|
Name |
Accession |
Description |
Interval |
E-value |
| PH_PLEKHD1 |
cd13281 |
Pleckstrin homology (PH) domain containing, family D (with coiled-coil domains) member 1 PH ... |
22-127 |
4.40e-66 |
|
Pleckstrin homology (PH) domain containing, family D (with coiled-coil domains) member 1 PH domain; Human PLEKHD1 (also called UPF0639, pleckstrin homology domain containing, family D (with M protein repeats) member 1) is a single transcript and contains a single PH domain. PLEKHD1 is conserved in human, chimpanzee, , dog, cow, mouse, chicken, zebrafish, and Caenorhabditis elegans. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.
Pssm-ID: 270099 Cd Length: 139 Bit Score: 208.72 E-value: 4.40e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 22 FFIIKESFLLYYSESERKSFETNKYFNIHPKGVIPLGGCLVEAREEPSMPYAMKISHQDFHGNVLLAAESEFEQTQWLEM 101
Cdd:cd13281 34 FFIIKEGFLLYYSESEKKDFEKTRHFNIHPKGVIPLGGCSIEAVEDPGKPYAISISHSDFKGNIILAADSEFEQEKWLDM 113
|
90 100
....*....|....*....|....*.
gi 755542439 102 LQESGKVTWKNAQLGEAMIKSLEAQG 127
Cdd:cd13281 114 LRESGKITWKNAQLGETMIEELEAQG 139
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
117-366 |
2.32e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.58 E-value: 2.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 117 EAMIKSLEAQGLQLAKEKQEYLDKLMEETEELclqREQREELERLNQVLEAEKQQFEEVVQELRVEQEQIKRELELTARC 196
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAEL---EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 197 LKGVEQEKKELRHLTESLQHTLEELS------IEKKKTLEMLEEDKNQPQPLTNQSEQppASDGLHSNLRQIEERMQELL 270
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEeleeelEEAEEELEEAEAELAEAEEALLEAEA--ELAEAEEELEELAEELLEAL 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 271 AEKLLAEKRMKENEERSRALEEEREFYSSQSQALQNSLQELTAEKQQAERELKAEVKVRMDLERRLREAEAALRSLEQGL 350
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
|
250
....*....|....*.
gi 755542439 351 NSKVRNKEKEERMRAD 366
Cdd:COG1196 473 ALLEAALAELLEELAE 488
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
132-386 |
1.10e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.19 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 132 KEKQEYLDKLMEETEELCLQREQREELERLNQVLEAEKQQFEEVVQELRVEQEQIKRELEltaRCLKGVEQEKKELRHLT 211
Cdd:COG1196 225 LEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELE---EAQAEEYELLAELARLE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 212 ESLQHtLEELSIEKKKTLEMLEEDKNQpqpltnqseqppasdgLHSNLRQIEERMQELLAEKLLAEKRMKENEERSRALE 291
Cdd:COG1196 302 QDIAR-LEERRRELEERLEELEEELAE----------------LEEELEELEEELEELEEELEEAEEELEEAEAELAEAE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 292 EEREFYSSQSQALQNSLQELTAEKQQAERELKAEVKVRMDLERRLREAEAALRSLEQGLNSKVRNKEKEERMRADVSHLK 371
Cdd:COG1196 365 EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEAL 444
|
250
....*....|....*
gi 755542439 372 RFFEECIRNAELEAK 386
Cdd:COG1196 445 EEAAEEEAELEEEEE 459
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
121-362 |
1.17e-10 |
|
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: 63.92 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 121 KSLEAQGLQLAKEKQ-EYLDKLMEETEELCLQREQ-----REELERLNQVLEAEKQQFEEVVQELRVEQEQIKRELELTA 194
Cdd:TIGR02168 664 GSAKTNSSILERRREiEELEEKIEELEEKIAELEKalaelRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 195 RCLKGVEQEKKELRHLTESLQHTLEELSIEKKKTLEMLEEDKNQPQPLTNQSEQPPASDGLHSNLRQIEERMQELLAEKL 274
Cdd:TIGR02168 744 QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLR 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 275 LA----EKRMKENEERSRALEEEREFYSSQSQALQNSLQELTAEKQQAERELKAEVKVRMDLERRLREAEAALRSLEQGL 350
Cdd:TIGR02168 824 ERleslERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEEL 903
|
250
....*....|..
gi 755542439 351 NSKVRNKEKEER 362
Cdd:TIGR02168 904 RELESKRSELRR 915
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
120-366 |
1.48e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.80 E-value: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 120 IKSLEAQGLQLAKEKQEYLDKLMEETEELCLQREQREELERLNQVLEAEKQQFEEVVQELRVEQEQIKRELeltarclkg 199
Cdd:COG1196 276 LEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL--------- 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 200 vEQEKKELRHLTESLQHTLEELSIEKKKTLEMLEEDKNQPQPLTNQSEQppaSDGLHSNLRQIEERMQELLAEKLLAEKR 279
Cdd:COG1196 347 -EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA---AAELAAQLEELEEAEEALLERLERLEEE 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 280 MKENEERSRALEEEREfyssqsqALQNSLQELTAEKQQAERELKAEVKVRMDLERRLREAEAALRSLEQGLNSKVRNKEK 359
Cdd:COG1196 423 LEELEEALAELEEEEE-------EEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495
|
....*..
gi 755542439 360 EERMRAD 366
Cdd:COG1196 496 LLEAEAD 502
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
92-352 |
4.09e-10 |
|
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: 62.38 E-value: 4.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 92 EFEQTQWLEMLQESGKVTWKNAQLGEAMIKSLEAQGLQLAKEKQEYLDKLMEETEELCLQREQREELERLNQVLEAEKQQ 171
Cdd:TIGR02168 721 LEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA 800
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 172 FEEVVQELRVE--------------QEQIKRELELTARCLKGVEQEKKELRHLTESLQHTLEELSIEKKKTLEMLEEDKN 237
Cdd:TIGR02168 801 LREALDELRAEltllneeaanlrerLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLN 880
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 238 QpqpltnqseqppaSDGLHSNLRQIEERMQELLAEKLLAEKRMKENEERSRALEEEREFYSSQSQALQNSLQELT---AE 314
Cdd:TIGR02168 881 E-------------RASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQerlSE 947
|
250 260 270
....*....|....*....|....*....|....*...
gi 755542439 315 KQQAERELKAEVKVRMDLErrLREAEAALRSLEQGLNS 352
Cdd:TIGR02168 948 EYSLTLEEAEALENKIEDD--EEEARRRLKRLENKIKE 983
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
120-368 |
1.23e-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: 60.84 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 120 IKSLEAQGLQLAKEKQEYLDKLMEETEELCLQREQREELERLNQVLEAEKQQ--------------FEEVVQELRVEQEQ 185
Cdd:TIGR02168 234 LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEElqkelyalaneisrLEQQKQILRERLAN 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 186 IKRELELTARCLKGVEQEKKELRHLTESLQHTLEELSIEKKKTLEMLEEDKNQPQPLTNQSEQP-PASDGLHSNLRQIEE 264
Cdd:TIGR02168 314 LERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELeEQLETLRSKVAQLEL 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 265 RMQELLAEKLLAEKRMKENEER-----SRALEEEREFYSSQSQALQNSLQELTAEKQQAERELKAEVKVRMDLERRLREA 339
Cdd:TIGR02168 394 QIASLNNEIERLEARLERLEDRrerlqQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEA 473
|
250 260
....*....|....*....|....*....
gi 755542439 340 EAALRSLEQGLNSKVRNKEKEERMRADVS 368
Cdd:TIGR02168 474 EQALDAAERELAQLQARLDSLERLQENLE 502
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
143-376 |
5.57e-09 |
|
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: 58.54 E-value: 5.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 143 EETEELCLQREQREELERLNQVLEAEKQQFEEVVQELRVEQEQIKRELELTARCLKGVEQEKKELRHLTESLQHTLEELS 222
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLE 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 223 IEK----------KKTLEMLEEDKNQPQPLTNQSEQPPAsdglHSNLRQIEERMQELLAEKLLAEKRMKENEERSRALEE 292
Cdd:TIGR02169 751 QEIenvkselkelEARIEELEEDLHKLEEALNDLEARLS----HSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 293 EREFYSSQSQALQNSLQELTAEKQQAERELKAEVKVRMDLERRLREAEAALRSLEQglnSKVRNKEKEERMRADVSHLKR 372
Cdd:TIGR02169 827 EKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLES---RLGDLKKERDELEAQLRELER 903
|
....
gi 755542439 373 FFEE 376
Cdd:TIGR02169 904 KIEE 907
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
131-386 |
2.39e-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: 56.60 E-value: 2.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 131 AKEKQEYLDKLMEETEELCLQREQREELERLNQVLEAEKQQFEEVVQELRVE-------QEQIKRELELTARCLKGVEQE 203
Cdd:TIGR02168 224 ELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEvseleeeIEELQKELYALANEISRLEQQ 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 204 KKELRHLTESLQHTLEELSIEKKKTLEMLEEDKNQPQPLTNQSEQppasdgLHSNLRQIEERMQELLAEKLLAEKRMKEN 283
Cdd:TIGR02168 304 KQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEE------LKEELESLEAELEELEAELEELESRLEEL 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 284 EERSRALEEEREFYSSQSQALQNSLQELTAEKQQAERELKAEVKVRMDLERRLREAEAALRSLEQGLNSKVRNK--EKEE 361
Cdd:TIGR02168 378 EEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEElqEELE 457
|
250 260
....*....|....*....|....*
gi 755542439 362 RMRADVSHLKRFFEEcIRNAELEAK 386
Cdd:TIGR02168 458 RLEEALEELREELEE-AEQALDAAE 481
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
151-373 |
4.38e-08 |
|
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: 55.16 E-value: 4.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 151 QREQREELERLNQVLEAEKQQFEEVVQELRVEQEQIKRELELTARCLKGVEQEKKELRHLTESLQHTLEELSIEKKKTLE 230
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 231 MLEEDKNQPQPLTN----QSEQPPASDGLHSNLRQIEERMQELLAEKLLA-EKRMKENEERSRALEEEREFYSSQSQALQ 305
Cdd:COG4942 98 ELEAQKEELAELLRalyrLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPArREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755542439 306 NSLQELTAEKQQAERELKAEVKVRMDLERRLREAEAALRSL---EQGLNSKVRNKEKEERMRADVSHLKRF 373
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELqqeAEELEALIARLEAEAAAAAERTPAAGF 248
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
132-390 |
5.75e-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: 55.46 E-value: 5.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 132 KEKQEYLDKLMEETE------ELCLQREQREELERLNQV--LEAEKQQFEEVVQELRVEQEQIKRELELTArclKGVEQE 203
Cdd:TIGR02169 194 DEKRQQLERLRREREkaeryqALLKEKREYEGYELLKEKeaLERQKEAIERQLASLEEELEKLTEEISELE---KRLEEI 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 204 KKELRHLTESLQHTLEELSIEKKKTLEMLEEDKNQPQpltnqseqppasdglhsnlRQIEErmqellaekllAEKRMKEN 283
Cdd:TIGR02169 271 EQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLE-------------------RSIAE-----------KERELEDA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 284 EERSRALEEEREFYSSQSQALQNSLQELTAEKQQAERELKAEVKVRMDLERRLREAEAALRSLEQGLNSKVR-----NKE 358
Cdd:TIGR02169 321 EERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREkleklKRE 400
|
250 260 270
....*....|....*....|....*....|..
gi 755542439 359 KEERMRADVSHLKRFFEECIRNAELEAKMPVI 390
Cdd:TIGR02169 401 INELKRELDRLQEELQRLSEELADLNAAIAGI 432
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
135-362 |
1.09e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.56 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 135 QEYLDKLMEETEELclqREQREELERlnqvlEAEK-QQFEEVVQELRVeqeqikRELELTARCLKGVEQEKKELRHLTES 213
Cdd:COG1196 185 EENLERLEDILGEL---ERQLEPLER-----QAEKaERYRELKEELKE------LEAELLLLKLRELEAELEELEAELEE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 214 LQHTLEELSIEKKKTLEMLEEDKNQPQPLTNQSEQppasdgLHSNLRQIEERMQELLAEKLLAEKRMKENEER-SRALEE 292
Cdd:COG1196 251 LEAELEELEAELAELEAELEELRLELEELELELEE------AQAEEYELLAELARLEQDIARLEERRRELEERlEELEEE 324
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 293 EREfYSSQSQALQNSLQELTAEKQQAERELKAEVKVRMDLERRLREAEAALRSLEQGLNSKVRNKEKEER 362
Cdd:COG1196 325 LAE-LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
128-349 |
1.60e-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: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 128 LQLAKEKQEYLDKLMEETEELCLQREQREELERLNQV------LEAEKQQFEEVVQELRVEQEQikRELELTARCLKGVE 201
Cdd:COG4913 224 FEAADALVEHFDDLERAHEALEDAREQIELLEPIRELaeryaaARERLAELEYLRAALRLWFAQ--RRLELLEAELEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 202 QEKKELRHLTESLQHTLEELsiekKKTLEMLEEDKNQpqpltnqseqppaSDGlhSNLRQIEERMQELLAEKLLAEKRMK 281
Cdd:COG4913 302 AELARLEAELERLEARLDAL----REELDELEAQIRG-------------NGG--DRLEQLEREIERLERELEERERRRA 362
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755542439 282 ENEERSRALE----EEREFYSSQSQALQNSLQELTAEKQQAERELKAEVKVRMDLERRLREAEAALRSLEQG 349
Cdd:COG4913 363 RLEALLAALGlplpASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| PH |
pfam00169 |
PH domain; PH stands for pleckstrin homology. |
21-105 |
2.25e-07 |
|
PH domain; PH stands for pleckstrin homology.
Pssm-ID: 459697 [Multi-domain] Cd Length: 105 Bit Score: 49.10 E-value: 2.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 21 MFFIIKESFLLYYSESERKSFETnkyfnihPKGVIPLGGCLVEAREEPSMP-----YAMKISHQDFHGNVLLAAESEFEQ 95
Cdd:pfam00169 21 RYFVLFDGSLLYYKDDKSGKSKE-------PKGSISLSGCEVVEVVASDSPkrkfcFELRTGERTGKRTYLLQAESEEER 93
|
90
....*....|
gi 755542439 96 TQWLEMLQES 105
Cdd:pfam00169 94 KDWIKAIQSA 103
|
|
| PH |
smart00233 |
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ... |
22-104 |
2.60e-07 |
|
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.
Pssm-ID: 214574 [Multi-domain] Cd Length: 102 Bit Score: 48.70 E-value: 2.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 22 FFIIKESFLLYYSESERKSFETnkyfnihPKGVIPLGGCLVEAREEPSM---PYAMKISHQDfHGNVLLAAESEFEQTQW 98
Cdd:smart00233 22 YFVLFNSTLLYYKSKKDKKSYK-------PKGSIDLSGCTVREAPDPDSskkPHCFEIKTSD-RKTLLLQAESEEEREKW 93
|
....*.
gi 755542439 99 LEMLQE 104
Cdd:smart00233 94 VEALRK 99
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
117-355 |
6.06e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 52.38 E-value: 6.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 117 EAMIKSLEAQGLQLAKEKQEYLDKLMEETEELCLQREQREELERLNQVLEAEKQQFEEVVQELRVEQEQIKRELELTARC 196
Cdd:TIGR02169 300 EAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKE 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 197 LKGVEQEKKELRHLTESLQHTLEELSIEKKKTLEMLEEdknqpqpLTNQSEQppasdgLHSNLRQIEERMQELLAEKLLA 276
Cdd:TIGR02169 380 FAETRDELKDYREKLEKLKREINELKRELDRLQEELQR-------LSEELAD------LNAAIAGIEAKINELEEEKEDK 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 277 EKRMKENEERSRALEEEREFYSSQSQALQNSLQELTAEKQQAEREL---KAEVKVRMDLERRLREAEAALRSLEQGLNSK 353
Cdd:TIGR02169 447 ALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELaeaEAQARASEERVRGGRAVEEVLKASIQGVHGT 526
|
..
gi 755542439 354 VR 355
Cdd:TIGR02169 527 VA 528
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
117-347 |
6.78e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.99 E-value: 6.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 117 EAMIKSLEAQGLQLAKEKQEYLDKLMEETEELCLQREQREELERLNQVLEAEKQQFEEVVQELRVEQEQIKREL-----E 191
Cdd:TIGR02169 715 SRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLshsriP 794
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 192 LTARCLKGVEQEKKELRHLTESLQHTLEELSIEKKKTLEMLEEDKNQPQPLTNQSEqppasdglhSNLRQIEE---RMQE 268
Cdd:TIGR02169 795 EIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIK---------SIEKEIENlngKKEE 865
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755542439 269 LLAEKLLAEKRMKENEERSRALEEEREFYSSQSQALQNSLQELTAEKQQAERELKAEVKVRMDLERRLREAEAALRSLE 347
Cdd:TIGR02169 866 LEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDE 944
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
117-386 |
9.15e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.68 E-value: 9.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 117 EAMIKSLEAQGLQLAKEKQEYLDKLMEETEELCLQREQREEL---------ERLNQVLEAEKQQFEEVVQELRVEQEQIK 187
Cdd:PTZ00121 1474 EAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAkkaeeakkaDEAKKAEEAKKADEAKKAEEKKKADELKK 1553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 188 RELELTARCLKGVEQEKKELRHLTESLQHTLEELSIEKKKTLEMLEEDKNQPQPLTNQSEQPPASDGLHSNLRQIEErmq 267
Cdd:PTZ00121 1554 AEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEE--- 1630
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 268 ellAEKLLAEKRMKENEERSRALEEEREFYSSQSQALQNSLQElTAEKQQAERELKAEVKVRMDLERRLREAEAAlRSLE 347
Cdd:PTZ00121 1631 ---EKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKA-EEDKKKAEEAKKAEEDEKKAAEALKKEAEEA-KKAE 1705
|
250 260 270
....*....|....*....|....*....|....*....
gi 755542439 348 QGLNSKVRNKEKEERMRADVSHLKRFFEECIRNAELEAK 386
Cdd:PTZ00121 1706 ELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKK 1744
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
152-360 |
1.18e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.07 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 152 REQREELERLNQVLEAEKQQFEEVVQELRVEQEQIKRELELTARCLKGVEQEKKelrhlTESLQHTLEELSIEkkktLEM 231
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEID-----VASAEREIAELEAE----LER 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 232 LEEDknqpqpltnqseqppasdglHSNLRQIEERMQELLAEKLLAEKRMKENEERSRALEEEREFYSSQSQALQNSLQEL 311
Cdd:COG4913 680 LDAS--------------------SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA 739
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 755542439 312 TAEKQQAERELKAEVKVRMDLERRLREAEAALRSLEQGLNSKVRNKEKE 360
Cdd:COG4913 740 EDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEE 788
|
|
| PH |
cd00821 |
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ... |
22-102 |
8.31e-06 |
|
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.
Pssm-ID: 275388 [Multi-domain] Cd Length: 92 Bit Score: 44.07 E-value: 8.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 22 FFIIKESFLLYYSESERKSFEtnkyfnihPKGVIPLGGCL-VEAREEPSMPYAMKISHQDfHGNVLLAAESEFEQTQWLE 100
Cdd:cd00821 20 WFVLFEGVLLYYKSKKDSSYK--------PKGSIPLSGILeVEEVSPKERPHCFELVTPD-GRTYYLQADSEEERQEWLK 90
|
..
gi 755542439 101 ML 102
Cdd:cd00821 91 AL 92
|
|
| PH_3BP2 |
cd13308 |
SH3 domain-binding protein 2 Pleckstrin homology (PH) domain; SH3BP2 (the gene that encodes ... |
22-105 |
1.08e-05 |
|
SH3 domain-binding protein 2 Pleckstrin homology (PH) domain; SH3BP2 (the gene that encodes the adaptor protein 3BP2), HD, ITU, IT10C3, and ADD1 are located near the Huntington's Disease Gene on Human Chromosome 4pl6.3. SH3BP2 lies in a region that is often missing in individuals with Wolf-Hirschhorn syndrome (WHS). Gain of function mutations in SH3BP2 causes enhanced B-cell antigen receptor (BCR)-mediated activation of nuclear factor of activated T cells (NFAT), resulting in a rare, genetic disorder called cherubism. This results in an increase in the signaling complex formation with Syk, phospholipase C-gamma2 (PLC-gamma2), and Vav1. It was recently discovered that Tankyrase regulates 3BP2 stability through ADP-ribosylation and ubiquitylation by the E3-ubiquitin ligase. Cherubism mutations uncouple 3BP2 from Tankyrase-mediated protein destruction, which results in its stabilization and subsequent hyperactivation of the Src, Syk, and Vav signaling pathways. SH3BP2 is also a potential negative regulator of the abl oncogene. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.
Pssm-ID: 270118 Cd Length: 113 Bit Score: 44.32 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 22 FFIIKESFLLYYSESERKSfetnkyfnihPKGVIPLGGCLVEAREE--PSMPYAMKISH-QDFHGNVLLAAESEFEQTQW 98
Cdd:cd13308 32 YVIIHQGCVYYYKNDQSAK----------PKGVFSLNGYNRRAAEErtSKLKFVFKIIHlSPDHRTWYFAAKSEDEMSEW 101
|
....*..
gi 755542439 99 LEMLQES 105
Cdd:cd13308 102 MEYIRRE 108
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
117-321 |
1.42e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 47.76 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 117 EAMIKSLEAQgLQLAKEKQEYLDKLMEETEELCLQ-REQREELERLNQVLEAEKQQFEEVVQELRVEQEQIKRELELTAR 195
Cdd:TIGR02169 811 EARLREIEQK-LNRLTLEKEYLEKEIQELQEQRIDlKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKK 889
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 196 CLKGVEQEKKELRHLTESLQHTLEELSI---EKKKTLEMLEE-----DKNQPQPLTNQSEQPPASDgLHSNLRQIEERMQ 267
Cdd:TIGR02169 890 ERDELEAQLRELERKIEELEAQIEKKRKrlsELKAKLEALEEelseiEDPKGEDEEIPEEELSLED-VQAELQRVEEEIR 968
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 755542439 268 ELLAEKLLAEKRMKENEERSRALEEEREFYSSQSQALQNSLQELTAEKQQAERE 321
Cdd:TIGR02169 969 ALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREVFME 1022
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
124-364 |
1.66e-05 |
|
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: 47.66 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 124 EAQGLQLAKEKQEYLDKLMEETEEL--CLQREQREELERLNQVLEAEKQQFEEVVQELRVEQEQIKRELELTARCLKGVE 201
Cdd:pfam02463 161 EAAGSRLKRKKKEALKKLIEETENLaeLIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERID 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 202 QEKKELRHLTESLQHTLEELSIEKKKTLEMLEEDKNQPQPLTNQSEQppaSDGLHSNLRQIEERMQELLAEKLLAEKRMK 281
Cdd:pfam02463 241 LLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEE---LKLLAKEEEELKSELLKLERRKVDDEEKLK 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 282 ENEERSRALEEEREFYSSQSQALQNSLQELTAEKQQAERELKAEVKVRMDLERRLREAEAALRSLEQGLNSKVRNKEKEE 361
Cdd:pfam02463 318 ESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEEL 397
|
...
gi 755542439 362 RMR 364
Cdd:pfam02463 398 ELK 400
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
133-359 |
2.60e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 133 EKQEYLDKLMEETEELCLQREQREELERLNQVLEAEKQQFEEVVQELRVEQEQIK---RELELTARCLKGVEQEKKELRH 209
Cdd:PRK03918 218 ELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKkeiEELEEKVKELKELKEKAEEYIK 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 210 LTESLQHTLEELSiEKKKTLEMLEEDKNQPQPLTnqseqppasdglhSNLRQIEERMQELLAEKLLAEKRMKENEERSRA 289
Cdd:PRK03918 298 LSEFYEEYLDELR-EIEKRLSRLEEEINGIEERI-------------KELEEKEERLEELKKKLKELEKRLEELEERHEL 363
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 290 LEEEREFySSQSQALQNSLQELTAEKqqAERELKAEVKVRMDLERRLREAEAALRSLEQGLNSKVRNKEK 359
Cdd:PRK03918 364 YEEAKAK-KEELERLKKRLTGLTPEK--LEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEE 430
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
132-384 |
3.80e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 46.27 E-value: 3.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 132 KEKQEYLDKLmeETEELCLQREQR-EELERLNQVLEAEKQQFEEVVQELRVEQEQIKRELElTARCLKGVEQEKKElRHL 210
Cdd:pfam17380 287 RQQQEKFEKM--EQERLRQEKEEKaREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAME-RERELERIRQEERK-REL 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 211 TESLQHTLEeLSIEKKKTLEMLEEDKNQPQPLTNQSEQPPASDGLHSNLRQIEERMQELLAEKLLAEK---RMKE----N 283
Cdd:pfam17380 363 ERIRQEEIA-MEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQeeaRQREvrrlE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 284 EERSRALEEEREFYSSQSQALQNSLQE--------LTAEKQQAERELkAEVKVRMDLERRLREAEAALrsLEQGLNSKVR 355
Cdd:pfam17380 442 EERAREMERVRLEEQERQQQVERLRQQeeerkrkkLELEKEKRDRKR-AEEQRRKILEKELEERKQAM--IEEERKRKLL 518
|
250 260
....*....|....*....|....*....
gi 755542439 356 NKEKEERMRADVSHLKRFFEECIRNAELE 384
Cdd:pfam17380 519 EKEMEERQKAIYEEERRREAEEERRKQQE 547
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
121-453 |
4.20e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 4.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 121 KSLEAQGLQLAKEKQEYLDKLMEE---TEELCLQREQREELERLNQVLEAEKQQFEEVVQelRVEQEQIKRELELTARCL 197
Cdd:PTZ00121 1445 KADEAKKKAEEAKKAEEAKKKAEEakkADEAKKKAEEAKKADEAKKKAEEAKKKADEAKK--AAEAKKKADEAKKAEEAK 1522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 198 KGVEQEKKELRHLTESLQHTLEELSIEKKKTLEMLE--EDKNQPQPLTNQSEQPPASDGLHSNLRQIEERMQELLAEKLL 275
Cdd:PTZ00121 1523 KADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKkaEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYE 1602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 276 AEKRMKENEERSralEEEREFYSSQSQALQNSLQELTAEKQQAERELKAEVKVRMDLERRLREAEAALRSLEQGLNSKVR 355
Cdd:PTZ00121 1603 EEKKMKAEEAKK---AEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEE 1679
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 356 NKEKEERMRADVSHLKRFFEECIRNAELEAKMPVIMKNSVYIHKAATRRIKSCRFHRRRSStswNDMKPSQSFMTSQLEA 435
Cdd:PTZ00121 1680 AKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAE---EDKKKAEEAKKDEEEK 1756
|
330
....*....|....*...
gi 755542439 436 NNIEELKEVAKRLSRDQR 453
Cdd:PTZ00121 1757 KKIAHLKKEEEKKAEEIR 1774
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
117-329 |
4.98e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.20 E-value: 4.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 117 EAMIKSLEAQGLQLAKEKQEYLDKLMEETEELCLQREQREELERLNQVLEAEKQQFEEVVQELRVEQEQIKRELELTARC 196
Cdd:TIGR02168 830 ERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESK 909
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 197 LKGVEQEKKELRHLTESLQHTLEELSIEKKKTLEMLEEDK--NQPQPLTNQSEQPPASDGLHSNLRQIEERMQELLAEKL 274
Cdd:TIGR02168 910 RSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYslTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNL 989
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 755542439 275 LAekrmkenEERSRALEEEREFYSSQSQALQNSLQELtaekQQAERELKAEVKVR 329
Cdd:TIGR02168 990 AA-------IEEYEELKERYDFLTAQKEDLTEAKETL----EEAIEEIDREARER 1033
|
|
| Nucleoporin_FG2 |
pfam15967 |
Nucleoporin FG repeated region; Nucleoporin_FG2, or nucleoporin p58/p45, is a family of ... |
159-317 |
9.72e-05 |
|
Nucleoporin FG repeated region; Nucleoporin_FG2, or nucleoporin p58/p45, is a family of chordate nucleoporins. The proteins carry many repeats of the FG sequence motif.
Pssm-ID: 435043 [Multi-domain] Cd Length: 586 Bit Score: 45.04 E-value: 9.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 159 ERLNQVLEAEKQQFEEVVQELRVEQEQIKReleLTARCLKGVEQEKKELRHL----TESLQHtlEELSIEKKKtLEMLEE 234
Cdd:pfam15967 243 ENLPPVICQDVENFQKFVKEQKQVQEEISR---MSSKAMLKVQDDIKALKQLlsvaASGLQR--NSLAIDKLK-IETAQE 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 235 DKN-------QPQPLTNQSEQPPASDGLHSNLRQIEERMQELlaekllaekrmkeneerSRALEEEREFYSSQSQALQNS 307
Cdd:pfam15967 317 LKNadialrtQKTPPGLQHENTAPADYFRSLVEQFEVQLQQY-----------------RQQIEELENHLTTQSSSSHIT 379
|
170
....*....|
gi 755542439 308 LQELTAEKQQ 317
Cdd:pfam15967 380 PQDLSLAMQK 389
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
151-348 |
1.16e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 151 QREQREELERLNQVLEAEKQQFEEVVQELRVEQEQIKRELELTArclkgVEQEKK----ELRHLTESLQHTLEELSiEKK 226
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVD-----LSEEAKlllqQLSELESQLAEARAELA-EAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 227 KTLEMLEEDKNQPQPLTNQSEQPPASDGLHSNLRQIEERMQELLAE------KLLAEKRMKENEERSRALEEEREFYSSQ 300
Cdd:COG3206 240 ARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARytpnhpDVIALRAQIAALRAQLQQEAQRILASLE 319
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 755542439 301 SQ--ALQNSLQELTAEKQQAERELKAEVKVRMDLERRLREAEAALRSLEQ 348
Cdd:COG3206 320 AEleALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYES 369
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
131-380 |
2.20e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 131 AKEKQEYLDKLMEETEELClqrEQREELERLNQVLEAEKQQFEEVVQELRVEQEQIKRELELTARCLKGVEQEKK---EL 207
Cdd:PRK03918 167 LGEVIKEIKRRIERLEKFI---KRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEeieEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 208 RHLTESLQHTLEELSIEKKKTLEMLEEDKNQPQPLTNQSEQPPASDGLHSNLRQIEERMQELLAEKLLAEKRMKENEERS 287
Cdd:PRK03918 244 EKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEI 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 288 RALEEEREFYSSQSqalqNSLQELTAEKQQAERELkAEVKVRMDLERRLREAEAALRSLEQGLnsKVRNKEKEERMRADV 367
Cdd:PRK03918 324 NGIEERIKELEEKE----ERLEELKKKLKELEKRL-EELEERHELYEEAKAKKEELERLKKRL--TGLTPEKLEKELEEL 396
|
250
....*....|...
gi 755542439 368 SHLKRFFEECIRN 380
Cdd:PRK03918 397 EKAKEEIEEEISK 409
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
117-386 |
2.48e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 117 EAMIKSLEAQGLQLAKEKQEYLDKLMEE---TEELCLQREQREELERLNQVLEAEKQqfeevVQELRVEQEQIKRELELT 193
Cdd:PTZ00121 1415 AAKKKADEAKKKAEEKKKADEAKKKAEEakkADEAKKKAEEAKKAEEAKKKAEEAKK-----ADEAKKKAEEAKKADEAK 1489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 194 arclKGVEQEKK---ELRHLTESLQHTLEELSIEKKKTLEMLE--EDKNQPQPLTNQSEQPPASDglhsnLRQIEERMQE 268
Cdd:PTZ00121 1490 ----KKAEEAKKkadEAKKAAEAKKKADEAKKAEEAKKADEAKkaEEAKKADEAKKAEEKKKADE-----LKKAEELKKA 1560
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 269 llAEKLLAEKRMKENEERSRALEEEREFYSSQSQALQNSLQELTAEKQQAERELKAEVKVRMDLErRLREAEAALRSLEQ 348
Cdd:PTZ00121 1561 --EEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAE-ELKKAEEEKKKVEQ 1637
|
250 260 270
....*....|....*....|....*....|....*...
gi 755542439 349 GLNSKVRNKEKEERMRADVSHLKRFFEECIRNAELEAK 386
Cdd:PTZ00121 1638 LKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKK 1675
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
151-329 |
2.71e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.77 E-value: 2.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 151 QREQREELERLNQVLEAEKQQFEEVVQELRVEQEQIKRELELTARCLKGVEQEKKELRHLTESLQHTLEELSIEKKKTLE 230
Cdd:COG1196 661 SLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEE 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 231 MLEEDKNQPQPLTNQSEQPPASDGLHSNLRQIEERMQELLAEKLLAEkrmkenEErSRALEEEREFYSSQSQALQNSLQE 310
Cdd:COG1196 741 LLEEEELLEEEALEELPEPPDLEELERELERLEREIEALGPVNLLAI------EE-YEELEERYDFLSEQREDLEEARET 813
|
170
....*....|....*....
gi 755542439 311 LtaekQQAERELKAEVKVR 329
Cdd:COG1196 814 L----EEAIEEIDRETRER 828
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
132-363 |
3.13e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.49 E-value: 3.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 132 KEKQEYLDKLMEETEE-LCLQREQREELERLNQVLEAEKQQFEEVVQELRVEQEQIKRELELTARCLKGVEQEKKELRHL 210
Cdd:PRK02224 515 EERREDLEELIAERREtIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERI 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 211 TESLqhtleELSIEKKKTLEMLEEDKNQPQPLTNQS-EQPPASDGLHSNLRQI--EERMQELLAEKLLAEKRMKENEERS 287
Cdd:PRK02224 595 RTLL-----AAIADAEDEIERLREKREALAELNDERrERLAEKRERKRELEAEfdEARIEEAREDKERAEEYLEQVEEKL 669
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755542439 288 RALEEEREFYSSQSQALQNSLQELtaekqQAERELKAEVKVRMDLERRLREAEAALRSLEQGLNSKVR--NKEKEERM 363
Cdd:PRK02224 670 DELREERDDLQAEIGAVENELEEL-----EELRERREALENRVEALEALYDEAEELESMYGDLRAELRqrNVETLERM 742
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
102-387 |
3.55e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 43.14 E-value: 3.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 102 LQESGKVTWKNAQLGE--AMIKSLEaqglqlakeKQEYLDKLMEETEELCLQREQREELERLNQVLEAEKQQFEEVVQEL 179
Cdd:COG5022 799 LQPLLSLLGSRKEYRSylACIIKLQ---------KTIKREKKLRETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETI 869
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 180 RVeqeQIKRELELTARCLKGVEQEKKELRHLTEsLQHTLEELSIEKKKTLEMLEEDKNqpqpltnqseqppasdglhsnl 259
Cdd:COG5022 870 YL---QSAQRVELAERQLQELKIDVKSISSLKL-VNLELESEIIELKKSLSSDLIENL---------------------- 923
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 260 rqieermqELLAEKLLAEKRMKENEERSRALEEERefyssQSQALQNSLQELTAEKQQAERELKAEVKVRMDLERRLREA 339
Cdd:COG5022 924 --------EFKTELIARLKKLLNNIDLEEGPSIEY-----VKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKA 990
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 755542439 340 EAALRSLEQGLNSKVRNKEKEERmradvsHLKRFFEECIRNAELEAKM 387
Cdd:COG5022 991 NSELKNFKKELAELSKQYGALQE------STKQLKELPVEVAELQSAS 1032
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
99-321 |
5.03e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 42.80 E-value: 5.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 99 LEMLQESGKVTWKNAQLGEAMIKSLEAQGLQ--LAKEKQEYLDKLMEETEELclQREQREELERLNQVLEAEK-QQFEEV 175
Cdd:pfam17380 374 ISRMRELERLQMERQQKNERVRQELEAARKVkiLEEERQRKIQQQKVEMEQI--RAEQEEARQREVRRLEEERaREMERV 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 176 VQELRVEQEQIK--RELELTARCLKGVEQEKKELRHLTESLQHTLEELSIEKKKTlEMLEEdKNQPQPLTNQSEQPPASD 253
Cdd:pfam17380 452 RLEEQERQQQVErlRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQ-AMIEE-ERKRKLLEKEMEERQKAI 529
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755542439 254 GLHSNLRQIEE---RMQELLAEKLLAEKRMKENEERSR--ALEEEREFYSsqsqalqnslQELTAEKQQAERE 321
Cdd:pfam17380 530 YEEERRREAEEerrKQQEMEERRRIQEQMRKATEERSRleAMEREREMMR----------QIVESEKARAEYE 592
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
125-327 |
5.21e-04 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 42.71 E-value: 5.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 125 AQGLQLAKEKQ---EYLDKLMEETEELCLQREqrEELERLNQVLEAEKQQFEEVVQELRVEQEQIKReleltarclkgVE 201
Cdd:pfam05667 303 TEKLQFTNEAPaatSSPPTKVETEEELQQQRE--EELEELQEQLEDLESSIQELEKEIKKLESSIKQ-----------VE 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 202 QEKKELRHLTESLQhtlEELSIeKKKTLEMLEEDKNQPQPLtnQSEQPPASDGLHSNLRQIEERMQELLAE-KLLAEKRM 280
Cdd:pfam05667 370 EELEELKEQNEELE---KQYKV-KKKTLDLLPDAEENIAKL--QALVDASAQRLVELAGQWEKHRVPLIEEyRALKEAKS 443
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 755542439 281 KENEERSRALEEEREFYSSQSQAlqnslQELTAEKQQAERELKAEVK 327
Cdd:pfam05667 444 NKEDESQRKLEEIKELREKIKEV-----AEEAKQKEELYKQLVAEYE 485
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
120-382 |
5.91e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 5.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 120 IKSLEAQGLQLAKEKQEYLDKLMEETEELCLQREQREELERLNQVLEAEkQQFEEVVQELRvEQEQIKRELELTARCLKG 199
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDE-IDVASAEREIA-ELEAELERLDASSDDLAA 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 200 VEQEKKELRHLTESLQHTLEELSIEKKKTLEMLEEDKNQPQPLTNQSEQPPASDGLHSNLRqIEERMQELLAEKLLAEKR 279
Cdd:COG4913 690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL-LEERFAAALGDAVERELR 768
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 280 mkeneersRALEEEREFYSSQSQALQNSLQELTAEKQQAERELKAEVKVRMDlerRLREAEAALRSLEQ-GLnskVRNKE 358
Cdd:COG4913 769 --------ENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLE---SLPEYLALLDRLEEdGL---PEYEE 834
|
250 260
....*....|....*....|....*....
gi 755542439 359 K-----EERMRADVSHLKRFFEECIRNAE 382
Cdd:COG4913 835 RfkellNENSIEFVADLLSKLRRAIREIK 863
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
141-358 |
6.78e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.19 E-value: 6.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 141 LMEETEELCLQREQREELERLNQVLEAEKQQFEEVVQELRVEQEQIKRELELTARCLKGVEQEKKELRHLTESLQHTLEE 220
Cdd:pfam07888 40 LQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 221 LSIEKKKTLEMLEEDKNQPQPLTNQSEQPPAsdglhsNLRQIEERMQELLAEKLLAEKRMKENEERSRALEEEREFYSSQ 300
Cdd:pfam07888 120 LLAQRAAHEARIRELEEDIKTLTQRVLERET------ELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKE 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755542439 301 SQALQNSLQELTAEKQQAERELKAEVKVRMDLERRLREAEAA---LRSLEQGLNSKVRNKE 358
Cdd:pfam07888 194 FQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALleeLRSLQERLNASERKVE 254
|
|
| PH_AtPH1 |
cd13276 |
Arabidopsis thaliana Pleckstrin homolog (PH) 1 (AtPH1) PH domain; AtPH1 is expressed in all ... |
22-99 |
7.93e-04 |
|
Arabidopsis thaliana Pleckstrin homolog (PH) 1 (AtPH1) PH domain; AtPH1 is expressed in all plant tissue and is proposed to be the plant homolog of human pleckstrin. Pleckstrin consists of two PH domains separated by a linker region, while AtPH has a single PH domain with a short N-terminal extension. AtPH1 binds PtdIns3P specifically and is thought to be an adaptor molecule since it has no obvious catalytic functions. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.
Pssm-ID: 270095 Cd Length: 106 Bit Score: 38.84 E-value: 7.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 22 FFIIKESFLLYYSESERKSFETnkyfnihPKGVIPLGGCLV--EAREEPSMPYAMKISHQdfHGNVLLAAESEFEQTQWL 99
Cdd:cd13276 19 WFVLKQGKLFWFKEPDVTPYSK-------PRGVIDLSKCLTvkSAEDATNKENAFELSTP--EETFYFIADNEKEKEEWI 89
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
120-321 |
8.63e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.92 E-value: 8.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 120 IKSLEAQGLQLAKEKQEYLDKLMEETEELCLQREQREElERLNQVLEAEKQqfEEVVQELRVEQEQIKRELELTAR---- 195
Cdd:PHA02562 204 IEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTD-ELLNLVMDIEDP--SAALNKLNTAAAKIKSKIEQFQKvikm 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 196 ---------CLKGVEQEKKELRHLTES---LQHTLEELsiekKKTLEMLEEDKNQPQPLTNqseqppASDGLHSNLRQIE 263
Cdd:PHA02562 281 yekggvcptCTQQISEGPDRITKIKDKlkeLQHSLEKL----DTAIDELEEIMDEFNEQSK------KLLELKNKISTNK 350
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 755542439 264 ERMQELLAEKLLAEKRMKEneersraLEEEREFYSSQSQALQNSLQELTAEKQQAERE 321
Cdd:PHA02562 351 QSLITLVDKAKKVKAAIEE-------LQAEFVDNAEELAKLQDELDKIVKTKSELVKE 401
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
104-348 |
8.78e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 8.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 104 ESGKVTWKNAQLGeAMIKSLEAQGLQLAKEKQEYLDKLMEETEELCLQREQREELERLNQVLEAEKQQFEEVVQELRVEQ 183
Cdd:COG4717 33 EAGKSTLLAFIRA-MLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAEL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 184 EQIKRELELTARCLKGVEQEKKElrhltESLQHTLEELSIEKKKTLEMLEEdknqpqpltnqseqppasdglhsnLRQIE 263
Cdd:COG4717 112 EELREELEKLEKLLQLLPLYQEL-----EALEAELAELPERLEELEERLEE------------------------LRELE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 264 ERMQELLAEklLAEKRMKENEERSRALEEEREfyssQSQALQNSLQELTAEKQQAERELKAEVKVRMDLERRLREAEAAL 343
Cdd:COG4717 163 EELEELEAE--LAELQEELEELLEQLSLATEE----ELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL 236
|
....*
gi 755542439 344 RSLEQ 348
Cdd:COG4717 237 EAAAL 241
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
145-370 |
9.01e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.54 E-value: 9.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 145 TEELCLQREQREELERLNQVLEAEKQqfeEVVQELRVEQEQIKREL-ELTARCLKGVEQEK------KELRHLTESLQHT 217
Cdd:PHA02562 194 QQQIKTYNKNIEEQRKKNGENIARKQ---NKYDELVEEAKTIKAEIeELTDELLNLVMDIEdpsaalNKLNTAAAKIKSK 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 218 LEELSiekkKTLEMLEEDKNQPQPLTNQSEQPPASDGLHSNLRQIEERMQELLAEKLLAEKRMKENEERSRALEEEREFY 297
Cdd:PHA02562 271 IEQFQ----KVIKMYEKGGVCPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKI 346
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755542439 298 SSQSQALQNSLQEltAEKQQAE-RELKAEVKVRmdlerrlREAEAALRSLEQGLNSKVRNKEKEERMRADVSHL 370
Cdd:PHA02562 347 STNKQSLITLVDK--AKKVKAAiEELQAEFVDN-------AEELAKLQDELDKIVKTKSELVKEKYHRGIVTDL 411
|
|
| PH_Ses |
cd13288 |
Sesquipedalian family Pleckstrin homology (PH) domain; The sesquipedalian family has 2 ... |
22-106 |
9.43e-04 |
|
Sesquipedalian family Pleckstrin homology (PH) domain; The sesquipedalian family has 2 mammalian members: Ses1 and Ses2, which are also callled 7 kDa inositol polyphosphate phosphatase-interacting protein 1 and 2. They play a role in endocytic trafficking and are required for receptor recycling from endosomes, both to the trans-Golgi network and the plasma membrane. Members of this family form homodimers and heterodimers. Sesquipedalian interacts with inositol polyphosphate 5-phosphatase OCRL-1 (INPP5F) also known as Lowe oculocerebrorenal syndrome protein, a phosphatase enzyme that is involved in actin polymerization and is found in the trans-Golgi network and INPP5B. Sesquipedalian contains a single PH domain. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.
Pssm-ID: 270105 [Multi-domain] Cd Length: 120 Bit Score: 39.14 E-value: 9.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 22 FFIIKESFLLYYSESERKSfetnkyfnihPKGVIPLGGCLVEAREEpSMPYAMKIShqdFHG----NVLLAAESEFEQTQ 97
Cdd:cd13288 28 WFVLKGNLLFYFEKKGDRE----------PLGVIVLEGCTVELAED-AEPYAFAIR---FDGpgarSYVLAAENQEDMES 93
|
....*....
gi 755542439 98 WLEMLQESG 106
Cdd:cd13288 94 WMKALSRAS 102
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
117-366 |
1.03e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.05 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 117 EAMIKSLEAQGLQLAKEKQEYLDKLMEETEELCLQREQR-------EELERLNQVLEAEKQQFEEVVQELRVEQEQIKRE 189
Cdd:PTZ00121 1555 EELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARieevmklYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKK 1634
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 190 LEltaRCLKGVEQEKKElrhlTESLQHTLEELSIEKKKTLEMLEEDKNQPQPLTNQSEQPpasdglhsnlRQIEERMQEL 269
Cdd:PTZ00121 1635 VE---QLKKKEAEEKKK----AEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDE----------KKAAEALKKE 1697
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 270 LAEKLLAEKRMKENEERSRALEEEREFYSSQSQALQNSLQELTAEKQQAERELKAE---VKVRMDLERRLREAEAALRSL 346
Cdd:PTZ00121 1698 AEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEeekKKIAHLKKEEEKKAEEIRKEK 1777
|
250 260
....*....|....*....|
gi 755542439 347 EQGLNSKVRNKEKEERMRAD 366
Cdd:PTZ00121 1778 EAVIEEELDEEDEKRRMEVD 1797
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
117-368 |
1.17e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 41.70 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 117 EAMIKSLEAQGLQLAKEKQEYLDKLMEETEeLClqreqrEELERLNQVLEAEKQQFEEVVQEL--RVEQEQikrelelta 194
Cdd:pfam01576 25 ESELKELEKKHQQLCEEKNALQEQLQAETE-LC------AEAEEMRARLAARKQELEEILHELesRLEEEE--------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 195 RCLKGVEQEKKELRHLTESLQHTLEE-------LSIEKKKT----------LEMLEEDKNQPQPLTNQSEQPPASdgLHS 257
Cdd:pfam01576 89 ERSQQLQNEKKKMQQHIQDLEEQLDEeeaarqkLQLEKVTTeakikkleedILLLEDQNSKLSKERKLLEERISE--FTS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 258 NLRQIEERMQELLAEKLLAEKRMKENEER--------------SRALEEEREFYSSQSQALQNSLQELTAEKQQAERELK 323
Cdd:pfam01576 167 NLAEEEEKAKSLSKLKNKHEAMISDLEERlkkeekgrqelekaKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQ 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 755542439 324 A-------EVKVRMDLERRLREAEAALRSLEQGLNSKVRNKEKEERMRADVS 368
Cdd:pfam01576 247 AalarleeETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLG 298
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
131-344 |
1.25e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.50 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 131 AKEKQEYLDKLMEETEE------LCLQREQREELERLNQVLEAEKQQFEEVVQELRVEQEQIKRELELTARCLKGVEQEK 204
Cdd:pfam02463 206 AKKALEYYQLKEKLELEeeyllyLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 205 KELRHLTESLQHTLEELSIEKKKTLEMLEEDKNQPQPLTNQSEQPPASDGLHSNLRQIEERMQELLAEKLLAEKRMKENE 284
Cdd:pfam02463 286 EELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQ 365
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 285 ERSRALEEEREFYSSQSQALQNSLQELTAEKQQAERELKAEVKVRMDLERRLREAEAALR 344
Cdd:pfam02463 366 EKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEK 425
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
131-340 |
1.41e-03 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 41.15 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 131 AKEKQEYLDKLMEETEElCLQREQREELERLNQVLEAEKQQFeevVQELRVEQEQIKREL--ELTARCLKGVEQEKKELR 208
Cdd:NF033838 60 AKEVESHLEKILSEIQK-SLDKRKHTQNVALNKKLSDIKTEY---LYELNVLKEKSEAELtsKTKKELDAAFEQFKKDTL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 209 HLTESLQHTLEELSIEKKKTLEMLEEDKNQPQPLTNQSeqppasdgLHSNLRQIEERMQELLAEKLLAEKRMKENEERSR 288
Cdd:NF033838 136 EPGKKVAEATKKVEEAEKKAKDQKEEDRRNYPTNTYKT--------LELEIAESDVEVKKAELELVKEEAKEPRDEEKIK 207
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 755542439 289 ALEEEREfySSQSQALQnsLQELTAEKQQAERELK--AEVKVRMDLERRLREAE 340
Cdd:NF033838 208 QAKAKVE--SKKAEATR--LEKIKTDREKAEEEAKrrADAKLKEAVEKNVATSE 257
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
146-366 |
1.52e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 41.31 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 146 EELCLQREQREELERLNQVLEAEKQQFEEvvqELRVEQEQIKRELELTArclkgveqEKKELRHLTESLQHTLEELSIEK 225
Cdd:pfam01576 12 EELQKVKERQQKAESELKELEKKHQQLCE---EKNALQEQLQAETELCA--------EAEEMRARLAARKQELEEILHEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 226 KKTLEMLEEDKNQPQPLTNQSEQPPASdgLHSNLRQIEERMQELLAEKLLAEKRMKENEERSRALEEEREFYSSQSQALQ 305
Cdd:pfam01576 81 ESRLEEEEERSQQLQNEKKKMQQHIQD--LEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755542439 306 NSLQELTAEKQQAERELKAEVKVRMDLERRLREAEAALRSLEQGLNSKVRNKEKEERMRAD 366
Cdd:pfam01576 159 ERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTD 219
|
|
| PH_IRS |
cd01257 |
Insulin receptor substrate (IRS) pleckstrin homology (PH) domain; Insulin receptor substrate ... |
31-104 |
1.85e-03 |
|
Insulin receptor substrate (IRS) pleckstrin homology (PH) domain; Insulin receptor substrate (IRS) molecules are mediators in insulin signaling and play a role in maintaining basic cellular functions such as growth and metabolism. They act as docking proteins between the insulin receptor and a complex network of intracellular signaling molecules containing Src homology 2 (SH2) domains. Four members (IRS-1, IRS-2, IRS-3, IRS-4) of this family have been identified that differ as to tissue distribution, subcellular localization, developmental expression, binding to the insulin receptor, and interaction with SH2 domain-containing proteins. IRS molecules have an N-terminal PH domain, followed by an IRS-like PTB domain which has a PH-like fold. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.cytoskeletal associated molecules, and in lipid associated enzymes.
Pssm-ID: 269959 Cd Length: 106 Bit Score: 38.04 E-value: 1.85e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755542439 31 LYYSESERKsFETNKyfniHPKGVIPLGGCL-VEAREEPSMPYAMKISHQDFHgnVLLAAESEFEQTQWLEMLQE 104
Cdd:cd01257 33 LEYYENEKK-FRRNA----EPKRVIPLSSCFnINKRADAKHKHLIALYTKDEC--FGLVAESEEEQDEWYQALLE 100
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
117-372 |
1.98e-03 |
|
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: 40.98 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 117 EAMIKSLEAQGLQLAKEKQEYLDklmEETEELCLQREQREELERLNQVLEAEKQQFEEVVQELRveqeqikreLELTArc 196
Cdd:pfam12128 247 QQEFNTLESAELRLSHLHFGYKS---DETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELN---------GELSA-- 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 197 LKGVEQEKKELRHLTESLQHTLEELSIEKKKT-LEMLEEDKNQpqpLTNQSEQPPASDGLHSNLRQIEERMQELLAEKL- 274
Cdd:pfam12128 313 ADAAVAKDRSELEALEDQHGAFLDADIETAAAdQEQLPSWQSE---LENLEERLKALTGKHQDVTAKYNRRRSKIKEQNn 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 275 -----LAEKRMKENEERSRALEEEREFYSSQSQALQNSLQELTAEKQQAERELK---AEVKVRMDlerrlrEAEAALRSL 346
Cdd:pfam12128 390 rdiagIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKsrlGELKLRLN------QATATPELL 463
|
250 260
....*....|....*....|....*....
gi 755542439 347 EQGLNSKV---RNKEKEERMRADVSHLKR 372
Cdd:pfam12128 464 LQLENFDErieRAREEQEAANAEVERLQS 492
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
200-356 |
2.11e-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: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 200 VEQEKKELRHLTESLQHTLEElsIEKKKTLEMLEEDKNQPQPLTNQSEQppasDGLHSNLRQIEERMQELLAEKLLAEKR 279
Cdd:COG4913 244 LEDAREQIELLEPIRELAERY--AAARERLAELEYLRAALRLWFAQRRL----ELLEAELEELRAELARLEAELERLEAR 317
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755542439 280 MKENEERSRALEEERefyssqSQALQNSLQELTAEKQQAERELKAEVKVRMDLERRLREAEAALRSLEQGLNSKVRN 356
Cdd:COG4913 318 LDALREELDELEAQI------RGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAE 388
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
140-313 |
2.19e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.71 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 140 KLMEETEELCLQREQREELERLNQVLEAEKQQfEEVVQELRVEQEQikrELEltarclkGVEQEKKELRHLTESLQHTLE 219
Cdd:PRK04863 521 RLSELEQRLRQQQRAERLLAEFCKRLGKNLDD-EDELEQLQEELEA---RLE-------SLSESVSEARERRMALRQQLE 589
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 220 ELSIEKKKtLEMLEEDKNQPQPLTNQ-SEQPPASDglhSNLRQIEERMQELLaekllaekrmkeneERSRALEEEREFYS 298
Cdd:PRK04863 590 QLQARIQR-LAARAPAWLAAQDALARlREQSGEEF---EDSQDVTEYMQQLL--------------ERERELTVERDELA 651
|
170
....*....|....*
gi 755542439 299 SQSQALQNSLQELTA 313
Cdd:PRK04863 652 ARKQALDEEIERLSQ 666
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
114-222 |
3.07e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.15 E-value: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 114 QLGEAMIKSLEAQGLQLAKE-----KQEYLDKLMEETEELclqREQREELERLNQVLEAEKQQFEEVVQELRVEQEQIKR 188
Cdd:PRK12704 38 EEAKRILEEAKKEAEAIKKEalleaKEEIHKLRNEFEKEL---RERRNELQKLEKRLLQKEENLDRKLELLEKREEELEK 114
|
90 100 110
....*....|....*....|....*....|....
gi 755542439 189 ELELTARCLKGVEQEKKELRHLTESLQHTLEELS 222
Cdd:PRK12704 115 KEKELEQKQQELEKKEEELEELIEEQLQELERIS 148
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
165-352 |
3.58e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.43 E-value: 3.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 165 LEAEKQQFEEVVQELRVEQEQIKRELELTARCLKGVEQEKKELRHLTESLQHTLEELSIEKKKTLEMLEEDKNQPQPLTN 244
Cdd:COG3883 28 LQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSYLDV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 245 --QSEQPpaSDGLH--SNLRQIEERMQELLAE----KLLAEKRMKENEERSRALEEEREFYSSQSQALQNSLQELTAEKQ 316
Cdd:COG3883 108 llGSESF--SDFLDrlSALSKIADADADLLEElkadKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLA 185
|
170 180 190
....*....|....*....|....*....|....*.
gi 755542439 317 QAERELKAEVKVRMDLERRLREAEAALRSLEQGLNS 352
Cdd:COG3883 186 QLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
86-318 |
3.95e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.75 E-value: 3.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 86 LLAAESEFEQTQWLEMLQESGkvtwknaqLGEAMIKSLEAQGLQLAKEKQEYLDKLMEETEELCLQREQREELERLNQVL 165
Cdd:COG4717 309 ALPALEELEEEELEELLAALG--------LPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAG 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 166 EAEKQQFEEVVQELRVEQEQIKRELELTARclkgVEQEKKELRHLTESLQ-HTLEELSIEKKKTLEMLEEDKNQpqpltn 244
Cdd:COG4717 381 VEDEEELRAALEQAEEYQELKEELEELEEQ----LEELLGELEELLEALDeEELEEELEELEEELEELEEELEE------ 450
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755542439 245 qseqppasdgLHSNLRQIEERMQELLAEKLLAEKRMKENEERSRALEEEREFYSSQ--SQALQNSLQELTAEKQQA 318
Cdd:COG4717 451 ----------LREELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKlaLELLEEAREEYREERLPP 516
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
87-355 |
4.24e-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: 39.94 E-value: 4.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 87 LAAESEFEQTQWLEMLQESGKVTWKNAQLGEAMIksLEAQGL-QLAKEKQEYLDKLMEETEELCLQREQREELERLNQVL 165
Cdd:COG3096 852 LAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANL--LADETLaDRLEELREELDAAQEAQAFIQQHGKALAQLEPLVAVL 929
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 166 EAEKQQFEEV---VQELRVEQEQIKREL----ELTARCL----KGVEQEKKELRHLTESLQHTLEELSIEKKKTLEMLEe 234
Cdd:COG3096 930 QSDPEQFEQLqadYLQAKEQQRRLKQQIfalsEVVQRRPhfsyEDAVGLLGENSDLNEKLRARLEQAEEARREAREQLR- 1008
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 235 dknQPQPLTNQSEQPPAS-DGLHSNLRQI-EERMQELLAEKLLAEKRMkenEERSRALEEEREFYSSQSQALQNSLqelt 312
Cdd:COG3096 1009 ---QAQAQYSQYNQVLASlKSSRDAKQQTlQELEQELEELGVQADAEA---EERARIRRDELHEELSQNRSRRSQL---- 1078
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 755542439 313 aEKQQAERELKAEvkvrmDLERRLREAEAALRSL-EQGLNSKVR 355
Cdd:COG3096 1079 -EKQLTRCEAEMD-----SLQKRLRKAERDYKQErEQVVQAKAG 1116
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
94-363 |
4.27e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 39.95 E-value: 4.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 94 EQTQWLEMLQESGKVTWKNAQLGEAMIKSLEAQGLQLAKEKQEYLDKLMEETEELCLQREQREELERLNQVLEAEKQQFE 173
Cdd:pfam02463 667 SLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKID 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 174 EVVQElrvEQEQIKRELELTARCLKGVEQEKKELRHLTESLQHTLEELSIEKKKTLEMLEEDKNQPQPLTNQSEQPPASD 253
Cdd:pfam02463 747 EEEEE---EEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLL 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 254 GLHSNLRQIEERMQELLAEKLLAEKRMKENEERSRALEEEREFYSSQSQALQ---NSLQELTAEKQQAERELKAEVKVRM 330
Cdd:pfam02463 824 IEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKeeeLEEQKLKDELESKEEKEKEEKKELE 903
|
250 260 270
....*....|....*....|....*....|...
gi 755542439 331 DLERRLREAEAALRSLEQGLNSKVRNKEKEERM 363
Cdd:pfam02463 904 EESQKLNLLEEKENEIEERIKEEAEILLKYEEE 936
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
88-448 |
5.07e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.53 E-value: 5.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 88 AAESEFEQTQWLEMLQESGKVTWKNAQLGEAMIKSLEAQGLQLAKEKQEYLDKLMEETEELCLQREQREELERLNQVLEA 167
Cdd:COG1196 422 ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 168 EKQQFEEVVQELRVEQEQIKRELELTARCLKGVEQEKKELRHLTESLQHTLEELSIEKKKTLEMLEEDK----------- 236
Cdd:COG1196 502 DYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKagratflpldk 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 237 ----NQPQPLTNQSEQPPASDGLHSNLRQIEERM---QELLAEKLLAEKRMKENEERSRALEEEREF-----------YS 298
Cdd:COG1196 582 irarAALAAALARGAIGAAVDLVASDLREADARYyvlGDTLLGRTLVAARLEAALRRAVTLAGRLREvtlegeggsagGS 661
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 299 SQSQALQNSLQELTAEKQQAERELKAEVKVRMDLERRLREAEAALRSLEQGLNSKVRNKEKEERMRADVSHLKR-FFEEC 377
Cdd:COG1196 662 LTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREeLLEEL 741
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755542439 378 IRNAELEAKMPVIMKNSVYIHKAATRRIKSCRfhRRRSstswndmkpsqsfmtsQLEANN---IEELKEVAKRL 448
Cdd:COG1196 742 LEEEELLEEEALEELPEPPDLEELERELERLE--REIE----------------ALGPVNllaIEEYEELEERY 797
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
114-348 |
5.89e-03 |
|
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: 39.18 E-value: 5.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 114 QLGEAMIKSLEAQGLQLAKEKQEYLDKLMEETEELCLQREQREELErlnqvleaEKQQFEEVVQELRVEQEQIKRELELT 193
Cdd:TIGR00618 208 LCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQE--------EQLKKQQLLKQLRARIEELRAQEAVL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 194 ARCLKGVEQEKKELRHLTES-----LQHTLEELSIEKKKTLEMLEEDKNQPQPLTNQSEQPPASDGLHSNLRQIEERMQE 268
Cdd:TIGR00618 280 EETQERINRARKAAPLAAHIkavtqIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRD 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 269 LLAEKLLAEK---RMKENEERSRALEEEREFYSSQSQALQNSLQELTAEKQQAERELKAEVKVRMDLERRLREAEAALRS 345
Cdd:TIGR00618 360 AHEVATSIREiscQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRY 439
|
...
gi 755542439 346 LEQ 348
Cdd:TIGR00618 440 AEL 442
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
120-370 |
6.15e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 39.33 E-value: 6.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 120 IKSLEAQGLQLAKEKQEYLDKLMEETEELCLQ--REQREELERLNQVLEAEKQQFEEVVQELRVEQEQIKRELELTARCL 197
Cdd:pfam15921 240 IFPVEDQLEALKSESQNKIELLLQQHQDRIEQliSEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQL 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 198 KGVEQEKKELRHLTESLQHTLEELSIEKKKTLEMLEEDKNQPQPLTNQSEQPPASdglhsnlrqIEERMQELLAEKLLAE 277
Cdd:pfam15921 320 SDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGN---------LDDQLQKLLADLHKRE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 278 KRMKENEERSRALEEEREFYSSQSQALQNSLQELTAEKQQAERELKA-EVKVRMDLERRLREAEAALRSLEQGLNSKVRN 356
Cdd:pfam15921 391 KELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAmKSECQGQMERQMAAIQGKNESLEKVSSLTAQL 470
|
250
....*....|....
gi 755542439 357 KEKEERMRADVSHL 370
Cdd:pfam15921 471 ESTKEMLRKVVEEL 484
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
131-353 |
6.84e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 38.66 E-value: 6.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 131 AKEKQEYLDKLMEETEELclqreqREELERLNQVLEAEKQQFEEVVQELRVEQEQIKrelELTARclkgVEQEKKELRHL 210
Cdd:COG3883 18 IQAKQKELSELQAELEAA------QAELDALQAELEELNEEYNELQAELEALQAEID---KLQAE----IAEAEAEIEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 211 TESLQHTLEELSIEKKKT--LEMLEEDKNQPQPLTNQSEQPPASDGLHSNLRQIEERMQELLAEKLLAEKRMKENEERSR 288
Cdd:COG3883 85 REELGERARALYRSGGSVsyLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755542439 289 ALEEEREFYSSQSQALQNSLQELTAEKQQAERELKAEVKVRMDLERRLREAEAALRSLEQGLNSK 353
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAA 229
|
|
| PH1_FARP1-like |
cd01220 |
FERM, RhoGEF and pleckstrin domain-containing protein 1 and related proteins Pleckstrin ... |
3-104 |
6.98e-03 |
|
FERM, RhoGEF and pleckstrin domain-containing protein 1 and related proteins Pleckstrin Homology (PH) domain, repeat 1; Members here include FARP1 (also called Chondrocyte-derived ezrin-like protein; PH domain-containing family C member 2), FARP2 (also called FIR/FERM domain including RhoGEF; FGD1-related Cdc42-GEF/FRG), and FARP6 (also called Zinc finger FYVE domain-containing protein 24). They are members of the Dbl family guanine nucleotide exchange factors (GEFs) which are upstream positive regulators of Rho GTPases. Little is known about FARP1 and FARP6, though FARP1 has increased expression in differentiated chondrocytes. FARP2 is thought to regulate neurite remodeling by mediating the signaling pathways from membrane proteins to Rac. It is found in brain, lung, and testis, as well as embryonic hippocampal and cortical neurons. FARP1 and FARP2 are composed of a N-terminal FERM domain, a proline-rich (PR) domain, Dbl-homology (DH), and two C-terminal PH domains. FARP6 is composed of Dbl-homology (DH), and two C-terminal PH domains separated by a FYVE domain. This hierarchy contains the first PH repeat. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.
Pssm-ID: 269928 Cd Length: 109 Bit Score: 36.14 E-value: 6.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 3 FLLHGLSSRPSETSYGLLMFFIIKEsFLLYYSeserKSFETNKYFNIHpkGVIPLGGCLVEARE-EPSMPYAMKISHQDF 81
Cdd:cd01220 8 FIREGCLQKLSKKGLQQRMFFLFSD-VLLYTS----RSPTPSLQFKVH--GQLPLRGLMVEESEpEWGVAHCFTIYGGNR 80
|
90 100
....*....|....*....|...
gi 755542439 82 HgnVLLAAESEFEQTQWLEMLQE 104
Cdd:cd01220 81 A--LTVAASSEEEKERWLEDLQR 101
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
243-354 |
7.93e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 38.91 E-value: 7.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 243 TNQSEQPPASDGLHSNLRQIEERMQELLAEKLLAEK-RMKENEERSRALEEEREFYSSQSQALQNSLQELTAEKQQAERE 321
Cdd:COG0542 404 MEIDSKPEELDELERRLEQLEIEKEALKKEQDEASFeRLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQR 483
|
90 100 110
....*....|....*....|....*....|...
gi 755542439 322 LKAEVkvrmDLERRLREAEAALRSLEQGLNSKV 354
Cdd:COG0542 484 YGKIP----ELEKELAELEEELAELAPLLREEV 512
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
111-329 |
9.65e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 38.80 E-value: 9.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 111 KNAQLGEAMIKSLEAQGLQLAKEKQEYLDKLMEETEELCLQREQREELERLNQVLEAEKQQFEEVVQELRVEQEQIKREL 190
Cdd:pfam02463 806 LEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLK 885
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 191 ELTARCLKGVEQEKKELRHLTESLQHTLE-ELSIEKKKTLEMLEEDKNQPQPLTNQSEQPPASDGLHSNLRQIEERMQEL 269
Cdd:pfam02463 886 DELESKEEKEKEEKKELEEESQKLNLLEEkENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRL 965
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 270 LAEKLLAEKRMKENEERSRALEEEREFYSSQSQalqnSLQELTAEKQQAERELKAEVKVR 329
Cdd:pfam02463 966 LLAKEELGKVNLMAIEEFEEKEERYNKDELEKE----RLEEEKKKLIRAIIEETCQRLKE 1021
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
225-386 |
9.94e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 38.39 E-value: 9.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 225 KKKTLEMLEEDKNQPQPLTNQSEQPPASDGLHSNLRQIEERMQE---LLAEKLLAEKRMKENEERSRALEE--EREFYSS 299
Cdd:pfam15709 344 EMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEeirLRKQRLEEERQRQEEEERKQRLQLqaAQERARQ 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542439 300 QSQALQNSLQELTAEKQQAERELKAEVKVRM-DLERRLREAEAALRSL--EQGLNSKVRNKEKEERMRADVSHLKRFFEE 376
Cdd:pfam15709 424 QQEEFRRKLQELQRKKQQEEAERAEAEKQRQkELEMQLAEEQKRLMEMaeEERLEYQRQKQEAEEKARLEAEERRQKEEE 503
|
170
....*....|
gi 755542439 377 CIRNAELEAK 386
Cdd:pfam15709 504 AARLALEEAM 513
|
|
| |
