQGLLQLD-MLHEKLRELEEENMALRSKVQFASLSS-NALWAALGDAEAC-----H 187
Cdd:PRK01156 253 ----------------RYESEIKTAESDLSMElEKNNYYKELEERHMKIINDPVYKNRNYiNDYFKYKNDIENKkqilsN 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 188 IKTETFTYEEKEQQLVNdcVKELRETNAQMSRMTEELSGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQ 267
Cdd:PRK01156 317 IDAEINKYHAIIKKLSV--LQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFIS 394
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1907070336 268 ASKDAQR----QLTMELHELQDRNMECLGMLHESQEEIKELRSK 307
Cdd:PRK01156 395 EILKIQEidpdAIKKELNEINVKLQDISSKVSSLNQRIRALREN 438
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
74-307 |
5.15e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 5.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 74 RNHVLsEQNEALE--EQLGQAFDQVNQLQHELSK----KDELLRIVSIASEESETDSSCSTPLRFNESFSLSQGLLQLDM 147
Cdd:COG4913 214 REYML-EEPDTFEaaDALVEHFDDLERAHEALEDareqIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLEL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 148 LHEKLRELEEENMALRSKVQFASlssnalwAALGDAEAchiktetfTYEEKEQQLVNDCVKELRETNAQMSRMTEELSGK 227
Cdd:COG4913 293 LEAELEELRAELARLEAELERLE-------ARLDALRE--------ELDELEAQIRGNGGDRLEQLEREIERLERELEER 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 228 SDELLRYQEEISSLLSQIVDLQHKLKEHvieKEELRLHLQASKDAQRQLTMELHELQDRNMECLGMLHESQEEIKELRSK 307
Cdd:COG4913 358 ERRRARLEALLAALGLPLPASAEEFAAL---RAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
143-307 |
5.47e-03 |
|
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: 39.52 E-value: 5.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 143 LQLDMLHEKLRELEEENMALRSKVQFASLSSNALWAALGDAEAchiktetfTYEEKEQqlvndcvkELRETNAQMSRMTE 222
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEK--------EIKRLEL--------EIEEVEARIKKYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 223 ELSG--KSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQDRNMECLGmlhESQEE 300
Cdd:COG1579 81 QLGNvrNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELA---ELEAE 157
|
....*..
gi 1907070336 301 IKELRSK 307
Cdd:COG1579 158 LEELEAE 164
|
|
| DUF4456 |
pfam14644 |
Domain of unknown function (DUF4456); This domain family is found in bacteria and eukaryotes, ... |
195-311 |
6.62e-03 |
|
Domain of unknown function (DUF4456); This domain family is found in bacteria and eukaryotes, and is approximately 210 amino acids in length. There is a single completely conserved residue E that may be functionally important.
Pssm-ID: 464232 Cd Length: 209 Bit Score: 38.81 E-value: 6.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 195 YEEKEQQLVNDCVKELREtnaQMSRMTEELSGKS----DELL-RYQEEISSLLSQIVD-LQHKLKEHVIEKE----ELRL 264
Cdd:pfam14644 41 YQEQADEYHNSCLQELRN---QVERLEELLPSVPelifESLLkRHLQKLERAMKNIAAeFSQKQKQLEQLKQqheqQLRP 117
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1907070336 265 HLQASKDAQrqltmELHEL----QDRNMECLGMLHESQEEIKELRSKSGPS 311
Cdd:pfam14644 118 TLGHPQNAQ-----ELEQLcdreEDRQKEHIELIQAHREALLEAVDKVAST 163
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
53-276 |
8.37e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.75 E-value: 8.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 53 LLAERDRDLELAARIGQALLKRNHVLSEQNEALEEQLGQAFDQVNQLQHELSKKDELLRIVSIASEESETDSScstplrf 132
Cdd:COG4717 68 LNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAE------- 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 133 nesfsLSQGLLQLDMLHEKLRELEEENMALRSKVQfaslssnalwaalgdaeachiktetfTYEEKEQQLVNDCVKELRE 212
Cdd:COG4717 141 -----LAELPERLEELEERLEELRELEEELEELEA--------------------------ELAELQEELEELLEQLSLA 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907070336 213 TNAQMSRMTEELSGKSDELLRYQEEISSLLSQIVDLQHKLKEhvIEKEELRLHLQASKDAQRQL 276
Cdd:COG4717 190 TEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQ--LENELEAAALEERLKEARLL 251
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
144-305 |
9.98e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 39.65 E-value: 9.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 144 QLDMLH------EKLRELEEEnmalrskvqfasLSSNALWAALGDAEACHIKTETFTYEEKE-QQLVNDCVKELRETNAQ 216
Cdd:TIGR02168 201 QLKSLErqaekaERYKELKAE------------LRELELALLVLRLEELREELEELQEELKEaEEELEELTAELQELEEK 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070336 217 MSRMTEELSGKSDELLRYQEEISSLLSQIVDLQHklkehviEKEELRLHLQASKDAQRQLTMELHELQDRNMECLGMLHE 296
Cdd:TIGR02168 269 LEELRLEVSELEEEIEELQKELYALANEISRLEQ-------QKQILRERLANLERQLEELEAQLEELESKLDELAEELAE 341
|
....*....
gi 1907070336 297 SQEEIKELR 305
Cdd:TIGR02168 342 LEEKLEELK 350
|
|
| |
